LiteFold/InterPro · Datasets at Hugging Face

IPR012700

12,700

ATP-binding protein PhnK

PhnK

Family

3,839

false

This entry represents the ATP-binding protein PhnK from Escherichia coli and similar sequences mainly found in bacteria. PhnK associates with the C-P lyase core complex (PhnGHIJ), which is essential for the conversion of phosphonate into 5-phosphoribosyl-α-1-diphosphate (PRPP) in an ATP-dependent fashion under low leve...

[]

0

[ "PIRSF", "NCBIFAM" ]

[ "PIRSF037116", "TIGR02323" ]

[ "CP_lyase_PhnK", "CP_lyasePhnK" ]

[ 3825, 3035 ]

2

[ "GP", "GP" ]

[ "GenProp0232", "GenProp1165" ]

[ "GP:GenProp0232", "GP:GenProp1165" ]

2

[ "7z15", "7z16", "7z17", "7z18", "7z19" ]

5

[ "PUB00016017", "PUB00103840", "PUB00103841", "PUB00103842" ]

[ "8388873", "36813778", "21705661", "26280334" ]

[ "Mutational analysis of an Escherichia coli fourteen-gene operon for phosphonate degradation, using TnphoA' elements.", "Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase.", "Five phosphonate operon gene products as components of a multi-subunit complex of the carbon-phosphoru...

[ 1993, 2023, 2011, 2015 ]

4

[]

0

null

[ "Bacteria", "Methanobacteriota", "Symbiodiniaceae", "ecological metagenomes" ]

[ 3792, 32, 2, 13 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

ATP-binding protein PhnK

PhnK

4

IPR012701

12,701

Phosphonate C-P lyase system, PhnL

CP_lyase_PhnL

Family

3,364

false

Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three-component ABC transporter, where is the permease, is the phosphonates binding protein, and is the ATP-binding cassette (ABC) protein. They differ, howeve...

[]

0

[ "NCBIFAM" ]

[ "TIGR02324" ]

[ "CP_lyasePhnL" ]

[ 3364 ]

1

[ "GP", "GP", "GP", "GP" ]

[ "GenProp0232", "GenProp1165", "GenProp1381", "GenProp1630" ]

[ "GP:GenProp0232", "GP:GenProp1165", "GP:GenProp1381", "GP:GenProp1630" ]

4

[ "7z15", "7z16" ]

2

[ "PUB00011420", "PUB00016017" ]

[ "1335942", "8388873" ]

[ "Molecular genetic studies of a 10.9-kb operon in Escherichia coli for phosphonate uptake and biodegradation.", "Mutational analysis of an Escherichia coli fourteen-gene operon for phosphonate degradation, using TnphoA' elements." ]

[ 1992, 1993 ]

2

[]

0

null

[ "Bacteria", "Halobacteriales", "Symbiodinium necroappetens", "ecological metagenomes" ]

[ 3354, 2, 1, 7 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Phosphonate C-P lyase system, PhnL

CP_lyase_PhnL

3

IPR012702

12,702

Phosphonate C-P lyase system, transcriptional regulator PhnF

CP_lyase_PhnF

Family

3,484

false

Members of this family are the PhnF protein associated with C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three-component ABC transporter, where is the permease, is the phosphonates binding protein, and is the ATP-binding cassette (ABC) protein. They d...

[]

0

[ "NCBIFAM" ]

[ "TIGR02325" ]

[ "C_P_lyase_phnF" ]

[ 3484 ]

1

[ "GP" ]

[ "GenProp0232" ]

[ "GP:GenProp0232" ]

1

[ "2fa1" ]

1

[ "PUB00016017", "PUB00062386" ]

[ "8388873", "18083811" ]

[ "Mutational analysis of an Escherichia coli fourteen-gene operon for phosphonate degradation, using TnphoA' elements.", "Differential regulation of high-affinity phosphate transport systems of Mycobacterium smegmatis: identification of PhnF, a repressor of the phnDCE operon." ]

[ 1993, 2008 ]

2

[]

0

null

[ "Bacteria", "Eukaryota", "ecological metagenomes" ]

[ 3478, 2, 4 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Phosphonate C-P lyase system, transcriptional regulator PhnF

CP_lyase_PhnF

4

IPR012703

12,703

2-aminoethylphosphonate--pyruvate transaminase

NH2EtPonate_pyrv_transaminase

Family

4,900

false

Phosphonates are a class of organophosphorus compounds, characterised by a stable C-P bond, which are found in a variety of biologically produced molecules including antiobiotics, lipids, proteins and polysaccharides [ ]. The functions of these molecules include phosphorus storage, cell communication, host recognition ...

[ "GO:0047304", "GO:0019700" ]

[ "2-aminoethylphosphonate-pyruvate transaminase activity", "organic phosphonate catabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "NCBIFAM", "NCBIFAM", "NCBIFAM" ]

[ "MF_01376", "NF010006", "TIGR02326", "TIGR03301" ]

[ "PhnW_aminotrans_5", "PRK13479.1", "transamin_PhnW", "PhnW-AepZ" ]

[ 4882, 4466, 3837, 4537 ]

4

[ "EC", "GP", "GP", "GP", "METACYC", "METACYC" ]

[ "2.6.1.37", "GenProp0238", "GenProp0713", "GenProp0724", "PWY-6832", "PWY-6839" ]

[ "EC:2.6.1.37", "GP:GenProp0238", "GP:GenProp0713", "GP:GenProp0724", "METACYC:PWY-6832", "METACYC:PWY-6839" ]

6

[ "1m32", "6pd1", "6pd2", "7e7g" ]

4

[ "PUB00027210", "PUB00033214" ]

[ "12403617", "11952414" ]

[ "Degradation pathway of the phosphonate ciliatine: crystal structure of 2-aminoethylphosphonate transaminase.", "Phosphonates and their degradation by microorganisms." ]

[ 2002, 2002 ]

2

[]

0

null

[ "Bacteria", "Eukaryota", "Mimiviridae sp. ChoanoV1", "unclassified sequences" ]

[ 4638, 224, 1, 37 ]

4

[]

0

true

Family

2-aminoethylphosphonate--pyruvate transaminase

NH2EtPonate_pyrv_transaminase

5

IPR012704

12,704

Signal transduction response regulator, propionate catabolism, transcriptional regulator PrpR

Sig_transdc_resp-reg_PrpR

Family

2,170

false

Two-component signal transduction systems enable bacteria to sense, respond, and adapt to a wide range of environments, stressors, and growth conditions [ ]. Some bacteria can contain up to as many as 200 two-component systems that need tight regulation to prevent unwanted cross-talk [ ]. These pathways have been adapt...

[ "GO:0000156", "GO:0003677", "GO:0000160", "GO:0019629", "GO:0005737" ]

[ "phosphorelay response regulator activity", "DNA binding", "phosphorelay signal transduction system", "propionate catabolic process, 2-methylcitrate cycle", "cytoplasm" ]

[ "molecular_function", "molecular_function", "biological_process", "biological_process", "cellular_component" ]

5

[ "NCBIFAM" ]

[ "TIGR02329" ]

[ "propionate_PrpR" ]

[ 2170 ]

1

[ "GP" ]

[ "GenProp0240" ]

[ "GP:GenProp0240" ]

1

[]

0

[ "PUB00010651", "PUB00011096", "PUB00020194", "PUB00033359", "PUB00042804", "PUB00042805", "PUB00042806", "PUB00042807" ]

[ "12372152", "10966457", "10648513", "9851993", "16176121", "18076326", "11934609", "11489844" ]

[ "Histidine protein kinases: key signal transducers outside the animal kingdom.", "Two-component signal transduction.", "prpR, ntrA, and ihf functions are required for expression of the prpBCDE operon, encoding enzymes that catabolize propionate in Salmonella enterica serovar typhimurium LT2.", "Studies of reg...

[ 2002, 2000, 2000, 1998, 2005, 2007, 2002, 2001 ]

8

[]

0

null

[ "Bacteria", "Opisthokonta", "metagenomes" ]

[ 2159, 2, 9 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Signal transduction response regulator, propionate catabolism, transcriptional regulator PrpR

Sig_transdc_resp-reg_PrpR

7

IPR012705

12,705

2-methylcitrate dehydratase PrpD

2Me_IsoCit_deHydtase_PrpD

Family

5,484

false

At least five distinct pathways exist for the catabolism of propionate by way of propionyl-CoA. Most members of this family are bacterial proteins known or predicted to act as 2-methylcitrate dehydratase; an enzyme which catalyses the third step the methylcitrate cycle of propionate catabolism [ ]. A related clade of a...

[ "GO:0047547", "GO:0051537", "GO:0019679" ]

[ "2-methylcitrate dehydratase activity", "2 iron, 2 sulfur cluster binding", "propionate metabolic process, methylcitrate cycle" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02330" ]

[ "prpD" ]

[ 5484 ]

1

[ "EC", "GP", "GP" ]

[ "4.2.1.79", "GenProp0240", "GenProp1687" ]

[ "EC:4.2.1.79", "GP:GenProp0240", "GP:GenProp1687" ]

3

[ "1szq", "5mux", "5mvi", "6s62" ]

4

[ "PUB00017752", "PUB00019867", "PUB00033360", "PUB00090961" ]

[ "11782506", "11294638", "8759838", "28956599" ]

[ "AcnC of Escherichia coli is a 2-methylcitrate dehydratase (PrpD) that can use citrate and isocitrate as substrates.", "In vitro conversion of propionate to pyruvate by Salmonella enterica enzymes: 2-methylcitrate dehydratase (PrpD) and aconitase Enzymes catalyze the conversion of 2-methylcitrate to 2-methylisoci...

[ 2002, 2001, 1996, 2017 ]

4

[ "IPR005656" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 3810, 1605, 69 ]

3

[ "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]

[ 1, 1, 1 ]

3

true

Family

2-methylcitrate dehydratase PrpD

2Me_IsoCit_deHydtase_PrpD

5

IPR012706

12,706

Rib/alpha/Esp surface antigen repeat

Rib_alpha_Esp_rpt

Repeat

1,139

false

This entry represents a region of about 79 amino acids found tandemly repeated up to fourteen times within the proteins that contain it. The repeats lack cysteines and are highly conserved, even at the DNA level, within and between proteins [ ]. Proteins containing these repeats include the Rib and alpha surface antige...

[]

0

[ "NCBIFAM" ]

[ "TIGR02331" ]

[ "rib_alpha" ]

[ 1139 ]

1

[]

0

[ "6s5x", "6s5y", "6s5z", "6sx1", "8yk7", "8yke" ]

6

[ "PUB00017753", "PUB00033362" ]

[ "8702550", "1438195" ]

[ "Identification of a family of streptococcal surface proteins with extremely repetitive structure.", "Large, identical, tandem repeating units in the C protein alpha antigen gene, bca, of group B streptococci." ]

[ 1996, 1992 ]

2

[]

0

null

[ "Bacteria", "human gut metagenome" ]

[ 1132, 7 ]

2

[]

0

true

Repeat

Rib/alpha/Esp surface antigen repeat

Rib_alpha_Esp_rpt

2

IPR012707

12,707

4-hydroxyphenylacetate permease

HPA_permease

Family

1,013

false

Among the different families of transporter only two occur ubiquitously in all classifications of organisms. These are the ATP-Binding Cassette (ABC) superfamily and the Major Facilitator Superfamily (MFS). The MFS transporters are single-polypeptide secondary carriers capable only of transporting small solutes in resp...

[ "GO:1901241", "GO:1900754" ]

[ "4-hydroxyphenylacetate transmembrane transporter activity", "4-hydroxyphenylacetate transport" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02332" ]

[ "HpaX" ]

[ 1013 ]

1

[ "GP" ]

[ "GenProp0231" ]

[ "GP:GenProp0231" ]

1

[]

0

[ "PUB00007278", "PUB00007279", "PUB00017754" ]

[ "9529885", "9868370", "9315705" ]

[ "Major facilitator superfamily.", "Sugar transporters from bacteria, parasites and mammals: structure-activity relationships.", "Identification of the 4-hydroxyphenylacetate transport gene of Escherichia coli W: construction of a highly sensitive cellular biosensor." ]

[ 1998, 1998, 1997 ]

3

[ "IPR011701" ]

[]

1

0

1

[ "Pseudomonadota" ]

[ 1013 ]

1

[]

0

true

Family

4-hydroxyphenylacetate permease

HPA_permease

4

IPR012708

12,708

2-methylisocitrate dehydratase AcnD, Fe/S-dependent

2Me_IsoCit_deHydtase_FeS-dep

Family

3,680

false

This entry represents Fe/S-dependent 2-methylisocitrate dehydratase (AcnD; ), which is part of the 2-methylcitrate (2-MC) cycle that occurs in certain fungi and bacteria. The 2-MC cycle is involved in the degradation of propionyl-CoA via 2-methylcitrate, with AcnD functioning after PrpD and before PrpB. AcnD acts to ca...

[ "GO:0019679" ]

[ "propionate metabolic process, methylcitrate cycle" ]

[ "biological_process" ]

1

[ "NCBIFAM" ]

[ "TIGR02333" ]

[ "2met_isocit_dHY" ]

[ 3680 ]

1

[ "GP" ]

[ "GenProp0240" ]

[ "GP:GenProp0240" ]

1

[]

0

[ "PUB00016694", "PUB00017755" ]

[ "12473114", "14702315" ]

[ "Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase.", "The acnD genes of Shewenella oneidensis and Vibrio cholerae encode a new Fe/S-dependent 2-methylcitrate dehydratase enzyme that requires prpF function in vivo." ]

[ 2002, 2004 ]

2

[ "IPR006249" ]

[]

1

0

1

[ "Bacteria", "Knufia peltigerae", "unclassified sequences" ]

[ 3658, 1, 21 ]

3

[]

0

true

Family

2-methylisocitrate dehydratase AcnD, Fe/S-dependent

2Me_IsoCit_deHydtase_FeS-dep

6

IPR012709

12,709

2-methyl-aconitate isomerase PrpF

PrpF

Family

3,860

false

PrpF is involved in the catabolism of short chain fatty acids (SCFA) via the 2-methylcitrate cycle II (propionate degradation route). PrpF catalyses the cis-trans isomerization of 2-methyl-aconitate through a base-catalyzed proton abstraction coupled with a rotation about C2-C3 bond of 2-methyl-aconitate [ , ].

[ "GO:0016853", "GO:0019629" ]

[ "isomerase activity", "propionate catabolic process, 2-methylcitrate cycle" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02334" ]

[ "prpF" ]

[ 3860 ]

1

[ "GP" ]

[ "GenProp0240" ]

[ "GP:GenProp0240" ]

1

[ "2h9f", "2pvz", "2pw0", "5k87" ]

4

[ "PUB00017755", "PUB00044740" ]

[ "14702315", "17567742" ]

[ "The acnD genes of Shewenella oneidensis and Vibrio cholerae encode a new Fe/S-dependent 2-methylcitrate dehydratase enzyme that requires prpF function in vivo.", "The three-dimensional crystal structure of the PrpF protein of Shewanella oneidensis complexed with trans-aconitate: insights into its biological func...

[ 2004, 2007 ]

2

[ "IPR007400" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 3835, 5, 20 ]

3

[]

0

true

Family

2-methyl-aconitate isomerase PrpF

PrpF

7

IPR012710

12,710

Phosphonoacetate hydrolase

Phosphonoacetate_hydro

Family

1,260

false

This family consists of examples of phosphonoacetate hydrolase, an enzyme specific for the cleavage of the C-P bond in phosphonoacetate. Phosphonates are organic compounds with a direct C-P bond that is far less labile than the C-O-P bonds of phosphate attachment sites. Phosphonates may be degraded for phosphorus and e...

[ "GO:0047400" ]

[ "phosphonoacetate hydrolase activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR02335" ]

[ "hydr_PhnA" ]

[ 1260 ]

1

[ "EC", "GP" ]

[ "3.11.1.2", "GenProp0713" ]

[ "EC:3.11.1.2", "GP:GenProp0713" ]

2

[ "1ei6", "3szy", "3szz", "3t00", "3t01", "3t02" ]

6

[ "PUB00015581" ]

[ "9300819" ]

[ "Cloning of the phosphonoacetate hydrolase gene from Pseudomonas fluorescens 23F encoding a new type of carbon-phosphorus bond cleaving enzyme and its expression in Escherichia coli and Pseudomonas putida." ]

[ 1997 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "ecological metagenomes" ]

[ 1055, 193, 12 ]

3

[]

0

true

Family

Phosphonoacetate hydrolase

Phosphonoacetate_hydro

1

IPR012711

12,711

Lacto-N-biose phosphorylase/D-galactosyl-beta-1->4-L-rhamnose phosphorylase

Lacto-N-biose_phosphorylase

Family

1,021

false

This entry includes a group of bacterial phosphorylases, including lacto-N-biose phosphorylase (lnpA) from Bifidobacterium [ ] and D-galactosyl-beta-1->4-L-rhamnose phosphorylase (Cphy_1920) from Lachnoclostridium phytofermentans [ ]. LnpA can reversibly phosphorolyzes lacto-N-biose to Gal1-P and N-acetylglucosamine (G...

[ "GO:0004645" ]

[ "1,4-alpha-oligoglucan phosphorylase activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR02336" ]

[ "" ]

[ 1021 ]

1

[ "EC" ]

[ "2.4.1.211" ]

[ "EC:2.4.1.211" ]

1

[ "2zus", "2zut", "2zuu", "2zuv", "2zuw", "3wfz" ]

6

[ "PUB00045013", "PUB00050451", "PUB00085054" ]

[ "15933016", "19124470", "19491100" ]

[ "Novel putative galactose operon involving lacto-N-biose phosphorylase in Bifidobacterium longum.", "The crystal structure of galacto-N-biose/lacto-N-biose I phosphorylase: a large deformation of a TIM barrel scaffold.", "Characterization of three beta-galactoside phosphorylases from Clostridium phytofermentans...

[ 2005, 2009, 2009 ]

3

[]

0

null

[ "Bacteria", "ecological metagenomes" ]

[ 1019, 2 ]

2

[]

0

true

Family

Lacto-N-biose phosphorylase/D-galactosyl-beta-1->4-L-rhamnose phosphorylase

Lacto-N-biose_phosphorylase

1

IPR012712

12,712

HTH-type transcriptional regulator HpaR/FarR

HpaR/FarR

Family

2,650

false

This Helix-Turn-Helix transcriptional regulator is a member of the MarR family. Proteins in this family include FarR from Neisseria gonorrhoeae and HpaR from E. coli. HpaR is found in association with operons for the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate. FarR negatively controls expression ...

[ "GO:0003677", "GO:0045892" ]

[ "DNA binding", "negative regulation of DNA-templated transcription" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02337" ]

[ "HpaR" ]

[ 2650 ]

1

[ "GP" ]

[ "GenProp0231" ]

[ "GP:GenProp0231" ]

1

[ "2fbi", "5aip", "5aiq", "7el2", "7el3" ]

5

[ "PUB00091686", "PUB00091687" ]

[ "14645274", "16796676" ]

[ "FarR regulates the farAB-encoded efflux pump of Neisseria gonorrhoeae via an MtrR regulatory mechanism.", "Integration Host Factor is required for FarR repression of the farAB-encoded efflux pump of Neisseria gonorrhoeae." ]

[ 2003, 2006 ]

2

[ "IPR039422" ]

[]

1

0

1

[ "Bacteria", "Symbiodiniaceae", "unclassified sequences" ]

[ 2635, 2, 13 ]

3

[]

0

true

Family

HTH-type transcriptional regulator HpaR/FarR

HpaR/FarR

5

IPR012713

12,713

Prefoldin subunit beta

PfdB

Family

904

false

Chaperonins are cytosolic, ATP-dependent molecular chaperones, with a conserved toroidal architecture, that assist in the folding of nascent and/or denatured polypeptide chains. The group I chaperonin system consists of GroEL and GroES, and are found (usually) in bacteria and eukaryotic organelles. The group II chapero...

[ "GO:0051082", "GO:0006457", "GO:0016272" ]

[ "unfolded protein binding", "protein folding", "prefoldin complex" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_00307", "TIGR02338" ]

[ "PfdB", "gimC_beta" ]

[ 903, 880 ]

2

[ "GP" ]

[ "GenProp0246" ]

[ "GP:GenProp0246" ]

1

[ "1fxk", "2zdi", "2zqm" ]

3

[ "PUB00017756" ]

[ "10581246" ]

[ "MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin." ]

[ 1999 ]

1

[ "IPR002777" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Geodia barretti", "ecological metagenomes" ]

[ 873, 2, 1, 28 ]

4

[]

0

true

Family

Prefoldin subunit beta

PfdB

1

IPR012714

12,714

Chaperonin/Thermosome

Chaperonin-like

Family

1,895

false

Thermosome (or cpn60) is the archaeal group II chaperonin (counterpart to the group I chaperonin, GroEL/GroES, in bacteria), a toroidal, ATP-dependent molecular chaperone that assists in the folding or refolding of nascent or denatured proteins [ ]. Cpn60 consists of two stacked octameric rings, which are composed of o...

[ "GO:0005524", "GO:0051082", "GO:0006457" ]

[ "ATP binding", "unfolded protein binding", "protein folding" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM", "CDD" ]

[ "TIGR02339", "cd03343" ]

[ "thermosome_arch", "cpn60" ]

[ 1877, 1727 ]

2

[ "EC", "GP" ]

[ "5.6.1.7", "GenProp0246" ]

[ "EC:5.6.1.7", "GP:GenProp0246" ]

2

[ "1a6d", "1a6e", "1q2v", "1q3q", "1q3r", "1q3s", "3aq1", "3iyf", "3izh", "3izi", "3izj", "3izk", "3izl", "3izm", "3izn", "3j02", "3j03", "3j1b", "3j1c", "3j1e", "3j1f", "3j3x", "3kfb", "3kfe", "3kfk", "3ko1", "3los", "3ruq", "3rus", "3ruv", "3ruw", "4xcd"...

48

[ "PUB00001019", "PUB00001034", "PUB00004124", "PUB00004127", "PUB00004129", "PUB00005432", "PUB00064264", "PUB00074264", "PUB00074265", "PUB00074266", "PUB00080867", "PUB00080868", "PUB00080869", "PUB00080871", "PUB00080873" ]

[ "15335898", "7953530", "1352040", "1352857", "1630492", "7846767", "7601114", "20194787", "18595008", "15027029", "11340060", "10753735", "10550210", "11580264", "12354605" ]

[ "TCP1 - molecular chaperonin of the cytoplasm?", "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin.", "What is a chaperonin?", "Protein folding. Cytosolic chaperonin confirmed.", "T-complex polypeptide-1 is a subunit of a heteromeric particle in the eu...

[ 1992, 1994, 1992, 1992, 1992, 1994, 1995, 2010, 2009, 2004, 2001, 2000, 1999, 2001, 2002 ]

15

[ "IPR017998" ]

[]

1

0

1

[ "Archaea", "Bacteria candidate phyla", "Geodia barretti", "unclassified sequences" ]

[ 1855, 2, 4, 34 ]

4

[]

0

true

Family

Chaperonin/Thermosome

Chaperonin-like

7

IPR012715

12,715

T-complex protein 1, alpha subunit

Chap_CCT_alpha

Family

4,331

false

This family consists exclusively of the CCT alpha subunit (part of a paralogous family) from animals, plants, fungi, and other eukaryotes. Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [ , ]. Chaperonins a...

[ "GO:0005524", "GO:0016887", "GO:0051082", "GO:0006457" ]

[ "ATP binding", "ATP hydrolysis activity", "unfolded protein binding", "protein folding" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "NCBIFAM", "CDD" ]

[ "TIGR02340", "cd03335" ]

[ "chap_CCT_alpha", "TCP1_alpha" ]

[ 3889, 4326 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-CEL-390471", "R-CEL-6814122", "R-DDI-390471", "R-DDI-6814122", "R-DME-390471", "R-DME-6814122", "R-HSA-389957", "R-HSA-389960", "R-HSA-390450", "R-HSA-390471", "R-HSA-5620922", "R-HSA-6814122", "R-HSA-8950505", "R-MMU-390471", "R-MMU-6814122", "R-RNO-390471", "R-RNO-6814122", "R...

[ "REACTOME:R-CEL-390471", "REACTOME:R-CEL-6814122", "REACTOME:R-DDI-390471", "REACTOME:R-DDI-6814122", "REACTOME:R-DME-390471", "REACTOME:R-DME-6814122", "REACTOME:R-HSA-389957", "REACTOME:R-HSA-389960", "REACTOME:R-HSA-390450", "REACTOME:R-HSA-390471", "REACTOME:R-HSA-5620922", "REACTOME:R-HSA...

21

[ "3iyg", "4b2t", "4v81", "4v8r", "4v94", "5gw4", "5gw5", "6krd", "6kre", "6ks6", "6ks7", "6ks8", "6nr8", "6nr9", "6nra", "6nrb", "6nrc", "6nrd", "6qb8", "7lum", "7lup", "7nvl", "7nvm", "7nvn", "7nvo", "7trg", "7ttn", "7ttt", "7tub", "7wu7", "7wz3", "7x0a"...

73

[ "PUB00001019", "PUB00001034", "PUB00004124", "PUB00004127", "PUB00004129", "PUB00005432", "PUB00064264", "PUB00074264", "PUB00074265", "PUB00074266", "PUB00080867", "PUB00080868", "PUB00080869", "PUB00080871", "PUB00080873" ]

[ "15335898", "7953530", "1352040", "1352857", "1630492", "7846767", "7601114", "20194787", "18595008", "15027029", "11340060", "10753735", "10550210", "11580264", "12354605" ]

[ "TCP1 - molecular chaperonin of the cytoplasm?", "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin.", "What is a chaperonin?", "Protein folding. Cytosolic chaperonin confirmed.", "T-complex polypeptide-1 is a subunit of a heteromeric particle in the eu...

[ 1992, 1994, 1992, 1992, 1992, 1994, 1995, 2010, 2009, 2004, 2001, 2000, 1999, 2001, 2002 ]

15

[ "IPR017998" ]

[]

1

0

1

[ "Eukaryota" ]

[ 4331 ]

1

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 3, 1, 1, 2, 2, 1, 1, 2, 3, 1, 1, 7 ]

12

true

Family

T-complex protein 1, alpha subunit

Chap_CCT_alpha

3

IPR012716

12,716

T-complex protein 1, beta subunit

Chap_CCT_beta

Family

4,827

false

Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [ , ]. Chaperonins are involved in productive folding of proteins [ ]. They share a common general morphology, a double toroid of 2 stacked rings. The archaeal...

[ "GO:0005524", "GO:0016887", "GO:0051082", "GO:0006457", "GO:0005829", "GO:0005832" ]

[ "ATP binding", "ATP hydrolysis activity", "unfolded protein binding", "protein folding", "cytosol", "chaperonin-containing T-complex" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component", "cellular_component" ]

6

[ "NCBIFAM", "CDD" ]

[ "TIGR02341", "cd03336" ]

[ "chap_CCT_beta", "TCP1_beta" ]

[ 4797, 4448 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-390471", "R-BTA-6798695", "R-BTA-6814122", "R-BTA-9013418", "R-BTA-9013422", "R-CEL-390471", "R-CEL-6798695", "R-CEL-6814122", "R-DDI-390471", "R-DDI-6798695", "R-DDI-6814122", "R-DDI-9013418", "R-DDI-9013422", "R-HSA-389957", "R-HSA-389960", "R-HSA-390450", "R-HSA-390471", ...

[ "REACTOME:R-BTA-390471", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-6814122", "REACTOME:R-BTA-9013418", "REACTOME:R-BTA-9013422", "REACTOME:R-CEL-390471", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-6814122", "REACTOME:R-DDI-390471", "REACTOME:R-DDI-6798695", "REACTOME:R-DDI-6814122", "REACTOME:R...

38

[ "3iyg", "3ktt", "4a0o", "4a0v", "4a0w", "4a13", "4b2t", "4v81", "4v8r", "4v94", "5gw4", "5gw5", "6krd", "6kre", "6ks6", "6ks7", "6ks8", "6nr8", "6nr9", "6nra", "6nrb", "6nrc", "6nrd", "6qb8", "7lum", "7lup", "7nvl", "7nvm", "7nvn", "7nvo", "7trg", "7ttn"...

78

[ "PUB00001019", "PUB00001034", "PUB00004124", "PUB00004127", "PUB00004129", "PUB00005432", "PUB00064264", "PUB00074264", "PUB00074265", "PUB00074266", "PUB00080867", "PUB00080868", "PUB00080869", "PUB00080871", "PUB00080873" ]

[ "15335898", "7953530", "1352040", "1352857", "1630492", "7846767", "7601114", "20194787", "18595008", "15027029", "11340060", "10753735", "10550210", "11580264", "12354605" ]

[ "TCP1 - molecular chaperonin of the cytoplasm?", "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin.", "What is a chaperonin?", "Protein folding. Cytosolic chaperonin confirmed.", "T-complex polypeptide-1 is a subunit of a heteromeric particle in the eu...

[ 1992, 1994, 1992, 1992, 1992, 1994, 1995, 2010, 2009, 2004, 2001, 2000, 1999, 2001, 2002 ]

15

[ "IPR017998" ]

[]

1

0

1

[ "Eukaryota" ]

[ 4827 ]

1

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 2, 1, 1, 1, 5, 3, 1, 6, 4, 1, 1, 20 ]

12

true

Family

T-complex protein 1, beta subunit

Chap_CCT_beta

5

IPR012718

12,718

T-complex protein 1, epsilon subunit

Chap_CCT_epsi

Family

4,757

false

Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [ , ]. Chaperonins are involved in productive folding of proteins [ ]. They share a common general morphology, a double toroid of 2 stacked rings. The archaeal...

[ "GO:0005524", "GO:0051082", "GO:0006457" ]

[ "ATP binding", "unfolded protein binding", "protein folding" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM", "CDD" ]

[ "TIGR02343", "cd03339" ]

[ "chap_CCT_epsi", "TCP1_epsilon" ]

[ 4644, 4670 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-CEL-390471", "R-CEL-6814122", "R-DDI-390471", "R-DDI-6814122", "R-HSA-389957", "R-HSA-389960", "R-HSA-390450", "R-HSA-390471", "R-HSA-5620922", "R-HSA-6814122", "R-MMU-390471", "R-MMU-6814122", "R-RNO-390471", "R-RNO-6814122", "R-SCE-390471", "R-SCE-6814122", "R-SPO-390471", "R-...

[ "REACTOME:R-CEL-390471", "REACTOME:R-CEL-6814122", "REACTOME:R-DDI-390471", "REACTOME:R-DDI-6814122", "REACTOME:R-HSA-389957", "REACTOME:R-HSA-389960", "REACTOME:R-HSA-390450", "REACTOME:R-HSA-390471", "REACTOME:R-HSA-5620922", "REACTOME:R-HSA-6814122", "REACTOME:R-MMU-390471", "REACTOME:R-MMU...

18

[ "3iyg", "4b2t", "4v81", "4v8r", "4v94", "5gw4", "5gw5", "5uyx", "5uyz", "6krd", "6kre", "6ks6", "6ks7", "6ks8", "6nr8", "6nr9", "6nra", "6nrb", "6nrc", "6nrd", "6qb8", "7lum", "7lup", "7nvl", "7nvm", "7nvn", "7nvo", "7trg", "7ttn", "7ttt", "7tub", "7wu7"...

77

[ "PUB00001019", "PUB00001034", "PUB00004124", "PUB00004127", "PUB00004129", "PUB00005432", "PUB00064264", "PUB00074264", "PUB00074265", "PUB00074266", "PUB00080867", "PUB00080868", "PUB00080869", "PUB00080871", "PUB00080873" ]

[ "15335898", "7953530", "1352040", "1352857", "1630492", "7846767", "7601114", "20194787", "18595008", "15027029", "11340060", "10753735", "10550210", "11580264", "12354605" ]

[ "TCP1 - molecular chaperonin of the cytoplasm?", "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin.", "What is a chaperonin?", "Protein folding. Cytosolic chaperonin confirmed.", "T-complex polypeptide-1 is a subunit of a heteromeric particle in the eu...

[ 1992, 1994, 1992, 1992, 1992, 1994, 1995, 2010, 2009, 2004, 2001, 2000, 1999, 2001, 2002 ]

15

[ "IPR017998" ]

[]

1

0

1

[ "Eukaryota" ]

[ 4757 ]

1

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 3, 1, 1, 3, 13, 1, 1, 3, 3, 1, 1, 12 ]

12

true

Family

T-complex protein 1, epsilon subunit

Chap_CCT_epsi

8

IPR012719

12,719

T-complex protein 1, gamma subunit

Chap_CCT_gamma

Family

4,845

false

Proteins in this entry consist exclusively of the CCT gamma chain from animals, plants, fungi, and other eukaryotes. Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [ , ]. Chaperonins are involved in product...

[ "GO:0005524", "GO:0016887", "GO:0051082", "GO:0006457" ]

[ "ATP binding", "ATP hydrolysis activity", "unfolded protein binding", "protein folding" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "NCBIFAM", "CDD" ]

[ "TIGR02344", "cd03337" ]

[ "chap_CCT_gamma", "TCP1_gamma" ]

[ 4729, 4631 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-BTA-390471", "R-BTA-6814122", "R-CEL-390471", "R-CEL-6814122", "R-DDI-390471", "R-DDI-6814122", "R-DME-390471", "R-DME-6814122", "R-HSA-389957", "R-HSA-389960", "R-HSA-390450", "R-HSA-390471", "R-HSA-5620922", "R-HSA-6814122", "R-MMU-390471", "R-MMU-6814122", "R-RNO-390471", "R-...

[ "REACTOME:R-BTA-390471", "REACTOME:R-BTA-6814122", "REACTOME:R-CEL-390471", "REACTOME:R-CEL-6814122", "REACTOME:R-DDI-390471", "REACTOME:R-DDI-6814122", "REACTOME:R-DME-390471", "REACTOME:R-DME-6814122", "REACTOME:R-HSA-389957", "REACTOME:R-HSA-389960", "REACTOME:R-HSA-390450", "REACTOME:R-HSA...

22

[ "3iyg", "4b2t", "4v81", "4v8r", "4v94", "5gw4", "5gw5", "6krd", "6kre", "6ks6", "6ks7", "6ks8", "6nr8", "6nr9", "6nra", "6nrb", "6nrc", "6nrd", "6qb8", "7lum", "7lup", "7nvl", "7nvm", "7nvn", "7nvo", "7trg", "7ttn", "7ttt", "7tub", "7wu7", "7wz3", "7x0a"...

74

[ "PUB00001019", "PUB00001034", "PUB00004124", "PUB00004127", "PUB00004129", "PUB00005432", "PUB00064264", "PUB00074264", "PUB00074265", "PUB00074266", "PUB00080867", "PUB00080868", "PUB00080869", "PUB00080871", "PUB00080873" ]

[ "15335898", "7953530", "1352040", "1352857", "1630492", "7846767", "7601114", "20194787", "18595008", "15027029", "11340060", "10753735", "10550210", "11580264", "12354605" ]

[ "TCP1 - molecular chaperonin of the cytoplasm?", "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin.", "What is a chaperonin?", "Protein folding. Cytosolic chaperonin confirmed.", "T-complex polypeptide-1 is a subunit of a heteromeric particle in the eu...

[ 1992, 1994, 1992, 1992, 1992, 1994, 1995, 2010, 2009, 2004, 2001, 2000, 1999, 2001, 2002 ]

15

[ "IPR017998" ]

[]

1

0

1

[ "Eukaryota" ]

[ 4845 ]

1

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 3, 1, 1, 2, 5, 5, 1, 5, 4, 1, 1, 12 ]

12

true

Family

T-complex protein 1, gamma subunit

Chap_CCT_gamma

5

IPR012720

12,720

T-complex protein 1, eta subunit

Chap_CCT_eta

Family

4,646

false

Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [ , ]. Chaperonins are involved in productive folding of proteins [ ]. They share a common general morphology, a double toroid of 2 stacked rings. The archaeal...

[ "GO:0005524", "GO:0016887", "GO:0051082", "GO:0006457" ]

[ "ATP binding", "ATP hydrolysis activity", "unfolded protein binding", "protein folding" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "NCBIFAM", "CDD" ]

[ "TIGR02345", "cd03340" ]

[ "chap_CCT_eta", "TCP1_eta" ]

[ 4474, 4602 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-390471", "R-BTA-6814122", "R-BTA-9013418", "R-BTA-9013422", "R-DDI-390471", "R-DDI-6814122", "R-DDI-9013418", "R-DDI-9013422", "R-HSA-389957", "R-HSA-389960", "R-HSA-390450", "R-HSA-390471", "R-HSA-6814122", "R-HSA-9013418", "R-HSA-9013422", "R-MMU-390471", "R-MMU-6814122", ...

[ "REACTOME:R-BTA-390471", "REACTOME:R-BTA-6814122", "REACTOME:R-BTA-9013418", "REACTOME:R-BTA-9013422", "REACTOME:R-DDI-390471", "REACTOME:R-DDI-6814122", "REACTOME:R-DDI-9013418", "REACTOME:R-DDI-9013422", "REACTOME:R-HSA-389957", "REACTOME:R-HSA-389960", "REACTOME:R-HSA-390450", "REACTOME:R-H...

24

[ "3iyg", "4b2t", "4v81", "4v8r", "4v94", "5gw4", "5gw5", "6krd", "6kre", "6ks6", "6ks7", "6ks8", "6nr8", "6nr9", "6nra", "6nrb", "6nrc", "6nrd", "6qb8", "7lum", "7lup", "7nvl", "7nvm", "7nvn", "7nvo", "7trg", "7ttn", "7ttt", "7tub", "7wu7", "7wz3", "7x0a"...

73

[ "PUB00001019", "PUB00001034", "PUB00004124", "PUB00004127", "PUB00004129", "PUB00005432", "PUB00064264", "PUB00074264", "PUB00074265", "PUB00074266", "PUB00080867", "PUB00080868", "PUB00080869", "PUB00080871", "PUB00080873" ]

[ "15335898", "7953530", "1352040", "1352857", "1630492", "7846767", "7601114", "20194787", "18595008", "15027029", "11340060", "10753735", "10550210", "11580264", "12354605" ]

[ "TCP1 - molecular chaperonin of the cytoplasm?", "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin.", "What is a chaperonin?", "Protein folding. Cytosolic chaperonin confirmed.", "T-complex polypeptide-1 is a subunit of a heteromeric particle in the eu...

[ 1992, 1994, 1992, 1992, 1992, 1994, 1995, 2010, 2009, 2004, 2001, 2000, 1999, 2001, 2002 ]

15

[ "IPR017998" ]

[]

1

0

1

[ "Eukaryota" ]

[ 4646 ]

1

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 2, 2, 1, 1, 5, 9, 1, 1, 3, 1, 1, 6 ]

12

true

Family

T-complex protein 1, eta subunit

Chap_CCT_eta

5

IPR012721

12,721

T-complex protein 1, theta subunit

Chap_CCT_theta

Family

5,083

false

Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [ , ]. Chaperonins are involved in productive folding of proteins [ ]. They share a common general morphology, a double toroid of 2 stacked rings. The archaeal...

[ "GO:0005524", "GO:0016887", "GO:0051082", "GO:0006457" ]

[ "ATP binding", "ATP hydrolysis activity", "unfolded protein binding", "protein folding" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "NCBIFAM", "CDD" ]

[ "TIGR02346", "cd03341" ]

[ "chap_CCT_theta", "TCP1_theta" ]

[ 5004, 4917 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-390471", "R-BTA-6798695", "R-BTA-6814122", "R-CEL-390471", "R-CEL-6798695", "R-CEL-6814122", "R-DDI-390471", "R-DDI-6798695", "R-DDI-6814122", "R-HSA-389957", "R-HSA-389960", "R-HSA-390450", "R-HSA-390471", "R-HSA-5620922", "R-HSA-6798695", "R-HSA-6814122", "R-MMU-390471", "...

[ "REACTOME:R-BTA-390471", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-6814122", "REACTOME:R-CEL-390471", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-6814122", "REACTOME:R-DDI-390471", "REACTOME:R-DDI-6798695", "REACTOME:R-DDI-6814122", "REACTOME:R-HSA-389957", "REACTOME:R-HSA-389960", "REACTOME:R-H...

25

[ "3iyg", "4b2t", "4v81", "4v8r", "4v94", "5gw4", "5gw5", "6krd", "6kre", "6ks6", "6ks7", "6ks8", "6nr8", "6nr9", "6nra", "6nrb", "6nrc", "6nrd", "6qb8", "7lum", "7lup", "7nvl", "7nvm", "7nvn", "7nvo", "7trg", "7ttn", "7ttt", "7tub", "7wu7", "7wz3", "7x0a"...

73

[ "PUB00001019", "PUB00001034", "PUB00004124", "PUB00004127", "PUB00004129", "PUB00005432", "PUB00064264", "PUB00074264", "PUB00074265", "PUB00074266", "PUB00080867", "PUB00080868", "PUB00080869", "PUB00080871", "PUB00080873" ]

[ "15335898", "7953530", "1352040", "1352857", "1630492", "7846767", "7601114", "20194787", "18595008", "15027029", "11340060", "10753735", "10550210", "11580264", "12354605" ]

[ "TCP1 - molecular chaperonin of the cytoplasm?", "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin.", "What is a chaperonin?", "Protein folding. Cytosolic chaperonin confirmed.", "T-complex polypeptide-1 is a subunit of a heteromeric particle in the eu...

[ 1992, 1994, 1992, 1992, 1992, 1994, 1995, 2010, 2009, 2004, 2001, 2000, 1999, 2001, 2002 ]

15

[ "IPR017998" ]

[]

1

0

1

[ "Eukaryota" ]

[ 5083 ]

1

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 2, 2, 3, 1, 3, 8, 1, 3, 4, 1, 1, 8 ]

12

true

Family

T-complex protein 1, theta subunit

Chap_CCT_theta

2

IPR012722

12,722

T-complex protein 1, zeta subunit

Chap_CCT_zeta

Family

5,108

false

Members of this eukaryotic family are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1 or Tailless Complex Polypeptide 1) or TRiC [ , ]. Chaperonins are involved in productive folding of proteins [ ]. They share a common general morphology, a double toroid of 2 stacked rings. The archaeal...

[ "GO:0005524", "GO:0016887", "GO:0051082", "GO:0006457" ]

[ "ATP binding", "ATP hydrolysis activity", "unfolded protein binding", "protein folding" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "NCBIFAM", "CDD" ]

[ "TIGR02347", "cd03342" ]

[ "chap_CCT_zeta", "TCP1_zeta" ]

[ 4807, 5054 ]

2

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME"...

[ "3.6.1.-", "PWY-5757", "PWY-6147", "PWY-6383", "PWY-6797", "PWY-7206", "PWY-7419", "PWY-7539", "PWY-7719", "PWY-7821", "PWY-8289", "R-BTA-390471", "R-BTA-6814122", "R-BTA-9013418", "R-CEL-390471", "R-CEL-6814122", "R-DDI-390471", "R-DDI-6814122", "R-DDI-9013418", "R-GGA-390471"...

[ "EC:3.6.1.-", "METACYC:PWY-5757", "METACYC:PWY-6147", "METACYC:PWY-6383", "METACYC:PWY-6797", "METACYC:PWY-7206", "METACYC:PWY-7419", "METACYC:PWY-7539", "METACYC:PWY-7719", "METACYC:PWY-7821", "METACYC:PWY-8289", "REACTOME:R-BTA-390471", "REACTOME:R-BTA-6814122", "REACTOME:R-BTA-9013418",...

35

[ "3iyg", "4b2t", "4v81", "4v8r", "4v94", "5gw4", "5gw5", "6krd", "6kre", "6ks6", "6ks7", "6ks8", "6nr8", "6nr9", "6nra", "6nrb", "6nrc", "6nrd", "6qb8", "7lum", "7lup", "7nvl", "7nvm", "7nvn", "7nvo", "7trg", "7ttn", "7ttt", "7tub", "7wu7", "7wz3", "7x0a"...

73

[ "PUB00001019", "PUB00001034", "PUB00004124", "PUB00004127", "PUB00004129", "PUB00005432", "PUB00064264", "PUB00074264", "PUB00074265", "PUB00074266", "PUB00080867", "PUB00080868", "PUB00080869", "PUB00080871", "PUB00080873" ]

[ "15335898", "7953530", "1352040", "1352857", "1630492", "7846767", "7601114", "20194787", "18595008", "15027029", "11340060", "10753735", "10550210", "11580264", "12354605" ]

[ "TCP1 - molecular chaperonin of the cytoplasm?", "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin.", "What is a chaperonin?", "Protein folding. Cytosolic chaperonin confirmed.", "T-complex polypeptide-1 is a subunit of a heteromeric particle in the eu...

[ 1992, 1994, 1992, 1992, 1992, 1994, 1995, 2010, 2009, 2004, 2001, 2000, 1999, 2001, 2002 ]

15

[ "IPR017998" ]

[]

1

0

1

[ "Eukaryota" ]

[ 5108 ]

1

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 7, 2, 1, 1, 7, 11, 1, 2, 5, 1, 1, 6 ]

12

true

Family

T-complex protein 1, zeta subunit

Chap_CCT_zeta

7

IPR012725

12,725

Chaperone DnaK

Chaperone_DnaK

Family

35,934

false

Molecular chaperones are a diverse family of proteins that function to protect proteins in the intracellular milieu from irreversible aggregation during synthesis and in times of cellular stress. The bacterial molecular chaperone DnaK is an enzyme that couples cycles of ATP binding, hydrolysis, and ADP release by an N-...

[ "GO:0005524", "GO:0051082", "GO:0006457" ]

[ "ATP binding", "unfolded protein binding", "protein folding" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_00332", "TIGR02350" ]

[ "DnaK", "prok_dnaK" ]

[ 35653, 35535 ]

2

[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...

[ "GenProp0244", "R-BTA-3371453", "R-BTA-6799198", "R-BTA-9837999", "R-BTA-9865881", "R-CEL-3371453", "R-CEL-9837999", "R-DDI-3371453", "R-DDI-6799198", "R-DDI-9837999", "R-DDI-9865881", "R-DME-6799198", "R-DME-9837999", "R-DME-9865881", "R-HSA-1268020", "R-HSA-3371453", "R-HSA-6799198...

[ "GP:GenProp0244", "REACTOME:R-BTA-3371453", "REACTOME:R-BTA-6799198", "REACTOME:R-BTA-9837999", "REACTOME:R-BTA-9865881", "REACTOME:R-CEL-3371453", "REACTOME:R-CEL-9837999", "REACTOME:R-DDI-3371453", "REACTOME:R-DDI-6799198", "REACTOME:R-DDI-9837999", "REACTOME:R-DDI-9865881", "REACTOME:R-DME-...

36

[ "2kho", "2v7y", "4ani", "4b9q", "4jn4", "4jne", "4rtf", "5nro", "5obu", "5obv", "6w6e", "7ko2", "7krt", "7kru", "7krv", "7krw", "7kzi", "7kzu", "7l6n", "8gb3", "9bls", "9blt", "9blu", "9dvi" ]

24

[ "PUB00000100" ]

[ "8280473" ]

[ "Role of the major heat shock proteins as molecular chaperones." ]

[ 1993 ]

1

[ "IPR013126" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 686, 27456, 7457, 5, 330 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 13, 1, 1, 2, 2, 9, 1, 1, 12, 3, 2, 1, 25 ]

13

true

Family

Chaperone DnaK

Chaperone_DnaK

1

IPR012727

12,727

Glycine oxidase ThiO

Gly_oxidase_ThiO

Family

7,204

false

This family consists of the homotetrameric, FAD-dependent glycine oxidase ThiO, from species such as Bacillus subtilis that use glycine in thiamine biosynthesis. In general, members of this family will not be found in species such as Escherichia coli that instead use tyrosine and the ThiH protein [ ].

[ "GO:0016491", "GO:0050660" ]

[ "oxidoreductase activity", "flavin adenine dinucleotide binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "NCBIFAM" ]

[ "TIGR02352" ]

[ "thiamin_ThiO" ]

[ 7204 ]

1

[ "EC", "GP", "METACYC", "METACYC" ]

[ "1.4.3.19", "GenProp0250", "PWY-7396", "PWY-7806" ]

[ "EC:1.4.3.19", "GP:GenProp0250", "METACYC:PWY-7396", "METACYC:PWY-7806" ]

4

[ "1ng3", "1ng4", "1ryi", "3if9", "4ysh", "6j38", "6j39", "7cyx" ]

8

[ "PUB00017059" ]

[ "12627963" ]

[ "Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamin biosynthesis in Bacillus subtilis." ]

[ 2003 ]

1

[]

0

null

[ "Bacteria", "Caldiarchaeum subterraneum", "Eukaryota", "metagenomes" ]

[ 7132, 1, 31, 40 ]

4

[]

0

true

Family

Glycine oxidase ThiO

Gly_oxidase_ThiO

2

IPR012728

12,728

Pls/PosA non-ribosomal peptide synthetases, C-terminal

Pls/PosA_C

Domain

4,222

false

This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size. This domains is found in PosA, a δ-poly-L-ornithine synthetase that produces δ-poly-L-ornithine [ ...

[]

0

[ "NCBIFAM" ]

[ "TIGR02353" ]

[ "NRPS_term_dom" ]

[ 4222 ]

1

[]

0

[]

0

[ "PUB00153570", "PUB00153571" ]

[ "37752201", "18997795" ]

[ "Structural and functional insights into δ-poly-L-ornithine polymer biosynthesis from Acinetobacter baumannii.", "Epsilon-poly-L-lysine dispersity is controlled by a highly unusual nonribosomal peptide synthetase." ]

[ 2023, 2008 ]

2

[]

0

null

[ "Bacteria", "Eukaryota", "ecological metagenomes" ]

[ 4028, 187, 7 ]

3

[]

0

true

Domain

Pls/PosA non-ribosomal peptide synthetases, C-terminal

Pls/PosA_C

4

IPR012729

12,729

Thiamine biosynthesis protein ThiF

ThiF_fam2

Family

1,134

false

Members of the HesA/MoeB/ThiF family of proteins ( ) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees. The Escherichia coli ThiF and MoeB proteins are seemingly more closely related than the E. coli T...

[]

0

[ "NCBIFAM", "CDD" ]

[ "TIGR02354", "cd01487" ]

[ "thiF_fam2", "E1_ThiF_like" ]

[ 1134, 393 ]

2

[ "GP" ]

[ "GenProp0250" ]

[ "GP:GenProp0250" ]

1

[]

0

[ "PUB00081807" ]

[ "12660720" ]

[ "Two-stepping with E1." ]

[ 2003 ]

1

[ "IPR045886" ]

[]

1

0

1

[ "Bacteria", "Methanobacteriati", "metagenomes" ]

[ 1118, 4, 12 ]

3

[]

0

true

Family

Thiamine biosynthesis protein ThiF

ThiF_fam2

2

IPR012730

12,730

Molybdopterin synthase sulfurylase MoeB

Mopterin_Synthase_Sase_MoeB

Family

2,130

false

This entry describes the molybdopterin biosynthesis protein MoeB in Escherichia coli and related species. MoeB and MoaD are involved in molybdenum cofactor biosynthesis, an evolutionarily conserved pathway. The MoeB enzyme covalently modifies the molybdopterin synthase MoaD by sulphurylation. The crystal structure of t...

[ "GO:0006777" ]

[ "Mo-molybdopterin cofactor biosynthetic process" ]

[ "biological_process" ]

1

[ "NCBIFAM" ]

[ "TIGR02355" ]

[ "moeB" ]

[ 2130 ]

1

[ "EC", "GP", "GP", "METACYC" ]

[ "2.7.7.80", "GenProp1158", "GenProp1711", "PWY-6823" ]

[ "EC:2.7.7.80", "GP:GenProp1158", "GP:GenProp1711", "METACYC:PWY-6823" ]

4

[ "1jw9", "1jwa", "1jwb" ]

3

[ "PUB00011756" ]

[ "11713534" ]

[ "Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex." ]

[ 2001 ]

1

[ "IPR045886" ]

[]

1

0

1

[ "Bacteria", "Opisthokonta" ]

[ 2128, 2 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Molybdopterin synthase sulfurylase MoeB

Mopterin_Synthase_Sase_MoeB

5

IPR012731

12,731

Thiazole biosynthesis adenylyltransferase ThiF

Adenyl_ThiF

Family

606

false

Members of the HesA/MoeB/ThiF family of proteins ( ) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees. The Escherichia coli ThiF and MoeB proteins are seemingly more closely related than the E. coli T...

[]

0

[ "NCBIFAM" ]

[ "TIGR02356" ]

[ "adenyl_thiF" ]

[ 606 ]

1

[ "GP", "GP" ]

[ "GenProp0250", "GenProp1175" ]

[ "GP:GenProp0250", "GP:GenProp1175" ]

2

[ "1zfn", "1zkm", "1zud" ]

3

[]

0

[ "IPR045886" ]

[]

1

0

1

[ "Bacteria", "Trichuris trichiura", "human gut metagenome" ]

[ 604, 1, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Thiazole biosynthesis adenylyltransferase ThiF

Adenyl_ThiF

3

IPR012732

12,732

Hydroxymethylpyrimidine transporter CytX

Thia_CytX

Family

1,530

false

On the basis of a phylogenomic study of thiamine biosynthetic, salvage, and transporter genes and a highly conserved RNA element THI, this protein family has been identified as a probable transporter of hydroxymethylpyrimidine (HMP). ThiD phosphorylates hydroxymethylpyrimidine and when joined (by ThiE) to hydroxyethylt...

[]

0

[ "NCBIFAM" ]

[ "TIGR02358" ]

[ "thia_cytX" ]

[ 1530 ]

1

[]

0

[]

0

[ "PUB00017761" ]

[ "12376536" ]

[ "Comparative genomics of thiamin biosynthesis in procaryotes. New genes and regulatory mechanisms." ]

[ 2002 ]

1

[ "IPR001248" ]

[]

1

0

1

[ "Archaea", "Bacteria", "unclassified sequences" ]

[ 21, 1505, 4 ]

3

[]

0

true

Family

Hydroxymethylpyrimidine transporter CytX

Thia_CytX

7

IPR012733

12,733

4-hydroxybenzoate 3-monooxygenase

HB_mOase

Family

3,633

false

4-hydroxybenzoate 3-monooxygenase is a flavoprotein that converts its substrate to 3,4-dihydroxybenzoate, which subsequently enters the beta-ketioadipate pathway of aromatic degradation, using molecular oxygen and NADPH as shown below [ ]. 4-hydroxybenzoate + NADPH + O(2) = 3,4-dihydroxybenzoate + NADP(+) + H(2)O 4-hyd...

[ "GO:0018659", "GO:0050660", "GO:0043639" ]

[ "4-hydroxybenzoate 3-monooxygenase activity", "flavin adenine dinucleotide binding", "benzoate catabolic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02360" ]

[ "pbenz_hydroxyl" ]

[ 3633 ]

1

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]

[ "1.14.13.2", "PWY-6215", "PWY-7700", "PWY-7757", "PWY-7934", "PWY-7935", "PWY-8002" ]

[ "EC:1.14.13.2", "METACYC:PWY-6215", "METACYC:PWY-7700", "METACYC:PWY-7757", "METACYC:PWY-7934", "METACYC:PWY-7935", "METACYC:PWY-8002" ]

7

[ "1bf3", "1bgj", "1bgn", "1bkw", "1cc4", "1cc6", "1cj2", "1cj3", "1cj4", "1d7l", "1dob", "1doc", "1dod", "1doe", "1ius", "1iut", "1iuu", "1iuv", "1iuw", "1iux", "1k0i", "1k0j", "1k0l", "1pbb", "1pbc", "1pbd", "1pbe", "1pbf", "1pdh", "1phh", "1pxa", "1pxb"...

39

[ "PUB00026602", "PUB00033186" ]

[ "11805318", "7737455" ]

[ "Protein and ligand dynamics in 4-hydroxybenzoate hydroxylase.", "Structure and mechanism of para-hydroxybenzoate hydroxylase." ]

[ 2002, 1995 ]

2

[ "IPR050641" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "ecological metagenomes" ]

[ 3623, 2, 8 ]

3

[]

0

true

Family

4-hydroxybenzoate 3-monooxygenase

HB_mOase

4

IPR012734

12,734

Dihydroxyacetone kinase

DhaK_ATP

Family

4,120

false

This family consists of examples of the single chain form of dihydroxyacetone kinase (also called glycerone kinase) that uses ATP ( ) as the phosphate donor, rather than a phosphoprotein as in Escherichia coli. This form has separable domains homologous to the K and L subunits of the E. coli enzyme, and is found in yea...

[ "GO:0004371", "GO:0005524", "GO:0006071" ]

[ "glycerone kinase activity", "ATP binding", "glycerol metabolic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02361" ]

[ "dak_ATP" ]

[ 4120 ]

1

[ "EC", "EC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.7.1.28", "2.7.1.29", "PWY-6131", "PWY-8404", "R-HSA-168928", "R-HSA-70350", "R-HSA-9692916", "R-HSA-9705671", "R-MMU-70350", "R-RNO-70350", "R-SCE-70350", "R-SPO-70350" ]

[ "EC:2.7.1.28", "EC:2.7.1.29", "METACYC:PWY-6131", "METACYC:PWY-8404", "REACTOME:R-HSA-168928", "REACTOME:R-HSA-70350", "REACTOME:R-HSA-9692916", "REACTOME:R-HSA-9705671", "REACTOME:R-MMU-70350", "REACTOME:R-RNO-70350", "REACTOME:R-SCE-70350", "REACTOME:R-SPO-70350" ]

12

[ "1un8", "1un9" ]

2

[ "PUB00016695", "PUB00017762", "PUB00060926", "PUB00060927", "PUB00060928" ]

[ "11985845", "12966101", "7635824", "16289032", "10091325" ]

[ "A tomato enzyme catalyzing the phosphorylation of 3,4-dihydroxy-2-butanone.", "Crystal structure of the Citrobacter freundii dihydroxyacetone kinase reveals an eight-stranded alpha-helical barrel ATP-binding domain.", "Biochemical and molecular characterization of the oxidative branch of glycerol utilization b...

[ 2002, 2003, 1995, 2005, 1999 ]

5

[]

0

null

[ "Eukaryota", "Pseudomonadati" ]

[ 3919, 201 ]

2

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "S...

[ 10, 1, 1, 3, 2, 2, 4, 5, 2, 2, 4 ]

11

true

Family

Dihydroxyacetone kinase

DhaK_ATP

9

IPR012736

12,736

Dihydroxyacetone kinase DhaK, subunit 1

DhaK_1

Domain

6,709

false

In bacteria, dihydroxyacetone is formed by the oxidation of glycerol or the aldol cleavage of fructose-6-phosphate. Dihydroxyacetone kinase converts this compound to the glycolytic intermediate dihydroxyacetone phosphate. Two forms of this enzyme have been shown to exist, using either ATP or a phosphoprotein of the pho...

[]

0

[ "NCBIFAM" ]

[ "TIGR02363" ]

[ "dhaK1" ]

[ 6709 ]

1

[ "EC", "GP", "GP" ]

[ "2.7.1.121", "GenProp1146", "GenProp1324" ]

[ "EC:2.7.1.121", "GP:GenProp1146", "GP:GenProp1324" ]

3

[ "1oi2", "1oi3", "1uod", "1uoe", "3ct4", "3pnk", "3pnl", "3pnm", "3pno", "3pnq", "4lrx", "4lry" ]

12

[ "PUB00017762", "PUB00029449", "PUB00033180" ]

[ "12966101", "12813127", "11350937" ]

[ "Crystal structure of the Citrobacter freundii dihydroxyacetone kinase reveals an eight-stranded alpha-helical barrel ATP-binding domain.", "A mechanism of covalent substrate binding in the x-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase.", "The dihydroxyacetone kinase of Escherichi...

[ 2003, 2003, 2001 ]

3

[ "IPR004006" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "Methanobacteriota", "unclassified sequences" ]

[ 6563, 4, 129, 13 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Dihydroxyacetone kinase DhaK, subunit 1

DhaK_1

7

IPR012737

12,737

Dihydroxyacetone kinase, subunit L

DhaK_L_YcgS

Domain

8,854

false

Two types of dihydroxyacetone kinase (glycerone kinase) are described. In yeast and a few bacteria, e.g. Citrobacter freundii, the enzyme is a single chain that uses ATP as phosphoryl donor and is designated . By contrast, Escherichia coli and many other bacterial species have a multisubunit form ( ) with a phosphoprot...

[ "GO:0016772" ]

[ "transferase activity, transferring phosphorus-containing groups" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR02365" ]

[ "dha_L_ycgS" ]

[ 8854 ]

1

[ "EC", "GP", "GP" ]

[ "2.7.1.121", "GenProp1146", "GenProp1324" ]

[ "EC:2.7.1.121", "GP:GenProp1146", "GP:GenProp1324" ]

3

[ "2btd", "3cr3", "3pnl", "4lrz" ]

4

[ "PUB00051102" ]

[ "18957416" ]

[ "X-ray structures of the three Lactococcus lactis dihydroxyacetone kinase subunits and of a transient intersubunit complex." ]

[ 2008 ]

1

[ "IPR004007" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 130, 8680, 10, 34 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Dihydroxyacetone kinase, subunit L

DhaK_L_YcgS

4

IPR012738

12,738

Transcription regulator DhaS

Tscrpt_reg_DhaS

Family

681

false

This entry represents a set of known and predicted TetR-like transcriptional regulators associated with operons encoding PEP-dependent dihydroxyacteone (Dha) kinases. The Lactococcus lactis DhaS protein has been shown to interact with the Dha-binding protein DhaQ to form a stable complex [ ]. In the presence of Dha thi...

[ "GO:0003700" ]

[ "DNA-binding transcription factor activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR02366" ]

[ "DHAK_reg" ]

[ 681 ]

1

[]

0

[ "2iu5" ]

1

[ "PUB00036010" ]

[ "16760471" ]

[ "Regulation of the Dha operon of Lactococcus lactis: a deviation from the rule followed by the Tetr family of transcription regulators." ]

[ 2006 ]

1

[ "IPR050624" ]

[]

1

0

1

[ "Bacillati", "bioreactor metagenome" ]

[ 679, 2 ]

2

[]

0

true

Family

Transcription regulator DhaS

Tscrpt_reg_DhaS

8

IPR012739

12,739

Pyrrolysyl-tRNA ligase

Pyrrolysyl-tRNA_ligase

Family

45

false

PylS is the archaeal enzyme responsible for charging the pyrrolysine tRNA, PylT, by ligating a free molecule of pyrrolysine [ ]. Pyrrolysine is encoded at an in-frame UAG (amber) at least in several corrinoid-dependent methyltransferases of the archaeal genera Methanosarcina and Methanococcoides, e.g. trimethylamine me...

[ "GO:0004812", "GO:0005524", "GO:0006418", "GO:0005737" ]

[ "aminoacyl-tRNA ligase activity", "ATP binding", "tRNA aminoacylation for protein translation", "cytoplasm" ]

[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

4

[ "HAMAP" ]

[ "MF_01573" ]

[ "Pyl_tRNA_synth" ]

[ 45 ]

1

[ "EC" ]

[ "6.1.1.26" ]

[ "EC:6.1.1.26" ]

1

[]

0

[ "PUB00017763" ]

[ "15329732" ]

[ "Direct charging of tRNA(CUA) with pyrrolysine in vitro and in vivo." ]

[ 2004 ]

1

[]

0

null

[ "Methanosarcinaceae" ]

[ 45 ]

1

[]

0

true

Family

Pyrrolysyl-tRNA ligase

Pyrrolysyl-tRNA_ligase

1

IPR012740

12,740

Trimethylamine methyltransferase, Methanosarcina

MttB_Methanosar

Family

59

false

This entry represents trimethylamine:corrinoid methyltransferases that contain a critical pyrrolysine residue incorporated during translation via a special tRNA for a TAG (amber) codon [ ]. Known members so far are from the genus Methanosarcina. It is one of a suite of three non-homologous enzymes with a critical UAG-e...

[ "GO:0008168", "GO:0015948" ]

[ "methyltransferase activity", "methanogenesis" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02369" ]

[ "trimeth_pyl" ]

[ 59 ]

1

[ "EC", "METACYC" ]

[ "2.1.1.250", "PWY-5250" ]

[ "EC:2.1.1.250", "METACYC:PWY-5250" ]

2

[ "7xcl", "7xcm", "7xcn" ]

3

[ "PUB00017766" ]

[ "10762254" ]

[ "The trimethylamine methyltransferase gene and multiple dimethylamine methyltransferase genes of Methanosarcina barkeri contain in-frame and read-through amber codons." ]

[ 2000 ]

1

[ "IPR010426" ]

[]

1

0

1

[ "Bacteria", "Methanobacteriati" ]

[ 13, 46 ]

2

[]

0

true

Family

Trimethylamine methyltransferase, Methanosarcina

MttB_Methanosar

2

IPR012741

12,741

Methyltransferase cognate corrinoid protein

Corrinoid_p

Domain

843

false

This entry describes a subfamily of the B12 binding domain proteins that include corrinoid proteins specific to four different, mutually non-homologous enzymes of the genus Methanosarcina. Three of the four cognate enzymes (trimethylamine, dimethylamine, and monomethylamine methyltransferases) all have the unusual, rib...

[ "GO:0031419", "GO:0050897", "GO:0015948" ]

[ "cobalamin binding", "cobalt ion binding", "methanogenesis" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02370" ]

[ "pyl_corrinoid" ]

[ 843 ]

1

[]

0

[ "1y80", "2i2x", "3ezx", "7xcn" ]

4

[]

0

[]

0

null

[ "Archaea", "Bacteria", "ecological metagenomes" ]

[ 603, 221, 19 ]

3

[]

0

true

Domain

Methyltransferase cognate corrinoid protein

Corrinoid_p

9

IPR012742

12,742

Alanine dehydrogenase, Archaeoglobus-type

Ala_DH_archaeglobus

Family

140

false

This enzyme, a homologue of bacterial ornithine cyclodeaminases and marsupial mu-crystallins, is a homodimeric NAD-dependent alanine dehydrogenase found in Archaeoglobus fulgidus and several other archaea [ , ].

[ "GO:0000286", "GO:0051287", "GO:0006522" ]

[ "alanine dehydrogenase activity", "NAD binding", "alanine metabolic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02371" ]

[ "ala_DH_arch" ]

[ 140 ]

1

[]

0

[ "1omo", "1vll" ]

2

[ "PUB00017767", "PUB00029492" ]

[ "15516582", "15313611" ]

[ "A novel archaeal alanine dehydrogenase homologous to ornithine cyclodeaminase and mu-crystallin.", "Structure of alanine dehydrogenase from Archaeoglobus: active site analysis and relation to bacterial cyclodeaminases and mammalian mu crystallin." ]

[ 2004, 2004 ]

2

[ "IPR028609" ]

[]

1

0

1

[ "Archaea", "Bacteria", "ecological metagenomes" ]

[ 129, 9, 2 ]

3

[]

0

true

Family

Alanine dehydrogenase, Archaeoglobus-type

Ala_DH_archaeglobus

7

IPR012744

12,744

Nitrite reductase [NAD(P)H] large subunit, NirB

Nitri_red_NirB

Domain

13,684

false

This entry describes NirB, the large subunit of nitrite reductase [NAD(P)H] (the assimilatory nitrite reductase), which associates with NirD, the small subunit ( ). In a few bacteria such as Klebsiella pneumoniae and in fungi, the two regions are fused.

[ "GO:0050660", "GO:0050661", "GO:0098809", "GO:0042128" ]

[ "flavin adenine dinucleotide binding", "NADP binding", "nitrite reductase activity", "nitrate assimilation" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "NCBIFAM" ]

[ "TIGR02374" ]

[ "nitri_red_nirB" ]

[ 13684 ]

1

[ "EC", "GP", "GP", "METACYC", "METACYC" ]

[ "1.7.1.4", "GenProp1554", "GenProp1746", "PWY-5675", "PWY-723" ]

[ "EC:1.7.1.4", "GP:GenProp1554", "GP:GenProp1746", "METACYC:PWY-5675", "METACYC:PWY-723" ]

5

[]

0

[]

0

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 13265, 350, 69 ]

3

[ "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]

[ 1, 1 ]

2

true

Domain

Nitrite reductase [NAD(P)H] large subunit, NirB

Nitri_red_NirB

2

IPR012745

12,745

Pseudoazurin

Family

1,656

false

Pseudoazurin, also called cupredoxin, is a small, blue periplasmic protein with a single bound copper atom. Pseudoazurin is related to plastocyanins [ ]. Several examples of pseudoazurin are encoded by a neighbouring gene for, or have been shown to transfer electrons to, copper-containing nitrite reductases ( ) of the ...

[ "GO:0005507" ]

[ "copper ion binding" ]

[ "molecular_function" ]

1

[ "NCBIFAM", "CDD" ]

[ "TIGR02375", "cd04218" ]

[ "pseudoazurin", "Pseudoazurin" ]

[ 1609, 1497 ]

2

[]

0

[ "1adw", "1bqk", "1bqr", "1paz", "1pmy", "1py0", "1pza", "1pzb", "1pzc", "1zia", "1zib", "2jkw", "2p80", "2ux6", "2ux7", "2uxf", "2uxg", "3ef4", "3erx", "3nyk", "3paz", "3tu6", "4bwt", "4bwu", "4bxv", "4paz", "4rh4", "4yl4", "5b1j", "5paz", "5x31", "5xmo"...

46

[ "PUB00036459", "PUB00038898", "PUB00081025", "PUB00081026", "PUB00081027" ]

[ "10364229", "8138527", "16138306", "22910335", "15475344" ]

[ "Crystal structure determinations of oxidized and reduced pseudoazurins from Achromobacter cycloclastes. Concerted movement of copper site in redox forms with the rearrangement of hydrogen bond at a remote histidine.", "Crystallization and preliminary X-ray studies on pseudoazurin from Achromobacter cycloclastes ...

[ 1999, 1993, 2005, 2012, 2004 ]

5

[ "IPR002386" ]

[]

1

0

1

[ "Bacteria", "Hemiselmis tepida", "ecological metagenomes" ]

[ 1645, 1, 10 ]

3

[]

0

true

Family

Pseudoazurin

2

IPR012747

12,747

MocE Rieske [2Fe-2S]

MocE_2FeS

Family

1,098

false

This entry describes a subfamily of the Rieske-like [2Fe-2S] family of ferredoxins that includes MocE, part of the rhizopine (3-O-methyl-scyllo-inosamine) catabolic cluster in Rhizobium. Members are related to, yet distinct from, the small subunit of nitrite reductase [NAD(P)H].

[]

0

[ "NCBIFAM" ]

[ "TIGR02377" ]

[ "MocE_fam_FeS" ]

[ 1098 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "hydrothermal vent metagenome" ]

[ 1097, 1 ]

2

[]

0

true

Family

MocE Rieske [2Fe-2S]

MocE_2FeS

9

IPR012748

12,748

Rieske-like [2Fe-2S] domain, NirD-type

Rieske-like_NirD

Domain

14,407

false

In Proteobacteria and Actinobacteria the main nitrite reductase activity is contributed by the NADH-dependent nitrite reductase, which detoxifies the nitrite formed as the product of nitrate reduction. The NADH-nitrite reductase operon consists of 4 genes: nirB, nirD, nirC and cysG. The enzyme is formed by the two subu...

[ "GO:0008942" ]

[ "nitrite reductase [NAD(P)H] activity" ]

[ "molecular_function" ]

1

[ "PFAM", "NCBIFAM", "CDD" ]

[ "PF13806", "TIGR02378", "cd03529" ]

[ "Rieske_2", "nirD_assim_sml", "Rieske_NirD" ]

[ 11762, 13032, 8859 ]

3

[ "EC" ]

[ "1.7.1" ]

[ "EC:1.7.1" ]

1

[ "2jo6", "2jza", "3c0d", "4aiv" ]

4

[ "PUB00014871", "PUB00043673", "PUB00043674", "PUB00043836", "PUB00043837", "PUB00080961", "PUB00080966" ]

[ "12665993", "8919448", "2200672", "16168954", "16271700", "8694757", "11460929" ]

[ "Characterisation and expression analysis of a nitrate transporter and nitrite reductase genes, two members of a gene cluster for nitrate assimilation from the symbiotic basidiomycete Hebeloma cylindrosporum.", "Nitrate reduction to ammonia by enteric bacteria: redundancy, or a strategy for survival during oxygen...

[ 2003, 1996, 1990, 2005, 2005, 1996, 2001 ]

7

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 17, 12178, 2128, 84 ]

4

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 3, 1, 1, 2, 4 ]

5

true

Domain

Rieske-like [2Fe-2S] domain, NirD-type

Rieske-like_NirD

5

IPR012749

12,749

dTDP-4-amino-4,6-dideoxygalactose transaminase WecE-like

WecE-like

Family

3,402

false

This family consists of dTDP-4-keto-6-deoxy-D-glucose transaminases, the WecE (formerly RffA) protein of enterobacterial common antigen (ECA) biosynthesis, from enterobacteria [ ]. It also includes closely matching sequence from species not expected to make ECA, but which contain other genes for the biosynthesis of dTD...

[]

0

[ "NCBIFAM" ]

[ "TIGR02379" ]

[ "ECA_wecE" ]

[ 3402 ]

1

[ "GP", "GP" ]

[ "GenProp0972", "GenProp1403" ]

[ "GP:GenProp0972", "GP:GenProp1403" ]

2

[ "4piw", "4zah", "6blg" ]

3

[ "PUB00076996" ]

[ "15271350" ]

[ "Characterization and investigation of substrate specificity of the sugar aminotransferase WecE from E. coli K12." ]

[ 2004 ]

1

[ "IPR000653" ]

[ "IPR032894" ]

1

0

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 7, 3244, 119, 32 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

dTDP-4-amino-4,6-dideoxygalactose transaminase WecE-like

WecE-like

6

IPR012750

12,750

Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphatetransferase

ECA_WecA-rel

Family

2,305

false

Members of this family are the WecA enzymes of enterobacterial common antigen (ECA) biosynthesis, undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphatetransferase ( ) [ ]. This family represents one narrow clade, and closely related sequences outside this clade may represent enzymes that catalyse the same speci...

[ "GO:0000287", "GO:0030145", "GO:0036380", "GO:0009103", "GO:0009276", "GO:0016020" ]

[ "magnesium ion binding", "manganese ion binding", "UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase activity", "lipopolysaccharide biosynthetic process", "Gram-negative-bacterium-type cell wall", "membrane" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component", "cellular_component" ]

6

[ "HAMAP", "NCBIFAM" ]

[ "MF_02030", "TIGR02380" ]

[ "WecA_Gammaproteo", "ECA_wecA" ]

[ 2275, 2266 ]

2

[ "EC", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METAC...

[ "2.7.8.33", "GenProp0970", "GenProp1270", "PWY-7290", "PWY-7530", "PWY-7815", "PWY-7816", "PWY-7819", "PWY-7905", "PWY-8204", "PWY-8205", "PWY-8206", "PWY-8207", "PWY-8208", "PWY-8209", "PWY-8211", "PWY-8212", "PWY-8217", "PWY-8218", "PWY-8219", "PWY-8220", "PWY-8221", "P...

[ "EC:2.7.8.33", "GP:GenProp0970", "GP:GenProp1270", "METACYC:PWY-7290", "METACYC:PWY-7530", "METACYC:PWY-7815", "METACYC:PWY-7816", "METACYC:PWY-7819", "METACYC:PWY-7905", "METACYC:PWY-8204", "METACYC:PWY-8205", "METACYC:PWY-8206", "METACYC:PWY-8207", "METACYC:PWY-8208", "METACYC:PWY-8209...

42

[]

0

[ "PUB00017060", "PUB00088369", "PUB00101155" ]

[ "11700352", "17237164", "18723618" ]

[ "Conserved amino acid residues found in a predicted cytosolic domain of the lipopolysaccharide biosynthetic protein WecA are implicated in the recognition of UDP-N-acetylglucosamine.", "Functional characterization and membrane topology of Escherichia coli WecA, a sugar-phosphate transferase initiating the biosynt...

[ 2001, 2007, 2008 ]

3

[ "IPR000715" ]

[]

1

0

1

[ "Bacteria", "Ecdysozoa", "metagenomes" ]

[ 2296, 2, 7 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphatetransferase

ECA_WecA-rel

3

IPR012751

12,751

CspD, cold shock

CspD

Family

2,733

false

This entry represents what appears to be a phylogenetically distinct clade, containing Escherichia coli CspD ( ) and related proteobacterial proteins within the larger family of cold shock domain proteins. The gene symbol cspD may have been used independently for other subfamilies of cold shock domain proteins, such as...

[ "GO:0003676", "GO:0006355", "GO:0005737" ]

[ "nucleic acid binding", "regulation of DNA-templated transcription", "cytoplasm" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "NCBIFAM" ]

[ "TIGR02381" ]

[ "cspD" ]

[ 2733 ]

1

[]

0

[]

0

[ "PUB00017061" ]

[ "11260474" ]

[ "CspD, a novel DNA replication inhibitor induced during the stationary phase in Escherichia coli." ]

[ 2001 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "ecological metagenomes" ]

[ 2720, 3, 10 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

CspD, cold shock

CspD

2

IPR012752

12,752

dTDP-fucosamine acetyltransferase WecD

AcTrfase_WecD

Family

1,592

false

This entry represents the WecD protein (also known as RffC), a TDP-fucosamine acetyltransferase involved in Enterobacterial common antigen (ECA) synthesis [ ]. ECA is a specific surface antigen (polysaccharide) shared by all members of the Enterobacteriaceae and is restricted to this family [ ]. ECA has been linked to ...

[ "GO:0008080", "GO:0009246" ]

[ "N-acetyltransferase activity", "enterobacterial common antigen biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "NCBIFAM" ]

[ "MF_02027", "TIGR02382" ]

[ "WecD_RffC", "wecD_rffC" ]

[ 1560, 1591 ]

2

[ "GP", "GP", "GP" ]

[ "GenProp0972", "GenProp1270", "GenProp1403" ]

[ "GP:GenProp0972", "GP:GenProp1270", "GP:GenProp1403" ]

3

[ "2fs5", "2ft0" ]

2

[ "PUB00040794", "PUB00060944", "PUB00060945" ]

[ "16855251", "12923112", "3078744" ]

[ "Crystal structure of TDP-fucosamine acetyltransferase (WecD) from Escherichia coli, an enzyme required for enterobacterial common antigen synthesis.", "Role for Salmonella enterica enterobacterial common antigen in bile resistance and virulence.", "ECA, the enterobacterial common antigen." ]

[ 2006, 2003, 1988 ]

3

[]

0

null

[ "Bacteria", "Eukaryota", "human gut metagenome" ]

[ 1589, 2, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

dTDP-fucosamine acetyltransferase WecD

AcTrfase_WecD

4

IPR012754

12,754

DNA-directed RNA polymerase, subunit beta-prime, bacterial type

DNA-dir_RpoC_beta_prime_bact

Family

25,447

false

DNA-directed RNA polymerases (also known as DNA-dependent RNA polymerases) are responsible for the polymerisation of ribonucleotides into a sequence complementary to the template DNA. In eukaryotes, there are three different forms of DNA-directed RNA polymerases transcribing different sets of genes. Most RNA polymerase...

[ "GO:0003677", "GO:0003899", "GO:0006351" ]

[ "DNA binding", "DNA-directed RNA polymerase activity", "DNA-templated transcription" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_01322", "TIGR02386" ]

[ "RNApol_bact_RpoC", "rpoC_TIGR" ]

[ 25031, 25195 ]

2

[ "EC", "GP", "REACTOME" ]

[ "2.7.7.6", "GenProp0262", "R-HSA-9639775" ]

[ "EC:2.7.7.6", "GP:GenProp0262", "REACTOME:R-HSA-9639775" ]

3

[ "1hqm", "1i6v", "1iw7", "1l9u", "1l9z", "1smy", "1ynj", "1ynn", "1zyr", "2a68", "2a69", "2a6e", "2a6h", "2be5", "2cw0", "2gho", "2o5i", "2o5j", "2ppb", "3aoh", "3aoi", "3dxj", "3eql", "3iyd", "3lu0", "3wod", "4g7h", "4g7o", "4g7z", "4gzy", "4gzz", "4jk1"...

630

[ "PUB00000061", "PUB00011749", "PUB00033173" ]

[ "3052291", "12000971", "10499798" ]

[ "Structure and function of bacterial sigma factors.", "Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A resolution.", "Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution." ]

[ 1988, 2002, 1999 ]

3

[ "IPR045867" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 25067, 92, 288 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

DNA-directed RNA polymerase, subunit beta-prime, bacterial type

DNA-dir_RpoC_beta_prime_bact

4

IPR012755

12,755

DNA-directed RNA polymerase, subunit gamma

DNA-dir_RpoC1_gamma

Family

621

false

DNA-directed RNA polymerases (also known as DNA-dependent RNA polymerases) are responsible for the polymerisation of ribonucleotides into a sequence complementary to the template DNA. In eukaryotes, there are three different forms of DNA-directed RNA polymerases transcribing different sets of genes. Most RNA polymerase...

[ "GO:0003677", "GO:0003899", "GO:0006351" ]

[ "DNA binding", "DNA-directed RNA polymerase activity", "DNA-templated transcription" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02387" ]

[ "rpoC1_cyan" ]

[ 621 ]

1

[ "EC", "GP" ]

[ "2.7.7.6", "GenProp0262" ]

[ "EC:2.7.7.6", "GP:GenProp0262" ]

2

[ "8gzg", "8gzh", "8h3v", "8h40", "8syi", "8urw", "9dvs", "9dvu" ]

8

[ "PUB00000061", "PUB00017773", "PUB00033173" ]

[ "3052291", "2495268", "10499798" ]

[ "Structure and function of bacterial sigma factors.", "Cyanobacterial RNA polymerase genes rpoC1 and rpoC2 correspond to rpoC of Escherichia coli.", "Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution." ]

[ 1988, 1989, 1999 ]

3

[ "IPR034678" ]

[]

1

0

1

[ "Cyanobacteriota", "Eukaryota" ]

[ 360, 261 ]

2

[]

0

true

Family

DNA-directed RNA polymerase, subunit gamma

DNA-dir_RpoC1_gamma

8

IPR012756

12,756

DNA-directed RNA polymerase, subunit beta''

DNA-dir_RpoC2_beta_pp

Family

15,592

false

The family consists of the product of the rpoC2 gene, a subunit of DNA-directed RNA polymerase of cyanobacteria and chloroplasts. RpoC2 corresponds largely to the C-terminal region of the RpoC (the beta' subunit) of other bacteria. Members of this family are designated beta'' in chloroplasts/plastids, and beta' (confus...

[ "GO:0003677", "GO:0003899", "GO:0006351" ]

[ "DNA binding", "DNA-directed RNA polymerase activity", "DNA-templated transcription" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_01324", "TIGR02388" ]

[ "RNApol_bact_RpoC2", "rpoC2_cyan" ]

[ 15116, 15164 ]

2

[ "EC", "GP" ]

[ "2.7.7.6", "GenProp0262" ]

[ "EC:2.7.7.6", "GP:GenProp0262" ]

2

[ "8emb", "8gzg", "8gzh", "8h3v", "8h40", "8qma", "8r5o", "8r6s", "8ras", "8rdj", "8syi", "8urw", "8w9z", "8wa0", "8wa1", "8xzv", "9dvs", "9dvu", "9epc" ]

19

[ "PUB00000061", "PUB00033173" ]

[ "3052291", "10499798" ]

[ "Structure and function of bacterial sigma factors.", "Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution." ]

[ 1988, 1999 ]

2

[]

0

null

[ "Bacteria", "Eukaryota" ]

[ 485, 15107 ]

2

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 8, 2, 2 ]

3

true

Family

DNA-directed RNA polymerase, subunit beta''

DNA-dir_RpoC2_beta_pp

3

IPR012757

12,757

DNA-directed RNA polymerase subunit Rpo1C

RPO1C

Family

889

false

This family consists of the archaeal Rpo1C subunit (also known as A'') of the DNA-directed RNA polymerase [ ]. DNA-directed RNA polymerases, also known as DNA-dependent RNA polymerases, are responsible for the polymerisation of ribonucleotides into a sequence complementary to the template DNA. Eukaryotes have three dif...

[ "GO:0003677", "GO:0003899", "GO:0006351" ]

[ "DNA binding", "DNA-directed RNA polymerase activity", "DNA-templated transcription" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "NCBIFAM", "CDD" ]

[ "MF_00411", "TIGR02389", "cd06528" ]

[ "RNApol_arch_Rpo1C", "RNA_pol_rpoA2", "RNAP_A''" ]

[ 878, 823, 850 ]

3

[ "EC" ]

[ "2.7.7.6" ]

[ "EC:2.7.7.6" ]

1

[ "2pmz", "2waq", "2wb1", "2y0s", "3hkz", "4ayb", "4qiw", "4v8s", "6kf3", "6kf4", "6kf9", "7ok0", "7oq4", "7oqy", "8cro", "8oki", "8orq", "8p2i", "8rbo", "9bct", "9bcu" ]

21

[ "PUB00059148", "PUB00059149" ]

[ "19419240", "19880312" ]

[ "Evolution of Complex RNA Polymerases: The Complete Archaeal RNA Polymerase Structure.", "Archaeal RNA polymerase." ]

[ 2009, 2009 ]

2

[]

0

null

[ "Archaea", "Geodia barretti", "unclassified sequences" ]

[ 874, 1, 14 ]

3

[]

0

true

Family

DNA-directed RNA polymerase subunit Rpo1C

RPO1C

2

IPR012758

12,758

DNA-directed RNA polymerase subunit Rpo1N

RPO1N

Family

939

false

This family consists of the archaeal Rpo1N subunit (also known as A' subunit) of the DNA-directed RNA polymerase [ ]. DNA-directed RNA polymerases, also known as DNA-dependent RNA polymerases, are responsible for the polymerisation of ribonucleotides into a sequence complementary to the template DNA. Eukaryotes have th...

[ "GO:0003677", "GO:0003899", "GO:0008270", "GO:0006351" ]

[ "DNA binding", "DNA-directed RNA polymerase activity", "zinc ion binding", "DNA-templated transcription" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "HAMAP", "NCBIFAM", "CDD" ]

[ "MF_00863", "TIGR02390", "cd02582" ]

[ "RNApol_arch_Rpo1N", "RNA_pol_rpoA1", "RNAP_archeal_A'" ]

[ 905, 903, 869 ]

3

[ "EC" ]

[ "2.7.7.6" ]

[ "EC:2.7.7.6" ]

1

[ "2pmz", "2waq", "2wb1", "2y0s", "3hkz", "4ayb", "4qiw", "4v8s", "6kf3", "6kf4", "6kf9", "7ok0", "7oq4", "7oqy", "8cro", "8oki", "8orq", "8p2i", "8rbo", "9bct", "9bcu" ]

21

[ "PUB00059148", "PUB00059149" ]

[ "19419240", "19880312" ]

[ "Evolution of Complex RNA Polymerases: The Complete Archaeal RNA Polymerase Structure.", "Archaeal RNA polymerase." ]

[ 2009, 2009 ]

2

[]

0

null

[ "Archaea", "Geodia barretti", "unclassified sequences" ]

[ 924, 1, 14 ]

3

[]

0

true

Family

DNA-directed RNA polymerase subunit Rpo1N

RPO1N

5

IPR012759

12,759

RNA polymerase sigma factor RpoH, proteobacteria

RNA_pol_sigma_RpoH_proteobac

Family

9,300

false

The bacterial core RNA polymerase complex, which consists of five subunits, is sufficient for transcription elongation and termination but is unable to initiate transcription. Transcription initiation from promoter elements requires a sixth, dissociable subunit called a sigma factor, which reversibly associates with th...

[ "GO:0003700", "GO:0016987", "GO:0006352", "GO:0006355" ]

[ "DNA-binding transcription factor activity", "sigma factor activity", "DNA-templated transcription initiation", "regulation of DNA-templated transcription" ]

[ "molecular_function", "molecular_function", "biological_process", "biological_process" ]

4

[ "HAMAP", "NCBIFAM" ]

[ "MF_00961", "TIGR02392" ]

[ "Sigma70_RpoH", "rpoH_proteo" ]

[ 8725, 9298 ]

2

[]

0

[ "8hkc" ]

1

[ "PUB00000061", "PUB00002181", "PUB00004340", "PUB00088319" ]

[ "3052291", "1597408", "3092189", "25596450" ]

[ "Structure and function of bacterial sigma factors.", "The sigma 70 family: sequence conservation and evolutionary relationships.", "Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins.", "Plastid sigma factors: Their individual functions and regulation in transcription."...

[ 1988, 1992, 1986, 2015 ]

4

[]

0

null

[ "Bacteria", "Candidatus Nitrosopumilus salarius BD31", "Eukaryota", "unclassified sequences" ]

[ 9174, 1, 15, 110 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

RNA polymerase sigma factor RpoH, proteobacteria

RNA_pol_sigma_RpoH_proteobac

9

IPR012760

12,760

RNA polymerase sigma factor RpoD, C-terminal

RNA_pol_sigma_RpoD_C

Domain

22,766

false

The bacterial core RNA polymerase complex, which consists of five subunits, is sufficient for transcription elongation and termination but is unable to initiate transcription. Transcription initiation from promoter elements requires a sixth, dissociable subunit called a sigma factor, which reversibly associates with th...

[ "GO:0003677", "GO:0016987", "GO:0006352", "GO:0006355" ]

[ "DNA binding", "sigma factor activity", "DNA-templated transcription initiation", "regulation of DNA-templated transcription" ]

[ "molecular_function", "molecular_function", "biological_process", "biological_process" ]

4

[ "NCBIFAM" ]

[ "TIGR02393" ]

[ "RpoD_Cterm" ]

[ 22766 ]

1

[]

0

[ "1iw7", "1l9u", "1l9z", "1smy", "1zyr", "2a68", "2a69", "2a6e", "2a6h", "2be5", "2cw0", "3dxj", "3eql", "3iyd", "3wod", "4g7h", "4g7o", "4g7z", "4jk1", "4jk2", "4jkr", "4kmu", "4kn4", "4kn7", "4ljz", "4lk0", "4lk1", "4llg", "4mex", "4mey", "4mq9", "4oin"...

289

[ "PUB00000061", "PUB00000942", "PUB00002181", "PUB00004340", "PUB00010042" ]

[ "3052291", "8858155", "1597408", "3092189", "11931761" ]

[ "Structure and function of bacterial sigma factors.", "Crystal structure of a sigma 70 subunit fragment from E. coli RNA polymerase.", "The sigma 70 family: sequence conservation and evolutionary relationships.", "Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins.", "...

[ 1988, 1996, 1992, 1986, 2002 ]

5

[ "IPR000943" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "Peduoviridae", "unclassified sequences" ]

[ 22388, 46, 2, 330 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

RNA polymerase sigma factor RpoD, C-terminal

RNA_pol_sigma_RpoD_C

4

IPR012761

12,761

RNA polymerase sigma factor RpoS

RNA_pol_sigma_RpoS

Family

4,670

false

The bacterial core RNA polymerase complex, which consists of five subunits, is sufficient for transcription elongation and termination but is unable to initiate transcription. Transcription initiation from promoter elements requires a sixth, dissociable subunit called a sigma factor, which reversibly associates with th...

[ "GO:0003677", "GO:0003700", "GO:0016987", "GO:0006352", "GO:0006355" ]

[ "DNA binding", "DNA-binding transcription factor activity", "sigma factor activity", "DNA-templated transcription initiation", "regulation of DNA-templated transcription" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "biological_process" ]

5

[ "HAMAP", "NCBIFAM" ]

[ "MF_00959", "TIGR02394" ]

[ "Sigma70_RpoS", "rpoS_proteo" ]

[ 4483, 4652 ]

2

[]

0

[ "5ipl", "5ipm", "5ipn", "6kj6", "6omf", "6utv", "6utw", "6utx", "6uty", "6utz", "6uu0", "6uu1", "6uu2", "6uu3", "6uu4", "6uu5", "6uu6", "6uu7", "6uu8", "6uu9", "6uua", "6uub", "6uuc", "7f0r", "7vf9", "7xl3", "7xl4" ]

27

[ "PUB00000061", "PUB00002181", "PUB00004340", "PUB00068874", "PUB00088319" ]

[ "3052291", "1597408", "3092189", "21639793", "25596450" ]

[ "Structure and function of bacterial sigma factors.", "The sigma 70 family: sequence conservation and evolutionary relationships.", "Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins.", "The RpoS-mediated general stress response in Escherichia coli.", "Plastid sigma f...

[ 1988, 1992, 1986, 2011, 2015 ]

5

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 4632, 6, 32 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

RNA polymerase sigma factor RpoS

RNA_pol_sigma_RpoS

3

IPR012763

12,763

DNA polymerase III, subunit gamma/ tau, N-terminal

DNA_pol_III_sug/sutau_N

Domain

29,955

false

This entry represents the well-conserved first N-terminal domain of DnaX (also known as DNA polymerase III subunit gamma/tau), approx. 365 aa. The full-length product of the dnaX gene in Escherichia coli encodes the DNA polymerase III tau subunit. A translational frameshift leads to early termination and a truncated pr...

[ "GO:0003887", "GO:0005524", "GO:0006260", "GO:0009360" ]

[ "DNA-directed DNA polymerase activity", "ATP binding", "DNA replication", "DNA polymerase III complex" ]

[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

4

[ "NCBIFAM" ]

[ "TIGR02397" ]

[ "dnaX_nterm" ]

[ 29955 ]

1

[ "EC", "GP" ]

[ "2.7.7.7", "GenProp0263" ]

[ "EC:2.7.7.7", "GP:GenProp0263" ]

2

[ "1jr3", "1njf", "1njg", "1xxh", "1xxi", "3glf", "3glg", "3glh", "3gli", "8giy", "8giz", "8gj0", "8gj1", "8gj2", "8gj3", "8val", "8vam", "8van", "8vap", "8vaq", "8var", "8vas", "8vat" ]

23

[ "PUB00095753", "PUB00101309", "PUB00101310" ]

[ "22210898", "12586888", "17522086" ]

[ "GLABROUS INFLORESCENCE STEMS (GIS) is required for trichome branching through gibberellic acid signaling in Arabidopsis.", "The Arabidopsis STICHEL gene is a regulator of trichome branch number and encodes a novel protein.", "Plastid genome sequence of the cryptophyte alga Rhodomonas salina CCMP1319: lateral t...

[ 2012, 2003, 2007 ]

3

[]

0

null

[ "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences", "uncultured marine thaumarchaeote KM3_70_D04" ]

[ 26931, 17, 2561, 445, 1 ]

5

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Mus musculus", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 25, 1, 1, 15, 41 ]

5

true

Domain

DNA polymerase III, subunit gamma/ tau, N-terminal

DNA_pol_III_sug/sutau_N

2

IPR012764

12,764

Glucosylglycerol-phosphate synthase

Gluc_glyc_Psyn

Family

580

false

Glucosylglycerol-phosphate synthase catalyses the key step in the biosynthesis of the osmolyte glucosylglycerol. It is known in several cyanobacteria and in Pseudomonas anguilliseptica. The enzyme is closely related to the alpha,alpha-trehalose-phosphate synthase, likewise involved in osmolyte biosynthesis, of Escheric...

[ "GO:0016758", "GO:0051473" ]

[ "hexosyltransferase activity", "glucosylglycerol biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02398" ]

[ "gluc_glyc_Psyn" ]

[ 580 ]

1

[ "EC", "GP", "METACYC" ]

[ "2.4.1.213", "GenProp0264", "PWY-7902" ]

[ "EC:2.4.1.213", "GP:GenProp0264", "METACYC:PWY-7902" ]

3

[]

0

[]

0

[ "IPR001830" ]

[]

1

0

1

[ "Bacteria", "ecological metagenomes" ]

[ 574, 6 ]

2

[]

0

true

Family

Glucosylglycerol-phosphate synthase

Gluc_glyc_Psyn

2

IPR012765

12,765

Glucosylglycerol-phospate 3-phosphatase

GGPPase

Family

116

false

Proteins in this family are glucosylglycerol-phosphate phosphatases, with the gene symbol stpA (Salt Tolerance Protein A). A motif characteristic of acid phosphatases is found, but otherwise this family shows little sequence similarity to other phosphatases. This enzyme acts on the glucosylglycerol phosphate, product o...

[ "GO:0050530" ]

[ "glucosylglycerol 3-phosphatase activity" ]

[ "molecular_function" ]

1

[ "PFAM", "PIRSF", "NCBIFAM" ]

[ "PF09506", "PIRSF020945", "TIGR02399" ]

[ "Salt_tol_Pase", "GGPPase", "salt_tol_Pase" ]

[ 116, 44, 115 ]

3

[ "GP" ]

[ "GenProp0264" ]

[ "GP:GenProp0264" ]

1

[]

0

[ "PUB00017780" ]

[ "9045835" ]

[ "The stpA gene form synechocystis sp. strain PCC 6803 encodes the glucosylglycerol-phosphate phosphatase involved in cyanobacterial osmotic response to salt shock." ]

[ 1997 ]

1

[]

0

null

[ "Bacteria" ]

[ 116 ]

1

[]

0

true

Family

Glucosylglycerol-phospate 3-phosphatase

GGPPase

9

IPR012766

12,766

Alpha,alpha-trehalose-phosphate synthase

Trehalose_OtsA

Family

6,571

false

This enzyme catalyzes the key, penultimate step in biosynthesis of trehalose, a compatible solute made as an osmoprotectant in some species in all three domains of life. The gene symbol OtsA stands for osmotically regulated trehalose synthesis A. Trehalose helps protect against both osmotic and thermal stresses, and is...

[ "GO:0003825", "GO:0005992" ]

[ "alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity", "trehalose biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02400" ]

[ "trehalose_OtsA" ]

[ 6571 ]

1

[ "EC", "GP" ]

[ "2.4.1.15", "GenProp0265" ]

[ "EC:2.4.1.15", "GP:GenProp0265" ]

2

[ "1gz5", "1uqt", "1uqu", "2wtx", "5hut", "5huu", "5huv", "5hvl", "5hvm", "5hvo", "5hxa", "5tvg", "5uof", "5v0t", "6jak", "6jbi", "6jbr", "6jbw", "9niq", "9nkb" ]

20

[ "PUB00016701" ]

[ "12890033" ]

[ "Three pathways for trehalose metabolism in Corynebacterium glutamicum ATCC13032 and their significance in response to osmotic stress." ]

[ 2003 ]

1

[ "IPR001830" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 45, 3749, 2775, 2 ]

4

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]

[ 9, 1, 1, 1, 1, 1, 9 ]

7

true

Family

Alpha,alpha-trehalose-phosphate synthase

Trehalose_OtsA

2

IPR012767

12,767

Maltooligosyl trehalose synthase

Trehalose_TreY

Family

8,269

false

This family describes the enzyme TreY. Maltooligosyl trehalose synthase (MTSase, TreY) and maltooligosyl trehalose trehalohydrolase (MTHase, TreZ) work together to produce trehalose. MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the...

[]

0

[ "NCBIFAM", "CDD" ]

[ "TIGR02401", "cd11336" ]

[ "trehalose_TreY", "AmyAc_MTSase" ]

[ 8200, 8104 ]

2

[ "EC", "GP", "METACYC", "REACTOME" ]

[ "5.4.99.15", "GenProp0266", "PWY-2661", "R-MTU-868688" ]

[ "EC:5.4.99.15", "GP:GenProp0266", "METACYC:PWY-2661", "REACTOME:R-MTU-868688" ]

4

[ "1iv8", "3hje", "5zcr", "6lcu", "6lcv" ]

5

[ "PUB00080591", "PUB00080592" ]

[ "15703182", "11471747" ]

[ "The OtsAB pathway is essential for trehalose biosynthesis in Mycobacterium tuberculosis.", "Trehalose-producing operon treYZ from Arthrobacter ramosus S34." ]

[ 2005, 2001 ]

2

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 59, 8177, 10, 23 ]

4

[]

0

true

Family

Maltooligosyl trehalose synthase

Trehalose_TreY

9

IPR012768

12,768

Malto-oligosyltrehalose trehalohydrolase

Trehalose_TreZ

Family

8,678

false

Members of this family are the trehalose biosynthetic enzyme malto-oligosyltrehalose trehalohydrolase, formally known as 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase ( ). It is the TreZ protein of the TreYZ pathway for trehalose biosynthesis, and alternative to the OtsAB system.

[ "GO:0004553", "GO:0005992" ]

[ "hydrolase activity, hydrolyzing O-glycosyl compounds", "trehalose biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PIRSF", "NCBIFAM" ]

[ "PIRSF006337", "TIGR02402" ]

[ "Trehalose_TreZ", "trehalose_TreZ" ]

[ 8447, 8526 ]

2

[ "EC", "GP", "METACYC", "REACTOME" ]

[ "3.2.1.141", "GenProp0266", "PWY-2661", "R-MTU-868688" ]

[ "EC:3.2.1.141", "GP:GenProp0266", "METACYC:PWY-2661", "REACTOME:R-MTU-868688" ]

4

[ "1eh9", "1eha", "2bhu", "2bhy", "2bhz", "2bxy", "2bxz", "2by0", "2by1", "2by2", "2by3", "3m07", "3vgb", "3vgd", "3vge", "3vgf", "3vgg", "3vgh" ]

18

[]

0

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 58, 8589, 8, 23 ]

4

[]

0

true

Family

Malto-oligosyltrehalose trehalohydrolase

Trehalose_TreZ

5

IPR012769

12,769

Trehalose-6-phosphate hydrolase

Trehalose_TreC

Family

4,628

false

Trehalose is a glucose disaccharide that serves in many biological systems as a compatible solute for protection against hyperosmotic and thermal stress. This family describes trehalose-6-phosphate hydrolase, product of the treC (or treA) gene, which is often found together with a trehalose uptake transporter and a tre...

[ "GO:0008788", "GO:0005993", "GO:0005737" ]

[ "alpha,alpha-phosphotrehalase activity", "trehalose catabolic process", "cytoplasm" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "NCBIFAM" ]

[ "TIGR02403" ]

[ "trehalose_treC" ]

[ 4628 ]

1

[ "GP", "GP" ]

[ "GenProp0271", "GenProp1394" ]

[ "GP:GenProp0271", "GP:GenProp1394" ]

2

[ "5brp", "5brq" ]

2

[ "PUB00033159" ]

[ "8083158" ]

[ "Trehalose-6-phosphate hydrolase of Escherichia coli." ]

[ 1994 ]

1

[]

0

null

[ "Bacteria", "Beauveria bassiana D1-5", "metagenomes" ]

[ 4625, 1, 2 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Trehalose-6-phosphate hydrolase

Trehalose_TreC

6

IPR012770

12,770

Trehalose operon transcriptional repressor

TreR

Family

2,669

false

This family consists of repressors of the GntR family typically associated with trehalose utilization operons. Trehalose is imported as trehalose-6-phosphate and then hydrolyzed by alpha,alpha-phosphotrehalase to glucose and glucose-6-P. This family includes repressors mostly from Gram-positive lineages (such as TreR f...

[]

0

[ "NCBIFAM" ]

[ "TIGR02404" ]

[ "trehalos_R_Bsub" ]

[ 2669 ]

1

[ "GP" ]

[ "GenProp0271" ]

[ "GP:GenProp0271" ]

1

[ "2ogg" ]

1

[]

0

[]

0

null

[ "Bacteria", "Phytophthora kernoviae 00238/432", "bioreactor metagenome" ]

[ 2666, 1, 2 ]

3

[]

0

true

Family

Trehalose operon transcriptional repressor

TreR

2

IPR012771

12,771

Trehalose operon repressor

Trehalos_R_gpbac

Family

1,448

false

Trehalose is a non-reducing disaccharide which can be used as both a carbon source and an osmoprotectant in bacteria. Trehalose uptake into the cytoplasm occurs via a trehalose-specific phosphotransferase system which phosphorylates trehalase to trehalose-6-phosphate (Tre6P) during transport into the cytoplasm, and a h...

[ "GO:0003677", "GO:0005991", "GO:0045892" ]

[ "DNA binding", "trehalose metabolic process", "negative regulation of DNA-templated transcription" ]

[ "molecular_function", "biological_process", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02405" ]

[ "trehalos_R_Ecol" ]

[ 1448 ]

1

[ "GP" ]

[ "GenProp0271" ]

[ "GP:GenProp0271" ]

1

[ "4xxh" ]

1

[ "PUB00023777", "PUB00033159", "PUB00033160" ]

[ "9865945", "8083158", "9148912" ]

[ "Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose.", "Trehalose-6-phosphate hydrolase of Escherichia coli.", "Characterization of TreR, the major regulator of...

[ 1998, 1994, 1997 ]

3

[]

0

null

[ "Bacteria", "Beauveria bassiana D1-5", "human gut metagenome" ]

[ 1446, 1, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Trehalose operon repressor

Trehalos_R_gpbac

6

IPR012772

12,772

L-2,4-diaminobutyric acid acetyltransferase

Ectoine_EctA

Family

3,948

false

This enzyme family is the EctA of ectoine biosynthesis. Ectoine is a compatible solute, analogous to trehalose, betaines, etc., found often in halotolerant organisms. EctA is L-2,4-diaminobutyric acid acetyltransferase, also called DABA acetyltransferase [ , , ].

[ "GO:0033816", "GO:0019491" ]

[ "diaminobutyrate acetyltransferase activity", "ectoine biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02406" ]

[ "ectoine_EctA" ]

[ 3948 ]

1

[ "EC", "GP" ]

[ "2.3.1.178", "GenProp0268" ]

[ "EC:2.3.1.178", "GP:GenProp0268" ]

2

[ "3d3s", "6sjy", "6sk1", "6sl8", "6slk", "6sll" ]

6

[ "PUB00060955", "PUB00060956", "PUB00060957" ]

[ "18488150", "16212543", "9864317" ]

[ "Cloning and heterologous expression of ectoine biosynthesis genes from Bacillus halodurans in Escherichia coli.", "Cloning, purification, and characterization of diaminobutyrate acetyltransferase from the halotolerant methanotroph Methylomicrobium alcaliphilum 20Z.", "Characterization of biosynthetic enzymes f...

[ 2008, 2005, 1999 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 20, 3904, 8, 16 ]

4

[]

0

true

Family

L-2,4-diaminobutyric acid acetyltransferase

Ectoine_EctA

2

IPR012773

12,773

Ectoine biosynthetic protein

Ectoine_EctB

Family

4,803

false

Members of this family of class III pyridoxal-phosphate-dependent aminotransferases are diaminobutyrate--2-oxoglutarate aminotransferase ( ) that catalyze the first step in ectoine biosynthesis from L-aspartate beta-semialdehyde. This family is readily separated phylogenetically from enzymes with the same substrate and...

[ "GO:0030170", "GO:0047307", "GO:0019491" ]

[ "pyridoxal phosphate binding", "diaminobutyrate-pyruvate transaminase activity", "ectoine biosynthetic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02407" ]

[ "ectoine_ectB" ]

[ 4803 ]

1

[ "EC", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]

[ "2.6.1.76", "GenProp0268", "PWY-6409", "PWY-6562", "PWY-761", "PWY-7855", "PWY-7988" ]

[ "EC:2.6.1.76", "GP:GenProp0268", "METACYC:PWY-6409", "METACYC:PWY-6562", "METACYC:PWY-761", "METACYC:PWY-7855", "METACYC:PWY-7988" ]

7

[ "6rl5" ]

1

[]

0

[ "IPR004637" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 26, 4757, 4, 16 ]

4

[]

0

true

Family

Ectoine biosynthetic protein

Ectoine_EctB

9

IPR012774

12,774

Ectoine dioxygenase

EctD

Family

2,837

false

Ectoine dioxygenase EctD is involved in the biosynthesis of ectoine ((S)-2-methyl-1,4,5,6-tetrahydropyrimidine-4-carboxylic acid) which is a highly soluble organic osmolyte, called compatible solute, use to avoid excessive water efflux, plasmolysis, molecular crowding of the cytoplasm, and cessation of growth in high s...

[ "GO:0016706" ]

[ "2-oxoglutarate-dependent dioxygenase activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR02408" ]

[ "ectoine_ThpD" ]

[ 2837 ]

1

[ "EC", "GP" ]

[ "1.14.11.55", "GenProp0268" ]

[ "EC:1.14.11.55", "GP:GenProp0268" ]

2

[ "3emr", "4mhr", "4mhu", "4nmi", "4q5o" ]

5

[ "PUB00077031" ]

[ "17636255" ]

[ "Osmotically induced synthesis of the compatible solute hydroxyectoine is mediated by an evolutionarily conserved ectoine hydroxylase." ]

[ 2007 ]

1

[ "IPR008775" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "Nitrososphaerota", "unclassified sequences" ]

[ 2819, 2, 8, 8 ]

4

[]

0

true

Family

Ectoine dioxygenase

EctD

7

IPR012775

12,775

Gamma-butyrobetaine hydroxylase-like

GBBH-like

Family

1,062

false

Members of this protein family are gamma-butyrobetaine hydroxylase (GBBH), both bacterial and eukaryotic. This enzyme catalyses the last step in the conversion of lysine to carnitine. Carnitine can serve as a compatible solvent in bacteria and also participates in fatty acid metabolism [ , ]. The structure of human GBB...

[ "GO:0005506", "GO:0045329" ]

[ "iron ion binding", "carnitine biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02409" ]

[ "carnitine_bodg" ]

[ 1062 ]

1

[ "EC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "1.14.11.1", "PWY-3621", "PWY-6100", "R-CEL-71262", "R-HSA-71262", "R-MMU-71262", "R-RNO-71262" ]

[ "EC:1.14.11.1", "METACYC:PWY-3621", "METACYC:PWY-6100", "REACTOME:R-CEL-71262", "REACTOME:R-HSA-71262", "REACTOME:R-MMU-71262", "REACTOME:R-RNO-71262" ]

7

[ "3ms5", "3n6w", "3o2g", "4bg1", "4bgk", "4bgm", "4bhf", "4bhg", "4bhi", "4c5w", "4c8r", "4cwd", "6npb", "6npc", "6npd" ]

15

[ "PUB00017784", "PUB00075680", "PUB00077362", "PUB00103931" ]

[ "8504802", "20599753", "861203", "30789718" ]

[ "gamma-Butyrobetaine hydroxylase. Structural characterization of the Pseudomonas enzyme.", "Crystal structure of human gamma-butyrobetaine hydroxylase.", "Purification and properties of gamma-butyrobetaine hydroxylase from Pseudomonas sp AK 1.", "A New Microbial Pathway for Organophosphonate Degradation Catal...

[ 1993, 2010, 1977, 2019 ]

4

[ "IPR050411" ]

[]

1

0

1

[ "Bacteria", "Bilateria" ]

[ 408, 654 ]

2

[ "Caenorhabditis elegans", "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 1, 2, 1, 3 ]

5

true

Family

Gamma-butyrobetaine hydroxylase-like

GBBH-like

8

IPR012776

12,776

Trimethyllysine dioxygenase

Trimethyllysine_dOase

Family

2,650

false

Trimethyllysine dioxygenase is involved in the carnitine biosynthesis. It converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML) [ , ].

[ "GO:0005506", "GO:0050353", "GO:0045329" ]

[ "iron ion binding", "trimethyllysine dioxygenase activity", "carnitine biosynthetic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02410" ]

[ "carnitine_TMLD" ]

[ 2650 ]

1

[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "1.14.11.8", "PWY-6100", "R-BTA-71262", "R-GGA-71262", "R-HSA-71262", "R-RNO-71262" ]

[ "EC:1.14.11.8", "METACYC:PWY-6100", "REACTOME:R-BTA-71262", "REACTOME:R-GGA-71262", "REACTOME:R-HSA-71262", "REACTOME:R-RNO-71262" ]

6

[]

0

[ "PUB00084964", "PUB00084965" ]

[ "11431483", "23092983" ]

[ "Molecular and Biochemical Characterization of Rat epsilon -N-Trimethyllysine Hydroxylase, the First Enzyme of Carnitine Biosynthesis.", "Analysis of the chromosome X exome in patients with autism spectrum disorders identified novel candidate genes, including TMLHE." ]

[ 2001, 2012 ]

2

[ "IPR050411" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "freshwater metagenome" ]

[ 16, 2631, 3 ]

3

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 1, 2, 1, 1, 3 ]

6

true

Family

Trimethyllysine dioxygenase

Trimethyllysine_dOase

7

IPR012777

12,777

Leukotriene A4 hydrolase/leucine aminopeptidase

LTA4H

Family

2,132

false

Members of this family represent a distinctive subset within the zinc metallopeptidases of MEROPS peptidase family M1 (aminopeptidase N, clan MA). This entry represents leukotriene A-4 hydrolase (LTA4), which in vertebrates has both epoxide hydrolase and aminopeptidase activity at the same active site [ ]. In contrast,...

[ "GO:0008270" ]

[ "zinc ion binding" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR02411" ]

[ "leuko_A4_hydro" ]

[ 2132 ]

1

[ "EC", "EC", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "3.3.2.10", "3.4.11.-", "GenProp1653", "PWY-6423", "PWY-6710", "PWY-7694", "PWY-7778", "PWY-7954", "PWY-8356", "PWY-8395", "PWY-8397", "PWY-8399", "PWY-8400", "R-BTA-2142691", "R-BTA-6798695", "R-BTA-9018676", "R-BTA-9018681", "R-BTA-9018896", "R-BTA-9020265", "R-BTA-9023661", ...

[ "EC:3.3.2.10", "EC:3.4.11.-", "GP:GenProp1653", "METACYC:PWY-6423", "METACYC:PWY-6710", "METACYC:PWY-7694", "METACYC:PWY-7778", "METACYC:PWY-7954", "METACYC:PWY-8356", "METACYC:PWY-8395", "METACYC:PWY-8397", "METACYC:PWY-8399", "METACYC:PWY-8400", "REACTOME:R-BTA-2142691", "REACTOME:R-BT...

55

[ "1gw6", "1h19", "1hs6", "1sqm", "2r59", "2vj8", "2xpy", "2xpz", "2xq0", "3b7r", "3b7s", "3b7t", "3b7u", "3cho", "3chp", "3chq", "3chr", "3chs", "3fh5", "3fh7", "3fh8", "3fhe", "3fts", "3ftu", "3ftv", "3ftw", "3ftx", "3fty", "3ftz", "3fu0", "3fu3", "3fu5"...

81

[ "PUB00017074", "PUB00054656" ]

[ "15805137", "21146536" ]

[ "Nuclear localization of leukotriene A4 hydrolase in type II alveolar epithelial cells in normal and fibrotic lung.", "A Leukotriene A(4) Hydrolase-Related Aminopeptidase from Yeast Undergoes Induced Fit upon Inhibitor Binding." ]

[ 2005, 2011 ]

2

[ "IPR034015" ]

[]

1

0

1

[ "Eukaryota" ]

[ 2132 ]

1

[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]

[ 1, 2, 3, 1, 1, 2, 1, 1 ]

8

true

Family

Leukotriene A4 hydrolase/leucine aminopeptidase

LTA4H

4

IPR012778

12,778

Peptidase M1, aminopeptidase

Pept_M1_aminopeptidase

Family

8,610

false

This family is a subset of the members of the zinc metallopeptidases belonging to MEROPS peptidase family M1 (aminopeptidase N, clan MA), with a single member characterised in Streptomyces lividans: aminopeptidase G [ ]. The rest of the members of this family are identified as aminopeptidase N of the actinomycete-type....

[ "GO:0004177", "GO:0006508" ]

[ "aminopeptidase activity", "proteolysis" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02412" ]

[ "pepN_strep_liv" ]

[ 8610 ]

1

[]

0

[ "7v9n", "7v9o", "7v9p", "7v9q", "8t41" ]

5

[ "PUB00003579", "PUB00017062" ]

[ "7674922", "7765336" ]

[ "Evolutionary families of metallopeptidases.", "Intracellular aminopeptidases in Streptomyces lividans 66." ]

[ 1995, 1994 ]

2

[]

0

null

[ "Bacteria", "Eukaryota", "Marine Group I thaumarchaeote", "metagenomes" ]

[ 8436, 18, 1, 155 ]

4

[]

0

true

Family

Peptidase M1, aminopeptidase

Pept_M1_aminopeptidase

1

IPR012779

12,779

Peptidase M1, alanyl aminopeptidase

Peptidase_M1_pepN

Family

11,945

false

The M1 family of zinc metallopeptidases contains a number of distinct, well-separated clades of proteins with aminopeptidase activity. Several are designated aminopeptidase N, , after the Escherichia coli enzyme, suggesting a similar activity profile (see for a description of catalytic activity). This group of zinc met...

[ "GO:0008270" ]

[ "zinc ion binding" ]

[ "molecular_function" ]

1

[ "PANTHER", "NCBIFAM" ]

[ "PTHR46322", "TIGR02414" ]

[ "", "pepN_proteo" ]

[ 11945, 10367 ]

2

[]

0

[ "2dq6", "2dqm", "2gtq", "2hpo", "2hpt", "2zxg", "3b2p", "3b2x", "3b34", "3b37", "3b3b", "3ebg", "3ebh", "3ebi", "3ked", "3puu", "3q43", "3q44", "3qjx", "3t8v", "4j3b", "4k5l", "4k5m", "4k5n", "4k5o", "4k5p", "4pu2", "4pvb", "4pw4", "4q4e", "4q4i", "4qhp"...

116

[ "PUB00003579", "PUB00017063", "PUB00017064" ]

[ "7674922", "15109723", "14663077" ]

[ "Evolutionary families of metallopeptidases.", "Actinobacillus pleuropneumoniae metalloprotease: cloning and in vivo expression.", "PepN is the major aminopeptidase in Escherichia coli: insights on substrate specificity and role during sodium-salicylate-induced stress." ]

[ 1995, 2004, 2003 ]

3

[ "IPR001930" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "Yasminevirus sp. GU-2018", "unclassified sequences" ]

[ 98, 9683, 2028, 1, 135 ]

5

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 11, 1, 4, 15 ]

4

true

Family

Peptidase M1, alanyl aminopeptidase

Peptidase_M1_pepN

3

IPR012780

12,780

Carbon-monoxide dehydrogenase, large subunit

CO_Mo_DH_lsu

Family

1,092

false

Carbon monoxide dehydrogenases catalyse the reversible oxidation of carbon monoxide to carbon dioxide as shown below [ , ]: CO + H(2)O + A == CO(2) + AH(2) A variety of electron acceptors can be used by these enzymes including ferredoxin, methyl viologen and benzyl viologen. Under anaerobic conditions, carbon monoxide ...

[ "GO:0005507", "GO:0030151", "GO:0043885" ]

[ "copper ion binding", "molybdenum ion binding", "anaerobic carbon-monoxide dehydrogenase activity" ]

[ "molecular_function", "molecular_function", "molecular_function" ]

3

[ "NCBIFAM" ]

[ "TIGR02416" ]

[ "CO_dehy_Mo_lg" ]

[ 1092 ]

1

[]

0

[ "1ffu", "1ffv", "1n5w", "1n60", "1n61", "1n62", "1n63", "1zxi", "8uem" ]

9

[ "PUB00015665", "PUB00015703", "PUB00019122", "PUB00032801" ]

[ "12475995", "11076018", "10430865", "11848835" ]

[ "Catalysis at a dinuclear [CuSMo(==O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution.", "The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase.", "Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcystein...

[ 2002, 2000, 1999, 1996 ]

4

[ "IPR016208" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "ecological metagenomes" ]

[ 49, 1011, 3, 29 ]

4

[]

0

true

Family

Carbon-monoxide dehydrogenase, large subunit

CO_Mo_DH_lsu

5

IPR012781

12,781

D-fructose-responsive transcription factor

Fruct_sucro_rep

Family

2,853

false

Members of this family belong the lacI helix-turn-helix family of DNA-binding transcriptional regulators. All members are from the proteobacteria. This entry includes sucrose operon repressor from Klebsiella pneumoniae and catabolite repressor/activator Cra from E. coli. Cra, also known as FruR, is a global transcripti...

[ "GO:0003677", "GO:0006355", "GO:0009750" ]

[ "DNA binding", "regulation of DNA-templated transcription", "response to fructose" ]

[ "molecular_function", "biological_process", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02417" ]

[ "fruct_sucro_rep" ]

[ 2853 ]

1

[]

0

[ "2iks", "3o74", "3o75", "7doa", "7dob", "7x7h", "8jff", "8jfv" ]

8

[ "PUB00092528", "PUB00099576", "PUB00099577" ]

[ "16115199", "33649152", "33476373" ]

[ "Systematic search for the Cra-binding promoters using genomic SELEX system.", "Cra and cAMP Receptor Protein Have Opposing Roles in the Regulation of <i>fruB</i> in Vibrio cholerae.", "Vibrio cholerae FruR facilitates binding of RNA polymerase to the fru promoter in the presence of fructose 1-phosphate." ]

[ 2005, 2021, 2021 ]

3

[]

0

null

[ "Bacteria", "Opisthokonta" ]

[ 2851, 2 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

D-fructose-responsive transcription factor

Fruct_sucro_rep

6

IPR012782

12,782

Acetolactate synthase, catabolic

Acetolactate_synth_catblc

Family

2,368

false

Acetolactate synthase is a thiamin pyrophosphate-dependent enzyme that combines two molecules of pyruvate to yield 2-acetolactate with the release of CO2. It exists in two distinct forms that have different properties, though they are clearly related [ , ]. The biosynthetic form, found in plants, fungi and bacteria, is...

[ "GO:0000287", "GO:0003984", "GO:0030976", "GO:0034077" ]

[ "magnesium ion binding", "acetolactate synthase activity", "thiamine pyrophosphate binding", "butanediol metabolic process" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "NCBIFAM" ]

[ "TIGR02418" ]

[ "acolac_catab" ]

[ 2368 ]

1

[ "EC", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]

[ "2.2.1.6", "GenProp0272", "PWY-5101", "PWY-5103", "PWY-5104", "PWY-5938", "PWY-5939", "PWY-6389", "PWY-7111" ]

[ "EC:2.2.1.6", "GP:GenProp0272", "METACYC:PWY-5101", "METACYC:PWY-5103", "METACYC:PWY-5104", "METACYC:PWY-5938", "METACYC:PWY-5939", "METACYC:PWY-6389", "METACYC:PWY-7111" ]

9

[ "1ozf", "1ozg", "1ozh", "4rji", "4rjj", "4rjk", "5d6r", "5dx6", "5wdg" ]

9

[ "PUB00015318", "PUB00028160", "PUB00028161" ]

[ "9099862", "2675968", "14557277" ]

[ "Cloning and phylogenetic analysis of the genes encoding acetohydroxyacid synthase from the archaeon Methanococcus aeolicus.", "Kinetics and mechanism of acetohydroxy acid synthase isozyme III from Escherichia coli.", "The crystal structures of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofac...

[ 1997, 1989, 2004 ]

3

[ "IPR045229" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "human gut metagenome" ]

[ 2091, 276, 1 ]

3

[]

0

true

Family

Acetolactate synthase, catabolic

Acetolactate_synth_catblc

6

IPR012783

12,783

Zinc finger, C4 DksA/TraR-type

Znf_C4_TraR

Family

3,795

false

Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt b...

[]

0

[ "NCBIFAM" ]

[ "TIGR02419" ]

[ "C4_traR_proteo" ]

[ 3795 ]

1

[]

0

[ "5w1s", "6n57", "6n58", "6psq", "6psr", "6pss", "6pst", "6psu", "6psv", "6psw" ]

10

[ "PUB00014077", "PUB00035804", "PUB00035805", "PUB00035806", "PUB00035807", "PUB00035812", "PUB00035853" ]

[ "12665246", "17210253", "15963892", "15718139", "10529348", "11179890", "15333933" ]

[ "Zinc fingers--folds for many occasions.", "Sticky fingers: zinc-fingers as protein-recognition motifs.", "Multiple modes of RNA recognition by zinc finger proteins.", "Zinc finger proteins: getting a grip on RNA.", "Zinc finger peptides for the regulation of gene expression.", "Zinc finger proteins: new ...

[ 2002, 2007, 2005, 2005, 1999, 2001, 2004 ]

7

[]

0

null

[ "Bacteria", "Thelohanellus kitauei", "Viruses", "metagenomes" ]

[ 3681, 1, 99, 14 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Zinc finger, C4 DksA/TraR-type

Znf_C4_TraR

7

IPR012784

12,784

RNA polymerase-binding transcription factor DksA

DksA_RNA_pol-bd

Family

9,586

false

DksA (DnaK suppressor A) is originally named as a multicopy suppressor of temperature sensitivity of dnaKJ mutants [ ]. DksA is a transcription factor that acts by binding directly to the RNA polymerase (RNAP). It is required for negative regulation of rRNA expression and positive regulation of several amino acid biosy...

[ "GO:0008270" ]

[ "zinc ion binding" ]

[ "molecular_function" ]

1

[ "HAMAP", "NCBIFAM" ]

[ "MF_00926", "TIGR02420" ]

[ "DksA", "dksA" ]

[ 9191, 9586 ]

2

[]

0

[ "1tjl", "4ijj", "5vsw", "5w1t", "7khe", "7khi" ]

6

[ "PUB00002103", "PUB00015435", "PUB00015436", "PUB00064839", "PUB00064840" ]

[ "2180916", "15294156", "15294157", "15948952", "16885445" ]

[ "Identification and characterization of a new Escherichia coli gene that is a dosage-dependent suppressor of a dnaK deletion mutation.", "Regulation through the secondary channel--structural framework for ppGpp-DksA synergism during transcription.", "DksA: a critical component of the transcription initiation ma...

[ 1990, 2004, 2004, 2005, 2006 ]

5

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 9435, 23, 128 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

RNA polymerase-binding transcription factor DksA

DksA_RNA_pol-bd

1

IPR012785

12,785

Protocatechuate 3,4-dioxygenase, beta subunit

Protocat_dOase_b

Family

5,610

false

Protocatechuate (3,4-dihydroxybenzene, PCA) is an aromatic compound which is a key intermediate in the degradation of the plant biopolymer lignin and other aromatic compounds. The key step of PCA degradation is the ring-cleavage performed by dioxygenases adding both atoms from molecular oxygen to specific carbon atoms ...

[ "GO:0005506", "GO:0018578", "GO:0019619" ]

[ "iron ion binding", "protocatechuate 3,4-dioxygenase activity", "3,4-dihydroxybenzoate catabolic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM", "CDD" ]

[ "TIGR02422", "cd03464" ]

[ "protocat_beta", "3_4-PCD_beta" ]

[ 5610, 1506 ]

2

[ "EC", "GP", "METACYC" ]

[ "1.13.11.3", "GenProp0273", "PWY-6041" ]

[ "EC:1.13.11.3", "GP:GenProp0273", "METACYC:PWY-6041" ]

3

[ "1eo2", "1eo9", "1eoa", "1eob", "1eoc", "1ykk", "1ykl", "1ykm", "1ykn", "1yko", "1ykp", "2bum", "2buq", "2bur", "2but", "2buu", "2buv", "2buw", "2bux", "2buy", "2buz", "2bv0", "2pcd", "3lkt", "3lmx", "3lxv", "3mfl", "3mi1", "3mi5", "3mv4", "3mv6", "3pca"...

52

[ "PUB00015256", "PUB00024603", "PUB00028144", "PUB00028145", "PUB00028146" ]

[ "10730195", "10891075", "15487948", "7990141", "9254599" ]

[ "Catechol dioxygenases.", "Structure of Acinetobacter strain ADP1 protocatechuate 3, 4-dioxygenase at 2.2 A resolution: implications for the mechanism of an intradiol dioxygenase.", "Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase1.", "Structure of protocatechuate 3,4-...

[ 1999, 2000, 2004, 1994, 1997 ]

5

[]

0

null

[ "Bacteria", "Eukaryota", "metagenomes" ]

[ 5596, 2, 12 ]

3

[]

0

true

Family

Protocatechuate 3,4-dioxygenase, beta subunit

Protocat_dOase_b

6

IPR012787

12,787

Pca transcription factor PcaQ

TF_PcaQ

Family

1,810

false

Members of this family are LysR-family transcription factors associated with operons for catabolism of protocatechuate [ ]. Members occur only in proteobacteria.

[ "GO:0003677", "GO:0019619", "GO:0045893" ]

[ "DNA binding", "3,4-dihydroxybenzoate catabolic process", "positive regulation of DNA-templated transcription" ]

[ "molecular_function", "biological_process", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02424" ]

[ "TF_pcaQ" ]

[ 1810 ]

1

[ "GP" ]

[ "GenProp0273" ]

[ "GP:GenProp0273" ]

1

[]

0

[ "PUB00033395" ]

[ "8655573" ]

[ "Conservation of PcaQ, a transcriptional activator of pca genes for catabolism of phenolic compounds, in Agrobacterium tumefaciens and Rhizobium species." ]

[ 1996 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "marine sediment metagenome" ]

[ 1807, 2, 1 ]

3

[]

0

true

Family

Pca transcription factor PcaQ

TF_PcaQ

7

IPR012788

12,788

4-carboxymuconolactone decarboxylase

Decarb_PcaC

Domain

5,374

false

Members of this entry are 4-carboxymuconolactone decarboxylases, which catalyses the third step in the catabolism of protocatechuate (and therefore the fourth step in the catabolism of para-hydroxybenzoate, of 3-hydroxybenzoate, of vanillate, etc.). Most members of this domain are encoded within protocatechuate catabol...

[]

0

[ "NCBIFAM" ]

[ "TIGR02425" ]

[ "decarb_PcaC" ]

[ 5374 ]

1

[ "GP" ]

[ "GenProp0273" ]

[ "GP:GenProp0273" ]

1

[]

0

[]

0

[ "IPR003779" ]

[]

1

0

1

[ "Bacteria", "Effrenium voratum", "metagenomes" ]

[ 5358, 1, 15 ]

3

[]

0

true

Domain

4-carboxymuconolactone decarboxylase

Decarb_PcaC

3

IPR012789

12,789

3-carboxy-cis,cis-muconate cycloisomerase-like

Protocat_PcaB-like

Family

4,207

false

Proteins in this entry are 3-carboxy-cis,cis-muconate cycloisomerases (CMLEs), which catalyse the second step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate can all be converted in one step to protocatechuate. All membe...

[ "GO:0019619" ]

[ "3,4-dihydroxybenzoate catabolic process" ]

[ "biological_process" ]

1

[ "NCBIFAM" ]

[ "TIGR02426" ]

[ "protocat_pcaB" ]

[ 4207 ]

1

[ "EC", "GP" ]

[ "5.5.1.2", "GenProp0273" ]

[ "EC:5.5.1.2", "GP:GenProp0273" ]

2

[ "1q5n", "1re5", "2fel", "2fen", "5xny", "5xnz" ]

6

[ "PUB00017793", "PUB00103676" ]

[ "15006791", "29505698" ]

[ "Diverse organization of genes of the beta-ketoadipate pathway in members of the marine Roseobacter lineage.", "Crystal structure of the nitrosuccinate lyase CreD in complex with fumarate provides insights into the catalytic mechanism for nitrous acid elimination." ]

[ 2004, 2018 ]

2

[ "IPR000362" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "marine metagenome" ]

[ 4140, 66, 1 ]

3

[]

0

true

Family

3-carboxy-cis,cis-muconate cycloisomerase-like

Protocat_PcaB-like

1

IPR012791

12,791

3-oxoacid CoA-transferase, subunit B

3-oxoacid_CoA-transf_B

Domain

23,875

false

This entry represents the B subunit of family I CoA-transferases, which contains the conserved active-site glutamate residue. This domain forms a three-layer α-β-α sandwich where the central layer is a mixed β-sheet, against which helices pack from both sides [ , ]. The active site is thought to be located at the inter...

[ "GO:0008410" ]

[ "CoA-transferase activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR02428" ]

[ "pcaJ_scoB_fam" ]

[ 23875 ]

1

[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.8.3.5", "GenProp0283", "R-CEL-77108", "R-CEL-9837999", "R-DDI-77108", "R-DDI-9837999", "R-DME-77108", "R-DME-9837999", "R-HSA-77108", "R-HSA-9837999", "R-MMU-77108", "R-MMU-9837999", "R-RNO-77108", "R-RNO-9837999", "R-SSC-77108", "R-SSC-9837999" ]

[ "EC:2.8.3.5", "GP:GenProp0283", "REACTOME:R-CEL-77108", "REACTOME:R-CEL-9837999", "REACTOME:R-DDI-77108", "REACTOME:R-DDI-9837999", "REACTOME:R-DME-77108", "REACTOME:R-DME-9837999", "REACTOME:R-HSA-77108", "REACTOME:R-HSA-9837999", "REACTOME:R-MMU-77108", "REACTOME:R-MMU-9837999", "REACTOME:...

16

[ "1m3e", "1o9l", "1ooy", "1ooz", "1ope", "2nrb", "2nrc", "3cdk", "3dlx", "3k6m", "3oxo", "3rrl", "4kgb", "5dbn", "6lp1", "8i3y", "8i40", "8k9h", "9cq2", "9cry", "9csc", "9ctd" ]

22

[ "PUB00019325", "PUB00028140", "PUB00028141", "PUB00028142" ]

[ "11749953", "10409616", "15388917", "12463743" ]

[ "A new family of CoA-transferases.", "Oxygen exchange between acetate and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentans. Implications for the mechanism of CoA-ester hydrolysis.", "Structure of the CoA transferase from pig heart to 1.7 A resolution.", "Structure...

[ 2001, 1999, 2004, 2002 ]

4

[]

0

null

[ "Bacteria", "Candidatus Lokiarchaeum ossiferum", "Eukaryota", "metagenomes" ]

[ 18522, 1, 5239, 113 ]

4

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus" ]

[ 1, 2, 3, 1, 8, 7, 2, 10 ]

8

true

Domain

3-oxoacid CoA-transferase, subunit B

3-oxoacid_CoA-transf_B

3

IPR012792

12,792

3-oxoacid CoA-transferase, subunit A

3-oxoacid_CoA-transf_A

Domain

23,199

false

This entry represents the CoA-binding A subunit of family I CoA-transferases. This domain forms a three-layer α-β-α sandwich where the central layer is an all parallel β-sheet, against which helices pack from both sides [ , ]. The active site is thought to be located at the interface of the A and B subunits and formed ...

[ "GO:0008410" ]

[ "CoA-transferase activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR02429" ]

[ "pcaI_scoA_fam" ]

[ 23199 ]

1

[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.8.3.5", "GenProp0283", "R-CEL-77108", "R-CEL-9837999", "R-DDI-77108", "R-DDI-9837999", "R-DME-77108", "R-DME-9837999", "R-HSA-77108", "R-HSA-9837999", "R-MMU-77108", "R-MMU-9837999", "R-RNO-77108", "R-RNO-9837999", "R-SSC-77108", "R-SSC-9837999" ]

[ "EC:2.8.3.5", "GP:GenProp0283", "REACTOME:R-CEL-77108", "REACTOME:R-CEL-9837999", "REACTOME:R-DDI-77108", "REACTOME:R-DDI-9837999", "REACTOME:R-DME-77108", "REACTOME:R-DME-9837999", "REACTOME:R-HSA-77108", "REACTOME:R-HSA-9837999", "REACTOME:R-MMU-77108", "REACTOME:R-MMU-9837999", "REACTOME:...

16

[ "1k6d", "1m3e", "1o9l", "1ooy", "1ooz", "1ope", "2nrb", "2nrc", "3cdk", "3dlx", "3k6m", "3oxo", "3rrl", "4kgb", "5dbn", "8k9h", "9cq2", "9cry", "9csc", "9ctd" ]

20

[ "PUB00019325", "PUB00026642", "PUB00028140", "PUB00028141" ]

[ "11749953", "12454473", "10409616", "15388917" ]

[ "A new family of CoA-transferases.", "Autotracing of Escherichia coli acetate CoA-transferase alpha-subunit structure using 3.4 A MAD and 1.9 A native data.", "Oxygen exchange between acetate and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentans. Implications for the...

[ 2001, 2002, 1999, 2004 ]

4

[]

0

null

[ "Bacteria", "Candidatus Lokiarchaeum ossiferum", "Eukaryota", "metagenomes" ]

[ 18428, 1, 4623, 147 ]

4

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus" ]

[ 1, 2, 3, 1, 6, 8, 2, 10 ]

8

true

Domain

3-oxoacid CoA-transferase, subunit A

3-oxoacid_CoA-transf_A

3

IPR012793

12,793

Beta-ketoadipyl CoA thiolase

PcaF

Family

7,328

false

This entry includes beta-ketoadipyl CoA thiolase, an enzyme that acts at the end of pathways for the degradation of protocatechuate (from benzoate and related compounds) and of phenylacetic acid. This entry also includes PaaJ, a 3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase [ ].

[ "GO:0016747", "GO:0019619" ]

[ "acyltransferase activity, transferring groups other than amino-acyl groups", "3,4-dihydroxybenzoate catabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02430" ]

[ "pcaF" ]

[ 7328 ]

1

[ "EC", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]

[ "2.3.1.174", "GenProp0283", "PWY-1361", "PWY-2361", "PWY-6185", "PWY-8347", "PWY-8354" ]

[ "EC:2.3.1.174", "GP:GenProp0283", "METACYC:PWY-1361", "METACYC:PWY-2361", "METACYC:PWY-6185", "METACYC:PWY-8347", "METACYC:PWY-8354" ]

7

[ "6pca", "6pcb", "6pcc", "6pcd", "8gqh" ]

5

[ "PUB00092532" ]

[ "17259607" ]

[ "Characterization of the last step of the aerobic phenylacetic acid degradation pathway." ]

[ 2007 ]

1

[ "IPR002155" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 7295, 8, 25 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Beta-ketoadipyl CoA thiolase

PcaF

4

IPR012794

12,794

Beta-ketoadipate transcriptional regulator, PcaR/PcaU/PobR

PcaR_PcaU

Family

5,741

false

Members of this family are IclR-type transcriptional regulators with similar DNA binding sites, able to bind at least three different metabolites related to protocatechuate metabolism. Beta-ketoadipate is the inducer for PcaR, p-hydroxybenzoate for PobR, and protocatechuate for PcaU.

[ "GO:0003677", "GO:0045893", "GO:0046278" ]

[ "DNA binding", "positive regulation of DNA-templated transcription", "3,4-dihydroxybenzoate metabolic process" ]

[ "molecular_function", "biological_process", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02431" ]

[ "pcaR_pcaU" ]

[ 5741 ]

1

[ "GP" ]

[ "GenProp0273" ]

[ "GP:GenProp0273" ]

1

[ "2g7u", "2ia2", "8eju", "8ejv", "9e6a" ]

5

[]

0

[]

0

null

[ "Bacteria", "Eukaryota", "ecological metagenomes" ]

[ 5710, 7, 24 ]

3

[]

0

true

Family

Beta-ketoadipate transcriptional regulator, PcaR/PcaU/PobR

PcaR_PcaU

5

IPR012795

12,795

tRNA(Ile)-lysidine synthase, N-terminal

tRNA_Ile_lys_synt_N

Domain

28,952

false

This entry represents the N-terminal domain of lysidine-tRNA(Ile) synthetase (TilS), which ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity ...

[ "GO:0000166", "GO:0005524", "GO:0016879", "GO:0008033" ]

[ "nucleotide binding", "ATP binding", "ligase activity, forming carbon-nitrogen bonds", "tRNA processing" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "NCBIFAM", "CDD" ]

[ "TIGR02432", "cd01992" ]

[ "lysidine_TilS_N", "TilS_N" ]

[ 28205, 28842 ]

2

[ "EC" ]

[ "6.3.4.19" ]

[ "EC:6.3.4.19" ]

1

[ "1ni5", "1wy5", "2e21", "2e89", "3a2k" ]

5

[ "PUB00014303", "PUB00016132" ]

[ "7731953", "12012333" ]

[ "A P-loop-like motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity.", "Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP, photolyase, and PP-ATPase nucleotide-binding domains: implications for protein evolution in the RNA." ]

[ 1994, 2002 ]

2

[ "IPR011063" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 25548, 2797, 24, 583 ]

4

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]

[ 7, 1, 1, 1, 1, 4 ]

6

true

Domain

tRNA(Ile)-lysidine synthase, N-terminal

tRNA_Ile_lys_synt_N

6

IPR012796

12,796

Lysidine-tRNA(Ile) synthetase, C-terminal

Lysidine-tRNA-synth_C

Domain

15,649

false

This entry represents the C-terminal domain of lysidine-tRNA(Ile) synthetase (TilS), which ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity ...

[ "GO:0000166", "GO:0005524", "GO:0016879", "GO:0008033", "GO:0005737" ]

[ "nucleotide binding", "ATP binding", "ligase activity, forming carbon-nitrogen bonds", "tRNA processing", "cytoplasm" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

5

[ "PFAM", "SMART", "NCBIFAM" ]

[ "PF11734", "SM00977", "TIGR02433" ]

[ "TilS_C", "TilS_C", "lysidine_TilS_C" ]

[ 14375, 15332, 15097 ]

3

[ "EC" ]

[ "6.3.4.19" ]

[ "EC:6.3.4.19" ]

1

[ "1ni5", "3a2k", "3hj7" ]

3

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00014303", "PUB00016132", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10673435", "2203971", "10447505", "7731953", "12012333", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 2000, 1990, 1999, 1994, 2002, 2000, 2002 ]

11

[]

0

null

[ "Bacteria", "Eukaryota", "Indivirus ILV1", "unclassified sequences" ]

[ 15351, 56, 1, 241 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Lysidine-tRNA(Ile) synthetase, C-terminal

Lysidine-tRNA-synth_C

1

IPR012797

12,797

Precorrin-6A synthase [deacetylating]

CobF

Family

4,090

false

Cobalamin (vitamin B12) is a structurally complex cofactor, consisting of a modified tetrapyrrole with a centrally chelated cobalt. Cobalamin is usually found in one of two biologically active forms: methylcobalamin and adocobalamin. Most prokaryotes, as well as animals, have cobalamin-dependent enzymes, whereas plants...

[ "GO:0043819", "GO:0009236" ]

[ "precorrin-6A synthase (deacetylating) activity", "cobalamin biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PIRSF", "NCBIFAM", "CDD" ]

[ "PIRSF036525", "TIGR02434", "cd11643" ]

[ "CobF", "CobF", "Precorrin-6A-synthase" ]

[ 3997, 4079, 4063 ]

3

[]

0

[ "2npn", "3nd1" ]

2

[ "PUB00009744", "PUB00014672", "PUB00015657", "PUB00035308", "PUB00035309", "PUB00035310", "PUB00070131" ]

[ "11215515", "11153269", "12869542", "17163662", "16042605", "12055304", "23922391" ]

[ "Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.", "Multiple biosynthetic pathways for vitamin B12: variations on a central theme.", "Comparative genomics of the vitamin B12 metabolism and regulation in prokaryotes.", "B12 trafficking in mammals: A for coenzyme escort service.", "Aerobic syn...

[ 2000, 2001, 2003, 2006, 2005, 2002, 2013 ]

7

[]

0

null

[ "Bacteria", "Rhynchospora breviuscula", "metagenomes" ]

[ 4076, 1, 13 ]

3

[]

0

true

Family

Precorrin-6A synthase [deacetylating]

CobF

9

IPR012799

12,799

Fatty oxidation complex, alpha subunit FadB

FadB

Family

4,175

false

Members of this family represent the alpha subunit of the multifunctional enzyme complex of the fatty acid degradation cycle. Activities include: enoyl-CoA hydratase ( ), dodecenoyl-CoA delta-isomerase activity ( ), 3-hydroxyacyl-CoA dehydrogenase ( ) and 3-hydroxybutyryl-CoA epimerase ( ). A representative is Escheric...

[ "GO:0003857", "GO:0004165", "GO:0004300", "GO:0008692", "GO:0009062", "GO:0036125" ]

[ "(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity", "delta(3)-delta(2)-enoyl-CoA isomerase activity", "enoyl-CoA hydratase activity", "3-hydroxybutyryl-CoA epimerase activity", "fatty acid catabolic process", "fatty acid beta-oxidation multienzyme complex" ]

[ "molecular_function", "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

6

[ "HAMAP", "NCBIFAM" ]

[ "MF_01621", "TIGR02437" ]

[ "FadB", "FadB" ]

[ 2827, 4165 ]

2

[ "EC", "EC", "EC", "EC", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", ...

[ "1.1.1.35", "4.2.1.17", "5.1.2.3", "5.3.3.8", "GenProp1486", "GenProp1562", "GenProp1717", "PWY-1361", "PWY-5136", "PWY-5137", "PWY-5138", "PWY-5177", "PWY-5789", "PWY-6435", "PWY-6443", "PWY-6446", "PWY-6458", "PWY-6583", "PWY-6837", "PWY-6863", "PWY-6883", "PWY-6944", "...

[ "EC:1.1.1.35", "EC:4.2.1.17", "EC:5.1.2.3", "EC:5.3.3.8", "GP:GenProp1486", "GP:GenProp1562", "GP:GenProp1717", "METACYC:PWY-1361", "METACYC:PWY-5136", "METACYC:PWY-5137", "METACYC:PWY-5138", "METACYC:PWY-5177", "METACYC:PWY-5789", "METACYC:PWY-6435", "METACYC:PWY-6443", "METACYC:PWY-6...

46

[ "1wdk", "1wdl", "1wdm", "2d3t", "6tnm" ]

5

[]

0

[]

0

null

[ "Bacteria", "Eukaryota", "metagenomes" ]

[ 4161, 2, 12 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Fatty oxidation complex, alpha subunit FadB

FadB

7

IPR012800

12,800

Catechol 1,2-dioxygenase, actinobacteria

Cchol_dOase_actb

Family

721

false

Members of this family are catechol 1,2-dioxygenases of the actinobacteria. They are more closely related to actinobacterial chlorocatechol 1,2-dioxygenases than to proteobacterial catechol 1,2-dioxygenases, and so form this separate entry. The member from Rhodococcus rhodochrous is described as a homodimer with bound ...

[]

0

[ "NCBIFAM" ]

[ "TIGR02438" ]

[ "catachol_actin" ]

[ 721 ]

1

[ "GP" ]

[ "GenProp0711" ]

[ "GP:GenProp0711" ]

1

[ "3hgi", "3hhx", "3hhy", "3hj8", "3hjq", "3hjs", "3hkp", "3i4v", "3i4y", "3i51" ]

10

[]

0

[]

0

null

[ "Bacteria", "metagenomes" ]

[ 718, 3 ]

2

[]

0

true

Family

Catechol 1,2-dioxygenase, actinobacteria

Cchol_dOase_actb

8

IPR012801

12,801

Catechol 1,2-dioxygenase, proteobacteria

Cchol_dOase_prob

Family

2,187

false

Members of this family known so far are catechol 1,2-dioxygenases of the proteobacteria. They are distinct from catechol 1,2-dioxygenases and chlorocatechol 1,2-dioxygenases of the actinobacteria, which are quite similar to each other and resolved by separate entries. This enzyme catalyses intradiol cleavage in which c...

[ "GO:0005506", "GO:0018576", "GO:0019614" ]

[ "iron ion binding", "catechol 1,2-dioxygenase activity", "catechol-containing compound catabolic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM", "CDD" ]

[ "TIGR02439", "cd03460" ]

[ "catechol_proteo", "1_2-CTD" ]

[ 2184, 1490 ]

2

[ "EC", "GP" ]

[ "1.13.11.1", "GenProp0711" ]

[ "EC:1.13.11.1", "GP:GenProp0711" ]

2

[ "1dlm", "1dlq", "1dlt", "1dmh", "2azq", "2xsr", "2xsu", "2xsv", "5td3", "5umh", "5vxt", "9dr5", "9dr6", "9dr8", "9dra" ]

15

[]

0

[]

0

null

[ "Eukaryota", "Pseudomonadati", "marine sediment metagenome" ]

[ 2, 2182, 3 ]

3

[]

0

true

Family

Catechol 1,2-dioxygenase, proteobacteria

Cchol_dOase_prob

1

IPR012802

12,802

Fatty oxidation complex, alpha subunit FadJ

FadJ

Family

2,505

false

Members of this family represent the alpha subunit of the multifunctional enzyme complex of the fatty acid degradation cycle, which plays a minor role in aerobic beta-oxidation of fatty acids [ ]. The FadJI complex is necessary for anaerobic growth on short-chain acids with nitrate as an electron acceptor. Activities i...

[ "GO:0003857", "GO:0004300", "GO:0008692", "GO:0051287", "GO:0006635" ]

[ "(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity", "enoyl-CoA hydratase activity", "3-hydroxybutyryl-CoA epimerase activity", "NAD binding", "fatty acid beta-oxidation" ]

[ "molecular_function", "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

5

[ "HAMAP", "NCBIFAM" ]

[ "MF_01617", "TIGR02440" ]

[ "FadJ", "FadJ" ]

[ 1802, 2504 ]

2

[ "EC", "EC", "EC", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", ...

[ "1.1.1.35", "4.2.1.17", "5.1.2.3", "GenProp1717", "PWY-1361", "PWY-5136", "PWY-5138", "PWY-5177", "PWY-5789", "PWY-6435", "PWY-6443", "PWY-6446", "PWY-6458", "PWY-6583", "PWY-6863", "PWY-6883", "PWY-6944", "PWY-6945", "PWY-6946", "PWY-7007", "PWY-7094", "PWY-7216", "PWY-7...

[ "EC:1.1.1.35", "EC:4.2.1.17", "EC:5.1.2.3", "GP:GenProp1717", "METACYC:PWY-1361", "METACYC:PWY-5136", "METACYC:PWY-5138", "METACYC:PWY-5177", "METACYC:PWY-5789", "METACYC:PWY-6435", "METACYC:PWY-6443", "METACYC:PWY-6446", "METACYC:PWY-6458", "METACYC:PWY-6583", "METACYC:PWY-6863", "MET...

35

[ "6ysv", "6ysw", "8bnr", "8bnu", "8brj" ]

5

[ "PUB00017800", "PUB00088374" ]

[ "12535077", "12270828" ]

[ "A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway.", "YfcX enables medium-chain-length poly(3-hydroxyalkanoate) formation from fatty acids in recombinant Escherichia coli fadB strains." ]

[ 2003, 2002 ]

2

[]

0

null

[ "Bacteria", "Opisthokonta", "marine sediment metagenome" ]

[ 2502, 2, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Fatty oxidation complex, alpha subunit FadJ

FadJ

9

IPR012803

12,803

Fatty acid oxidation complex, alpha subunit, mitochondrial

Fa_ox_alpha_mit

Family

2,002

false

Members of this family represent the alpha subunit of the mitochondrial multifunctional fatty acid degradation enzyme complex. Subunit activities include: enoyl-CoA hydratase ( ) and 3-hydroxyacyl-CoA dehydrogenase ( ). Some characterisation of these proteins has been done in human ( ), pig ( ) and rat ( ). The beta su...

[ "GO:0003857", "GO:0004300", "GO:0006635", "GO:0005739", "GO:0016507" ]

[ "(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity", "enoyl-CoA hydratase activity", "fatty acid beta-oxidation", "mitochondrion", "mitochondrial fatty acid beta-oxidation multienzyme complex" ]

[ "molecular_function", "molecular_function", "biological_process", "cellular_component", "cellular_component" ]

5

[ "NCBIFAM" ]

[ "TIGR02441" ]

[ "fa_ox_alpha_mit" ]

[ 2002 ]

1

[ "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METAC...

[ "1.1.1.211", "2.3.1.-", "4.2.1.17", "PWY-1361", "PWY-3602", "PWY-361", "PWY-4801", "PWY-4922", "PWY-5048", "PWY-5136", "PWY-5138", "PWY-5139", "PWY-5268", "PWY-5284", "PWY-5292", "PWY-5307", "PWY-5313", "PWY-5317", "PWY-5318", "PWY-5353", "PWY-5400", "PWY-5473", "PWY-5475...

[ "EC:1.1.1.211", "EC:2.3.1.-", "EC:4.2.1.17", "METACYC:PWY-1361", "METACYC:PWY-3602", "METACYC:PWY-361", "METACYC:PWY-4801", "METACYC:PWY-4922", "METACYC:PWY-5048", "METACYC:PWY-5136", "METACYC:PWY-5138", "METACYC:PWY-5139", "METACYC:PWY-5268", "METACYC:PWY-5284", "METACYC:PWY-5292", "M...

263

[ "5zqz", "5zrv", "6dv2" ]

3

[]

0

[]

0

null

[ "Opisthokonta" ]

[ 2002 ]

1

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 3, 2, 2, 6, 1, 2 ]

6

true

Family

Fatty acid oxidation complex, alpha subunit, mitochondrial

Fa_ox_alpha_mit

3

IPR012804

12,804

Cobaltochelatase subunit, putative

Cob_chelat_sub_put

Family

1,480

false

Cobaltochelatase is responsible for the insertion of cobalt into the corrin ring of coenzyme B12 during its biosynthesis. Cobalamin (vitamin B12) can be complexed with metal via ATP-dependent reactions (aerobic pathway) (e.g., in Pseudomonas denitrificans) or via ATP-independent reactions (anaerobic pathway) (e.g., in ...

[]

0

[ "NCBIFAM" ]

[ "TIGR02442" ]

[ "Cob-chelat-sub" ]

[ 1480 ]

1

[]

0

[]

0

[ "PUB00006361", "PUB00009744", "PUB00011189", "PUB00033893" ]

[ "8905078", "11215515", "11469861", "11607197" ]

[ "Cobalamin (coenzyme B12): synthesis and biological significance.", "Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.", "Interplay between an AAA module and an integrin I domain may regulate the function of magnesium chelatase.", "In vitro assay of the chlorophyll biosynthetic enzyme Mg-chelata...

[ 1996, 2000, 2001, 1991 ]

4

[ "IPR045006" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Geodia barretti", "ecological metagenomes" ]

[ 51, 1422, 2, 5 ]

4

[]

0

true

Family

Cobaltochelatase subunit, putative

Cob_chelat_sub_put

1

IPR012805

12,805

Acetyl-CoA C-acyltransferase FadA

FadA

Family

3,704

false

This subunit of the FadBA complex has acetyl-CoA C-acyltransferase ( ) activity, and is also known as beta-ketothiolase and fatty oxidation complex, beta subunit. This protein is almost always located adjacent to FadB ( ). The FadBA complex is the major complex active for beta-oxidation of fatty acids in Escherichia co...

[ "GO:0003988", "GO:0006631", "GO:0016042", "GO:0005737" ]

[ "acetyl-CoA C-acyltransferase activity", "fatty acid metabolic process", "lipid catabolic process", "cytoplasm" ]

[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]

4

[ "HAMAP", "NCBIFAM" ]

[ "MF_01620", "TIGR02445" ]

[ "FadA", "fadA" ]

[ 3384, 3702 ]

2

[ "EC", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METAC...

[ "2.3.1.16", "GenProp1562", "GenProp1717", "PWY-481", "PWY-5109", "PWY-5136", "PWY-6080", "PWY-6435", "PWY-6443", "PWY-6458", "PWY-6944", "PWY-6945", "PWY-6946", "PWY-6948", "PWY-7094", "PWY-7288", "PWY-7337", "PWY-7338", "PWY-7339", "PWY-7340", "PWY-735", "PWY-7606", "PWY...

[ "EC:2.3.1.16", "GP:GenProp1562", "GP:GenProp1717", "METACYC:PWY-481", "METACYC:PWY-5109", "METACYC:PWY-5136", "METACYC:PWY-6080", "METACYC:PWY-6435", "METACYC:PWY-6443", "METACYC:PWY-6458", "METACYC:PWY-6944", "METACYC:PWY-6945", "METACYC:PWY-6946", "METACYC:PWY-6948", "METACYC:PWY-7094"...

30

[ "1wdk", "1wdl", "1wdm", "2d3t", "3goa" ]

5

[]

0

[ "IPR050215" ]

[]

1

0

1

[ "Bacteria", "Tuber aestivum", "metagenomes" ]

[ 3691, 1, 12 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Acetyl-CoA C-acyltransferase FadA

FadA

1

IPR012806

12,806

Acetyl-CoA C-acyltransferase FadI

Ac-CoA_C-AcTrfase_FadI

Family

2,248

false

This subunit of the FadJI complex has acetyl-CoA C-acyltransferase ( ) activity, and is also known as beta-ketothiolase and fatty oxidation complex, beta subunit, and YfcY. This protein is almost always located adjacent to FadJ ( ). The FadJI complex is needed for anaerobic beta-oxidation of short-chain fatty acids in ...

[ "GO:0003988", "GO:0006631", "GO:0016042", "GO:0005737" ]

[ "acetyl-CoA C-acyltransferase activity", "fatty acid metabolic process", "lipid catabolic process", "cytoplasm" ]

[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]

4

[ "HAMAP", "NCBIFAM" ]

[ "MF_01618", "TIGR02446" ]

[ "FadI", "FadI" ]

[ 2066, 2243 ]

2

[ "EC", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "...

[ "2.3.1.16", "GenProp1717", "PWY-481", "PWY-5109", "PWY-5136", "PWY-6080", "PWY-6435", "PWY-6443", "PWY-6458", "PWY-6944", "PWY-6945", "PWY-6946", "PWY-6948", "PWY-7094", "PWY-7288", "PWY-7337", "PWY-7338", "PWY-7339", "PWY-7340", "PWY-735", "PWY-7606", "PWY-7654", "PWY-77...

[ "EC:2.3.1.16", "GP:GenProp1717", "METACYC:PWY-481", "METACYC:PWY-5109", "METACYC:PWY-5136", "METACYC:PWY-6080", "METACYC:PWY-6435", "METACYC:PWY-6443", "METACYC:PWY-6458", "METACYC:PWY-6944", "METACYC:PWY-6945", "METACYC:PWY-6946", "METACYC:PWY-6948", "METACYC:PWY-7094", "METACYC:PWY-728...

29

[ "8bnr", "8bnu", "8brj" ]

3

[]

0

[ "IPR002155" ]

[]

1

0

1

[ "Bacteria", "Opisthokonta", "marine sediment metagenome" ]

[ 2245, 2, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Acetyl-CoA C-acyltransferase FadI

Ac-CoA_C-AcTrfase_FadI

8

IPR012807

12,807

Anti-sigma-E factor ChrR

Anti-sigma_ChrR

Family

2,642

false

The member of this family from Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides) has been shown both to form a complex with sigma(E) [ ] and to negatively regulate tetrapyrrole biosynthesis. ChrR comprises two structural and functional domains: the N-terminal anti-sigma domain (ASD) binds a Zn(2+) ion, contacts si...

[]

0

[ "NCBIFAM", "CDD" ]

[ "TIGR02451", "cd20301" ]

[ "anti_sig_ChrR", "cupin_ChrR" ]

[ 2611, 2563 ]

2

[]

0

[ "2q1z", "2z2s" ]

2

[ "PUB00048845", "PUB00096310" ]

[ "17803943", "21295582" ]

[ "A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria.", "Features of Rhodobacter sphaeroides ChrR required for stimuli to promote the dissociation of σ(E)/ChrR complexes." ]

[ 2007, 2011 ]

2

[]

0

null

[ "Bacteria", "Opisthokonta", "unclassified sequences" ]

[ 2620, 4, 18 ]

3

[]

0

true

Family

Anti-sigma-E factor ChrR

Anti-sigma_ChrR

4

IPR012808

12,808

Conserved hypothetical protein CHP02453

CHP02453

Family

8,531

false

Members of this family are widely (though sparsely) distributed bacterial proteins, about 230 residues in length and in fungal proteins, which are around 400 residues in length. All members have a motif RxxRDxRFxxx[DN]KxxY. The function of this protein family is unknown.

[]

0

[ "PFAM", "PANTHER", "NCBIFAM" ]

[ "PF09365", "PTHR36452", "TIGR02453" ]

[ "DUF2461", "", "" ]

[ 8503, 8223, 7676 ]

3

[]

0

[]

0

[]

0

[]

[ "IPR015996" ]

0

1

0

[ "Bacteria", "Eukaryota", "metagenomes" ]

[ 6922, 1472, 137 ]

3

[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]

[ 1 ]

1

true

Family

Conserved hypothetical protein CHP02453

CHP02453

2

IPR012809

12,809

Cobalt ECF transporter T component CbiQ

ECF_CbiQ

Family

6,464

false

This family consists of CbiQ and NikQ. CbiQ is part of the ECF transporter complex CbiMNOQ involved in cobalt import [ ]. It can also transport nickel with a very low affinity [ , ]. NikQ is part of ECF transporter complex NikMNQO involved in nickel import. Similarly, it can also transport cobalt, but with a very low a...

[ "GO:0006824", "GO:0005886", "GO:0043190" ]

[ "cobalt ion transport", "plasma membrane", "ATP-binding cassette (ABC) transporter complex" ]

[ "biological_process", "cellular_component", "cellular_component" ]

3

[ "NCBIFAM" ]

[ "TIGR02454" ]

[ "ECF_T_CbiQ" ]

[ 6464 ]

1

[ "GP" ]

[ "GenProp0277" ]

[ "GP:GenProp0277" ]

1

[ "5x3x", "5x41" ]

2

[ "PUB00035607", "PUB00056802", "PUB00062129" ]

[ "16352848", "20868747", "11157936" ]

[ "Comparative and functional genomic analysis of prokaryotic nickel and cobalt uptake transporters: evidence for a novel group of ATP-binding cassette transporters.", "A bipartite S unit of an ECF-type cobalt transporter.", "Novel genes affecting urease acivity in Actinobacillus pleuropneumoniae." ]

[ 2006, 2010, 2001 ]

3

[ "IPR003339" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Cladocopium goreaui", "unclassified sequences" ]

[ 610, 5743, 1, 110 ]

4

[]

0

true

Family

Cobalt ECF transporter T component CbiQ

ECF_CbiQ

6

IPR012810

12,810

Trehalose synthase/alpha-amylase, N-terminal

TreS/a-amylase_N

Domain

6,304

false

Trehalose synthase interconverts maltose and alpha,alpha-trehalose by transglucosylation. This is one of at least three mechanisms for biosynthesis of trehalose, an important and widespread compatible solute. However, it is not driven by phosphate activation of sugars and its physiological role may tend toward trehalos...

[ "GO:0003824", "GO:0005975" ]

[ "catalytic activity", "carbohydrate metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02456" ]

[ "treS_nterm" ]

[ 6304 ]

1

[ "EC", "EC", "METACYC", "METACYC", "REACTOME" ]

[ "3.2.1.1", "5.4.99.16", "PWY-2622", "PWY-7900", "R-MTU-868688" ]

[ "EC:3.2.1.1", "EC:5.4.99.16", "METACYC:PWY-2622", "METACYC:PWY-7900", "REACTOME:R-MTU-868688" ]

5

[ "3zo9", "3zoa", "4lxf", "4tvu", "4wf7", "5gtw", "5h2t", "5jy7", "5x7u", "5ykb", "8uqv", "8uzh", "8ywd", "8z2l", "8z2q", "8z2r", "8z2s", "8z2t", "8z2u", "9ezl" ]

20

[ "PUB00016712" ]

[ "15378530" ]

[ "Isolation of mak1 from Actinoplanes missouriensis and evidence that Pep2 from Streptomyces coelicolor is a maltokinase." ]

[ 2004 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 16, 6263, 11, 14 ]

4

[]

0

true

Domain

Trehalose synthase/alpha-amylase, N-terminal

TreS/a-amylase_N

3

IPR012811

12,811

Trehalose synthase/probable maltokinase, C-terminal domain

TreS_maltokin_C_dom

Domain

2,810

false

Three pathways exist for the biosynthesis of trehalose, an osmoprotectant that in some species is also a precursor of certain cell wall glycolipids. Trehalose synthase, TreS, can interconvert maltose and trehalose, but while the equilibrium favours trehalose, physiological concentrations of trehalose may be much greate...

[]

0

[ "NCBIFAM" ]

[ "TIGR02457" ]

[ "TreS_Cterm" ]

[ 2810 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Archaea", "Bacteria", "Bdelloidea", "metagenomes" ]

[ 2, 2791, 6, 11 ]

4

[]

0

true

Domain

Trehalose synthase/probable maltokinase, C-terminal domain

TreS_maltokin_C_dom

1