interpro_id string | interpro_numeric_id int64 | name string | short_name string | entry_type string | protein_count int64 | is_llm bool | is_llm_reviewed bool | abstract string | go_ids list | go_terms list | go_categories list | go_count int64 | member_databases list | member_accessions list | member_names list | member_protein_counts list | member_count int64 | external_databases list | external_accessions list | external_xrefs list | external_xref_count int64 | pdb_ids list | structure_count int64 | publication_ids list | pubmed_ids list | publication_titles list | publication_years list | publication_count int64 | parent_ids list | child_ids list | parent_count int64 | child_count int64 | tree_depth float64 | taxonomy_names list | taxonomy_protein_counts list | taxonomy_count int64 | key_species_names list | key_species_protein_counts list | key_species_count int64 | in_entry_list bool | entry_list_type string | entry_list_name string | names_dat_name string | short_names_dat_name string | split_bucket int64 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR054818 | 54,818 | Variant surface antigen A, N-terminal region | VlpA_N | Domain | 4 | false | false | This entry represents the N-terminal region of the highly repetitive surface antigen VlpA (variant lipoprotein A) of Mycoplasma hyorhinis, a pig pathogen, and similar sequences. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045729"
] | [
"VlpA_Nterm"
] | [
4
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154762"
] | [
"34954543"
] | [
"The variable lipoprotein family participates in the interaction of Mycoplasma hyorhinis with host extracellular matrix and plasminogen."
] | [
2022
] | 1 | [] | [] | 0 | 0 | null | [
"Mesomycoplasma hyorhinis"
] | [
4
] | 1 | [] | [] | 0 | true | Domain | Variant surface antigen A, N-terminal region | Variant surface antigen A, N-terminal region | VlpA_N | 3 |
IPR054819 | 54,819 | Variant surface antigen C, N-terminal region | VlpC_N | Domain | 4 | false | false | This entry represents the N-terminal region of the highly repetitive surface antigen VlpC (variant lipoprotein C) of Mycoplasma hyorhinis, a pig pathogen. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045730"
] | [
"VlpC_Nterm"
] | [
4
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154762"
] | [
"34954543"
] | [
"The variable lipoprotein family participates in the interaction of Mycoplasma hyorhinis with host extracellular matrix and plasminogen."
] | [
2022
] | 1 | [
"IPR049890"
] | [] | 1 | 0 | 1 | [
"Mesomycoplasma hyorhinis"
] | [
4
] | 1 | [] | [] | 0 | true | Domain | Variant surface antigen C, N-terminal region | Variant surface antigen C, N-terminal region | VlpC_N | 8 |
IPR054820 | 54,820 | MPN555 chaperone-like | MPN555-like | Family | 39 | false | false | This entry includes MNP55 from Mycoplasma pneumoniae, also known as MG377 homolog. According to structural homology, this protein may be involved in protein folding as a molecular chaperone [ ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045756"
] | [
"MPN555"
] | [
39
] | 1 | [] | [] | [] | 0 | [
"1zxj"
] | 1 | [
"PUB00039059",
"PUB00154763",
"PUB00154765"
] | [
"16204885",
"22373819",
"32732422"
] | [
"Structure of the hypothetical Mycoplasma protein MPN555 suggests a chaperone function.",
"Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium.",
"In-cell architecture of an actively transcribing-translating expressome."
] | [
2005,
2012,
2020
] | 3 | [] | [] | 0 | 0 | null | [
"Mycoplasmatota"
] | [
39
] | 1 | [] | [] | 0 | true | Family | MPN555 chaperone-like | MPN555 chaperone-like | MPN555-like | 4 |
IPR054821 | 54,821 | Transcciptional activator PmfR | Trans_act_PmfR | Family | 4 | false | false | This family includes transcriptional activator PmfR, a transcriptional regulator involved in the activation of the purU-mabO-folD-nepA-nepB and mao-ORF55-nbr operons implicated in the nicotine catabolic pathway. The sequence GTTT-14 bp-AAAC seems to be the core binding site of the regulator upstream of the -35 promoter... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045769"
] | [
"TransActPmfR"
] | [
4
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154649",
"PUB00154650",
"PUB00154866"
] | [
"17293530",
"15838033",
"17464069"
] | [
"An NAD(P)H-nicotine blue oxidoreductase is part of the nicotine regulon and may protect Arthrobacter nicotinovorans from oxidative stress during nicotine catabolism.",
"Characterization of PmfR, the transcriptional activator of the pAO1-borne purU-mabO-folD operon of Arthrobacter nicotinovorans.",
"A two-compo... | [
2007,
2005,
2007
] | 3 | [] | [] | 0 | 0 | null | [
"Micrococcaceae"
] | [
4
] | 1 | [] | [] | 0 | true | Family | Transcciptional activator PmfR | Transcciptional activator PmfR | Trans_act_PmfR | 7 |
IPR054822 | 54,822 | Sulfate reduction electron transfer complex DsrMKJOP subunit DsrO-like | DsrO-like | Family | 1,933 | false | false | This family represents a group of prokaryotic members of the DsrMKJOP dissimilatory sulfate reduction complex that contain an iron-sulphur binding domain ( ), including subunit DsrO from Desulfovibrio desulfuricans ( ), a periplasmic FeS protein. This membrane-bound redox complex is involved in sulfate reduction in sul... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045797"
] | [
"DsrO"
] | [
1933
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00088715",
"PUB00105534",
"PUB00109129",
"PUB00154667",
"PUB00154668"
] | [
"15009189",
"16388601",
"11952791",
"21747791",
"38285932"
] | [
"Two distinct heterodisulfide reductase-like enzymes in the sulfate-reducing archaeon Archaeoglobus profundus.",
"Characterization of the Desulfovibrio desulfuricans ATCC 27774 DsrMKJOP complex--a membrane-bound redox complex involved in the sulfate respiratory pathway.",
"Purification and characterization of a... | [
2004,
2006,
2002,
2011,
2024
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Ecdysozoa",
"unclassified sequences"
] | [
78,
1787,
2,
66
] | 4 | [] | [] | 0 | true | Family | Sulfate reduction electron transfer complex DsrMKJOP subunit DsrO-like | Sulfate reduction electron transfer complex DsrMKJOP subunit DsrO-like | DsrO-like | 9 |
IPR054823 | 54,823 | Sulfate reduction electron transfer complex DsrMKJOP subunit DsrP-like | DsrP-like | Family | 520 | false | false | This family represents a group of prokaryotic proteins, including the DsrP subunit of the DsrMKJOP dissimilatory sulfate reduction complex from Desulfovibrio desulfuricans ( ), a highly hydrophobic protein [ ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045798"
] | [
"DsrP"
] | [
520
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00105534",
"PUB00154668"
] | [
"16388601",
"38285932"
] | [
"Characterization of the Desulfovibrio desulfuricans ATCC 27774 DsrMKJOP complex--a membrane-bound redox complex involved in the sulfate respiratory pathway.",
"DsrMKJOP is the terminal reductase complex in anaerobic sulfate respiration."
] | [
2006,
2024
] | 2 | [
"IPR005614"
] | [] | 1 | 0 | 1 | [
"Archaeoglobus sulfaticallidus PM70-1",
"Bacteria",
"ecological metagenomes"
] | [
1,
502,
17
] | 3 | [] | [] | 0 | true | Family | Sulfate reduction electron transfer complex DsrMKJOP subunit DsrP-like | Sulfate reduction electron transfer complex DsrMKJOP subunit DsrP-like | DsrP-like | 8 |
IPR054824 | 54,824 | Gas vesicle protein GvpO-like, N-terminal domain | GvpO-like_N | Domain | 97 | false | false | This entry represents the N-terminal domain of gas vesicle protein GvpO sequences from halobacteria. It is around 35-amino acids long and has three invariant Cys residues. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045806"
] | [
"GvpO_arch_Nterm"
] | [
97
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR043914"
] | [] | 1 | 0 | 1 | [
"Halobacteriales"
] | [
97
] | 1 | [] | [] | 0 | true | Domain | Gas vesicle protein GvpO-like, N-terminal domain | Gas vesicle protein GvpO-like, N-terminal domain | GvpO-like_N | 9 |
IPR054825 | 54,825 | Surface lipoprotein P68-like | P68-like | Family | 376 | false | false | This entry represents a group of proteins from Mycoplasmatota, including P68 from Mesomycoplasma hyopneumoniae ( , Mhp390, a membrane-associated lipoprotein). P68 plays an important role in binding to swine tracheal cilia. It contributes to the production of proinflammatory cytokines and could induce significant apopto... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045826"
] | [
"lipo_P68"
] | [
376
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154764",
"PUB00154802",
"PUB00154804"
] | [
"23297388",
"35873172",
"30385395"
] | [
"Implication of glycerol and phospholipid transporters in Mycoplasma pneumoniae growth and virulence.",
"<i>Mycoplasma hyopneumoniae</i> Infection Activates the NOD1 Signaling Pathway to Modulate Inflammation.",
"Surface proteins mhp390 (P68) contributes to cilium adherence and mediates inflammation and apoptos... | [
2013,
2022,
2019
] | 3 | [] | [] | 0 | 0 | null | [
"Mycoplasmatota",
"Vespula germanica"
] | [
375,
1
] | 2 | [] | [] | 0 | true | Family | Surface lipoprotein P68-like | Surface lipoprotein P68-like | P68-like | 4 |
IPR054826 | 54,826 | Thiol peroxidase Prx-SUH | Perox_SUH | Family | 62 | false | false | This entry represents a group of thiol peroxidases Prx from Epsilonproteobacteria in which the last six amino acids are typically CCGXCH or CCGSUH, where U is selenocysteine. The function if this C-terminal hexapeptide region is not yet well understood [ ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045827"
] | [
"perox_SUH"
] | [
62
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00081206"
] | [
"26342139"
] | [
"Evolution of the Selenoproteome in Helicobacter pylori and Epsilonproteobacteria."
] | [
2015
] | 1 | [
"IPR002065"
] | [] | 1 | 0 | 1 | [
"Campylobacterales",
"bioreactor metagenome"
] | [
61,
1
] | 2 | [] | [] | 0 | true | Family | Thiol peroxidase Prx-SUH | Thiol peroxidase Prx-SUH | Perox_SUH | 7 |
IPR054827 | 54,827 | TCP-1 chaperonin-like | TCP-1-like | Family | 30,241 | true | true | This entry represents members of the TCP-1 chaperonin family, which includes Chaperonin and T-complex protein 1 (TCP1) subunits. These proteins function as molecular chaperones, assisting in the folding of proteins upon ATP hydrolysis. The Chaperonin subunits, found in archaea, bind unfolded polypeptides and have weak ... | [] | [] | [] | 0 | [
"NCBIFAM",
"NCBIFAM"
] | [
"NF041082",
"NF041083"
] | [
"thermosome_alpha",
"TCP-1_chaperonin"
] | [
23064,
30221
] | 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-DME-390471",
"R-DME-6814122",
"R-GGA-390471",
"R-GGA-6814122",
... | [
"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... | 44 | [
"1a6d",
"1a6e",
"1q2v",
"1q3q",
"1q3r",
"1q3s",
"3aq1",
"3iyg",
"3izh",
"3izi",
"3izj",
"3izm",
"3j1b",
"3j1c",
"3j1e",
"3j1f",
"3j3x",
"3kfb",
"3ko1",
"3ktt",
"3los",
"3ruq",
"3rus",
"3ruv",
"3ruw",
"4a0o",
"4a0v",
"4a0w",
"4a13",
"4b2t",
"4v81",
"4v8r"... | 124 | [
"PUB00106164",
"PUB00106165",
"PUB00106166"
] | [
"10508614",
"7867646",
"9023959"
] | [
"Recurrent paralogy in the evolution of archaeal chaperonins.",
"The thermosome of Thermoplasma acidophilum and its relationship to the eukaryotic chaperonin TRiC.",
"In vitro stabilization and in vivo solubilization of foreign proteins by the beta subunit of a chaperonin from the hyperthermophilic archaeon Pyr... | [
1999,
1995,
1997
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured virus"
] | [
2367,
3,
27803,
64,
4
] | 5 | [
"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... | [
22,
6,
7,
11,
30,
30,
7,
20,
22,
5,
7,
46
] | 12 | true | Family | TCP-1 chaperonin-like | TCP-1 chaperonin-like | TCP-1-like | 2 |
IPR054828 | 54,828 | Vitamin B12-binding protein | Vit_B12_bind_prot | Family | 14,633 | true | false | This entry represents the Vitamin B12-binding protein, also known as the Cobalamin-binding protein or BtuF family protein. These proteins are part of the ABC transporter complex BtuCDF involved in the import of vitamin B12 (cobalamin). They bind vitamin B12 and deliver it to the periplasmic surface of BtuC. The functio... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF038402"
] | [
"Vit_B12_bind_prot"
] | [
14633
] | 1 | [] | [] | [] | 0 | [
"1n2z",
"1n4a",
"1n4d",
"2qi9",
"4dbl",
"4fi3",
"4m7o",
"5b58",
"5giz",
"5m29",
"5m2q",
"5m34",
"5m3b",
"5ovw",
"5y89",
"5y8a",
"5ysc"
] | 17 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
612,
13783,
10,
228
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Vitamin B12-binding protein | Vitamin B12-binding protein | Vit_B12_bind_prot | 4 |
IPR054829 | 54,829 | Ferredoxin-1 | FdxA | Family | 7,580 | true | false | Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. These proteins are found in various bacterial species including Pseudomonas aeruginosa, Pseudomonas putida, Rickettsia prowazekii, Rickettsia bellii, Rhodobacter capsulatus, Azotobacter vinelandii, Stutzerimonas stutz... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045490"
] | [
"FdxA"
] | [
7580
] | 1 | [] | [] | [] | 0 | [
"1a6l",
"1axq",
"1b0t",
"1b0v",
"1d3w",
"1f5b",
"1f5c",
"1fd2",
"1fda",
"1fdb",
"1fdd",
"1fer",
"1ff2",
"1frh",
"1fri",
"1frj",
"1frk",
"1frl",
"1frm",
"1frx",
"1ftc",
"1g3o",
"1g6b",
"1gao",
"1pc4",
"1pc5",
"2fd2",
"5fd1",
"6fd1",
"6fdr",
"7fd1",
"7fdr"... | 32 | [
"PUB00021173",
"PUB00153553",
"PUB00153554"
] | [
"10593945",
"2388848",
"7751303"
] | [
"Alteration of the reduction potential of the [4Fe-4S](2+/+) cluster of Azotobacter vinelandii ferredoxin I.",
"Nucleotide sequence of fdxA encoding a 7Fe ferredoxin of Rhodobacter capsulatus.",
"Synthesis of the Caulobacter ferredoxin protein, FdxA, is cell cycle controlled."
] | [
1999,
1990,
1995
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"unclassified sequences",
"uncultured Caudovirales phage"
] | [
7463,
6,
110,
1
] | 4 | [] | [] | 0 | true | Family | Ferredoxin-1 | Ferredoxin-1 | FdxA | 6 |
IPR054830 | 54,830 | Ferredoxin | FdxA_Actino | Family | 6,092 | true | false | Ferredoxins are iron-sulfur proteins that play a crucial role in electron transfer across a variety of metabolic reactions. These proteins are characterized by their ability to transfer electrons, which is essential for numerous biochemical processes. The ferredoxins described here are found in various Actinobacteria, ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045480"
] | [
"FdxA_Actino"
] | [
6092
] | 1 | [
"REACTOME"
] | [
"R-MTU-936721"
] | [
"REACTOME:R-MTU-936721"
] | 1 | [
"2v2k"
] | 1 | [
"PUB00153550"
] | [
"2055472"
] | [
"Cloning and characterization of the Saccharopolyspora erythraea fdxA gene encoding ferredoxin."
] | [
1991
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
5970,
2,
120
] | 3 | [] | [] | 0 | true | Family | Ferredoxin | Ferredoxin | FdxA_Actino | 6 |
IPR054831 | 54,831 | UPF0122 family protein | UPF0122_fam_protein | Family | 4,538 | true | false | The UPF0122 family proteins are a group of conserved proteins that are believed to be involved in the signal recognition particle (SRP) pathway. This inference is based on the conservation of their genetic proximity to ftsY/ffh genes, which are key components of the SRP pathway. The exact function of these proteins is ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045758"
] | [
"UPF0122_fam_protein"
] | [
4538
] | 1 | [] | [] | [] | 0 | [
"1s7o",
"1xsv"
] | 2 | [
"PUB00154737",
"PUB00154738"
] | [
"31445891",
"24659773"
] | [
"Determination of the Gene Regulatory Network of a Genome-Reduced Bacterium Highlights Alternative Regulation Independent of Transcription Factors.",
"YlxM is a newly identified accessory protein that influences the function of signal recognition particle pathway components in Streptococcus mutans."
] | [
2019,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"Siphoviridae sp. ctDiR9",
"metagenomes"
] | [
4505,
2,
1,
30
] | 4 | [] | [] | 0 | true | Family | UPF0122 family protein | UPF0122 family protein | UPF0122_fam_protein | 7 |
IPR054832 | 54,832 | Transposase IS91-like | Transpos_IS91 | Family | 4,468 | true | true | The IS91 family transposase is involved in the transposition of insertion sequence elements [ ]. Members of this family are found in various bacterial species, including Pseudomonas savastanoi pv. phaseolicola and Sinorhizobium americanum. These transposases belong to the transposase 32 family and play a crucial role i... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF033538"
] | [
"transpos_IS91"
] | [
4468
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00162882"
] | [
"20625149"
] | [
"Structural characterization of ISCR8, ISCR22, and ISCR23, subgroups of IS91-like insertion elements."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanomicrobia",
"unclassified sequences"
] | [
4322,
15,
20,
111
] | 4 | [] | [] | 0 | true | Family | Transposase IS91-like | Transposase IS91-like | Transpos_IS91 | 7 |
IPR054833 | 54,833 | Acetamidase/formamidase family | FormamaseFmdA | Family | 4,141 | true | false | This entry represents formamidases, which are enzymes that hydrolyze formamide to produce ammonia, which can be used as a nitrogen source for growth. These enzymes may also act on other amides such as acetamide, propanamide, and butanamide, albeit more slowly. Members of this family include the putative formamidase C86... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045496"
] | [
"FormamaseFmdA"
] | [
4141
] | 1 | [] | [] | [] | 0 | [
"2wkn"
] | 1 | [
"PUB00020777"
] | [
"8841393"
] | [
"Molecular characterisation of formamidase from Methylophilus methylotrophus."
] | [
1996
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Catovirus CTV1",
"Eukaryota",
"Halobacteriales",
"metagenomes"
] | [
2179,
1,
1864,
82,
15
] | 5 | [
"Arabidopsis thaliana",
"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"
] | [
16,
2,
3,
1,
6
] | 5 | true | Family | Acetamidase/formamidase family | Acetamidase/formamidase family | FormamaseFmdA | 8 |
IPR054834 | 54,834 | Small archaeal modifier protein 1/3 | SAMP1_3 | Family | 1,887 | true | false | Small archaeal modifier proteins 1 and 3 (SAMP1 and SAMP3) from Haloferax volcanii function as protein modifiers covalently attached to lysine residues of substrate proteins. This modification process, termed sampylation, involves the formation of an isopeptide bond between the C-terminal glycine carboxylate of SAMP pr... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041918"
] | [
"SAMP1_3"
] | [
1887
] | 1 | [] | [] | [] | 0 | [
"1v8c",
"1vjk",
"2g1e",
"2k22",
"2l52",
"2l83",
"2m19",
"3po0",
"4hro"
] | 9 | [
"PUB00058155",
"PUB00138936"
] | [
"20054389",
"21216237"
] | [
"Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax volcanii.",
"Crystal structure of ubiquitin-like small archaeal modifier protein 1 (SAMP1) from Haloferax volcanii."
] | [
2010,
2011
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
964,
856,
8,
59
] | 4 | [] | [] | 0 | true | Family | Small archaeal modifier protein 1/3 | Small archaeal modifier protein 1/3 | SAMP1_3 | 8 |
IPR054835 | 54,835 | ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase | G3PDH_Arsen | Family | 2,534 | true | false | This entry represents ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase (GAPDH 3), an enzyme that catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The reaction involves the formation of a hemiacetal intermediate between G3P and a... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF033735"
] | [
"G3PDH_Arsen"
] | [
2534
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00105284"
] | [
"26991003"
] | [
"Synergistic interaction of glyceraldehydes-3-phosphate dehydrogenase and ArsJ, a novel organoarsenical efflux permease, confers arsenate resistance."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
2422,
75,
37
] | 3 | [] | [] | 0 | true | Family | ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase | ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase | G3PDH_Arsen | 3 |
IPR054836 | 54,836 | Transposase for transposon Tn5 | Tn5_transposase | Family | 1,851 | true | false | This entry represents the transposase for transposon Tn5, a protein that mediates the transposition of the Tn5 transposon in Escherichia coli. The transposase operates via a 'cut and paste' mechanism. Initially, the monomeric transposase binds to the 19 bp inverted DNA repeats flanking the transposon. Dimerization of t... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF033590"
] | [
"Tn5_transposase"
] | [
1851
] | 1 | [] | [] | [] | 0 | [
"1b7e",
"1mm8",
"1muh",
"1mus",
"3ecp",
"4dm0"
] | 6 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"ecological metagenomes",
"plasmids"
] | [
1768,
13,
35,
33,
2
] | 5 | [] | [] | 0 | true | Family | Transposase for transposon Tn5 | Transposase for transposon Tn5 | Tn5_transposase | 7 |
IPR054837 | 54,837 | Galactofuranose ABC transporter, galactofuranose-binding protein YtfQ | YtfQ_transport | Family | 1,399 | true | false | This entry represents the galactofuranose-binding protein YtfQ, which is part of the ABC transporter complex YtfQRT-YjfF involved in galactofuranose transport in Escherichia coli (strain K12). YtfQ binds to both alpha- and beta-galactofuranose. It belongs to the bacterial solute-binding protein 2 family. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041827"
] | [
"YtfQ_transport"
] | [
1399
] | 1 | [] | [] | [] | 0 | [
"2vk2"
] | 1 | [
"PUB00152883"
] | [
"30698741"
] | [
"The y-ome defines the 35% of Escherichia coli genes that lack experimental evidence of function."
] | [
2019
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Trichuris trichiura",
"human gut metagenome"
] | [
1397,
1,
1
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Galactofuranose ABC transporter, galactofuranose-binding protein YtfQ | Galactofuranose ABC transporter, galactofuranose-binding protein YtfQ | YtfQ_transport | 8 |
IPR054838 | 54,838 | Adenylyltransferase SelO | adnlytase_SelO | Family | 1,214 | true | false | Protein adenylyltransferase SelO is an enzyme that catalyzes the transfer of adenosine 5'-monophosphate (AMP) to serine, threonine, or tyrosine residues of target proteins, a process known as AMPylation. This enzyme belongs to the SELO family and is found in various bacterial species, including Escherichia coli and Sal... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040880"
] | [
"adnlytase_SelO"
] | [
1214
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.7.7.-",
"2.7.7.108",
"PWY-6322",
"PWY-6626",
"PWY-6749",
"PWY-6955",
"PWY-6998",
"PWY-7127",
"PWY-7419",
"PWY-7529",
"PWY-7706",
"PWY-7719",
"PWY-7735",
"PWY-7737",
"PWY-7769",
"PWY-7888",
"PWY-7904",
"PWY-8117",
"PWY-8179"
] | [
"EC:2.7.7.-",
"EC:2.7.7.108",
"METACYC:PWY-6322",
"METACYC:PWY-6626",
"METACYC:PWY-6749",
"METACYC:PWY-6955",
"METACYC:PWY-6998",
"METACYC:PWY-7127",
"METACYC:PWY-7419",
"METACYC:PWY-7529",
"METACYC:PWY-7706",
"METACYC:PWY-7719",
"METACYC:PWY-7735",
"METACYC:PWY-7737",
"METACYC:PWY-7769"... | 19 | [
"6iii",
"6iny",
"6k20",
"6lna"
] | 4 | [
"PUB00092455"
] | [
"30270044"
] | [
"Protein AMPylation by an Evolutionarily Conserved Pseudokinase."
] | [
2018
] | 1 | [] | [] | 0 | 0 | null | [
"Gammaproteobacteria"
] | [
1214
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Adenylyltransferase SelO | Adenylyltransferase SelO | adnlytase_SelO | 8 |
IPR054839 | 54,839 | Photosynthetic complex putative assembly protein PuhB | puhB_PGC | Family | 639 | true | false | This entry represents the photosynthetic complex putative assembly protein PuhB. The protein is involved in the assembly of photosynthetic complexes, which are crucial for the photosynthetic process in organisms such as Rhodobacter capsulatus. The exact function of PuhB remains to be fully characterized, but it is beli... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040894"
] | [
"puhB_PGC"
] | [
639
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00106049"
] | [
"29795276"
] | [
"Horizontal operon transfer, plasmids, and the evolution of photosynthesis in Rhodobacteraceae."
] | [
2018
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadati",
"Symbiodinium necroappetens",
"freshwater sediment metagenome"
] | [
637,
1,
1
] | 3 | [] | [] | 0 | true | Family | Photosynthetic complex putative assembly protein PuhB | Photosynthetic complex putative assembly protein PuhB | puhB_PGC | 1 |
IPR054840 | 54,840 | 1-hydroxy-gamma-carotene desaturase | hydcarot_desat_CrtD | Family | 619 | true | false | This entry represents 1-hydroxycarotenoid 3,4-desaturase, an enzyme that catalyzes the introduction of a C-3,4 double bond into 1'-hydroxy-gamma-carotene and rhodopin (1-hydroxylycopene) to yield 1'-hydroxytorulene and (3E)-3,4-didehydrorhodopin, respectively. It can also act on 1-hydroxy-all-trans-1,2-dihydro-neurospo... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF042421"
] | [
"hydcarot_desat_CrtD"
] | [
619
] | 1 | [] | [] | [] | 0 | [
"4rep"
] | 1 | [
"PUB00153527",
"PUB00153528"
] | [
"26138397",
"15251462"
] | [
"Crystal structure of 1'-OH-carotenoid 3,4-desaturase from Nonlabens dokdonensis DSW-6.",
"1-Hydroxy monocyclic carotenoid 3,4-dehydrogenase from a marine bacterium that produces myxol."
] | [
2015,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Pseudomonadati",
"ecological metagenomes"
] | [
616,
3
] | 2 | [] | [] | 0 | true | Family | 1-hydroxy-gamma-carotene desaturase | 1-hydroxy-gamma-carotene desaturase | hydcarot_desat_CrtD | 1 |
IPR054841 | 54,841 | 1-hydroxycarotenoid 3,4-desaturase | carotdesatCrtD | Family | 636 | true | false | This entry represents the 1-hydroxycarotenoid 3,4-desaturase (CrtD), which belongs to the carotenoid/retinoid oxidoreductase family. The enzyme catalyzes the introduction of C-3,4 double bonds into 1-hydroxyneurosporene (1-HO-Neu) to yield demethylspheroidene (DMS). The preferred substrates for this enzyme include 1-hy... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045637"
] | [
"carotdesatCrtD"
] | [
636
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"1.3.99.27",
"PWY-6581",
"PWY-7947"
] | [
"EC:1.3.99.27",
"METACYC:PWY-6581",
"METACYC:PWY-7947"
] | 3 | [] | 0 | [
"PUB00154721",
"PUB00154722"
] | [
"10880364",
"9393712"
] | [
"Substrate specificity of the expressed carotenoid 3,4-desaturase from Rubrivivax gelatinosus reveals the detailed reaction sequence to spheroidene and spirilloxanthin.",
"Purification and biochemical characterization of a hydroxyneurosporene desaturase involved in the biosynthetic pathway of the carotenoid spher... | [
2000,
1997
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"freshwater sediment metagenome"
] | [
635,
1
] | 2 | [] | [] | 0 | true | Family | 1-hydroxycarotenoid 3,4-desaturase | 1-hydroxycarotenoid 3,4-desaturase | carotdesatCrtD | 9 |
IPR054842 | 54,842 | Probable dimethyl sulfoxide reductase chain YnfF | DMSO_reductase_YnfF | Family | 935 | true | false | The protein YnfF from Escherichia coli (strain K12) is a probable dimethyl sulfoxide (DMSO) reductase chain. It functions as a terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. YnfF is also annotated as a selenate/tellurate reductase subunit. This protein belongs to the prokaryotic ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041884"
] | [
"DMSO_reductase_YnfF"
] | [
935
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00034653",
"PUB00152968"
] | [
"14522592",
"33136147"
] | [
"The Escherichia coli ynfEFGHI operon encodes polypeptides which are paralogues of dimethyl sulfoxide reductase (DmsABC).",
"Genetic analysis of tellurate reduction reveals the selenate/tellurate reductase genes ynfEF and the transcriptional regulation of moeA by NsrR in Escherichia coli."
] | [
2003,
2021
] | 2 | [] | [] | 0 | 0 | null | [
"Gammaproteobacteria"
] | [
935
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Probable dimethyl sulfoxide reductase chain YnfF | Probable dimethyl sulfoxide reductase chain YnfF | DMSO_reductase_YnfF | 4 |
IPR054843 | 54,843 | Slam-dependent hemophilin, C-terminal domain | Slam_hemophilin_C | Domain | 820 | false | false | This entry represents the C-terminal domain of Slam-dependent hemophilins found in Acinetobacter baumannii, Haemophilus influenzae and related Gram-negative bacteria, which consists of a β-barrel. Hemophilins are part of a high affinity heme acquisition system [ , , ]. It functions as a hemophore that acquires heme fro... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041636"
] | [
"slam_lipo"
] | [
820
] | 1 | [] | [] | [] | 0 | [
"5ee2",
"6om5",
"7re4",
"7rea",
"7red",
"8glo",
"8gm3",
"8gmm"
] | 8 | [
"PUB00095100",
"PUB00154014",
"PUB00155018"
] | [
"28620585",
"34725337",
"38814789"
] | [
"Identification of a Large Family of Slam-Dependent Surface Lipoproteins in Gram-Negative Bacteria.",
"A Slam-dependent hemophore contributes to heme acquisition in the bacterial pathogen Acinetobacter baumannii.",
"Prevalence of Slam-dependent hemophilins in Gram-negative bacteria."
] | [
2017,
2021,
2024
] | 3 | [] | [
"IPR054536"
] | 0 | 1 | 0 | [
"Bacteria",
"Opisthokonta",
"marine sediment metagenome"
] | [
815,
3,
2
] | 3 | [] | [] | 0 | true | Domain | Slam-dependent hemophilin, C-terminal domain | Slam-dependent hemophilin, C-terminal domain | Slam_hemophilin_C | 6 |
IPR054844 | 54,844 | HTH-type transcriptional regulator BhcR | TransRegBhcR | Family | 537 | true | false | HTH-type transcriptional regulator BhcR is a protein found in Paracoccus denitrificans (strain Pd 1222). It functions as a transcriptional regulator of the bhc gene cluster, which is involved in glycolate and glyoxylate assimilation via the beta-hydroxyaspartate cycle (BHAC). The interaction of BhcR with the promoter r... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045644"
] | [
"TransRegBhcR"
] | [
537
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154623"
] | [
"31723261"
] | [
"Marine Proteobacteria metabolize glycolate via the β-hydroxyaspartate cycle."
] | [
2019
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadota",
"ecological metagenomes"
] | [
532,
5
] | 2 | [] | [] | 0 | true | Family | HTH-type transcriptional regulator BhcR | HTH-type transcriptional regulator BhcR | TransRegBhcR | 3 |
IPR054845 | 54,845 | CsxC family protein | Exosporium_prot_C | Family | 857 | true | false | Exosporium protein C (CsxC) is a protein found in Clostridium sporogenes (strain ATCC 15579). It is part of the CsxC family, which is characterized by its role in the exosporium, a protective layer surrounding the spore. The CsxC family proteins are involved in the formation and maintenance of this layer, which is cruc... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045794"
] | [
"Exosporium_prot_C"
] | [
857
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacillota",
"bioreactor metagenome"
] | [
854,
3
] | 2 | [] | [] | 0 | true | Family | CsxC family protein | CsxC family protein | Exosporium_prot_C | 2 |
IPR054847 | 54,847 | Reactive chlorine resistance oxidoreductase RclA | chlor_oxi_RclA | Family | 793 | true | false | Reactive chlorine resistance oxidoreductase RclA is a probable pyridine nucleotide-disulfide oxidoreductase found in Escherichia coli (strain K12). It belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family and is likely involved in reactive chlorine species (RCS) stress resistance. This enzyme plays... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040477"
] | [
"chlor_oxi_RclA"
] | [
793
] | 1 | [] | [] | [] | 0 | [
"6kgy",
"6kod",
"6kyy"
] | 3 | [
"PUB00085116"
] | [
"24078635"
] | [
"The RclR protein is a reactive chlorine-specific transcription factor in Escherichia coli."
] | [
2013
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
793
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Reactive chlorine resistance oxidoreductase RclA | Reactive chlorine resistance oxidoreductase RclA | chlor_oxi_RclA | 3 |
IPR054848 | 54,848 | Geranylgeranyl pyrophosphate synthase CRTE-like | GGPPSyn_CRT-like | Family | 416 | false | false | Geranylgeranyl diphosphate synthase CRTE (GGPPS) is an enzyme that catalyses the condensation of farnesyl diphosphate (FPP) and isopentenyl diphosphate (IPP) to yield geranylgeranyl diphosphate (GGPP) [ ]. This reaction is crucial for the biosynthesis of carotenoids and diterpenes. The enzyme belongs to the FPP/GGPP sy... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045685"
] | [
"GGPPSynCrtE"
] | [
416
] | 1 | [] | [] | [] | 0 | [
"6sxl",
"7mxz",
"7my0",
"7my1",
"7my6",
"7my7"
] | 6 | [
"PUB00100305",
"PUB00154610",
"PUB00154611"
] | [
"24180436",
"32523588",
"10412909"
] | [
"Biosynthesis of ambiguine indole alkaloids in cyanobacterium Fischerella ambigua.",
"Crystal Structure of Geranylgeranyl Pyrophosphate Synthase (CrtE) Involved in Cyanobacterial Terpenoid Biosynthesis.",
"A thermophilic cyanobacterium Synechococcus elongatus has three different Class I prenyltransferase genes.... | [
2014,
2020,
1999
] | 3 | [
"IPR053378"
] | [] | 1 | 0 | 1 | [
"Cyanobacteriota",
"Eukaryota"
] | [
364,
52
] | 2 | [] | [] | 0 | true | Family | Geranylgeranyl pyrophosphate synthase CRTE-like | Geranylgeranyl pyrophosphate synthase CRTE-like | GGPPSyn_CRT-like | 5 |
IPR054849 | 54,849 | UPF0336 | UPF0336_fam | Family | 659 | true | true | This entry represents a family of proteins known as UPF0336. Members of this family are found in various Mycobacterium species, including Mycobacterium bovis, Mycobacterium leprae, Mycobacterium tuberculosis, and Mycolicibacterium paratuberculosis. The exact function of UPF0336 family proteins is currently unknown, but... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040624"
] | [
"UPF0336_fam"
] | [
659
] | 1 | [] | [] | [] | 0 | [
"4rlj",
"4rlt",
"4rlu",
"4rlw",
"4rv2",
"7svt",
"8y21"
] | 7 | [
"PUB00104910",
"PUB00105858"
] | [
"17804795",
"26104214"
] | [
"The missing piece of the type II fatty acid synthase system from Mycobacterium tuberculosis.",
"The Molecular Genetics of Mycolic Acid Biosynthesis."
] | [
2007,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Mycobacteriales",
"freshwater metagenome"
] | [
658,
1
] | 2 | [] | [] | 0 | true | Family | UPF0336 | UPF0336 | UPF0336_fam | 5 |
IPR054850 | 54,850 | Xylan 1,4-beta-xylosidase | Xylosidase_Xyl3A | Family | 577 | true | false | Xylan 1,4-beta-xylosidase (Xyl3A) from Xylanibacter ruminicola is a member of the glycosyl hydrolase 3 family. This enzyme is involved in the degradation of plant cell wall polysaccharides. It exhibits beta-xylosidase activity by hydrolyzing glycosidic linkages of beta-1,4-xylo-oligosaccharides of various lengths (X2 t... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041776"
] | [
"Xylosidase_Xyl3A"
] | [
577
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00097679"
] | [
"19304844"
] | [
"Biochemical analysis of a beta-D-xylosidase and a bifunctional xylanase-ferulic acid esterase from a xylanolytic gene cluster in Prevotella ruminicola 23."
] | [
2009
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteroidota/Chlorobiota group",
"metagenomes"
] | [
574,
3
] | 2 | [] | [] | 0 | true | Family | Xylan 1,4-beta-xylosidase | Xylan 1,4-beta-xylosidase | Xylosidase_Xyl3A | 7 |
IPR054851 | 54,851 | Prenyl lipid carboxyl methyltransferase | Isoprenylcys_mtase | Family | 439 | true | false | This entry represents protein-S-isoprenylcysteine O-methyltransferase, an enzyme that catalyzes the methylation of isoprenylated cysteine residues in proteins. The enzyme exhibits activity towards prenyl lipids, including N-acetyl-S-farnesyl-L-cysteine (AFC) and S-farnesylthioacetic acid (FTA), an analog of AFC. It bel... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040696"
] | [
"Isoprenylcys_mtase"
] | [
439
] | 1 | [] | [] | [] | 0 | [
"4a2n"
] | 1 | [
"PUB00065859"
] | [
"22195972"
] | [
"Mechanism of isoprenylcysteine carboxyl methylation from the crystal structure of the integral membrane methyltransferase ICMT."
] | [
2011
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanomicrobia",
"marine sediment metagenome"
] | [
422,
7,
9,
1
] | 4 | [] | [] | 0 | true | Family | Prenyl lipid carboxyl methyltransferase | Prenyl lipid carboxyl methyltransferase | Isoprenylcys_mtase | 2 |
IPR054852 | 54,852 | Arginine ABC transporter substrate-binding protein ArtI | ArtI_ABC_transporter | Family | 699 | true | false | This entry represents the putative ABC transporter arginine-binding protein ArtI from Escherichia coli (strain K12). ArtI is part of the ABC transporter complex ArtPIQMJ, which is involved in the transport of arginine. Proteins in this family belong to the bacterial solute-binding protein 3 family. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041764"
] | [
"ArtI_ABC_transporter"
] | [
699
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00152883"
] | [
"30698741"
] | [
"The y-ome defines the 35% of Escherichia coli genes that lack experimental evidence of function."
] | [
2019
] | 1 | [] | [] | 0 | 0 | null | [
"Gammaproteobacteria"
] | [
699
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Arginine ABC transporter substrate-binding protein ArtI | Arginine ABC transporter substrate-binding protein ArtI | ArtI_ABC_transporter | 1 |
IPR054853 | 54,853 | Lipid II isoglutaminyl synthase subunit MurT | isoglutsynth_MurT | Family | 597 | true | false | The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The MurT subunit catalyzes the ATP-dependent amidation of the D-glutamate residue of lipid II, converting it to an isoglutamine residue. This function is essential for the proper formation... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045635"
] | [
"isoglutsynth_MurT"
] | [
597
] | 1 | [] | [] | [] | 0 | [
"6fqb"
] | 1 | [
"PUB00154652",
"PUB00154653"
] | [
"30093673",
"24044435"
] | [
"Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae.",
"In vitro reconstitution of peptidoglycan assembly from the Gram-positive pathogen Streptococcus pneumoniae."
] | [
2018,
2013
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
597
] | 1 | [] | [] | 0 | true | Family | Lipid II isoglutaminyl synthase subunit MurT | Lipid II isoglutaminyl synthase subunit MurT | isoglutsynth_MurT | 1 |
IPR054854 | 54,854 | 3-hydroxy-D-aspartate aldolase BhcC | HdxyAspAldBhcC | Family | 487 | true | false | 3-hydroxy-D-aspartate aldolase (BhcC) is an enzyme that catalyzes the condensation of glyoxylate and glycine into (2R,3S)-beta-hydroxyaspartate ((3S)-3-hydroxy-D-aspartate). This enzyme plays a crucial role in the glyoxylate assimilation pathway known as the beta-hydroxyaspartate cycle (BHAC). In Paracoccus denitrifica... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045642"
] | [
"HdxyAspAldBhcC"
] | [
487
] | 1 | [] | [] | [] | 0 | [
"6qkb"
] | 1 | [
"PUB00154623",
"PUB00154624"
] | [
"31723261",
"12835921"
] | [
"Marine Proteobacteria metabolize glycolate via the β-hydroxyaspartate cycle.",
"A novel enzyme, D-3-hydroxyaspartate aldolase from Paracoccus denitrificans IFO 13301: purification, characterization, and gene cloning."
] | [
2019,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"ecological metagenomes"
] | [
482,
5
] | 2 | [] | [] | 0 | true | Family | 3-hydroxy-D-aspartate aldolase BhcC | 3-hydroxy-D-aspartate aldolase BhcC | HdxyAspAldBhcC | 5 |
IPR054855 | 54,855 | Cis-3-hydroxy-L-proline dehydratase, mandelate racemase/muconate lactonizing enzyme family | HProlDhtase | Family | 184 | true | false | Cis-3-hydroxy-L-proline dehydratase is an enzyme that catalyzes the dehydration of cis-3-hydroxy-L-proline (c3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). This enzyme is likely involved in a degradation pathway that converts c3LHyp to L-proline, allowing certain bacteria such as Roseibium aggregatum and Ancylobac... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF043002"
] | [
"HProlDhtase"
] | [
184
] | 1 | [] | [] | [] | 0 | [
"4mgg"
] | 1 | [
"PUB00083792"
] | [
"25608448"
] | [
"A unique cis-3-hydroxy-l-proline dehydratase in the enolase superfamily."
] | [
2015
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"ecological metagenomes"
] | [
161,
9,
3,
11
] | 4 | [] | [] | 0 | true | Family | Cis-3-hydroxy-L-proline dehydratase, mandelate racemase/muconate lactonizing enzyme family | Cis-3-hydroxy-L-proline dehydratase, mandelate racemase/muconate lactonizing enzyme family | HProlDhtase | 4 |
IPR054857 | 54,857 | Cyclic nucleotide-degrading phosphodiesterase | cyc_nuc_deg_phdiest | Family | 590 | true | false | This entry represents a family of cyclic nucleotide-degrading phosphodiesterases. These enzymes are involved in the hydrolysis of cyclic nucleotides, such as cAMP and cGMP, into their corresponding nucleoside monophosphates. Members of this family include uncharacterized proteins from various Mycobacterium species, suc... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041851"
] | [
"cyc_nuc_deg_phdiest"
] | [
590
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00152928"
] | [
"36760076"
] | [
"Mycobacterial phosphodiesterase Rv0805 is a virulence determinant and its cyclic nucleotide hydrolytic activity is required for propionate detoxification."
] | [
2023
] | 1 | [] | [] | 0 | 0 | null | [
"Mycobacteriales",
"freshwater metagenome"
] | [
589,
1
] | 2 | [] | [] | 0 | true | Family | Cyclic nucleotide-degrading phosphodiesterase | Cyclic nucleotide-degrading phosphodiesterase | cyc_nuc_deg_phdiest | 3 |
IPR054858 | 54,858 | Peptidoglycan-N-acetylglucosamine deacetylase BC_1974 | PgAcgDac_BC_1974 | Family | 466 | false | false | Peptidoglycan-N-acetylglucosamine deacetylase (BC_1974) from Bacillus cereus (strain ATCC 14579) catalyses the deacetylation of N-acetylglucosamine (GlcNAc) residues in peptidoglycan. This enzyme belongs to the polysaccharide deacetylase family and is involved in modifying the peptidoglycan structure, which is crucial ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045822"
] | [
"PgAcgDacpgdA2_Bac"
] | [
466
] | 1 | [] | [] | [] | 0 | [
"5n1j",
"5n1p",
"5nc6",
"5nc9",
"5ncd",
"5nek",
"5nel"
] | 7 | [
"PUB00154682"
] | [
"29983281"
] | [
"Polysaccharide deacetylases serve as new targets for the design of inhibitors against Bacillus anthracis and Bacillus cereus."
] | [
2018
] | 1 | [
"IPR050248"
] | [] | 1 | 0 | 1 | [
"Bacillus"
] | [
466
] | 1 | [] | [] | 0 | true | Family | Peptidoglycan-N-acetylglucosamine deacetylase BC_1974 | Peptidoglycan-N-acetylglucosamine deacetylase BC_1974 | PgAcgDac_BC_1974 | 7 |
IPR054859 | 54,859 | Lipid II isoglutaminyl synthase subunit GatD | isoglutsynth_GatD | Family | 561 | true | false | The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The GatD subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia. The resulting ammonia molecule is channeled to the active site of MurT. This function is critical for the b... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045636"
] | [
"isoglutsynth_GatD"
] | [
561
] | 1 | [] | [] | [] | 0 | [
"6fqb",
"9sq9",
"9sqj"
] | 3 | [
"PUB00154652"
] | [
"30093673"
] | [
"Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae."
] | [
2018
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
561
] | 1 | [] | [] | 0 | true | Family | Lipid II isoglutaminyl synthase subunit GatD | Lipid II isoglutaminyl synthase subunit GatD | isoglutsynth_GatD | 7 |
IPR054860 | 54,860 | Iminosuccinate reductase BhcD | BhcD-like | Family | 463 | true | true | Iminosuccinate reductase BhcD is an enzyme that catalyzes the NADH-dependent reduction of iminosuccinate to L-aspartate [ ]. This enzyme is essential for the growth of Paracoccus denitrificans in the presence of glycolate and glyoxylate, as it functions in glyoxylate assimilation via the beta-hydroxyaspartate cycle (BH... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045643"
] | [
"ImmsucRedBhcD"
] | [
463
] | 1 | [] | [] | [] | 0 | [
"6rqa"
] | 1 | [
"PUB00154623"
] | [
"31723261"
] | [
"Marine Proteobacteria metabolize glycolate via the β-hydroxyaspartate cycle."
] | [
2019
] | 1 | [] | [] | 0 | 0 | null | [
"Effrenium voratum",
"Pseudomonadota",
"ecological metagenomes"
] | [
1,
457,
5
] | 3 | [] | [] | 0 | true | Family | Iminosuccinate reductase BhcD | Iminosuccinate reductase BhcD | BhcD-like | 2 |
IPR054861 | 54,861 | Endo-beta-N-acetylglucosaminidase H | Endoglyc_H | Family | 507 | true | false | This entry represents endo-beta-N-acetylglucosaminidase H, a member of the glycosyl hydrolase 18 family. These enzymes cleave asparagine-linked oligomannose and hybrid, but not complex, oligosaccharides from glycoproteins. The proteins matched by this entry include endo-beta-N-acetylglucosaminidase H from Streptomyces ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045482"
] | [
"Endoglyc_H"
] | [
507
] | 1 | [] | [] | [] | 0 | [
"1c3f",
"1c8x",
"1c8y",
"1c90",
"1c91",
"1c92",
"1c93",
"1edt",
"6ve1"
] | 9 | [
"PUB00021308",
"PUB00024509"
] | [
"10595536",
"7663942"
] | [
"Mutations of endo-beta-N-acetylglucosaminidase H active site residueAs sp130 anG glu132: activities and conformations.",
"Crystal structure of endo-beta-N-acetylglucosaminidase H at 1.9 A resolution: active-site geometry and substrate recognition."
] | [
1999,
1995
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta"
] | [
502,
5
] | 2 | [] | [] | 0 | true | Family | Endo-beta-N-acetylglucosaminidase H | Endo-beta-N-acetylglucosaminidase H | Endoglyc_H | 6 |
IPR054862 | 54,862 | DNA protection during starvation protein | DNA_prot_starvation | Family | 459 | true | false | The DNA protection during starvation protein (Dps) is a member of the Dps family, which plays a crucial role in protecting DNA from oxidative damage. This protection is achieved by sequestering intracellular Fe(2+) ions and storing them in the form of Fe(3+) oxyhydroxide mineral. The process involves the oxidation of t... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041388"
] | [
"DNA_prot_starvation"
] | [
459
] | 1 | [] | [] | [] | 0 | [
"1moj",
"1tjo",
"1tk6",
"1tko",
"1tkp"
] | 5 | [
"PUB00016788",
"PUB00080655"
] | [
"15365182",
"12147354"
] | [
"Iron-oxo clusters biomineralizing on protein surfaces: structural analysis of Halobacterium salinarum DpsA in its low- and high-iron states.",
"The DpsA-homologue of the archaeon Halobacterium salinarum is a ferritin."
] | [
2004,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Halobacteria"
] | [
11,
448
] | 2 | [] | [] | 0 | true | Family | DNA protection during starvation protein | DNA protection during starvation protein | DNA_prot_starvation | 7 |
IPR054863 | 54,863 | L-aspartate--glyoxylate aminotransferase | AspGlyoxATase | Family | 423 | true | false | L-aspartate--glyoxylate aminotransferase (BhcA) from Paracoccus denitrificans (strain Pd 1222) is an enzyme that catalyzes the transamination of glyoxylate into glycine using L-aspartate as the preferred amino group donor. This enzyme is essential for the growth of P. denitrificans in the presence of glycolate and glyo... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045640"
] | [
"AspGlyoxATase"
] | [
423
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154623"
] | [
"31723261"
] | [
"Marine Proteobacteria metabolize glycolate via the β-hydroxyaspartate cycle."
] | [
2019
] | 1 | [] | [] | 0 | 0 | null | [
"Effrenium voratum",
"Pseudomonadota",
"ecological metagenomes"
] | [
1,
420,
2
] | 3 | [] | [] | 0 | true | Family | L-aspartate--glyoxylate aminotransferase | L-aspartate--glyoxylate aminotransferase | AspGlyoxATase | 2 |
IPR054864 | 54,864 | Oligopeptide ABC transporter permease OppC | OppC_permease | Family | 461 | true | false | This entry represents the oligopeptide ABC transporter permease OppC, also known as AmiD, found in Streptococcus pneumoniae. These proteins are part of the binding-protein-dependent transport system for oligopeptides and are likely responsible for the translocation of substrates across the membrane. They belong to the ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF043080"
] | [
"OppC_permease"
] | [
461
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153514",
"PUB00153515"
] | [
"31308405",
"20488990"
] | [
"Environmental conditions shape the nature of a minimal bacterial genome.",
"Creation of a bacterial cell controlled by a chemically synthesized genome."
] | [
2019,
2010
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
461
] | 1 | [] | [] | 0 | true | Family | Oligopeptide ABC transporter permease OppC | Oligopeptide ABC transporter permease OppC | OppC_permease | 3 |
IPR054865 | 54,865 | Superoxide dismutase [Mn], archaeal | Superox_dis_Halo | Family | 413 | true | false | This entry represents superoxide dismutase [Mn] enzymes found in various archaeal species, including Halobacterium salinarum, Haloferax volcanii, and Haloarcula marismortui. These enzymes belong to the iron/manganese superoxide dismutase family and are responsible for the destruction of superoxide anion radicals, which... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041312"
] | [
"Superox_dis_Halo"
] | [
413
] | 1 | [
"EC",
"METACYC"
] | [
"1.15.1.1",
"PWY-6854"
] | [
"EC:1.15.1.1",
"METACYC:PWY-6854"
] | 2 | [] | 0 | [
"PUB00106319",
"PUB00106320",
"PUB00106321"
] | [
"3104309",
"3341765",
"8449865"
] | [
"Superoxide dismutase from the extremely halophilic archaebacterium Halobacterium cutirubrum.",
"Purification of a manganese-containing superoxide dismutase from Halobacterium halobium.",
"Characterization of paralogous and orthologous members of the superoxide dismutase gene family from genera of the halophili... | [
1987,
1988,
1993
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea"
] | [
413
] | 1 | [] | [] | 0 | true | Family | Superoxide dismutase [Mn], archaeal | Superoxide dismutase [Mn], archaeal | Superox_dis_Halo | 7 |
IPR054866 | 54,866 | 15-cis-phytoene synthase | PhytoSynCyanob | Family | 287 | true | false | This entry represents 15-cis-phytoene synthase, also known as CrtB, which is involved in the biosynthesis of carotenoids. The enzyme catalyzes the condensation of two molecules of geranylgeranyl diphosphate (GGPP) to form prephytoene diphosphate (PPPP), followed by the rearrangement of the cyclopropylcarbinyl intermedi... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045686"
] | [
"PhytoSynCyanob"
] | [
287
] | 1 | [
"EC"
] | [
"2.5.1.32"
] | [
"EC:2.5.1.32"
] | 1 | [] | 0 | [
"PUB00154612",
"PUB00154613"
] | [
"1537409",
"8018713"
] | [
"Molecular cloning and expression in Escherichia coli of a cyanobacterial gene coding for phytoene synthase, a carotenoid biosynthesis enzyme.",
"Cloning and expression in Escherichia coli of the gene coding for phytoene synthase from the cyanobacterium Synechocystis sp. PCC6803."
] | [
1992,
1994
] | 2 | [] | [] | 0 | 0 | null | [
"Cyanobacteriota"
] | [
287
] | 1 | [] | [] | 0 | true | Family | 15-cis-phytoene synthase | 15-cis-phytoene synthase | PhytoSynCyanob | 7 |
IPR054867 | 54,867 | Glutamate dehydrogenase B | GluDhGdhB | Family | 452 | true | false | This entry represents glutamate dehydrogenases from Halobacterium salinarum, including Glutamate dehydrogenase B (GdhB) and NAD-specific glutamate dehydrogenase A (GdhX). These enzymes belong to the Glu/Leu/Phe/Val dehydrogenases family. Glutamate dehydrogenases are involved in the reversible oxidative deamination of g... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041398"
] | [
"GluDhGdhB"
] | [
452
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00106375"
] | [
"15780999"
] | [
"The discovery of four distinct glutamate dehydrogenase genes in a strain of Halobacterium salinarum."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Halobacteria"
] | [
452
] | 1 | [] | [] | 0 | true | Family | Glutamate dehydrogenase B | Glutamate dehydrogenase B | GluDhGdhB | 6 |
IPR054868 | 54,868 | Archaetidylinositol phosphate synthase, archaeal | archin_ph_syn | Family | 195 | true | false | Archaetidylinositol phosphate synthase (AIPS) is an enzyme that catalyzes the formation of archaetidylinositol phosphate (AIP) from CDP-archaeol (CDP-ArOH or CDP-2,3-bis-(O-phytanyl)-sn-glycerol) and 1L-myo-inositol 1-phosphate (IP or 1D-myo-inositol 3-phosphate). AIP is a precursor of archaetidyl-myo-inositol (AI), an... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040950"
] | [
"archin_ph_syn"
] | [
195
] | 1 | [
"EC",
"METACYC",
"METACYC"
] | [
"2.7.8.39",
"PWY-6350",
"PWY-8365"
] | [
"EC:2.7.8.39",
"METACYC:PWY-6350",
"METACYC:PWY-8365"
] | 3 | [] | 0 | [
"PUB00106084"
] | [
"24269814"
] | [
"Ubiquitous distribution of phosphatidylinositol phosphate synthase and archaetidylinositol phosphate synthase in Bacteria and Archaea, which contain inositol phospholipid."
] | [
2014
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Thermosulfidibacter takaii",
"bioreactor metagenome"
] | [
193,
1,
1
] | 3 | [] | [] | 0 | true | Family | Archaetidylinositol phosphate synthase, archaeal | Archaetidylinositol phosphate synthase, archaeal | archin_ph_syn | 3 |
IPR054869 | 54,869 | Aldehyde dehydrogenase, thermostable | AlphKGSA_gudD | Family | 493 | true | false | This entry represents alpha-ketoglutaric semialdehyde dehydrogenase (GucD) and thermostable aldehyde dehydrogenase from Bacillus subtilis (strain 168) and Geobacillus stearothermophilus, respectively. These enzymes belong to the aldehyde dehydrogenase family and catalyze the NAD(P)(+)-dependent oxidation of alpha-ketog... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF042993"
] | [
"AlphKGSA_gudD"
] | [
493
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00095200"
] | [
"17202142"
] | [
"alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, D-galactarate, and hydroxy-L-proline. Molecular and metabolic convergent evolution."
] | [
2007
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillales"
] | [
493
] | 1 | [] | [] | 0 | true | Family | Aldehyde dehydrogenase, thermostable | Aldehyde dehydrogenase, thermostable | AlphKGSA_gudD | 7 |
IPR054870 | 54,870 | N-acyl homoserine lactonase AiiA | AiiA | Family | 387 | true | true | This entry represents N-acyl homoserine lactonase AiiA enzymes from bacilalles. which belong to the metallo-beta-lactamase superfamily. AiiA catalyses the hydrolysis of N-acyl homoserine lactones (AHLs) [ ], which are signalling molecules used in quorum sensing by various bacteria. The enzyme shows activity towards bot... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045699"
] | [
"AHLLactAiiA"
] | [
387
] | 1 | [
"EC"
] | [
"3.1.1.81"
] | [
"EC:3.1.1.81"
] | 1 | [
"2a7m",
"2br6",
"2btn",
"3dha",
"3dhb",
"3dhc",
"4j5f",
"4j5h",
"5eh9",
"5eht",
"7l5f"
] | 11 | [
"PUB00154679",
"PUB00154680",
"PUB00163187",
"PUB00163188",
"PUB00163189"
] | [
"10716724",
"11459062",
"16972128",
"27444875",
"34095651"
] | [
"AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora.",
"Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase.",
"Identification of the critical role of Tyr-194 in the catalytic activity of a nov... | [
2000,
2001,
2006,
2016,
2021
] | 5 | [
"IPR051013"
] | [] | 1 | 0 | 1 | [
"Bacteria"
] | [
387
] | 1 | [] | [] | 0 | true | Family | N-acyl homoserine lactonase AiiA | N-acyl homoserine lactonase AiiA | AiiA | 2 |
IPR054871 | 54,871 | Bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase | KDG_KDGal_kin_Halo | Family | 352 | true | false | This entry represents bifunctional enzymes that exhibit both 2-dehydro-3-deoxygluconokinase and 2-dehydro-3-deoxygalactonokinase activities. These enzymes are involved in the degradation of glucose via the semi-phosphorylative Entner-Doudoroff pathway and galactose catabolism. They catalyze the phosphorylation of 2-ket... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041332"
] | [
"KDG_KDGal_kin_Halo"
] | [
352
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00106336"
] | [
"25287957"
] | [
"Identification and characterization of 2-keto-3-deoxygluconate kinase and 2-keto-3-deoxygalactonate kinase in the haloarchaeon Haloferax volcanii."
] | [
2014
] | 1 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
352
] | 1 | [] | [] | 0 | true | Family | Bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase | Bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase | KDG_KDGal_kin_Halo | 2 |
IPR054873 | 54,873 | Peroxynitrite isomerase | PeroxynitIsom | Family | 383 | true | false | This entry represents peroxynitrite isomerases, which belong to the nitrobindin family. These proteins form a 10-stranded antiparallel beta-barrel structure capable of accommodating a hydrophobic ligand in its interior. The fold hosts a heme group located in a wide surface cleft. The primary function of these proteins ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045819"
] | [
"PeroxynitIsom"
] | [
383
] | 1 | [] | [] | [] | 0 | [
"2fr2",
"6r3w",
"6r3y"
] | 3 | [
"PUB00099650"
] | [
"32295384"
] | [
"Mycobacterial and Human Nitrobindins: Structure and Function."
] | [
2020
] | 1 | [] | [] | 0 | 0 | null | [
"Actinomycetota",
"Populus alba x Populus x berolinensis",
"freshwater metagenome"
] | [
381,
1,
1
] | 3 | [] | [] | 0 | true | Family | Peroxynitrite isomerase | Peroxynitrite isomerase | PeroxynitIsom | 6 |
IPR054875 | 54,875 | Indole-3-glycerol phosphate synthase, archaeal | Indglycph_syn_Halo_TrpC | Family | 330 | true | false | Indole-3-glycerol phosphate synthase (IGPS) is an enzyme that catalyses the conversion of 1-(2-carboxyphenylamino)-1-deoxyribulose-5-phosphate to indole-3-glycerol phosphate, a key step in the biosynthesis of tryptophan. This enzyme is part of the TrpC family and is found in various archaeal species, including Halofera... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041303"
] | [
"Indglycph_syn_Halo_TrpC"
] | [
330
] | 1 | [
"EC"
] | [
"4.1.1.48"
] | [
"EC:4.1.1.48"
] | 1 | [] | 0 | [
"PUB00106307"
] | [
"2118654"
] | [
"Genes for tryptophan biosynthesis in the archaebacterium Haloferax volcanii."
] | [
1990
] | 1 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
330
] | 1 | [] | [] | 0 | true | Family | Indole-3-glycerol phosphate synthase, archaeal | Indole-3-glycerol phosphate synthase, archaeal | Indglycph_syn_Halo_TrpC | 2 |
IPR054876 | 54,876 | RIO-type serine/threonine-protein kinase Rio1 | RIO1_kinase | Family | 324 | true | false | RIO-type serine/threonine-protein kinase Rio1 is a serine/threonine-protein kinase that is capable of autophosphorylation and can phosphorylate proteasome subunit alpha 1 (PsmA1) in vitro. Despite having a protein kinase domain, it is proposed to function predominantly as an ATPase. This protein belongs to the protein ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041310"
] | [
"RIO1_kinase"
] | [
324
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00106316"
] | [
"20671954"
] | [
"Phosphorylation and methylation of proteasomal proteins of the haloarcheon Haloferax volcanii."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
324
] | 1 | [] | [] | 0 | true | Family | RIO-type serine/threonine-protein kinase Rio1 | RIO-type serine/threonine-protein kinase Rio1 | RIO1_kinase | 4 |
IPR054877 | 54,877 | Phthiotriol/phenolphthiotriol dimycocerosates methyltransferase | PthPhpthDimycoMt | Family | 343 | true | false | This entry represents phthiotriol/phenolphthiotriol dimycocerosates methyltransferases, which are enzymes that catalyze the methylation of the lipid moiety of intermediate compounds such as phthiotriol and glycosylated phenolphthiotriol dimycocerosates. This methylation process results in the formation of phthiocerol d... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045823"
] | [
"PthPhpthDimycoMt"
] | [
343
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"... | [
"2.1.1.-",
"PWY-1061",
"PWY-2083",
"PWY-3542",
"PWY-4021",
"PWY-4161",
"PWY-4202",
"PWY-5059",
"PWY-5105",
"PWY-5301",
"PWY-5305",
"PWY-5479",
"PWY-5665",
"PWY-5729",
"PWY-5748",
"PWY-5765",
"PWY-5773",
"PWY-5846",
"PWY-5883",
"PWY-5975",
"PWY-5987",
"PWY-601",
"PWY-6045"... | [
"EC:2.1.1.-",
"METACYC:PWY-1061",
"METACYC:PWY-2083",
"METACYC:PWY-3542",
"METACYC:PWY-4021",
"METACYC:PWY-4161",
"METACYC:PWY-4202",
"METACYC:PWY-5059",
"METACYC:PWY-5105",
"METACYC:PWY-5301",
"METACYC:PWY-5305",
"METACYC:PWY-5479",
"METACYC:PWY-5665",
"METACYC:PWY-5729",
"METACYC:PWY-5... | 146 | [] | 0 | [
"PUB00053670"
] | [
"15292265"
] | [
"Molecular dissection of the role of two methyltransferases in the biosynthesis of phenolglycolipids and phthiocerol dimycoserosate in the Mycobacterium tuberculosis complex."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
343
] | 1 | [] | [] | 0 | true | Family | Phthiotriol/phenolphthiotriol dimycocerosates methyltransferase | Phthiotriol/phenolphthiotriol dimycocerosates methyltransferase | PthPhpthDimycoMt | 2 |
IPR054878 | 54,878 | Endonuclease VIII Nei2 | Endonuc_Nei2 | Family | 342 | true | false | This entry represents endonuclease VIII Nei2, a member of the FPG family. Endonuclease VIII Nei2 is involved in the base excision repair of DNA damaged by oxidation or mutagenic agents. It functions as a DNA glycosylase that recognizes and removes damaged bases, and has AP (apurinic/apyrimidinic) lyase activity. The en... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040775"
] | [
"Endonuc_Nei2"
] | [
342
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"3.2.2.-",
"4.2.99.18",
"PWY-2681",
"PWY-5316",
"PWY-5381",
"PWY-7342",
"PWY-7564",
"PWY-8106"
] | [
"EC:3.2.2.-",
"EC:4.2.99.18",
"METACYC:PWY-2681",
"METACYC:PWY-5316",
"METACYC:PWY-5381",
"METACYC:PWY-7342",
"METACYC:PWY-7564",
"METACYC:PWY-8106"
] | 8 | [
"8tjg"
] | 1 | [
"PUB00105955",
"PUB00105956"
] | [
"28955788",
"34820919"
] | [
"Biochemical characterization and novel inhibitor identification of <i>Mycobacterium tuberculosis</i> Endonuclease VIII 2 (Rv3297).",
"Mycobacterium tuberculosis Endonuclease VIII 2 (Nei2) forms a prereplicative BER complex with DnaN: Identification, characterization, and disruption of complex formation."
] | [
2017,
2022
] | 2 | [] | [] | 0 | 0 | null | [
"Mycobacteriales"
] | [
342
] | 1 | [] | [] | 0 | true | Family | Endonuclease VIII Nei2 | Endonuclease VIII Nei2 | Endonuc_Nei2 | 6 |
IPR054879 | 54,879 | Rad50/Mre11 complex component | Mre11_Halo | Family | 319 | true | false | The DNA double-strand break repair protein Mre11 is a crucial component of the Rad50/Mre11 complex, which plays a significant role in the early steps of DNA double-strand break (DSB) repair. Mre11 binds to DSB ends and exhibits both double-stranded 3'-5' exonuclease activity and single-stranded endonuclease activity. I... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041030"
] | [
"Mre11_Halo"
] | [
319
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00076983",
"PUB00153517"
] | [
"19593371",
"18502851"
] | [
"Mre11-Rad50 promotes rapid repair of DNA damage in the polyploid archaeon Haloferax volcanii by restraining homologous recombination.",
"Rad50 is not essential for the Mre11-dependent repair of DNA double-strand breaks in Halobacterium sp. strain NRC-1."
] | [
2009,
2008
] | 2 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
319
] | 1 | [] | [] | 0 | true | Family | Rad50/Mre11 complex component | Rad50/Mre11 complex component | Mre11_Halo | 9 |
IPR054880 | 54,880 | Menaquinone reductase | MkRedMenJ | Family | 345 | true | false | Menaquinone reductase, also known as MenJ, is an enzyme that catalyzes the reduction of a single double bond in the isoprenoid tail of menaquinone (MK-9) in mycobacteria, likely the beta-isoprene unit. This reaction forms the predominant form of menaquinone found in mycobacteria, MK-9(II-H2). The enzyme belongs to the ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045655"
] | [
"MkRedMenJ"
] | [
345
] | 1 | [
"EC",
"METACYC"
] | [
"1.3.99.38",
"PWY-7993"
] | [
"EC:1.3.99.38",
"METACYC:PWY-7993"
] | 2 | [] | 0 | [
"PUB00154698"
] | [
"26436137"
] | [
"Partial Saturation of Menaquinone in <i>Mycobacterium tuberculosis</i>: Function and Essentiality of a Novel Reductase, MenJ."
] | [
2015
] | 1 | [] | [] | 0 | 0 | null | [
"Mycobacteriaceae"
] | [
345
] | 1 | [] | [] | 0 | true | Family | Menaquinone reductase | Menaquinone reductase | MkRedMenJ | 3 |
IPR054881 | 54,881 | 3-phenylpropionate/cinnamic acid dioxygenase subunit beta | 3PPDioc_HcaF | Family | 313 | true | false | This entry represents the beta subunit of the multicomponent 3-phenylpropionate/cinnamic acid dioxygenase enzyme complex. This enzyme complex is responsible for the conversion of 3-phenylpropionic acid (PP) and cinnamic acid (CI) into their respective dihydrodiol forms, 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) a... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF042947"
] | [
"3PPDioc_HcaF"
] | [
313
] | 1 | [
"EC",
"METACYC"
] | [
"1.14.12.19",
"PWY-6690"
] | [
"EC:1.14.12.19",
"METACYC:PWY-6690"
] | 2 | [
"8k0a"
] | 1 | [
"PUB00054929"
] | [
"9603882"
] | [
"Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
313
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | 3-phenylpropionate/cinnamic acid dioxygenase subunit beta | 3-phenylpropionate/cinnamic acid dioxygenase subunit beta | 3PPDioc_HcaF | 4 |
IPR054882 | 54,882 | Outer membrane protein Omp38 | Omp38 | Family | 251 | true | false | Outer membrane protein Omp38 is a member of the outer membrane OOP (TC 1.B.6) superfamily. This protein functions as a porin, facilitating the transport of molecules across the outer membrane. In Acinetobacter baumannii, Omp38 has been shown to induce apoptosis in human cell lines through caspase-dependent and AIF-depe... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045788"
] | [
"Omp38"
] | [
251
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00065666",
"PUB00154795",
"PUB00154796"
] | [
"21965596",
"9928952",
"16008580"
] | [
"Mechanism of anchoring of OmpA protein to the cell wall peptidoglycan of the gram-negative bacterial outer membrane.",
"Purification and characterization of a major 40 kDa outer membrane protein of Acinetobacter baumannii.",
"Outer membrane protein 38 of Acinetobacter baumannii localizes to the mitochondria an... | [
2012,
1999,
2005
] | 3 | [] | [] | 0 | 0 | null | [
"Moraxellaceae",
"Oppiella nova"
] | [
250,
1
] | 2 | [] | [] | 0 | true | Family | Outer membrane protein Omp38 | Outer membrane protein Omp38 | Omp38 | 8 |
IPR054883 | 54,883 | 3-phenylpropionate/cinnamic acid dioxygenase subunit alpha | 3PPDioc_HcaE | Family | 298 | true | false | This entry represents the alpha subunit of the 3-phenylpropionate/cinnamic acid dioxygenase enzyme complex. This multicomponent dioxygenase converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into their respective dihydrodiol forms, 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF042946"
] | [
"3PPDioc_HcaE"
] | [
298
] | 1 | [
"EC",
"METACYC"
] | [
"1.14.12.19",
"PWY-6690"
] | [
"EC:1.14.12.19",
"METACYC:PWY-6690"
] | 2 | [
"8k0a"
] | 1 | [
"PUB00054929"
] | [
"9603882"
] | [
"Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadota",
"bioreactor metagenome"
] | [
297,
1
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | 3-phenylpropionate/cinnamic acid dioxygenase subunit alpha | 3-phenylpropionate/cinnamic acid dioxygenase subunit alpha | 3PPDioc_HcaE | 4 |
IPR054884 | 54,884 | DGGGPL reductase | Dggglyphlred_Halo | Family | 296 | true | false | Digeranylgeranylglycerophospholipid reductase (DGGGPL reductase) is an enzyme involved in the biosynthesis of archaeal membrane lipids. It catalyzes the reduction of 2,3-digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3-diphytanylglycerophospholipids (saturated archaeols). This enzyme can fully redu... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041385"
] | [
"Dggglyphlred_Halo"
] | [
296
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00089906"
] | [
"22469971"
] | [
"A predicted geranylgeranyl reductase reduces the ω-position isoprene of dolichol phosphate in the halophilic archaeon, Haloferax volcanii."
] | [
2012
] | 1 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
296
] | 1 | [] | [] | 0 | true | Family | DGGGPL reductase | DGGGPL reductase | Dggglyphlred_Halo | 5 |
IPR054885 | 54,885 | (2E,6E)-farnesyl diphosphate synthase | FPP_synthase | Family | 316 | true | false | This entry represents (2E,6E)-farnesyl diphosphate synthase, an enzyme that catalyzes the sequential condensations of isopentenyl pyrophosphate (IPP) with dimethylallyl diphosphate (DMAPP) to yield geranyl diphosphate (GPP) and with GPP to yield (2E,6E)-farnesyl diphosphate (E,E-FPP). The enzyme contains two aspartate-... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF042416"
] | [
"FPP_synthase"
] | [
316
] | 1 | [] | [] | [] | 0 | [
"8f8f",
"8f8k",
"8f8l"
] | 3 | [
"PUB00153500"
] | [
"32495977"
] | [
"Insight into Isoprenoid Biosynthesis by Functional Analysis of Isoprenyl Diphosphate Synthases from Mycobacterium vanbaalenii and Mycobacterium tuberculosis."
] | [
2020
] | 1 | [] | [] | 0 | 0 | null | [
"Mycobacteriaceae"
] | [
316
] | 1 | [] | [] | 0 | true | Family | (2E,6E)-farnesyl diphosphate synthase | (2E,6E)-farnesyl diphosphate synthase | FPP_synthase | 3 |
IPR054886 | 54,886 | UDP-glucose 6-dehydrogenase AglM | UDPGDh_AglM | Family | 287 | true | false | UDP-glucose 6-dehydrogenase AglM is an enzyme involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins in Haloferax volcanii. It plays a crucial role in the biosynthesis of the hexuronic acids found at both positions 2 and 3 of the pentasaccharide. The activity of th... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041297"
] | [
"UDPGDh_AglM"
] | [
287
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00106302",
"PUB00106303"
] | [
"20487296",
"22730124"
] | [
"N-glycosylation in Archaea: on the coordinated actions of Haloferax volcanii AglF and AglM.",
"N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella."
] | [
2010,
2012
] | 2 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
287
] | 1 | [] | [] | 0 | true | Family | UDP-glucose 6-dehydrogenase AglM | UDP-glucose 6-dehydrogenase AglM | UDPGDh_AglM | 5 |
IPR054887 | 54,887 | Dolichyl-phosphate hexose transferase | DPhHxTase | Family | 261 | true | false | Dolichyl-phosphate hexose transferase is a glycosyltransferase that belongs to the glycosyltransferase 2 family. This enzyme is responsible for adding a monosaccharide to dolichol phosphate, thereby generating one of the three monosaccharide-modified dolichol phosphates. The specific subunit onto which additional sugar... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041391"
] | [
"DPhHxTase"
] | [
261
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00060477"
] | [
"20802039"
] | [
"AglJ adds the first sugar of the N-linked pentasaccharide decorating the Haloferax volcanii S-layer glycoprotein."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Halobacteria"
] | [
261
] | 1 | [] | [] | 0 | true | Family | Dolichyl-phosphate hexose transferase | Dolichyl-phosphate hexose transferase | DPhHxTase | 3 |
IPR054888 | 54,888 | Olefin beta-lactone synthetase | OlefBLtnSyn | Family | 309 | true | false | Olefin beta-lactone synthetase is an enzyme involved in the biosynthesis of olefins. It catalyzes the conversion of beta-hydroxy acid substrates to beta-lactones in the presence of ATP. This enzyme can use various stereoisomers of 2-hexyl-3-hydroxydecanoic acid and 2-alkyl-3-hydroxyalkanoic acids as substrates. The enz... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045786"
] | [
"OlefBLtnSyn"
] | [
309
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154644",
"PUB00154645",
"PUB00154646"
] | [
"21266575",
"20823539",
"27238740"
] | [
"Purification and characterization of OleA from Xanthomonas campestris and demonstration of a non-decarboxylative Claisen condensation reaction.",
"Cloning, purification, crystallization and preliminary X-ray diffraction of the OleC protein from Stenotrophomonas maltophilia involved in head-to-head hydrocarbon bi... | [
2011,
2010,
2016
] | 3 | [] | [] | 0 | 0 | null | [
"Knufia peltigerae",
"Pseudomonadati"
] | [
1,
308
] | 2 | [] | [] | 0 | true | Family | Olefin beta-lactone synthetase | Olefin beta-lactone synthetase | OlefBLtnSyn | 9 |
IPR054889 | 54,889 | N-acyl homoserine lactonase AttM | AttM | Family | 269 | true | true | This protein family includes N-acyl homoserine lactonase AttM from Agrobacterium tumefaciens and similar proteins mainly found in proteobacteria. N-acyl homoserine lactonase AttM is an enzyme that belongs to the metallo-beta-lactamase superfamily. This enzyme is involved in the hydrolysis of N-acyl homoserine lactones ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045700"
] | [
"AHLLactAttM"
] | [
269
] | 1 | [
"EC"
] | [
"3.1.1.81"
] | [
"EC:3.1.1.81"
] | 1 | [
"9kho",
"9khq"
] | 2 | [
"PUB00154627"
] | [
"11930013"
] | [
"Genetic control of quorum-sensing signal turnover in Agrobacterium tumefaciens."
] | [
2002
] | 1 | [
"IPR051013"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Ricinus communis",
"marine metagenome"
] | [
260,
1,
8
] | 3 | [] | [] | 0 | true | Family | N-acyl homoserine lactonase AttM | N-acyl homoserine lactonase AttM | AttM | 7 |
IPR054890 | 54,890 | ATP-dependent DNA ligase LigA | LigA_Halo | Family | 263 | true | false | This entry represents ATP-dependent DNA ligases, specifically the LigA type found in various halophilic archaea. DNA ligases are essential enzymes that seal nicks in double-stranded DNA during DNA replication, recombination, and repair. These enzymes utilize ATP to catalyze the formation of a phosphodiester bond betwee... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041331"
] | [
"LigA_Halo"
] | [
263
] | 1 | [
"EC"
] | [
"6.5.1.1"
] | [
"EC:6.5.1.1"
] | 1 | [] | 0 | [
"PUB00106335"
] | [
"16420348"
] | [
"ATP- and NAD+-dependent DNA ligases share an essential function in the halophilic archaeon Haloferax volcanii."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
263
] | 1 | [] | [] | 0 | true | Family | ATP-dependent DNA ligase LigA | ATP-dependent DNA ligase LigA | LigA_Halo | 6 |
IPR054891 | 54,891 | D-2-hydroxyacid dehydrogenase | Dhydh_Halo | Family | 262 | true | false | This entry represents D-2-hydroxyacid dehydrogenase, an enzyme that catalyzes the stereospecific NAD(P)H-dependent reduction of 2-ketocarboxylic acids into the corresponding D-2-hydroxycarboxylic acids. The enzyme can utilize both NADPH and NADH as reductants, with a marked preference for NADPH. It exhibits broad subst... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041369"
] | [
"Dhydh_Halo"
] | [
262
] | 1 | [] | [] | [] | 0 | [
"5mh5",
"5mh6",
"5mha",
"8qza",
"8qzb",
"9ibe"
] | 6 | [
"PUB00106360"
] | [
"17049749"
] | [
"A new D-2-hydroxyacid dehydrogenase with dual coenzyme-specificity from Haloferax mediterranei, sequence analysis and heterologous overexpression."
] | [
2006
] | 1 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
262
] | 1 | [] | [] | 0 | true | Family | D-2-hydroxyacid dehydrogenase | D-2-hydroxyacid dehydrogenase | Dhydh_Halo | 5 |
IPR054892 | 54,892 | Lateral flagellin LafA | lat_flg_LafA | Family | 282 | true | false | Lateral flagellin LafA is a protein found in Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633). It is the subunit protein that polymerizes to form the filaments of bacterial flagella, which are essential for lateral flagellar synthesis and swarming motility. This protein belongs to the bacterial flagellin fa... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF038071"
] | [
"lat_flg_LafA"
] | [
282
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00104072",
"PUB00104251",
"PUB00105550"
] | [
"15170400",
"16428388",
"4010543"
] | [
"Dual flagellar systems enable motility under different circumstances.",
"Analysis of the lateral flagellar gene system of Aeromonas hydrophila AH-3.",
"Lateral flagellar antigen of Vibrio alginolyticus and Vibrio harveyi: existence of serovars common to the two species."
] | [
2004,
2006,
1985
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"bioreactor metagenome"
] | [
281,
1
] | 2 | [] | [] | 0 | true | Family | Lateral flagellin LafA | Lateral flagellin LafA | lat_flg_LafA | 3 |
IPR054893 | 54,893 | Methenyltetrahydrofolate cyclohydrolase | MthfCyhylase | Family | 165 | true | false | Methenyltetrahydrofolate cyclohydrolase (MTHF cyclohydrolase) is an enzyme that plays a crucial role in the metabolism of one-carbon (C1) and two-carbon (C2) units. This enzyme is part of the cyclodeaminase/cyclohydrolase family and is required for the interconversion of 5,10-methenyltetrahydrofolate to 10-formyltetrah... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045657"
] | [
"MthfCyhylase"
] | [
165
] | 1 | [] | [] | [] | 0 | [
"7vg4",
"7vg5"
] | 2 | [
"PUB00002257",
"PUB00020619",
"PUB00154625"
] | [
"7961516",
"10215859",
"35051495"
] | [
"Genetics of the serine cycle in Methylobacterium extorquens AM1: identification, sequence, and mutation of three new genes involved in C1 assimilation, orf4, mtkA, and mtkB.",
"A methenyl tetrahydromethanopterin cyclohydrolase and a methenyl tetrahydrofolate cyclohydrolase in Methylobacterium extorquens AM1.",
... | [
1994,
1999,
2022
] | 3 | [] | [] | 0 | 0 | null | [
"Pseudomonadati",
"ecological metagenomes"
] | [
163,
2
] | 2 | [] | [] | 0 | true | Family | Methenyltetrahydrofolate cyclohydrolase | Methenyltetrahydrofolate cyclohydrolase | MthfCyhylase | 9 |
IPR054894 | 54,894 | Assimilatory nitrate reductase NasA | Nitr_red_NasA | Family | 225 | true | false | Assimilatory nitrate reductase NasA is a key enzyme involved in the first step of nitrate assimilation. It catalyzes the reduction of nitrate to nitrite, using ferredoxin as the electron donor. This enzyme can also use reduced methyl viologen but neither NADPH nor NADH as electron donors. The activity of NasA is inhibi... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041323"
] | [
"Nitr_red_NasA"
] | [
225
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00073482",
"PUB00106331"
] | [
"11731152",
"16182473"
] | [
"Assimilatory nitrate reductase from the haloarchaeon Haloferax mediterranei: purification and characterisation.",
"Identification and transcriptional analysis of nitrate assimilation genes in the halophilic archaeon Haloferax mediterranei."
] | [
2001,
2005
] | 2 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
225
] | 1 | [] | [] | 0 | true | Family | Assimilatory nitrate reductase NasA | Assimilatory nitrate reductase NasA | Nitr_red_NasA | 4 |
IPR054895 | 54,895 | Peptidoglycan-N-acetylglucosamine deacetylase BC_1960 | PGN_GlcNAc_Dac_BC_1960 | Family | 202 | true | true | Peptidoglycan-N-acetylglucosamine deacetylase BC_1960 catalyses the deacetylation of N-acetylglucosamine (GlcNAc) residues in peptidoglycan [ , ]. It also acts on soluble chitin substrates and N-acetylchitooligomers. This protein acts on cell wall peptidoglycan from the Gram-positive bacteria B.cereus and B.subtilis an... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045821"
] | [
"PGN_GlcNAc_Dac"
] | [
202
] | 1 | [] | [] | [] | 0 | [
"4l1g",
"5o6y"
] | 2 | [
"PUB00093393",
"PUB00154681",
"PUB00154682"
] | [
"15961396",
"18323609",
"29983281"
] | [
"Peptidoglycan N-acetylglucosamine deacetylases from Bacillus cereus, highly conserved proteins in Bacillus anthracis.",
"Purification, crystallization and preliminary X-ray analysis of the peptidoglycan N-acetylglucosamine deacetylase BC1960 from Bacillus cereus in the presence of its substrate (GlcNAc)6.",
"P... | [
2005,
2008,
2018
] | 3 | [
"IPR050248"
] | [] | 1 | 0 | 1 | [
"Bacillaceae"
] | [
202
] | 1 | [] | [] | 0 | true | Family | Peptidoglycan-N-acetylglucosamine deacetylase BC_1960 | Peptidoglycan-N-acetylglucosamine deacetylase BC_1960 | PGN_GlcNAc_Dac_BC_1960 | 2 |
IPR054896 | 54,896 | Lycopene cyclase, cyanobacteria | CrtY_cyanobact | Family | 85 | false | false | This family represents Lycopene beta cyclase (CrtY) mainly found in cyanobacteria. Lycopene cyclase is a key enzyme which converts the acyclic carotenoid lycopene into the cyclic carotenoid beta-carotene [ ]. It is thought that CrtY lycopene cyclases use reduced flavin adenine dinucleotide (redFAD) as a cofactor, which... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045687"
] | [
"LycopCycCtrL"
] | [
85
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00011302",
"PUB00011586",
"PUB00053852",
"PUB00106873",
"PUB00106874",
"PUB00154704",
"PUB00154705"
] | [
"9168123",
"8837512",
"20178989",
"12782726",
"25943989",
"8344419",
"7919981"
] | [
"Cloning, sequencing and expressing the carotenoid biosynthesis genes, lycopene cyclase and phytoene desaturase, from the aerobic photosynthetic bacterium Erythrobacter longus sp. strain Och101 in Escherichia coli.",
"Functional analysis of the beta and epsilon lycopene cyclase enzymes of Arabidopsis reveals a me... | [
1997,
1996,
2010,
2003,
2015,
1993,
1994
] | 7 | [
"IPR010108"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Paulinella"
] | [
81,
4
] | 2 | [] | [] | 0 | true | Family | Lycopene cyclase, cyanobacteria | Lycopene cyclase, cyanobacteria | CrtY_cyanobact | 3 |
IPR054898 | 54,898 | Enoyl-CoA hydratase DpgD | EnCoAhydt_DpgD | Family | 226 | true | false | Enoyl-CoA hydratase DpgD is a member of the enoyl-CoA hydratase/isomerase family, found in Amycolatopsis orientalis. This enzyme is involved in the biosynthesis of the nonproteinogenic amino acid monomer (S)-3,5-dihydroxyphenylglycine (Dpg), which is crucial for the production of the antibiotics vancomycin and teicopla... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF042430"
] | [
"EnCoAhydt_DpgD"
] | [
226
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00014465"
] | [
"11752437"
] | [
"Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"prokaryotic environmental samples"
] | [
223,
3
] | 2 | [] | [] | 0 | true | Family | Enoyl-CoA hydratase DpgD | Enoyl-CoA hydratase DpgD | EnCoAhydt_DpgD | 5 |
IPR054899 | 54,899 | Acidic tetraheme cytochrome c3 TmcA | c3_cytochr_TmcA | Family | 86 | true | false | Acidic tetraheme cytochrome c3 TmcA is a protein found in Desulfocurvibacter africanus. This protein is involved in electron transfer processes, specifically exchanging electrons with the basic cytochrome c3. The protein is characterized by the presence of four heme groups, which are essential for its function in elect... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045722"
] | [
"c3_cytochr_TmcA"
] | [
86
] | 1 | [] | [] | [] | 0 | [
"3cao",
"3car"
] | 2 | [
"PUB00154735",
"PUB00154758",
"PUB00154759"
] | [
"16922512",
"8573595",
"9392524"
] | [
"The Tmc complex from Desulfovibrio vulgaris hildenborough is involved in transmembrane electron transfer from periplasmic hydrogen oxidation.",
"Biochemical studies of the c-type cytochromes of the sulfate reducer Desulfovibrio africanus. Characterization of two tetraheme cytochromes c3 with different specificit... | [
2006,
1996,
1997
] | 3 | [] | [] | 0 | 0 | null | [
"Thermodesulfobacteriota",
"hydrocarbon metagenome"
] | [
85,
1
] | 2 | [] | [] | 0 | true | Family | Acidic tetraheme cytochrome c3 TmcA | Acidic tetraheme cytochrome c3 TmcA | c3_cytochr_TmcA | 3 |
IPR054900 | 54,900 | Sulfate respiration complex protein HmcC | sulf_resp_HmcC | Family | 95 | true | false | This entry represents the sulfate respiration complex protein HmcC, also known as high-molecular-weight cytochrome c (HmcC). HmcC is part of a transmembrane protein complex that facilitates electron flow from the periplasmic hydrogenase to cytoplasmic enzymes involved in sulfate reduction. The protein is encoded by the... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045714"
] | [
"sulf_resp_HmcC"
] | [
95
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00021717",
"PUB00154757"
] | [
"12356749",
"8335628"
] | [
"Sulfate respiration in Desulfovibrio vulgaris Hildenborough. Structure of the 16-heme cytochrome c HmcA AT 2.5-A resolution and a view of its role in transmembrane electron transfer.",
"The hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough encodes a potential transmembrane redox protein complex.... | [
2002,
1993
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
95
] | 1 | [] | [] | 0 | true | Family | Sulfate respiration complex protein HmcC | Sulfate respiration complex protein HmcC | sulf_resp_HmcC | 6 |
IPR054901 | 54,901 | 2-isopropylmalate synthase LeuA2 | IPMS_Lepto | Family | 135 | true | false | This entry represents 2-isopropylmalate synthase 2 (LeuA2) from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601). The enzyme catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isop... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF042434"
] | [
"IPMS_Lepto"
] | [
135
] | 1 | [] | [] | [] | 0 | [
"4ov4",
"4ov9"
] | 2 | [
"PUB00153491"
] | [
"15292141"
] | [
"Isoleucine biosynthesis in Leptospira interrogans serotype lai strain 56601 proceeds via a threonine-independent pathway."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
135
] | 1 | [] | [] | 0 | true | Family | 2-isopropylmalate synthase LeuA2 | 2-isopropylmalate synthase LeuA2 | IPMS_Lepto | 8 |
IPR054902 | 54,902 | 1-phosphofructokinase | pfkB_Halo | Family | 145 | true | false | 1-phosphofructokinase (pfkB) from Haloferax volcanii catalyzes the ATP-dependent phosphorylation of fructose-1-phosphate to fructose-1,6-bisphosphate. This enzyme plays a crucial role in the utilization of fructose as a sole carbon and energy source. It belongs to the carbohydrate kinase PfkB family, which is character... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041320"
] | [
"pfkB_Halo"
] | [
145
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00060540"
] | [
"22493022"
] | [
"Fructose degradation in the haloarchaeon Haloferax volcanii involves a bacterial type phosphoenolpyruvate-dependent phosphotransferase system, fructose-1-phosphate kinase, and class II fructose-1,6-bisphosphate aldolase."
] | [
2012
] | 1 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
145
] | 1 | [] | [] | 0 | true | Family | 1-phosphofructokinase | 1-phosphofructokinase | pfkB_Halo | 7 |
IPR054903 | 54,903 | Sulfate respiration complex protein HmcE | sulf_resp_HmcE | Family | 90 | true | false | The sulfate respiration complex protein HmcE is part of a high-molecular-weight cytochrome c (HMWC) complex. This complex, which includes ORF2, ORF3, ORF4, ORF5, and ORF6 in the HMC operon, forms a transmembrane protein assembly that facilitates electron flow from the periplasmic hydrogenase to the cytoplasmic enzymes ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045716"
] | [
"sulf_resp_HmcE"
] | [
90
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00021717",
"PUB00154757"
] | [
"12356749",
"8335628"
] | [
"Sulfate respiration in Desulfovibrio vulgaris Hildenborough. Structure of the 16-heme cytochrome c HmcA AT 2.5-A resolution and a view of its role in transmembrane electron transfer.",
"The hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough encodes a potential transmembrane redox protein complex.... | [
2002,
1993
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"bioreactor metagenome"
] | [
89,
1
] | 2 | [] | [] | 0 | true | Family | Sulfate respiration complex protein HmcE | Sulfate respiration complex protein HmcE | sulf_resp_HmcE | 1 |
IPR054904 | 54,904 | Non-specific acid phosphatase | Acid_Phosphatase_PhoC | Family | 150 | true | false | This entry represents non-specific acid phosphatases, including major phosphate-irrepressible acid phosphatases from various bacterial species such as Providencia stuartii and Morganella morganii. These enzymes belong to the class A bacterial acid phosphatase family. Acid phosphatases catalyse the hydrolysis of phospha... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045654"
] | [
"Acid_Phosphatase_PhoC"
] | [
150
] | 1 | [] | [] | [] | 0 | [
"1d2t",
"1eoi",
"1iw8",
"8yc1",
"9jq0"
] | 5 | [
"PUB00003588",
"PUB00154799"
] | [
"8081499",
"10877772"
] | [
"Characterization and sequence of PhoC, the principal phosphate-irrepressible acid phosphatase of Morganella morganii.",
"Phosphorylation of nucleosides by the mutated acid phosphatase from Morganella morganii."
] | [
1994,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Beauveria bassiana D1-5"
] | [
149,
1
] | 2 | [] | [] | 0 | true | Family | Non-specific acid phosphatase | Non-specific acid phosphatase | Acid_Phosphatase_PhoC | 1 |
IPR054905 | 54,905 | Succinyl-CoA:mesaconate CoA-transferase | Scnl_mescCoAtase | Family | 134 | true | false | Succinyl-CoA:mesaconate CoA-transferase is an enzyme involved in the methylaspartate cycle. It catalyzes the transfer of the CoA moiety from succinyl-CoA to mesaconate, generating mesaconyl-CoA (2-methylfumaryl-CoA) and succinate. This enzyme belongs to the CoA-transferase III family. In Haloarcula hispanica, the enzym... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041294"
] | [
"Scnl_mescCoAtase"
] | [
134
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00070126",
"PUB00093662"
] | [
"21252347",
"28932214"
] | [
"A methylaspartate cycle in haloarchaea.",
"Succinyl-CoA:Mesaconate CoA-Transferase and Mesaconyl-CoA Hydratase, Enzymes of the Methylaspartate Cycle in Haloarcula hispanica."
] | [
2011,
2017
] | 2 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
134
] | 1 | [] | [] | 0 | true | Family | Succinyl-CoA:mesaconate CoA-transferase | Succinyl-CoA:mesaconate CoA-transferase | Scnl_mescCoAtase | 4 |
IPR054906 | 54,906 | 2,3-Digeranylgeranylglycerophospholipid reductase | DGGGPL_red | Family | 86 | true | false | This entry represents digeranylgeranylglycerophospholipid reductase, an enzyme involved in the biosynthesis of archaeal membrane lipids. The enzyme catalyzes the reduction of 2,3-digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3-diphytanylglycerophospholipids (saturated archaeols). This process invo... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041080"
] | [
"DGGGPL_red"
] | [
86
] | 1 | [] | [] | [] | 0 | [
"3atq",
"3atr",
"4opc",
"4opd",
"4opg",
"4opi",
"4opl",
"4opt",
"4opu"
] | 9 | [
"PUB00106161",
"PUB00106162"
] | [
"18375567",
"21515284"
] | [
"Specific partial reduction of geranylgeranyl diphosphate by an enzyme from the thermoacidophilic archaeon Sulfolobus acidocaldarius yields a reactive prenyl donor, not a dead-end product.",
"Structure and mutation analysis of archaeal geranylgeranyl reductase."
] | [
2008,
2011
] | 2 | [] | [] | 0 | 0 | null | [
"Thermoprotei"
] | [
86
] | 1 | [] | [] | 0 | true | Family | 2,3-Digeranylgeranylglycerophospholipid reductase | 2,3-Digeranylgeranylglycerophospholipid reductase | DGGGPL_red | 2 |
IPR054907 | 54,907 | (R)-citramalate synthase | CitmalSynth_CimA | Family | 122 | true | false | This entry represents (R)-citramalate synthase (CimA), an enzyme found in Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601). CimA catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate. The enzyme shows strict substrate specificity for pyruvate and cannot use ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF042433"
] | [
"CitmalSynth_CimA"
] | [
122
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00050683",
"PUB00153491"
] | [
"18498255",
"15292141"
] | [
"Molecular basis of the substrate specificity and the catalytic mechanism of citramalate synthase from Leptospira interrogans.",
"Isoleucine biosynthesis in Leptospira interrogans serotype lai strain 56601 proceeds via a threonine-independent pathway."
] | [
2008,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Leptospira"
] | [
122
] | 1 | [] | [] | 0 | true | Family | (R)-citramalate synthase | (R)-citramalate synthase | CitmalSynth_CimA | 9 |
IPR054908 | 54,908 | PTS phosphocarrier protein HPr | PTS-HPr | Family | 97 | true | false | Phosphocarrier protein HPr is a general (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. T... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041319"
] | [
"PTS-HPr"
] | [
97
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00060540"
] | [
"22493022"
] | [
"Fructose degradation in the haloarchaeon Haloferax volcanii involves a bacterial type phosphoenolpyruvate-dependent phosphotransferase system, fructose-1-phosphate kinase, and class II fructose-1,6-bisphosphate aldolase."
] | [
2012
] | 1 | [] | [] | 0 | 0 | null | [
"Halobacteriales"
] | [
97
] | 1 | [] | [] | 0 | true | Family | PTS phosphocarrier protein HPr | PTS phosphocarrier protein HPr | PTS-HPr | 9 |
IPR054909 | 54,909 | Fructose-bisphosphate aldolase class II | Fbpase2 | Family | 102 | true | false | Fructose-bisphosphate aldolase class II (Fbpase class II) enzymes catalyse the aldol condensation of dihydroxyacetone phosphate (DHAP) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. These enzymes are required for the utilization o... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF041368"
] | [
"Fbpase2"
] | [
102
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00060540"
] | [
"22493022"
] | [
"Fructose degradation in the haloarchaeon Haloferax volcanii involves a bacterial type phosphoenolpyruvate-dependent phosphotransferase system, fructose-1-phosphate kinase, and class II fructose-1,6-bisphosphate aldolase."
] | [
2012
] | 1 | [] | [] | 0 | 0 | null | [
"Methanobacteriota"
] | [
102
] | 1 | [] | [] | 0 | true | Family | Fructose-bisphosphate aldolase class II | Fructose-bisphosphate aldolase class II | Fbpase2 | 2 |
IPR054910 | 54,910 | Olefin beta-lactone synthetase, Shewanella oneidensis | OlefBLtnSynShew | Family | 112 | true | false | Olefin beta-lactone synthetase is an enzyme involved in the biosynthesis of olefins. It catalyzes the conversion of 2-alkyl-3-hydroxyalkanoic acids to beta-lactones in the presence of ATP. This enzyme belongs to the ATP-dependent AMP-binding enzyme family. In Shewanella oneidensis, the oleABCD gene cluster is responsib... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045785"
] | [
"OlefBLtnSynShew"
] | [
112
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00153446"
] | [
"20418444"
] | [
"Structure, function, and insights into the biosynthesis of a head-to-head hydrocarbon in Shewanella oneidensis strain MR-1."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Gammaproteobacteria"
] | [
112
] | 1 | [] | [] | 0 | true | Family | Olefin beta-lactone synthetase, Shewanella oneidensis | Olefin beta-lactone synthetase, Shewanella oneidensis | OlefBLtnSynShew | 9 |
IPR054911 | 54,911 | Sulfate respiration complex protein HmcD | sulf_resp_HmcD | Family | 71 | true | false | The sulfate respiration complex protein HmcD is part of a high-molecular-weight cytochrome c (HMWC) complex involved in electron transfer. This protein is encoded by the DVU_0533 gene in Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough). HmcD, along with ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045712"
] | [
"sulf_resp_HmcD"
] | [
71
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00021717",
"PUB00154757"
] | [
"12356749",
"8335628"
] | [
"Sulfate respiration in Desulfovibrio vulgaris Hildenborough. Structure of the 16-heme cytochrome c HmcA AT 2.5-A resolution and a view of its role in transmembrane electron transfer.",
"The hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough encodes a potential transmembrane redox protein complex.... | [
2002,
1993
] | 2 | [
"IPR060724"
] | [] | 1 | 0 | 1 | [
"Bacteria"
] | [
71
] | 1 | [] | [] | 0 | true | Family | Sulfate respiration complex protein HmcD | Sulfate respiration complex protein HmcD | sulf_resp_HmcD | 6 |
IPR054912 | 54,912 | Multifunctional alkaline phosphatase PehA | HdlasePehA | Family | 106 | true | false | This entry represents the multifunctional alkaline phosphatase PehA, a member of the alkaline phosphatase superfamily. PehA exhibits a broad substrate specificity, hydrolyzing phosphate diesters and phosphonate monoesters. It also acts on phosphate mono- and triesters, sulfate monoesters, and sulfonate monoesters. PehA... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045661"
] | [
"HdlasePehA"
] | [
106
] | 1 | [] | [] | [] | 0 | [
"2vqr",
"2w8s",
"9gvd",
"9gve"
] | 4 | [
"PUB00049859",
"PUB00136051",
"PUB00154626"
] | [
"18793651",
"20133613",
"8824203"
] | [
"A new member of the alkaline phosphatase superfamily with a formylglycine nucleophile: structural and kinetic characterisation of a phosphonate monoester hydrolase/phosphodiesterase from Rhizobium leguminosarum.",
"An efficient, multiply promiscuous hydrolase in the alkaline phosphatase superfamily.",
"Identif... | [
2008,
2010,
1996
] | 3 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
106
] | 1 | [] | [] | 0 | true | Family | Multifunctional alkaline phosphatase PehA | Multifunctional alkaline phosphatase PehA | HdlasePehA | 5 |
IPR054914 | 54,914 | F(420)H(2) dehydrogenase subunit D | F420_dehyd_FpoD | Family | 63 | true | false | The F(420)H(2) dehydrogenase subunit D is a component of the F(420)H(2) dehydrogenase (FPO complex), which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. This system plays a crucial role in the metabolism of methylotrophic methanogens, particularly when these organisms grow on methan... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040602"
] | [
"F420_dehyd_FpoD"
] | [
63
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00009994"
] | [
"10751389"
] | [
"The F420H2 dehydrogenase from Methanosarcina mazei is a Redox-driven proton pump closely related to NADH dehydrogenases."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Methanomicrobia",
"hydrocarbon metagenome"
] | [
62,
1
] | 2 | [] | [] | 0 | true | Family | F(420)H(2) dehydrogenase subunit D | F(420)H(2) dehydrogenase subunit D | F420_dehyd_FpoD | 8 |
IPR054915 | 54,915 | Outer membrane protein OmpV | OmpV | Family | 116 | true | false | The outer membrane protein OmpV is a member of the MipA/OmpV family, which is found in various Vibrio species, including Vibrio anguillarum and Vibrio cholerae. These proteins are integral components of the bacterial outer membrane and are involved in maintaining membrane integrity and function. The OmpV protein from V... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045789"
] | [
"OmpV"
] | [
116
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154647"
] | [
"3031428"
] | [
"Nucleotide sequence of ompV, the gene for a major Vibrio cholerae outer membrane protein."
] | [
1986
] | 1 | [] | [] | 0 | 0 | null | [
"Gammaproteobacteria"
] | [
116
] | 1 | [] | [] | 0 | true | Family | Outer membrane protein OmpV | Outer membrane protein OmpV | OmpV | 5 |
IPR054916 | 54,916 | Fatty-acid O-methyltransferase | FAmtase_mtf2 | Family | 90 | true | false | Fatty-acid O-methyltransferase (Mtf2) is an enzyme that modifies the hydroxy group of fatty acids through methylation. Oleate is identified as the most effective fatty acid acceptor for this enzyme. This protein belongs to the methyltransferase superfamily and is found in Mycolicibacterium smegmatis (strain ATCC 700084... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045825"
] | [
"FAmtase_mtf2"
] | [
90
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00154699"
] | [
"12368441"
] | [
"Modification of glycopeptidolipids by an O-methyltransferase of Mycobacterium smegmatis."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Actinomycetes"
] | [
90
] | 1 | [] | [] | 0 | true | Family | Fatty-acid O-methyltransferase | Fatty-acid O-methyltransferase | FAmtase_mtf2 | 1 |
IPR054917 | 54,917 | Oxalate oxidoreductase subunit alpha | OxalOxred_alpha | Family | 41 | true | true | This entry represents Oxalate oxidoreductase subunit alpha also known as OOR subunit alpha. OOR is an enzyme that catalyses the anaerobic oxidation of oxalate using a broad range of electron acceptors, including ferredoxin and the nickel-dependent carbon monoxide dehydrogenase. This enzyme does not require coenzyme A a... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045791"
] | [
"OxalOxredalpha"
] | [
41
] | 1 | [] | [] | [] | 0 | [
"5c4i",
"5exd",
"5exe"
] | 3 | [
"PUB00078738"
] | [
"20956531"
] | [
"Identification and characterization of oxalate oxidoreductase, a novel thiamine pyrophosphate-dependent 2-oxoacid oxidoreductase that enables anaerobic growth on oxalate."
] | [
2010
] | 1 | [
"IPR050722"
] | [] | 1 | 0 | 1 | [
"Bacteria"
] | [
41
] | 1 | [] | [] | 0 | true | Family | Oxalate oxidoreductase subunit alpha | Oxalate oxidoreductase subunit alpha | OxalOxred_alpha | 2 |
IPR054918 | 54,918 | UPF0167 protein CbrC | UPF0167_CbrC | Family | 92 | true | false | This entry represents the UPF0167 protein CbrC, which is involved in colicin E2 tolerance. The CbrC protein belongs to the UPF0167 family and is found in Escherichia coli (strain K12). The exact function of CbrC is not fully characterized, but it is known to play a role in the bacterial response to colicin E2. Colicins... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040891"
] | [
"UPF0167_CbrC"
] | [
92
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00106048"
] | [
"20418396"
] | [
"YieJ (CbrC) mediates CreBC-dependent colicin E2 tolerance in Escherichia coli."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Trichuris trichiura"
] | [
91,
1
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | UPF0167 protein CbrC | UPF0167 protein CbrC | UPF0167_CbrC | 2 |
IPR054919 | 54,919 | Mycoplasma-type histidine triad protein HinT | M_plasma_HinT | Family | 111 | true | false | This entry represents a Mycoplasma-type histidine triad (HIT) protein, HinT. HIT proteins are characterized by a conserved histidine triad motif (HφHφHφ, where φ is a hydrophobic residue) and are involved in various biochemical processes, including nucleotide binding and hydrolysis. The specific function of this protei... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045834"
] | [
"M_plasma_HinT"
] | [
111
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00035586",
"PUB00154805"
] | [
"15904496",
"15579213"
] | [
"HinT proteins and their putative interaction partners in Mollicutes and Chlamydiaceae.",
"P80, the HinT interacting membrane protein, is a secreted antigen of Mycoplasma hominis."
] | [
2005,
2004
] | 2 | [] | [] | 0 | 0 | null | [
"Mycoplasmatota"
] | [
111
] | 1 | [] | [] | 0 | true | Family | Mycoplasma-type histidine triad protein HinT | Mycoplasma-type histidine triad protein HinT | M_plasma_HinT | 9 |
IPR054920 | 54,920 | NAD(P)-dependent benzaldehyde dehydrogenase | BenzalDHMdlD | Family | 96 | true | false | NAD(P)-dependent benzaldehyde dehydrogenase is an enzyme that catalyzes the conversion of benzaldehyde into benzoate in the (R)-mandelate degradation pathway. This enzyme can utilize either NAD or NADP as a cofactor. It belongs to the aldehyde dehydrogenase family and is encoded by the mdlD gene in Pseudomonas putida. ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045701"
] | [
"BenzalDHMdlD"
] | [
96
] | 1 | [] | [] | [] | 0 | [
"5ucd"
] | 1 | [
"PUB00000334",
"PUB00154734"
] | [
"2271624",
"12670968"
] | [
"Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli.",
"Identification and characterization of a mandelamide hydrolase and an NAD(P)+-dependen... | [
1990,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Pseudomonadati"
] | [
96
] | 1 | [] | [] | 0 | true | Family | NAD(P)-dependent benzaldehyde dehydrogenase | NAD(P)-dependent benzaldehyde dehydrogenase | BenzalDHMdlD | 6 |
IPR054921 | 54,921 | Tyrosine isonitrile synthase | TyIsonSynPvcA | Family | 128 | true | false | L-tyrosine isonitrile synthase is an enzyme involved in the biosynthesis of rhabduscin, a tyrosine derivative that acts as a potent inhibitor of phenoloxidase, a key component of the insect's innate immune system. This enzyme is responsible for the synthesis of the isonitrile group on tyrosine, using the C2 of ribulose... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF045653"
] | [
"TyIsonSynPvcA"
] | [
128
] | 1 | [] | [] | [] | 0 | [
"9dh4",
"9dhm",
"9dhn"
] | 3 | [
"PUB00100306"
] | [
"22711807"
] | [
"Small molecule perimeter defense in entomopathogenic bacteria."
] | [
2012
] | 1 | [] | [] | 0 | 0 | null | [
"Enterobacterales"
] | [
128
] | 1 | [] | [] | 0 | true | Family | Tyrosine isonitrile synthase | Tyrosine isonitrile synthase | TyIsonSynPvcA | 2 |
IPR054922 | 54,922 | FPO subunit F | FPO_su_F | Family | 60 | true | true | The F420H2 dehydrogenase subunit F (FpoF) is a component of the F420H2 dehydrogenase (FPO complex), which is part of the energy-conserving F420H2:heterodisulfide oxidoreductase system. This membrane-bound electron transfer system plays a crucial role in the metabolism of methylotrophic methanogens, particularly when th... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF040616"
] | [
"F420_dehyd_sub_F"
] | [
60
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00009994"
] | [
"10751389"
] | [
"The F420H2 dehydrogenase from Methanosarcina mazei is a Redox-driven proton pump closely related to NADH dehydrogenases."
] | [
2000
] | 1 | [
"IPR045220"
] | [] | 1 | 0 | 1 | [
"Methanosarcinales"
] | [
60
] | 1 | [] | [] | 0 | true | Family | FPO subunit F | FPO subunit F | FPO_su_F | 2 |
IPR054923 | 54,923 | Decorin-binding protein A | Decorin_bind_prot_A | Family | 101 | true | false | Decorin-binding protein A (DbpA) is a member of the decorin-binding protein family found in Borreliella burgdorferi, the causative agent of Lyme disease. This protein binds to decorin, a component of the extracellular matrix, which may facilitate the adherence of B. burgdorferi to collagen fibers in skin and other tiss... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"NF033713"
] | [
"Decorin_bind_prot_A"
] | [
101
] | 1 | [] | [] | [] | 0 | [
"2lqu",
"2mtc",
"2mtd",
"4onr",
"9bqw"
] | 5 | [
"PUB00105264",
"PUB00105265",
"PUB00105266"
] | [
"18507835",
"21628660",
"25079227"
] | [
"Assessment of decorin-binding protein A to the infectivity of Borrelia burgdorferi in the murine models of needle and tick infection.",
"Decorin binding by DbpA and B of Borrelia garinii, Borrelia afzelii, and Borrelia burgdorferi sensu Stricto.",
"Strain-specific variation of the decorin-binding adhesin DbpA ... | [
2008,
2011,
2014
] | 3 | [] | [] | 0 | 0 | null | [
"Borreliaceae"
] | [
101
] | 1 | [] | [] | 0 | true | Family | Decorin-binding protein A | Decorin-binding protein A | Decorin_bind_prot_A | 3 |
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