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Full Name
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⌀
taxon
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sequence
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2.75k
function
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5.51k
AlphaFoldDB
stringlengths
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10
Q1GAP9
TIG_LACDA
PPIase
Lactobacillus
MSANWKTTGKTTGELSFEISQDEIKKSLDKAFGRVKKSLRVPGFRKGHVSRVIFNQYYGEEALYEDALNFALPEAYSAAVKETGIKAVGQPQIVPVSMGKNKAWEMKAIVTVEPEVELGQYTEIEVPKQNTRVYQKDIDAELTKRQEQNAEMVLKNDKAENGDTVTIDYVGTVDGVEFDGGSAQNYSLELGSNTFIPGFEDQLVGHGAGEEVDVVVTFPEDYGAKDLAGKEAHFATKIHEVKAKQLPELDDEFAKDVDDSVETLDELKEKIKAELKSEKEEAAKAAIQEAAITTAVKNATVEEIPDVMIQEDVDNQLNQYLGDMQRQGIDPQTYFKLTNTTEDQLRSQLSANAAERVKTNLVLEAIVAKEGFEASKEEIDAEIKDLADNYNMSEKAVRNALSDEMLAHDINVRKAMDLITDSAKQVAKAKLEEGSEEDK
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Q1GAP9
Q8QZY4
RTBDN_MOUSE
Retbindin
Mus
MAHEGHSQHSGLVWALRPILAWIFLVACGWSHPLQTRSWGHPGLAAKVRTGQLQPAGHPQSSVLPSYPRIQVPGSQTPPVPVPCCTAEIDRPESLLESCGAPSPECEFFLGQLQGALRDRFHPQLFGARPVQPLCPELCQIWFTTCQADFICGPTWLQSSGERGCEPSCRTYGQTFANATDLCHSVLGHVLRVAAPGSSHCLNVSISSPGARRRPRAWISNVVGSGSGSGSGDSPEPMFGFQYVSLP
Riboflavin-binding protein which might have a role in retinal flavin transport.
Q8QZY4
C0NUL6
RCF1_AJECG
Respiratory supercomplex factor 1, mitochondrial
Histoplasma
MSNTPLPSSFDAHPEFFQETKWQKFTRRIKEEPLIPIGYAATSYALWRAYKSMKAGDSIELNRMFRARIYGHAFTLFAIVAGGIYYGQERRQRKEFEKALQQKQDQEKRDAWLKELEIRDKEDKDWRQRHAAIEMAAKEAEKKRG
Cytochrome c oxidase subunit which plays a role in assembly of respiratory supercomplexes.
C0NUL6
P0AER8
GLTS_ECOLI
Glutamate permease
Escherichia
MFHLDTLATLVAATLTLLLGRKLVHSVSFLKKYTIPEPVAGGLLVALALLVLKKSMGWEVNFDMSLRDPLMLAFFATIGLNANIASLRAGGRVVGIFLIVVVGLLVMQNAIGIGMASLLGLDPLMGLLAGSITLSGGHGTGAAWSKLFIERYGFTNATEVAMACATFGLVLGGLIGGPVARYLVKHSTTPNGIPDDQEVPTAFEKPDVGRMITSLVLIETIALIAICLTVGKIVAQLLAGTAFELPTFVCVLFVGVILSNGLSIMGFYRVFERAVSVLGNVSLSLFLAMALMGLKLWELASLALPMLAILVVQTIFMALYAIFVTWRMMGKNYDAAVLAAGHCGFGLGATPTAIANMQAITERFGPSHMAFLVVPMVGAFFIDIVNALVIKLYLMLPIFAG
Catalyzes the sodium-dependent, binding-protein-independent transport of glutamate.
P0AER8
B2USP3
AROQ_HELPS
Type II DHQase
Helicobacter
MKILVIQGPNLNMLGHRDPRLYGMVTLDQIHEIMQTFVKQGNLDVELEFFQTNFEGEIIDKIQESVGSDYEGIIINPGAFSHTSIAIADAIMLAGKPVIEVHLTNIQAREEFRKNSYTGAACGGVIMGFGPLGYNMALMAMVNILAEMKAFQEAQQNNPNNPINNQK
Catalyzes a trans-dehydration via an enolate intermediate.
B2USP3
Q92IL5
THYX_RICCN
Thymidylate synthase ThyX
spotted fever group
MHNTTKRVTVPALEEILYEPIKVLDYGFIRVIDYMGDDSAIVQAARVSYGKGTKQLNQDKGLINYLLRHYHTTPFEMCDIKFHIKLPIFIARQWIRHRTASVNEYSARYSILGNEFYLPEPANIASQSAVNKQCREGDSLPKEVAEKVLAILEEDARQCYGHYKELMNADEEGNIIDENATGIARELARMNLTLNYYTEWYWKINLHNLLHFLRLRADPHAQYEIRVYAEKMLEIVKAWVPFVYEAFEEYRLQGANISRKGLDVIKRMINGEKVTHETSDMTKREWEELMKIFG
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as the reductant.
Q92IL5
Q6LNU2
PDXB_PHOPR
Erythronate-4-phosphate dehydrogenase
Photobacterium
MKILIDENMPYAAELFGQLGEVVTKPGRTLSADDLIDIDALMIRSVTKVNHNLISKANKLQFVGTATAGQDHVDQALLAERGITFTSAPGCNKVGVAEYVLSALMVIGQQQGFSIFDKTIGIIGAGNVGSYLAQCLDALGIPYLLNDPIKEQEGDTRQFHSLEAIKAQCDVITVHTPITKDGEYPTHHLINEAFIDALQPDAILINAARGPVTDNQALKKALQLSQSGLGKKLTAVLDVFEFEPHVDLELLPLLAFATPHIAGYGLEGKARGTTMVFNRYCAFLNIDQAVEASSLLPIAPVPNVSLSRKWDDATLFSLIQLIYDIRKDDALFRRNMVVTKGNEAQMATAFDQMRKNYWDRREYSAITVTGKVGFGVESLAKLGFTVVEDIQ
Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Q6LNU2
Q6FSW5
RCF1_CANGA
Respiratory supercomplex factor 1, mitochondrial
Nakaseomyces/Candida clade
MSRLPSSFDVEDADVEELSFADKIVYHCKQQPLVPIGTLLTTGAVILAAQNMRIGNRKKTQFYFRWRVGLQAATLAALVAGSFIYGKDKYDQKKKEDQMKEKAKLREQLWIKELERRDAEAQDRKKKAEAARLKTKENEAAIQKLEQELKELEAKASK
Cytochrome c oxidase subunit which plays a role in assembly of respiratory supercomplexes.
Q6FSW5
Q64689
SIA8C_MOUSE
Sialyltransferase St8Sia III
Mus
MRNCKMARVASVLGLVMLSVALLILSLISYVSLKKENIFTTPKYASPGAPRMYMFHAGFRSQFALKFLDQSFVPITNSLTHELQEKPSKWTFNRTAFLHQRQEILQHVDVIKNFSLTKSSVRIGQLMHYDYSSHKYVFSISNNFRSLLPDVSPIMNKRYNVCAVVGNSGILTGSQCGQEIDKSDFVFRCNFAPTEAFHKDVGRKTNLTTFNPSILEKYYNNLLTIQDRNNFFLSLKKLDGAILWIPAFFFHTSATVTRTLVDFFVEHRGQLKVQLAWPGNIMQHVNRYWKNKHLSPKRLSTGILMYTLASAICEEIHLYGFWPFGFDPNTREDLPYHYYDKKGTKFTTKWQESHQLPAEFQLLYRMHGEGLTKLTLSHCA
Catalyzes the transfer of sialic acid from a CMP-linked sialic acid donor onto the terminal sialic acid of an acceptor through alpha-2,8-linkages. Is active with alpha-2,3-linked, alpha-2,6-linked and alpha-2,8-linked sialic acid of N-linked oligosaccharides of glycoproteins and glycolipids. Displays preference for substrates with alpha-2,3-linked terminal sialic acid. It can form polysialic acid in vitro directly on alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid.
Q64689
P70691
UD12_MOUSE
UDP-glucuronosyltransferase 1A2
Mus
MDTGLCVPLRGISGLLLLLCALPWAEGAKVLVLPMEGSQWLSMRDVVRELHARGHQTVVLASEVTVHIKGEDFFTLKTYAFPYTKEEYQQEILSDIEKTFKTQHFVKAFFETTASIRNFFDLYSNSCIALLHNKMLIQQLNSSFFDVILTDPIFPCGAVLAKYLQIPAVFILRSLSCGIEYEATQCPNPSSYIPNLLTRLSDHMDFLQRVQNMLYYLVLKYICRLSITPYESLASELLQREVSLVEVLSHASVWLFRGDFVLDYPRPIMPNMVFIGGINCVTKKPLSQEFEAYVNASGEHGIVVFSLGSMVSEIPEKKAMEIAEALGRIPQTVLWRYTGTRPSNLAKNTILVKWLPQNDLLGHPKTRAFITHSGSHGIYEGICNGVPMVMMPLFGDQMDNAKRMETRGAGVTLNVLEMTADDLENALKTVINNKSYKENIMRLSSLHKDRPIEPLDLAVFWVEYVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAIVLTVVFIVFKCCAYGCRKCFGGKGRVKKSHKSKTH
UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds.
P70691
Q9XZK4
O165_CONST
Omega-conotoxin-like SO-5
Pionoconus
MKLTCVMIVAVLLLTACQLITADDSRGTQKHRSLRSTTKVSKSTSCMEAGSYCGSTTRICCGYCAYFGKKCIDYPSN
Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav).
Q9XZK4
A4XQ00
RL9_PSEMY
50S ribosomal protein L9
Pseudomonas
MEVILLEKIANLGNLGDKVNVKAGYGRNFLLPQGKATAATAENVAAFEARRAELEKLAAEKKASAEARAAQLAELEVTITATAGDEGKLFGSIGTHDIADALTASGVEVAKAEVRLPNGTIRQVGEYDVALHLHTDVEATVKVIVVAA
Binds to the 23S rRNA.
A4XQ00
F1MRW8
RN169_BOVIN
RING-type E3 ubiquitin transferase RNF169
Bos
MSGRAKVAGEEALVGVAAPQPVPAGILDECTNVTVSQPPSPPRPEESDCAGCLETPGEAAALPCGHSLCRGCAQRAADAAGPCCPRCRARGAGWARRRARDDWQADAEVLGERARRGPPERCRPRRDGGAAAAGPRPEQESRAAPAEPEFIFRAPIKLSKPGEFREEYESLRKLREEKLQEEKTSEDQIHKLLPEDTEIGKRKMDEQKKRDEPVVLKTNLEHCPARLSDSENEEPSRGKMIQTHRSAFVSKSSSYSLAFLAGNLNSKMERSQSCSDTGQDRAKSRLRAAPTSKAKATAMTPTSNPIIGVLLSTRNHRCLSAPDLTVEKRLPFSSLSALASLHKPERSISPESNDSISEELNHFKPIVCSPCTPPKRLPDGRVLSPLIIKSTPRNLNRSLQKQTSYEASPRILKKWEQIFQERQIKKTLSKATLTSLAPETGDDLLVSEVTQSNKEKPLLALNTRLSSGQVLSECTGPTAPDLDYFSSVSQTKAEQGSDRKKNTEIPLETCCSSELPVGASGTSLEREQSERSGSSPDAKLDKTRITASMKISAVNSVLPKNSVLGGVLKTKKQLKTVNHFDLPNGVLADNLGDEPLPSLRRGRKRRCKTKHLEQNGSLKKLRQSSGEVGLAPTDPVLREMEQKLQQEEEDRQLALQLQRMFDNERRTVSRRKGSVDQYLLRSSSMAGAK
Probable E3 ubiquitin-protein ligase that acts as a regulator of double-strand breaks (DSBs) repair following DNA damage. Functions in a non-canonical fashion to harness RNF168-mediated protein recruitment to DSB-containing chromatin, thereby contributing to regulation of DSB repair pathway utilization. Once recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168, competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby favouring homologous recombination repair (HRR) and single-strand annealing (SSA) instead of non-homologous end joining (NHEJ) mediated by TP53BP1. E3 ubiquitin-protein ligase activity is not required for regulation of DSBs repair.
F1MRW8
Q84ND0
TPS2_ANTMA
Terpenoid synthase Oc15
Antirrhinum
MAFCISYVGALLPCSLSTRTKFAICHNTSKLHRAAYKTSRWNIPGDVGSTPPPSKLHQALCLNEHSLSCMAELPMDYEGKIKETRHLLHLKGENDPIESLIFVDATLRLGVNHHFQKEIEEILRKSYATMKSPIICEYHTLHEVSLFFRLMRQHGRYVSADVFNNFKGESGRFKEELKRDTRGLVELYEAAQLSFEGERILDEAENFSRQILHGNLAGMEDNLRRSVGNKLRYPFHTSIARFTGRNYDDDLGGMYEWGKTLRELALMDLQVERSVYQEELLQVSKWWNELGLYKKLNLARNRPFEFYTWSMVILADYINLSEQRVELTKSVAFIYLIDDIFDVYGTLDELIIFTEAVNKWDYSATDTLPENMKMCCMTLLDTINGTSQKIYEKHGYNPIDSLKTTWKSLCSAFLVEAKWSASGSLPSANEYLENEKVSSGVYVVLVHLFCLMGLGGTSRGSIELNDTQELMSSIAIIFRLWNDLGSAKNEHQNGKDGSYLNCYKKEHINLTAAQAHEHALELVAIEWKRLNKESFNLNHDSVSSFKQAALNLARMVPLMYSYDHNQRGPVLEEYVKFMLSD
Contributes to floral scent emission.
Q84ND0
Q9VWL5
INX5_DROME
Innexin inx5
Sophophora
MFSAVKPLSKYLQFKSIRIYDSVFTIHSRCTVVILLTCSLLLSARQYFGDPIQCISEEKNIEYIQSYCWTMGTYILKLDDFGDQEQALVSPNQEVSYNSAFFSSATTNAPQSSSRVRTRPHFRSSLRRIGEYNEAYARSLSIAEGVGPEIRGQTERQYLRYYQWVIILLLFQSFVFYFPSCLWKVWEGRRLKQLCSEVGDALLSEETYNTRLRMLVKYFTTDYEDMHFCYMAKYVFCEVLNFLISVVNIIVLEVFLNGFWSKYLRALATIPFYDWDRWNRVSSSVFPKIAKCEVLKFGGSGTANVMDNLCILPLNILNEKIFVFLWAWFLLMALMSGLNLLCRLAMICSRYLREQMIRSQLRFMTKRHVKRALRDLTIGDWFLMMKVSVNVNPMLFRDLMQELCELRTSASGSTLESPV
Structural component of the gap junctions.
Q9VWL5
Q5G8B1
NDB2T_TITCO
Anionic peptide clone 8
Tityus
MVSKSLIVLLLVSVLVSTFFTTEAYPASYDDDFDALDDLDDLDLDDLLDLEPADLVLLDMWANMLDSQDFEDFE
May be an antimicrobial peptide.
Q5G8B1
O88637
PCY2_RAT
Phosphorylethanolamine transferase
Rattus
MIRNGHGAGGAAGLKGPGGQRTVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKHNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHHSSQEMSSEYREYADSFGKPPHPTPAGDTLSSEVSSQCPGGQSPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKRPYVIAGLHFDQEVNRYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYSVTAELLNHFKVDLVCHGKTEIVPDRDGSDPYEEPKRRGIFCQIDSGSDLTTDLIVQRIIKNRLEYEARNQKKEAKELAFLEALRQQEAQPRGETD
Ethanolamine-phosphate cytidylyltransferase that catalyzes the second step in the synthesis of phosphatidylethanolamine (PE) from ethanolamine via the CDP-ethanolamine pathway. Phosphatidylethanolamine is a dominant inner-leaflet phospholipid in cell membranes, where it plays a role in membrane function by structurally stabilizing membrane-anchored proteins, and participates in important cellular processes such as cell division, cell fusion, blood coagulation, and apoptosis.
O88637
A4WPT1
NADD_CERS5
Nicotinate mononucleotide adenylyltransferase
Cereibacter
MVVGLLGGSFDPPHAGHVHISLEALKRFRLDRVWWLVSPGNPLKPRPPAPLPARLAEARRLMRHPRVVVTDIEARLGTRFTAETLAALRARYPGVRFVWLMGADNLAQFHRWDRWQGIMRTVPVGVLARPGAGLRSRTSPAARIYARARVGAADLAAARPPAWCFLNLPMVDLSSTAIRATGRWR
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
A4WPT1
Q2YMD1
PDXH_BRUA2
Pyridoxal 5'-phosphate synthase
Brucella
MEPVKMTNSSDDFTQSAEPFKLFAEWLADAAKSEPNDPNAVALATVDPDGLPNVRMVLLKDFDETGFVFYTNYESKKGQEILSAEKAAMCFHWKSLRRQVRVRGPVEKVSDAEADAYYASRPRGSRIGAWASKQSRPLESRFALEKAVAEYTAKYAIGDIPRPPYWSGFRIRPVSIEFWHDRPFRLHDRVLFTRPTPEGDWNKDRLYP
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Q2YMD1
B8HAZ5
ATP6_PSECP
F-ATPase subunit 6
Pseudarthrobacter
MIALALPAQDSGEFTPPGINEMHLPAILPWGAAEGFSKQMLLVLLSVVFIAVFFVLAARKQQLVPGKLQFAGEAAYGFVRNGIAKDIIGGRDFIKYVPLLFSLFFFILVNNIYGAIPLIQLPTFSHVGGAYVLAGIVYFTWIAIGIKKNGLRYFKLATVPSGVPWFILPIVIPIEIISNFVVRPVTHSLRLFATMLAGHLIVMIAGSGIEYLVMQESILLKGTSVLVLAGAIAMYMLEALIMVLQAYVFTLLTAIYIEGALHADSH
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
B8HAZ5
Q7VQL3
DNAJ_BLOFL
Chaperone protein DnaJ
Candidatus Blochmannia
MVKSDYYEILGVSKNADEREIKKSYKRLAMKFHPDRNPGDVSAESKFKEIKEAYEVLSNPEKRSAYDQYGHAIFEQNSGGMGGSNTGGSDFSDIFGDVFGDIFGGSRRSRSRRGSDLRYDIELSLEEAVKGVVREICVPTLVTCLQCRGSGAKSSASIVSCVTCHGHGQIQMRQGFFSVQQSCPSCNGHGKIIKEICNKCRGSGRIERTKTLSVKIPAGVSTGDRIRLSGEGESGKNGAPAGDLYVQVQIKKHPIFDREEKNLYCEVPISFSMAALGGEIEVPTLDGRVKLKIPPETQTGKLFRMRGKGVKSVRGIGGHGDLLCRVVVETPVRLSDRQKQLLQDLSDSFGGPYGHKNSPKSKTFFDGVKKFFDDLTR
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Q7VQL3
Q88D09
MCPQ_PSEPK
Methyl-accepting chemotaxis protein McpQ
Pseudomonas
MYQWLAQSLGNVSVNRKLGLGFGLVLLLTLAITLTGWHGMDSIIDRGDKLGNISVIQQYTQELRIARQQYDRRRDDASLAELEKALSNLDRQVQLMLGQIEQPADHQRLEQQREAVRIYQQAFNELKQADQRREASRDVLGSSADKAVDLIGRVQRSLLQGANINQYQHAVDVSALLQQARFQVRGYTYSGNADYQQTALKAIDQALAELRALPAKVPAEHAASLDDAATAMGGYRDAVTQFGNAQLASEQALQRMVEQGTVLLQASQMMTASQTEVRDAAAAQAKTLLTVATVLALALGLLAAWAITRQIIIPLRQTLRAAERVASGDLTQSLQVQRRDELGQLQASMHRMTQGLRELIGGIGDGVTQIASAAEELSAVTEQTSAGVNNQKVETDQVATAMNQMTATVHEVARNAEQASEAALMADQQAREGDRVVGEAVAQIERLASEVVNSSEAMNLLKTESDKIGSVLDVIKSVAQQTNLLALNAAIEAARAGEAGRGFAVVADEVRSLAQRTQQSTEEIEELIAGLQSGTQRVASVMDNSRQLTDSSVELTRRAGSSLETITRTVSSIQAMNQQIATAAEEQTAVAEEINRSVMNVRDISDQTSAASEETASSSVELARLGTHLQGLVGRFRL
Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. McpQ recognizes specifically citrate and citrate/metal(2+) complexes. Binds citrate/metal(2+) complexes with higher affinity than free citrate, and mediates preferentially chemotaxis toward citrate/metal(2+) complexes.
Q88D09
A7IGG9
THIE_XANP2
Thiamine-phosphate pyrophosphorylase
Xanthobacter
MPKPFDLTLYLVTDPRLVAARGLLTTVDAAVKGGATIVQLRDPDAHGRALVEQARALKALLAPLGIPLIINDRVDVAVAADADGVHLGQDDMTPADARAVLGPQRILGLSVGNPAEYAASDLSGVDYLGVGPVKATGTKADAGGAIGAAGVGAVRALTRLPLVGIGGLATADVADVIRAGADGVAVVSSICAASDPEQAARALKAAVLAAR
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
A7IGG9
P25437
FRMA_ECOLI
Glutathione-dependent formaldehyde dehydrogenase
Escherichia
MKSRAAVAFAPGKPLEIVEIDVAPPKKGEVLIKVTHTGVCHTDAFTLSGDDPEGVFPVVLGHEGAGVVVEVGEGVTSVKPGDHVIPLYTAECGECEFCRSGKTNLCVAVRETQGKGLMPDGTTRFSYNGQPLYHYMGCSTFSEYTVVAEVSLAKINPEANHEHVCLLGCGVTTGIGAVHNTAKVQPGDSVAVFGLGAIGLAVVQGARQAKAGRIIAIDTNPKKFDLARRFGATDCINPNDYDKPIKDVLLDINKWGIDHTFECIGNVNVMRAALESAHRGWGQSVIIGVAVAGQEISTRPFQLVTGRVWKGSAFGGVKGRSQLPGMVEDAMKGDIDLEPFVTHTMSLDEINDAFDLMHEGKSIRTVIRY
Has high formaldehyde dehydrogenase activity in the presence of glutathione and catalyzes the oxidation of normal alcohols in a reaction that is not GSH-dependent. In addition, hemithiolacetals other than those formed from GSH, including omega-thiol fatty acids, also are substrates.
P25437
P46606
HD1_BRANA
Homeobox protein HD1
Brassica
MQEAALGMIGATVGGGGDGDAAVVAEQNRQMKGEIATHPMYDQLLAAHVACLRVATPIDQLPIIEAQLSHSHHLLRSYASTAVGFSHHDRQELDNFLAQYVMVLCSFKEQLQQHVRVHAVEAVMACREIENNLHSLTGATLGEGSGATMSEDEDDLQMDFSSDNSGVDFSGGHDMTGFGPLLPTESERSLMERVRQELKLELKQGFKSRIEDVREEIMRKRRAGKLPGDTTTVLKNWWQQHCKWPYPTEDDKAKLVEETGLQLKQINNWFINQRKRNWHNNSHSLTSLKSKRKH
Possible developmental regulator.
P46606
Q494C2
ATPE_BLOPB
F-ATPase epsilon subunit
Candidatus Blochmannia
MSECTYYLTVVSVEREIFSGVVRKIQVTGIEGEMGVFPGHTPLLTSIKPGVLRIVKSHDNEEYIYISGGILEVQRNIVTILADTAIRAEELDEKKAKEAKHEAEKHIKNYRHSSDIDYIKITSDISKAIAKLRLMELTKKNKYM
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Q494C2
Q662I1
FLIW_BORGP
Flagellar assembly factor FliW
Borreliella
MINEKSIGFDFPEGILGFENIKKFIIKDSKYKPFSIMQSINKEVSFLVTSPFNFLSEYLPNIQEKDWSDIKAKEEDERVILCIINMHVNDYKDITANLKAPIIINKKKLLGKQAICTNEKYSLHHKVFKE
Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum.
Q662I1
P35852
PURL_LACCA
Phosphoribosylformylglycinamidine synthase subunit II
Lacticaseibacillus
MYVVHVEMSPEAIATQKPYLDLGLTEAEYDRFAELIGHQPNDTEIGLASGMWSEHCAYKYSKPVLRQFWTKNERVLMGPGEGAGVIDIGEGKAVVFKAESHNHPSAVEPYEGAATGVGGIIRDIFSIGAKPVAMLDSLAFGDIEQPHTQHLVDRIVAGIGGYGNAIGIPTVGGETNFDGSYTRNPLVNAMCVGIMDKDQIQKGKAAGVGNALIYVGAKTGRDGINGASFASGDFSDEEAADRSAVQVGDPFMEKLLMDACLEITGHHQEALVGIQDMGAAGLVSSSVEMAGKANSGMVLDLDLIPQREAEMTPFEIMLSESQERMLLCVRAGFEQEVLAVFADYDLDAAIVGHVIAGHQYQLYHHGKLVCDVPVSSLTDDAPIYHQQGKMPKRLAQPAADFDPIITDPVQIWTDMMAMPTIADKSSLYKRYDAQVQTNTVVLPGSDAAVIRIRGTHRALAMTTDSKDVTCILIAGGCGNECWLKRARNLVASGAEPLGITDCLNFGDPTKPEAFYELAEAAKGIIAATKAFNAPVISGNVSLYNETNGEAIYPTPMIGMVGLIEDLSTITTAAFKQADDLIYLVGETHGDFNGSELQKLQTGEVTGKLFDFDLEAEKQHQHFVLKAIREHLITAAHDLSDGGLLVALAEMGFDAQLGAQINVTLPTAWGFSETQGRFLLTVSPENQAAFEALHGPAQLIGRVQAPPEFEVTTVNQHFSASLQQLQTAFEEALPCHMNQKA
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
P35852
Q2NHQ3
CBIA_METST
Ni-sirohydrochlorin a,c-diamide synthetase
Methanosphaera
MKRVVLTGTGSGVGKTTIATGIMKALSDEHKIQPFKVGPDYIDPSYHNCATGVSSRNLDSFFMSDGQIRQSFKNGMTSSHADYGIIEGVRGLYEGISPTNDIGSTSSIAKALNSPVILIINSRSLVRSAAAMTLGFKALDSRIDIEGVILNNVKSQKHYLKTKEAVEKLANTRVLGGIERDNSISMEQRHLGLIPAVEQERISGLVEKWGELIRENIDLDALMEIMDNSNPIINEYEPIWSPNKTKHKTRIAVPFDEAFNFYYKENLEALEYNNAKIEYFSPIHDEQLPSVDALYIGGGYPEIFKKELSKNTTMLESIKEFSQDNHPIYAECGGLMYLCKTIDSLPMVDVFPYHSMLTKRVQGLSYTIAHVQRDNPILKKNTTYHGHEFHYSKVEYTGSNSNDFAFSMRRGVGITGKYDGLLKNNTLASYIHTHTACLPDFGYNFTQSAYENK
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.
Q2NHQ3
B6JNC0
TRPD_HELP2
Anthranilate phosphoribosyltransferase
Helicobacter
MKEILNALYHQKDLSDKEVKKLFTLIIHEKVSPVQLGAILCALKIKGESFKEISVAATTLLEHAPKPFDSGLDLIDNCGTGGDGLKTINISTIAALIASSMGLSMAKHGSRSVSSHSGSADLLENLGVNIEMDPTQLENCFKQTHFGFLFAPLYHQSFKKSAPLRKELFTKTIFNCLGPLINPLRPKIQLLGVYDKSLCKTMALALKALGVKRAMVVNGGGTDEIVLHDITHAYELKNNEILEYDLNAKDFDLPPYDLKELQIENAQESVQACLDILENKGKDSHTMVVVANVASLLYLSHKAKDLKEGVSMTLEHLKTKAPYVHLQKIIRLSHA
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
B6JNC0
Q6D159
UPPP_PECAS
Undecaprenyl pyrophosphate phosphatase
Pectobacterium
MTDLHSLLIAFILGVVEGLTEFLPVSSTGHMIIVGHWLGFVDEKAKTFEVIIQLGSILAVVVMFWRRLFGLIGIHFGKVPHEGKTSGRLKLTHILLAMIPAVVLGLIFHDVIKSLFYPQNVMYSLVIGGFLLLAAEWFKPKEPRAVGLDDITHRQAFMIGCFQCLALWPGFSRSGATISGGMLMGVSRYAASEFSFILAVPMMMGATVLDLYKSWHFLSLADVPMFAVGFVTAFVVALIAIKTFLKIIKRISFIPFAIYRFIVAGVVYMVFM
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Q6D159
A5WG13
ENO_PSYWF
2-phosphoglycerate dehydratase
Psychrobacter
MYAENITNAVEIQDIRAREILDSRGNPTIEADVILADGSMGRAAAPSGASTGSREALELRDGDKSRYLGKGVTKAVANVNSQIRSALLESDATDQQGIDNILIELDGTANKDHLGANAMLAVSLATAKAAAISQNLPLHQYIANLRGQTSLTMPVPMMNILNGGEHADNTVDIQEFMIEPTGFSSFSEALRAGVEIFHSLKSVLKSQGLNTAVGDEGGFAPNLRTNEEAITVIMQAIEQAGYKAGKDIHLALDCAASEFYKNGQYILAGEGNKTFDSQGFSDYLVKLTEQYPIISIEDGLDESDWEGWAYLTSKLGKKVQLVGDDLFVTNPAILQEGIDKQIANAILIKFNQIGTLSETLDAIYLAKKNGYATVISHRSGETEDSTIADLAVGTAAGQIKTGSLCRSDRVAKYNQLLRIEQQVRASYRGGEEFIGLRG
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
A5WG13
Q2I2R5
CLE1_CONLT
Alpha-conotoxin LtXIVA
Elisaconus
MKLSVMFIVFLMLTMPMTCAGISRSATNGGEADVRAHDKAANLMALLQERMCPPLCKPSCTNCG
Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them . This synthetic peptide displays analgesic activity in a hot plate assay . Analgesia is also observed against second phase pain in formalin-induced inflammatory pain model, and in a rat model of mechanically-induced pain . Effects downstream of nAChR are inhibition of calcium influx, inhibition of ERK1/2 phosphorylation and inhibition of c-fos/NOS expression . Genes associated with drug dependence are not up-regulated by this toxin . Treatment with this toxin reversed morphine withdrawal symptoms in mice .
Q2I2R5
Q3JE31
CCA_NITOC
Phosphatase
Nitrosococcus
MEVYLVGGAVRDKLLGRPVKERDYVVVGTTPANLLAQGYRPVGKDFPVFLHPQTQEEYALARTERKTGPGYKGFEVDAAPDVTLEEDLQRRDLTINAIAEAADGSLLDPFGGQQDLARGILRHVSPAFAEDPVRILRAARFAARFNFKVAPETLALMEAMVTAGEADHLVPERVWRELERALGESYPRRFFEILRACGALARIFPEIECLFGVPQPRRYHPEIDTGIHTLKVLEIAAHLSSDTQVRFAALTHDLGKGQTPSHEWPHHYGHGERGVALVLTLCQRLRVPKAYQALAVQVARYHNLVHQAQELRPGTILKLLNRVDAFRRPSRFEQFLLACEADARGRSGLENRPYPQANQLRLAFRAAAAVTARPLVAAGLRGEAIAEQLQQQRIKAIKQAVHTERG
Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases.
Q3JE31
A7MPG4
RS8_CROS8
30S ribosomal protein S8
Cronobacter
MSMQDPIADMLTRIRNGQAANKAAVTMPSSKLKVAIANVLKEEGFIEDFKVEGDTKPELELTLKYFQGKAVVESIQRVSRPGLRIYKKKDELPKVMAGLGIAVISTSKGVMTDRAARQAGLGGEIICYVA
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
A7MPG4
B7IRS8
UNG_BACC2
Uracil-DNA glycosylase
Bacillus cereus group
MENVLRNDWGPLLAPEFEKEYYLTLSSFLTEEYSTHVVYPKVEDIFNALQYTSYENTKVVILGQDPYHGPNQAHGLSFSVQPGVKTPPSLLNMYKELRDEYGYEIPNNGYLVKWAEQGVLLLNTVLTVRQSEANSHKGKGWEHFTDRVIQLLNEREKPVIFILWGRHAQAKKKLITNPNHHIIESVHPSPLSARRGFFGSKPYSKVNTILANMGEREIDWEIPNL
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
B7IRS8
Q11GG5
GREA_CHESB
Transcript cleavage factor GreA
unclassified Chelativorans
MNKVPMTLAGYESLKEELRWRQQEERPRIIEAIAEARAHGDLSENAEYHAAKEAQSLNEGRISELEDLIARAEVIDVTKLSGDTVKFGATVVLVDEDTEEEKTYQIVGDQEADVKSGRISISSPIARALIGKGVGDLIEVNAPGGARGYEVLRVQYG
Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides.
Q11GG5
A8AYI5
ARGB_STRGC
NAG kinase
Streptococcus
MKDVIVIKIGGVAAKKLSDKFIKQMQEWIAAGKKIVVVHGGGLVINQLMKERQLPTRKVKGLRVTAKSDLPIIQQALLGQVGRTLTQELNYSDIESLQLVSHLGKTVSADFIDKDVYGYVGQVKAIQTAYLEQLLAADIVPVLASLGENAAGELLNINADYLAAAVASSLQAEKLILMTDIEGVLEDKKVLPQILTSQVSKKIQTGVIKGGMIPKIESAVQTVLSGVGQVLIGDNLLTGTLIAEG
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
A8AYI5
Q636L3
IF2_BACCZ
Translation initiation factor IF-2
Bacillus cereus group
MSKIRVHEYAKKHNISSKDLMTKLKEMNIEVSNHMTMLDDEVVNKLDNEYQAEKPSVADEFEVEEKVVRSKKNSNKKKKKGKGNEDKRQENFAGRQQTQTVETPDKITFSGSLTVGDLAKKLSKEPSEIIKKLFMLGIMATINQDLDKDTIELIANDYGIEVEEEVIVSETEFETFIDEQDDEENLKERPAVVTIMGHVDHGKTTLLDSIRNSKVTAGEAGGITQHIGAYQVEVNDKKITFLDTPGHAAFTTMRARGAQVTDITILVVAADDGVMPQTVEAINHAKAAGVPIIVAVNKMDKPAANPDRVMQELTEYELVPEAWGGDTIFVPISAIQGEGIDNLLEMILLVSEVEEYKANPNRYATGTVIEAQLDKGKGTIATLLVQNGTLRVGDPIVVGTSFGRVRAMVSDIGRRVKVAGPSTPVEITGLNEVPQAGDRFMAFADEKKARQIGESRAQEALLAQRGEKSKLSLEDLFQQIQEGDVKEINLIVKADVQGSVEAMAASLRKIDVEGVKVKIIHTGVGAITESDIILASASNAIVIGFNVRPDVNAKRTAELENVDIRLHRIIYKVIEEIEAAMQGMLDPEFEEKVIGQAEVRQTFKVTKVGTIAGCYVTDGKITRDSGVRIIRDGVVIFEGQLDTLKRFKDDVKEVAQNYECGITIERYNDLKEGDIIEAYIMEEVKR
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
Q636L3
A1TJT2
RL6_ACIAC
50S ribosomal protein L6
Acidovorax
MSRVGKMPVAIPNGVDVTITEEQISVKGSGGTLSVAQNRLVKIVNKDGKLSFEPADESREANAMSGTIRQLVNNMVVGVSKGFEKKLNLIGVGYKAQASGAKLNLAVGYSHPVNFDMPAGITVATPTPTEIVIKGADRQRVGQLAAEIRAVRPPEPYKGKGIRYSDEKVTIKETKKK
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
A1TJT2
Q64578
AT2A1_RAT
Endoplasmic reticulum class 1/2 Ca(2+) ATPase
Rattus
MEAAHSKSTEECLSYFGVSETTGLTPDQVKRHLEKYGPNELPAEEGKSLWELVVEQFEDLLVRILLLAACISFVLAWFEEGEETVTAFVEPFVILLILIANAIVGVWQERNAENAIEALKEYEPEMGKVYRADRKSVQRIKARDIVPGDIVEVAVGDKVPADIRILSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAVGIVATTGVSTEIGKIRDQMAATEQDKTPLQQKLDEFGEQLSKVISLICVAVWLINIGHFNDPVHGGSWFRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCKMFIIDKVDGDICSLNEFSITGSTYAPEGEVLKNDKPVRAGQYDGLVELATICALCNDSSLDFNETKGVYEKVGEATETALTTLVEKMNVFNTEVRSLSKVERANACNSVIRQLMKKEFTLEFSRDRKSMSVYCSPAKSSRAAVGNKMFVKGAPEGVIDRCNYVRVGTTRVPLTGPVKEKIMSVIKEWGTGRDTLRCLALATRDTPPKREEMVLDDSAKFMEYEMDLTFVGVVGMLDPPRKEVTGSIQLCRDAGIRVIMITGDNKGTAIAICRRIGIFSENEEVADRAYTGREFDDLPLAEQREACRRACCFARVEPSHKSKIVEYLQSYDEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMDRPPRSPKEPLISGWLFFRYMAIGGYVGAATVGAAAWWFLYAEDGPHVSYHQLTHFMQCTEHNPEFDGLDCEVFEAPEPMTMALSVLVTIEMCNALNSLSENQSLLRMPPWVNIWLLGSICLSMSLHFLILYVDPLPMIFKLRALDFTQWLMVLKISLPVIGLDELLKFIARNYLEG
Key regulator of striated muscle performance by acting as the major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction.
Q64578
Q885J7
ASTD_PSESM
Succinylglutamic semialdehyde dehydrogenase
Pseudomonas
MSTLYIAGAWQAGQGELFHSLNPVTLHVLWSGQGATAEQVDHAVQAARQAFPAWALLSLDQRIAVLDAFAVSLKAHADELANCIGEETGKPLWESATEVTSMVNKIAISVQSYRERTGEKSAPLGDATAVLRHKPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVLFKPSELTPKVAELTVKCWIEAGLPAGVLNLLQGGRETGIALAANPGIDGLFFTGSSRTGNALHQQFAGRPDKILALEMGGNNPLVVDQVQDIDAAVYTIIQSAFISAGQRCTCARRLLVPEGDWGDALLARLVAVSATLDVGAFDQQPAPFMGSVISLEAARALLDAQRHLLANGAVTLLEMRQPQPGAALLTPGIVDVSAVANRPDVELFGPLLQVVRYAGFDAAIAEANATQYGLAAGLLSDSEARYQQFWLQSRAGIVNWNKQLTGAASSAPFGGVGASGNHRASAYYAADYCAYPVASLETGSLTLPATLTPGVRLS
Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Q885J7
Q9P359
PGLR2_ASPAW
Polygalacturonase X2
Aspergillus
MHSFASLLRYGLAAGATLASASPIEARDSCTFTTAAAAKAGKAKCSTITLDSIKVPAGTTLDLTGLTSGTKVIFEGTTTFDYEDWAGPLISMSGKDITVTGASGHLINCDGSRWWDGKGTSGKKKPKFFYAHGLDSSSITGLNIKNTPLMAFSVESDDITLTDITINNADGDSLGGHNTDAFDVGNSVGVNIIKPWVHNQDDCLAINSGENIWFTGGTCIGGHGLSIGSVGDRSNNVVKNVTIEHSTVSNSENAVRIKTISGATGSVSEITYSNIVMSGISDYGVVIQQDYEDGKPTGKPTNGVTITDVKLESVTGTVDSKATDIYLLCGSGSCSDWTWDDVKVTGGKKSSACKNLPSVASC
Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.
Q9P359
P23833
SCO1_YEAST
Protein SCO1, mitochondrial
Saccharomyces
MLKLSRSANLRLVQLPAARLSGNGAKLLTQRGFFTVTRLWQSNGKKPLSRVPVGGTPIKDNGKVREGSIEFSTGKAIALFLAVGGALSYFFNREKRRLETQKEAEANRGYGKPSLGGPFHLEDMYGNEFTEKNLLGKFSIIYFGFSNCPDICPDELDKLGLWLNTLSSKYGITLQPLFITCDPARDSPAVLKEYLSDFHPSILGLTGTFDEVKNACKKYRVYFSTPPNVKPGQDYLVDHSIFFYLMDPEGQFVDALGRNYDEKTGVDKIVEHVKSYVPAEQRAKQKEAWYSFLFK
Required for the accumulation of subunits 1 and 2 of cytochrome c oxidase complex. Thought to play a role in either mitochondrial copper transport or insertion of copper into the active site of COX.
P23833
C5CHW7
ARGC_KOSOT
N-acetyl-glutamate semialdehyde dehydrogenase
Kosmotoga
MIRVGIIGATGYTGLELVRILTNHPDVKITFLSSRSFAGKKLNDVYPFSLKNETLEEIDPEKISKNCDVVFTALPAGVSYEIARKLKDVRIIDLGADFRFDDPAVYEEWYSKKLPDYDPTERVYGLTELYREKIKNARFVGNPGCYPTSVLLATAPLLKNGSLDEETIIVDSKSGVSGAGKKESIDYSFSELSGSLKAYNVSKHRHVPEMEQEMSKLCGKRLKLVFTPHLVPMVRGILSTIYVKTDLSLDEVYELYREYYGKEKFIHVLQPGVYPSTKWTYGSNHAFISMAKDDRTDTLILISVIDNLVKGASGQAVQNMNVMFSLAEDAGLSFNPIYP
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
C5CHW7
W6Q2D7
IFGG_PENRF
Old yellow enzyme homolog ifgG
Penicillium
MTIIPKHPSPTLFKPLALGKCQLQHRIVMSPTTRYRADEAAVPLPFVKEYYAQRASDPGALLITEATNICPNSVGEAHIPGIWSKTQCEAWREVVSQVHAKECYIFCQIYATGRSADPELLASRGFEQVSSSAVAAEPGCQPPRALDEEEIQKYISDYAQAARNAIEVGFDGVEIHGANGYLIDQFTQASCNQRTDEWGGDIPNRARFALQVTMAVINAIGPDRVGMKLSPWSQYSGMGIMGDLVPQFEYLILQLRQLGIAYLHLANSRWLDQMTTHPDPNHLTFVKVWGRSLPVILAGGYDATSAPEVIEMVYADYDNVAIGFGRYFTSTPDLPFRMKNGIALQKYDRSSFYTCLTKTGYLDYPYSPEYLCRSS
Chanoclavine-I aldehyde reductase; part of the gene cluster that mediates the biosynthesis of isofumigaclavines, fungal ergot alkaloids . The tryptophan dimethylallyltransferase ifgA catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan . The second step is catalyzed by the methyltransferase ifgB that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of N-methyl-dimethylallyl-L-tryptophan . The catalase ifgD and the FAD-dependent oxidoreductase ifgC then transform N-methyl-dimethylallyl-L-tryptophan to chanoclavine-I which is further oxidized by ifgE in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde . The chanoclavine-I aldehyde reductases ifgG and/or fgaOx3 reduce chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline . The festuclavine dehydrogenases ifgF1 and/or ifgF2 then catalyze the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine . Hydrolysis of festuclavine by a yet undetermined cytochrome P450 monooxygenase (called ifgH) then leads to the formation of isofumigaclavine B which is in turn acetylated by ifgI to isofumigaclavine A . Penicillium roqueforti has interestingly at least two sets of genes for the consumption of chanoclavine-I aldehyde on three different loci, the OYEs ifgG/fgaOx3 and the festuclavine synthase homologs ifgF1/ifgF2 . The reason for the duplication of these genes is unclear, probably to ensure the conversion of chanoclavine-I aldehyde by differential gene expression under various environmental conditions .
W6Q2D7
A6V1E5
LPXB_PSEA7
Lipid-A-disaccharide synthase
Pseudomonas
MAGRLRVALVAGEASGDILGSGLMQALRARHPEIEFIGVGGPRMEAEGLSSYFPMERLSVMGLVEVLGRLPELLRRRKRLIRTLIDARPDVMIGIDAPDFTLGVEHRLRQAGLRTVHYVSPSVWAWRQKRVLKIREACDLMLALFPFEARFYEEHGVPVRFVGHPLANTIPLQADRVAARERLGLPLDGQVVALMPGSRGGEVGKLGELFLDTAQRLLGERPGLRFVLPCASAARREQIERMLQGREPLPLTLLDGASHEALAACDAVLIASGTATLEALLYKRPMVVAYRVAGLTYRILKRLVKSPYISLPNLLAGRLLVPELIQDAATPRALATTLSPLLDDGSQQVEFFDAIHRALRQDASAQAAEAVLQLVERR
Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
A6V1E5
O55091
IMPCT_MOUSE
Imprinted and ancient gene protein
Mus
MAEEEVGNSQRQSEEIEAMAAIYGEEWCVIDENAKIFCIRVTDFMDDPKWTLCLQVMLPSEYPGTAPPSYQLNAPWLKGQERADLSNSLEEIYVHNMGESILYQWVEKIRDALIQKSQITEPDPDVKKKTEEVEVESEEDPILEHPPENPVKTLDLKISEETQPETEELPPVAHGVPITDRRSTFQAHVAPVVCPEQVKLVLAKLYENKKIASATHNIYAYRIFCEDKQTFLQDCEDDGETAAGGRLLHLMEILNVKNVMVVVSRWYGGILLGPDRFKHINNCARNILVEKNFTNTPDESTKNLGKKKVKKDKKKNDH
Translational regulator that ensures constant high levels of translation upon a variety of stress conditions, such as amino acid starvation, UV-C irradiation, proteasome inhibitor treatment and glucose deprivation. Plays a role as a negative regulator of the EIF2AK4/GCN2 kinase activity; impairs GCN1-mediated EIF2AK4/GCN2 activation, and hence EIF2AK4/GCN2-mediated eIF-2-alpha phosphorylation and subsequent down-regulation of protein synthesis . May be required to regulate translation in specific neuronal cells under amino acid starvation conditions by preventing GCN2 activation and therefore ATF4 synthesis . Through its inhibitory action on EIF2AK4/GCN2, plays a role in differentiation of neuronal cells by stimulating neurite outgrowth .
O55091
Q3AZE2
SYY_SYNS9
Tyrosyl-tRNA synthetase
unclassified Synechococcus
MPETNPSLPSWLNRGMADLFPAGEPSDVDQSLAARLAAAEAEGRPLRVKLGIDPTGSNIHLGHSILFRKLRAFQDAGHIAVLIIGDFTARIGDPTGKSATRVQLSKNDVAVNASTYLRQLGQDQPKETALLDFETPGRLEVRYNSEWLEGMDLPAVIGLLGTGTVGQMLAKEDFSNRYNSGTPIALHEFLYPLLQGYDSVAVNADVELGGTDQKFNVAMGRDLQRHFGRGTQFGLLLPILVGLDGAQKMSKTLGNTVGLEDDPLSMYSKLEKVGDTAINDYVTLLTDLNVEALPENPREKQKAMALAVTATRHGTDAAAKAQLDAGNLVGGAGDASADVPEASLLAVNFPAKAFYLMSAVGICASSSEARRQIKGGAARLDGEKITDPNQEFASAAELDGRVLQLGKKTFRRLTA
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Q3AZE2
B5FA77
RIMP_ALIFM
Ribosome maturation factor RimP
Aliivibrio
MTGLERQLTEMLEAPVGALGYELVGLEFVRAGEHSTLRVFIDHENGIFVEDCAEASRQISAVMDVEDPITVAYNLEVSSPGLERPLFKAAHYQQFVGHEVSLVLKMPMNNRRKWKGDILEVNGEIVTVTVDGNNEEFALSNISKANLVPKF
Required for maturation of 30S ribosomal subunits.
B5FA77
A6GWU1
EFTS_FLAPJ
Elongation factor Ts
Flavobacterium
MATITAADVNKLRTITGAGMMDCKKALVESDGDFDLAIENLRKKGQKVAANRSDRESTEGAAIAVVNADNTVGVVITLNCETDFVGMNENFVKMAVEMANLALNFNNKEEFLASDFNGITIADKLIEQTGVIGEKLEIRTFEKLEGAFVGSYIHSGNKIATLTAFSAKADGIEEAARNVAMQAAAMNPIALNEEGVDADTIAKEIEIAKDMLRAEGKPEAMIENIAKGKLGRFFKDNTLVNQDYIKDSSMSVANYVKSIDANLIVTGFKRAALG
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
A6GWU1
B4RVY8
DXS_ALTMD
1-deoxyxylulose-5-phosphate synthase
Alteromonas
MSLDLQHYPTLALAQTPDKLRQLPQDKLRELADELREYLLNSVSQTSGHFASGLGTVELTVALHYVYNTPFDRLLWDVGHQAYPHKILTGRAERMSTIRQKNGLHPFPWPPESEYDTFAVGHSSTSISAALGMAVAAEKEGKDRKVVSVIGDGAMTAGMAFEALNHAGDIKKDMVVVLNDNEMSISENVGALNSHLARLLTGNFFNSIRDGGKKLLSNVPPIKEFASRAEEHLKGMVVPGTIFEELGFNYIGPIDGHDVNAVVDTLRNMRNFDGPQLLHVVTKKGKGYAVAEEDPIKFHAVPKFNPADNALPKSKPSAPTYSAIFGQWLCDMAAQDPKLMAVTPAMREGSGMVEFSQRFPEQYFDVAIAEQHAVTFGAGLAKDGMNAVVAIYSSFLQRAYDQLIHDVAIQDLPVLFAIDRAGIVGADGPTHQGAFDIAFLRCIPNMVVMAPSDENECRQMLYTGHKLQKPAAVRYPRGAGMGVTPDEAMTALEIGKSRTCRETAKDKSESVAILNFGCLLPYALEAAVAIDATVIDMRFIKPLDGDAVLKAANEHSALITLEDGCIMGGAGSAVLEHLQQNGVLKAVKMLGLPDSFILQGTQQEMYKEHGLDAEGIIAAAKSLIG
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
B4RVY8
B1X9L5
FADI_ECODH
Fatty acid oxidation complex subunit beta
Escherichia
MGQVLPLVTRQGDRIAIVSGLRTPFARQATAFHGIPAVDLGKMVVGELLARSEIPAEVIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYSVSRACATSFQAVANVAESLMAGTIRAGIAGGADSSSVLPIGVSKKLARVLVDVNKARTMSQRLKLFSRLRLRDLMPVPPAVAEYSTGLRMGDTAEQMAKTYGITREQQDALAHRSHQRAAQAWSDGKLKEEVMTAFIPPYKQPLVEDNNIRGNSSLADYAKLRPAFDRKHGTVTAANSTPLTDGAAAVILMTESRAKELGLVPLGYLRSYAFTAIDVWQDMLLGPAWSTPLALERAGLTMSDLTLIDMHEAFAAQTLANIQLLGSERFAREALGRAHATGEVDDSKFNVLGGSIAYGHPFAATGARMITQTLHELRRRGGGFGLVTACAAGGLGAAMVLEAE
Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed.
B1X9L5
Q5MBR3
NCED5_ORYSJ
9-cis-epoxycarotenoid dioxygenase NCED5, chloroplastic
Oryza sativa
MPTTFTPNSPASSCSIHHRASPSRGARNSVRFTRPRAAAAATNSVLSAPSSVPPAYVPPPPPPPTKMFPEAGDAAAAKAAARRCGKKKDGLNFFQRAAAVALDAFEEGFITNVLERPHALPRTADPAVQIAGNFAPVGEQPPVRSLPVSGRIPPFINGVYARNGANPHFEPTAGHHLFDGDGMVHAVRIRNGAAESYACRFTETARLGQERALGRAVFPKAIGELHGHSGIARLALFYARGLCGLVDPSHGTGVANAGLVYFNGRLLAMSEDDLPYQVRVTADGDLETVGRYDFDGQLGCAMIAHPKLDPVSGELFALSYDVIKKPYLKYFYFDADGTKSPDVEIELEQPTMIHDFAITENFVVVPDHQVVFKLGEMFRGGSPVVLDREKTSRFGVLPKHATSSLEMVWVDVPDCFCFHLWNAWEEAESGEVVVVGSCMTPADSIFNESDEHLESVLTEIRLNTRTGESTRRAVLPPAAQVNLEVGMVNRAMLGRKTRYAYLAVAEPWPKVSGFAKVDLATGELTKFEYGEGRFGGEPCFVPMGGAGAAASPARGEDDGYILSFVRDEAAGTSELLVVNAADMRLEATVQLPSRVPYGFHGTFINAGELATQA
Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid biosynthesis from carotenoids.
Q5MBR3
O33347
RELF_MYCTU
Antitoxin RelF
Mycobacterium tuberculosis complex
MRILPISTIKGKLNEFVDAVSSTQDQITITKNGAPAAVLVGADEWESLQETLYWLAQPGIRESIAEADADIASGRTYGEDEIRAEFGVPRRPH
Induces its own promoter, in combination with RelG represses its own promoter. Has been seen to bind DNA in complex with toxin RelG but not alone.
O33347
Q8CN53
LRGB_STAES
Antiholin-like protein LrgB
Staphylococcus
MIEHLGINTPYFGILVSLIPFVIATYFYKKTNGFFLLAPLFVSMVAGIAFLKLTGISYENYKIGGDIINFFLEPATICFAIPLYRKREVLKRYWLQIFGGIAVGTIIALLLIYLVAITFQFGNQIIASMLPQAATTAIALPVSDGIGGVKELTSLAVILNAVVISALGAKIVKLFKISNPIARGLALGTSGHTLGVAAAKELGETEESMGSIAVVIVGVIVVAVVPILAPILL
Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like proteins CidA and/or CidB. The LrgAB and CidAB proteins may affect the proton motive force of the membrane. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses.
Q8CN53
Q6DGF6
F220A_RAT
STAT3-interacting protein as a repressor
Rattus
MRAGRGTLGVCLASVKQSQGGDLDKLACGLKRRSEKRNPSPSDVPSWTDQPVADTHGKSRAMAAASSEMKRDQSKASLILHSGFKALQYLKESMGRNSTPAASLSMAVVLSSAPSEEHGAGVSGGIGDTLGSDWPAREPRTTDSCGQYLKGEAWVSGWQGHPKVREVGFLRGEPLSAVPKGLGTRSELSYCSELCQLPYTYPYYEALPEDKTRCVSLDHLSPVFSEETVEDEKTLSSTSDGLQIVMGLLALQSSRLTSL
May negatively regulate STAT3.
Q6DGF6
Q1WTT3
PFKA_LIGS1
Phosphohexokinase
Ligilactobacillus
MKRIGILTSGGDAAGMNAAVRAIARSAMNAGLEAYGINYGYKGLVEGNIFKMESTKLDEIINRGGTILYSARFPEFAETETQLKGIEQLKKFGIEALVVIGGDGSYHGAEKLTMHGYNSIGVPGTIDNDIPGTDFTIGFDTAANVAMEALDRINDTATSHQRVFVVEVMGRGAGDIALWSGIATGADAIVIPEREYDIEAIANKISENRKNGKDHGLIVLAEGVMGAAEFKEKLDQYGDFDSRAITLGHIQRGGNPTVKDRVLATRLGDYAIRLLLEGKGGLAIGIHDNQLVATDIIDTLENHKHQTDVSLQDLNDRVRF
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Q1WTT3
Q057J0
OBG_BUCCC
GTP-binding protein Obg
Buchnera
MKFVDSVIINVSAGKGGDGCISFRREKFVPKGGPDGGNGGDGGNIWIVSNTNINTLTDYRIKKIFQSENGKNGLNSNRSGKNGKDIYIPVPLGTRIIDNDTKKIIIEILKINQKFLVAKGGKRGLGNTNFKSSINQTPRKKTYGTLGENKNILLELILIADIGTLGLPNSGKSTLITSMSNAKTKIDIYPFTTLIPILGTVKAKKKKFIIADIPGIIKNASLGIGLGIKFLKHLSRCKLLLHIIDITINKKKINKIRYIILKELKNFNKKLFQKTRWLIFNKIDLLKPKKISQIKKYIKKKIEKNKKYYFISAKKNIGIKKLSKDIIKYLYKKNKEYI
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Q057J0
P06352
H3_STRPU
Histone H3, embryonic
Strongylocentrotus
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTELRFQSSAVMALQEASEAYLVRLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
P06352
O47583
CYB_MOSMO
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Moschus
MTNIRKSHPLMKIVNNAFIDLPAPSNISSWWNFGSLLGICLILQILTGLFLAMHYTSDTMTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLFMHVGRGLYYGSYTFLETWNIGVILLFTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFILPFIIAALAMVHLLFLHETGSNNPTGITSDMDKIPFHPYYTIKDILGILLLILILMALVLFTPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILILIFMPLLHTSKQRSMMFRPLSQCLFWILVADLLTLTWIGGQPVEHPYIIIGQLASIMYFLLILVMMPVASMVENNLLKW
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
O47583
Q8EMZ1
RPIA2_OCEIH
Phosphoriboisomerase A 2
Oceanobacillus
MEYSDKQIAAQEAVRYIKDGMVIGIGSGSTVNEFLYCLAARMRKERLQVVGIPASKKSERLATELGIPLTTFATYQNVDIAIDGTDEIDDQLYLVKGGGGSLVREKMIDLVAETFIVIASGKKKIKKLGSFPVPVEVVPFGWQATEQRLQQFGCQTNLRMVEEDIFVSDNQNYIIDCDFKEIDDAEALHRSLKQIVGVIETGIFINMVDKAIVADNGELSILEK
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Q8EMZ1
Q8K363
DDX18_MOUSE
DEAD box protein 18
Mus
MSQLQMKLLRRKIEKRNAKLRQRNLKLQETSDTSLSQPQNGDVPKETGKGGKVKKALKRSVPVDSAEAQSGGMPEETLENGKVKKSPQKLTTLANGEAAPTPPPDSEVKKKKKKKRKMANDAGPDTKKAKTEESAEACEEPEDDVKKADDSEVPSLPLGLTGAFEDTSFASLSNLVNENTLKAIEEMGFKRMTEIQHKSIRPLLEGRDLLAAAKTGSGKTLAFLIPVIELIVKLKFMPRNGTGVLILSPTRELAMQTFGVLKELMTHHVHTYGLIMGGSNRSAEVQKLLNGINIIVATPGRLLDHMQNTPGFMYKNLQCLVIDEADRILDVGFEEELKQIIKLLPARRQTMLFSATQTRKVEDLARISLKKEPLYVGVDDDKEVATVDGLEQGYVVCPSEKRFLLLFTFLKKNRKKKVMVFFSSCMSVKYHYELLNYIDLPVLAIHGKQKQNKRTTTFFQFCNADSGILLCTDVAARGLDIPEVDWIVQYDPPDDPKEYIHRVGRTARGLNGRGHALLILRPEELGFLRYLKQSKVPLNQFDFSWSKVSDIQSQLEKLIEKNYFLHKSAQEAYKSYIRAYDSHSLKQIFNVNNLNLPQVALSFGFKVPPFVDLNVSSHDGKLKKRGGGGGFGYQKTKKVEKSKIFKHISKKPADRRQFSH
Probable RNA-dependent helicase.
Q8K363
B6J0W1
TIG_COXB2
PPIase
Coxiella
MRGNFMSSIEKLGGLKQRLTITVPAEEVDKAYKSRLLKVARTAKIPKFRPGKASPAVVEKLYGKAILQEVGSELIQSSLREAVEEHQLQVAGAPDIKMDKILRGEPFKYVVNFEVYPEITLESLAGETIERTQVEITEEDLDKMLEALRKQYAEWKEVDRPAKADDRVIIDFEGTLDGKPFERGSAKDFQLELGSKRMIAGFEEGIEGMKPGESKALDITFPADYPSEDLAGKAAVFNITLQKVMAPELPVLDEQFAERLGIKEGGLEALRQKVRTNMEKEVHHHMENKLKMAVLDKLIERNPIEVPESLIEAEIDHLQQMTRQQVAMQTHKPDEAKKMELPRDPYREQATKRVKLGLLLAEVVKQHKIKADPEQLRARVEEVAASYQDPEKVISWYYSNKQMLSEIESVVLEDQAVAQLMSELEVKDQAIPYEEAVKQIQQ
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
B6J0W1
Q08HK6
NU4LM_ZALCA
NADH dehydrogenase subunit 4L
Zalophus
MSMMYFNIFMAFTVSLVGLLMYRSHLMSSLLCLEGMMLSLFVMMSVTILNNHFTLASMAPIILLVFAACEAALGLSLLVMVSNTYGTDYVQNLNLLQC
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor.
Q08HK6
Q9NUE0
ZDH18_HUMAN
Zinc finger DHHC domain-containing protein 18
Homo
MKDCEYQQISPGAAPLPASPGARRPGPAASPTPGPGPAPPAAPAPPRWSSSGSGSGSGSGSLGRRPRRKWEVFPGRNRFYCGGRLMLAGHGGVFALTLLLILTTTGLFFVFDCPYLARKLTLAIPIIAAILFFFVMSCLLQTSFTDPGILPRATVCEAAALEKQIDNTGSSTYRPPPRTREVLINGQMVKLKYCFTCKMFRPPRTSHCSVCDNCVERFDHHCPWVGNCVGRRNYRFFYAFILSLSFLTAFIFACVVTHLTLRAQGSNFLSTLKETPASVLELVICFFSIWSILGLSGFHTYLVASNLTTNEDIKGSWSSKRGGEASVNPYSHKSIITNCCAVLCGPLPPSLIDRRGFVQSDTVLPSPIRSDEPACRAKPDASMVGGHP
Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates, such as CGAS, HRAS and LCK . Acts as a negative regulator of the cGAS-STING pathway be mediating palmitoylation and inactivation of CGAS . May also have a palmitoyltransferase activity toward the beta-2 adrenergic receptor/ADRB2 and therefore regulate G protein-coupled receptor signaling .
Q9NUE0
Q19443
SID5_CAEEL
Systemic RNA interference defective protein 5
Caenorhabditis
MPSKNCAKNLHACQWERDIALVFLGLMVLFNIGQVVYMNRARLYRLIRRGAEQIPADDEEPIIGIRD
Plays a role in RNA-mediated gene silencing by mediating transport of both ingested and endogenous dsRNA between cells. Not required for the uptake of dsRNA from the intestinal lumen.
Q19443
Q8ZY36
HIS1_PYRAE
ATP phosphoribosyltransferase
Pyrobaculum
MLLAVPSKGRLQEPTLKLLEAVGIRPLASDERALVVPTSWSDVNLIRARPEDIPYLVESGRVWAGITGHDYVVESGSNVAEVLELEFGRGKLVVAVPRSSGITSVEDLPPGARIATKFVNIAYNYFAELGKRVRIIRVTGSVEVLPQLGIADAILDVMATGTTLEVHGLVPIATVLETSARLVVNPQYVEHDLTKKLVTFIKGFYAAQGKKMVFLNVPASRLDAVLAVLPAMEAPSVTKLAKGDVYEVFSVVPEDVLPDLVMKLKEAGARDIVITPIEKLIV
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Q8ZY36
B7LEG3
TRUD_ECO55
tRNA-uridine isomerase D
Escherichia
MIEFDNLTYLHGKPQGTGLLKANPEDFVVVEDLGFEPDGEGEHILVRILKNGCNTRFVADALAKFLKIHAREVSFAGQKDKHAVTEQWLCARVPGKEMPELSAFQLEGCQVLEYARHKRKLRLGALKGNAFTLVLREVSNRDDVEQRLIDICVKGVPNYFGAQRFGIGGSNLQGALRWAQTNTPVRDRNKRSFWLSAARSALFNQIVAERLKKADVNQVVDGDALQLAGRGSWFVATTEELAELQRRVNDKELMITAALPGSGEWGTQREALAFEQAAVAAETELQALLVREKVEAARRAMLLYPQQLSWNWWDDVTVEIRFWLPAGSFATSVVRELINTTGDYAHIAE
Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
B7LEG3
Q88XW5
KAD_LACPL
Adenylate monophosphate kinase
Lactiplantibacillus
MSTMNLILMGLPGAGKGTQAQKILEDFDIPHISTGDIFRAAIKNETKMGLEAKKYIDAGNLVPDEVTNGIVRDRLAEADTKNGFLLDGYPRNIDQAHALKQIGEELNKPLDGVINIHVEPAVLVERLSGRFICRTCGATYHKLYNKPKVEGTCDVCGGHDFYQRDDDKPATVKNRLDVNIKLNTPLIDYYGQEKLLYNVDGDRDIDDVYKDIKKILDNL
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Q88XW5
P04803
SYWM_YEAST
Tryptophanyl-tRNA synthetase
Saccharomyces
MSNKQAVLKLISKRWISTVQRADFKLNSEALHSNATVFSMIQPTGCFHLGNYLGATRVWTDLCELKQPGQELIFGVADLHAITVPKPDGEMFRKFRHEAVASILAVGVDPEKASVIYQSAIPQHSELHWLLSTLASMGLLNRMTQWKSKSNIKQSTNGDYLVNDSDVGKVRLGLFSYPVLQAADILLYKSTHVPVGDDQSQHLELTRHLAEKFNKMYKKNFFPKPVTMLAQTKKVLSLSTPEKKMSKSDPNHDSVIFLNDEPKAIQKKIRKALTDSISDRFYYDPVERPGVSNLINIVSGIQRKSIEDVVEDVSRFNNYRDFKDYVSEVIIEELKGPRTEFEKYINEPTYLHSVVESGMRKAREKAAKNLADIHKIMGF
Mitochondrial aminoacyl-tRNA synthetase that catalyzes the attachment of tryptophan to tRNA(Trp).
P04803
Q15VD0
GLGB_PSEA6
Glycogen branching enzyme
Pseudoalteromonas
MQLEKQLQHAQCTFPFSHLGLLKTDNAFTITAWVPNATGIKVIDLATDKAIGSLKRQAQSDLFTAEFTKGNPPAVYAFEVKNAQGSYRIIDPYQFQDQAFHAVHFVDHLPKNVYQQLGAQLIDLDVGLKTPIAATRFAVFAPNASAVSVIGDFNYWDGSCLPMQKTDFGYWVLVVPGVKAGDKYKYQIKDAHGNELPHKADPVGFYAEQYPSHASVVFDHEQYQWQDTKWQQQVKGDKYTQAMSIYEVHLGSWKRPDSQSGKTYLSYHELVDELIPYVKDMGYTHLELLPISEFPFDGSWGYQPVGLFAPTSRFGGPDDFKYFVDQCHQNGIGVIIDWVPAHFPEDGHGLARFDGTHVYEYEDPRKGWHPDWNSCIYDFGKDTVRQFLVANALFWLDKYHVDGLRVDAVASMLYLDYSREADEWVPNVDGGNHNYEAISLLQWMNKEVYSHYPNAMTIAEESTSFAKVSRPVFEGGLGFGFKWNMGWMHDSLHYISKDPSYRRYHHGEMTFSMVYAYDESFVLPISHDEVVHGKGSLLRKMPGDEWQQAANLRCYAAFMYAHPGKKLNFMGNEIGQSAEWNHDSSINWHLLDYDKHSGIQALYRDLNTLYAEYPALHELDHDPAGFEWIDHENAEQSTLAMLRQSKGGKQQVYALSNFTPVPRTNFRLGVKAPGEYSILLNTDDKQYWGSGHSQNKTIKADKTPWNNQAYSISVSLPPLATVFILYKGQ
Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Q15VD0
A5D3W2
YBEY_PELTS
Endoribonuclease YbeY
Pelotomaculum
MPVLVSNLQGKVAVDEALTGLLTRAAQEVLKAEGYGEEAEVSLVFVDDAYIHGLNRQYRGVDAPTDVLSFAMQEGEPLAGGEEELILGDVVISLQAAERQAGEYGHSLQREAAYLAVHGVLHLLGYDHQGEEERKIMRRKEEEVLGRLNLTR
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
A5D3W2
A4VRN4
ILVD_PSEU5
Dihydroxy-acid dehydratase
Pseudomonas
MPDYRSKTSTHGRNMAGARALWRATGMKDEDFKKPIIAIANSFTQFVPGHVHLKDMGQLVAREIEKHGGVAKEFNTIAVDDGIAMGHDGMLYSLPSREIIADSVEYMVNAHCADAIVCISNCDKITPGMLMAALRLNIPVVFVSGGPMEAGKTKLANHGLDLVDAMVVAADDSCSDEKVAEYERSACPTCGSCSGMFTANSMNCLTEALGLSLPGNGTTLATHADREQLFLRAGRIAVELCKRYYQDGDESVLPRNVASRKAFENAMTLDIAMGGSTNTILHLLAAAQEAEVDFDLRDIDALSRKVPQLCKVAPNIQKYHMEDVHRAGGIFSILGELARGGLLHTDASTVHSPSMADAIAEWDITQTQDEAVHTFFKAGPAGIPTQVAFSQATRWPSLDLDRAEGCIRSVEHAYSQEGGLAVLYGNIALDGCVVKTAGVDESIHVFEGTAKIFESQDSAVKGILNDEVKAGDIVIIRYEGPKGGPGMQEMLYPTSYLKSKGLGKECALLTDGRFSGGTSGLSIGHASPEAAAGGAIGLVQDGDKVLIDIPNRSIQLQVSDEELAHRRIEQDKKGWKPAQPRARKVSTALKAYALLATSADKGAVRDKAMLDG
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
A4VRN4
Q21K87
ACP_SACD2
Acyl carrier protein
Saccharophagus
MSSIEERVKKIVAEQLGVKEEEVKNEASFVEDLGADSLDTVELVMALEEEFETEIPDEEAEKITTVQLAINYINENLA
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Q21K87
B8DR41
SAHH_DESVM
S-adenosyl-L-homocysteine hydrolase
Desulfovibrio
MTDAKRAQALDLSLANKVADMALADFGHKEMQLSEREVPGLMELIRMYGVSKPLKGLRVTGSLHMTIQTAMLIKTLYELGADIRWASCNIFSTQDHAAAAIADSGMAKVFAWKGETLEDYWWCTEMALTWPDGSGPDLLVDDGGDATLMIHKGVEVENNPELLKQAYDNKEFQIIMDRLALAYQNDPGRWQRVAARVRGVSEETTTGVHRLYQLEQEGKLLFPAINVNDSVTKSKFDNLYGCRESLADGIKRATDVMVAGKVVVVAGYGDVGKGCAQSMRGFGARVLVTEIDPICALQAAMEGYEVTTMEKAVEEGDIFVTATGNYKVITGEHMEAMKDEAIVCNIGHFDNEIDMHYLETTPGCTCLNIKPQVDKWTLKSGRSIIVLAEGRLVNLGCATGHPSFVMSNSFTNQTLAQIELATNPDLERKVYILPKKLDEQVARLHLARLGVTLTTLTKEQADYIGVPVDGPYKPGHYRY
May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
B8DR41
Q9S9Z2
MYB93_ARATH
Myb-related protein 93
Arabidopsis
MGRSPCCDENGLKKGPWTPEEDQKLIDYIHKHGHGSWRALPKLADLNRCGKSCRLRWTNYLRPDIKRGKFSAEEEQTILHLHSILGNKWSAIATHLQGRTDNEIKNFWNTHLKKKLIQMGIDPVTHQPRTDLFASLPQLIALANLKDLIEQTSQFSSMQGEAAQLANLQYLQRMFNSSASLTNNNGNNFSPSSILDIDQHHAMNLLNSMVSWNKDQNPAFDPVLELEANDQNQDLFPLGFIIDQPTQPLQQQKYHLNNSPSELPSQGDPLLDHVPFSLQTPLNSEDHFIDNLVKHPTDHEHEHDDNPSSWVLPSLIDNNPKTVTSSLPHNNPADASSSSSYGGCEAASFYWPDICFDESLMNVIS
Transcription factor that acts as negative regulator of lateral root (LR) development. Required for normal auxin responses during LR development. May be part of a negative feedback loop stimulated specifically in the endodermis upon LR initiation to ensure that LRs are formed only in the correct place.
Q9S9Z2
Q9X9Q0
HOA_STRTE
4-hydroxy-2-oxopentanoate aldolase
Streptomyces
MSQEAARDAAAGRPVQIHDPTLRDGQHAVRHSLGAEQFRAYLKAADAAAVPVVEVGHGNGLAASSLQVGRARLSDDEMMSIARETLTTSKLGVLMFPGWATTQDIKNALAYEVDLVRIATHCTEASVAERHLGFLRDEGVEAHGMVVMTHMASPDQLAEECARLVGYGATGVGILDSSGHFLPSDVTARIGAICAAVDVPVMFHGHNNLGMAVANSIAAAQAGAGILDACARGFGAGAGNTQLEVLVPVLERLGFRTGIDLYRLLDAADIAGRELMPAPPTIDSVSIVSGLAGVFSGFKKPVLDIAAREGVDPRDIFFELGRRQVVAGQEDLIVEVALALRAARDGASPASSGTGPC
Involved in the biosynthesis of the peptidyl nucleoside antibiotic nikkomycin.
Q9X9Q0
Q9AB66
ATPF_CAUVC
F-type ATPase subunit b
Caulobacter
MEHQSLFSFSNPEFWVLAALVIFFGLLVVLKVLPGALFGALDGYAAKIKAELDEAQQLREEAQALLADVKAQREDAERQAAAMLEAAKADAKRLAEEAKEKLEEQIKRRAEMAERKIAQAEAQAAADVKAAAVDLAAQAAETVLAARLAGAKGDTLVDAAIGQMGAKLQ
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Q9AB66
B5XPH8
SBMC_KLEP3
DNA gyrase inhibitor
Klebsiella
MNYSITTLGKKTIAGFHLVGPWDQTVKQGVEQLMMWVENHQVPAREWLAVYYDNPEEVPAEKLRCATVVAVDEDYVIPANSEGVILAAVAGGDYACARARVVDYDFATPWMQFFDSLLQSTTYRVAPRPCFEIYLNDGNHDGYWDIDMYVPVERVAS
Inhibits the supercoiling activity of DNA gyrase. Acts by inhibiting DNA gyrase at an early step, prior to (or at the step of) binding of DNA by the gyrase. It protects cells against toxins that target DNA gyrase, by inhibiting activity of these toxins and reducing the formation of lethal double-strand breaks in the cell.
B5XPH8
Q8KA20
RNFB_BUCAP
Rnf electron transport complex subunit B
Buchnera
MSITIILIFSILSFLLGIILSYVKYIFPIKKNSIIAEVDDLLPQSQCAQCGYSGCYPYAKAIVKNNENIDKCIPGGNNLKFKIAKVLNIKNIKYSLDNLNAKNEKNIHTTVLIDEKNCVGCSKCASFCPVDAIIGTPNFMHTVLQKFCTGCNICLLHCPTNCIKIIKE
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Q8KA20
Q4KHS7
MLTF_PSEF5
Murein lyase F
Pseudomonas
MFSPMALRPRCAKWLIVTGLFLMLGACVEKPSTLERVKEDGVLRVVTRNSPATYFQDRNGETGFEYELVKRFADDLGVELKIETADNLDDLFDQLGQPKGPVLAAAGLVSSEQRKQQVRFSHPYLEVTPQVIYRNGRSRPTTAQDLVGKHIMVLKGSTHAEQLAELKLKYPGIEYEESDAVEVVDLLRMVDEGQIDLTLVDSNELAMNQVYFPNVRVAFDLGDARSQSWAVAAGDDNSLLNEINSFLDKVEKNGTLQRLKDRYYGHVDVLGYVGAYTFAQHLQQRLPKYEKHFKASAKQEKLDWRLLAAVGYQESMWQAEVTSKTGVRGLMMLTQNTAQAMGVSNRLDPKQSISGGAKYLAYIKEQLDDKIEEPDRTWFALAAYNVGTGHLDDARKLAEKEGLNPNKWLDVKKMLPRLSQKQWYSKTRYGYARGGEPVHFVANIRRYYDILTWVTQPQLEGDQVAEGNLHVPGVNKTKPPEENPPL
Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella.
Q4KHS7
A5FL33
ATPD_FLAJ1
F-type ATPase subunit delta
Flavobacterium
MASTRAAIRYAKAILDLANSKGVAEAVNNDMKSIASAIETNTELSTFIQNPTTTVEVKESALLEVFADVNGVTKGLFHLLFENKRFEILDAIAVEYNKLFDESNGVEVAKVTTAIPMDAALEAKVLAKVATLSDKKITIENVVDPSIIGGFILRIGDNQYNASVANRLQVLKRELSN
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
A5FL33
B4S096
RL22_ALTMD
50S ribosomal protein L22
Alteromonas
MEALAKHRFARTSAQKARLVADQIRGLHVEKALEVLAYSPKKSAALVKKVLESAIANAEHNEGADIDELVVAKVFVDEGPTMKRIKPRAKGRADRIFKRSSHITVVVADN
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
B4S096
Q8BPG6
SUMF2_MOUSE
Sulfatase-modifying factor 2
Mus
MRSEFWFPSMGSLLPPVLLLWLLSCPRLQLGHAQDPAMVHLPGGRFLMGTDAPDGRDGEGPAREVTVKPFAIDIFPVTNKDFREFVREKKYQTEAEAFGWSFVFEDFVSPELRKQENLMPAVHWWQPVPKAFWRQPAGPGSGIREKLELPVVHVSWNDAGAYCAWRGRRLPTEEEWEFAARGGLKGQVYPWGNRFQPNRTNLWQGKFPKGDKAEDGFHGLSPVNAFPPQNNYGLYDLMGNVWEWTASTYQPAGQDMRVLRGASWIDTADGSANHRARVTTRMGNTPDSASDNLGFRCASSAGRPKEDL
Lacks formylglycine generating activity and is unable to convert newly synthesized inactive sulfatases to their active form. Inhibits the activation of sulfatases by SUMF1.
Q8BPG6
Q06637
BFSP1_CHICK
Filensin N-terminal fragment
Gallus
MYRSSFLREVRKEKYERSDAYDELRGSPEFDSLAQAQGLENLQELNERFASYINRARVLEQRNTILRKQLETFQRMDELVGLDEAFAGQIEFNRQRMRELASDRAKLEREEKDAQRMLDEYHNKYRNEREYQQKLKETLERLNKEADEALLCNLELQIESQFLQDDINATKDRYKKNLMEIQTYVNILQQIIQTTPRVSPITTGISEEKLVAERRIPVLQSQLEEYKSILCQLQAQKYKLQTETTMLEQAIKNTQESYDDEIQLYNEQIENLRKGIEEAERTLEKYTTDCRQLVIYQQSLENELERYKRIIENEDSRLNSAIAGTPVTLFTQIYRPVQPQASRGRDITQAMQEIASVKPRQKALTKKLSRKKEIMSKDITDGLSPEKLYERTVEVFDQDQLEFRHEGSVTCEPGQEELELVEKEAVPEDVPDGAQISKAFDKLCNLVKEKIRVYKRPEAKVDSHPKGRYVLVTGEEGYEEPCFSSIPAGGGITVSTSNGKVTIGGDVEPIPELPEPSEPSEKEKRDICERRDEFETQDKLKEEEKEDLFEWGKIRGKIEQVTKYPDVSEPEAVPSPGLISPAEPGVLQETDHDREDKQGLLFREAGLPGSVSYEKVEVVESIEKFSDDRIQTYEETAMIVETMIEKTSKKKPGDKGS
Required for the correct formation of lens intermediate filaments.
Q06637
Q5JIZ5
TKSP_THEKO
Tk-SP
Thermococcus
MKKFGAVVLALFLVGLMAGSVLAAPQKPAVRNVSQQKNYGLLTPGLFKKVQRMSWDQEVSTIIMFDNQADKEKAVEILDFLGAKIKYNYHIIPALAVKIKVKDLLIIAGLMDTGYFGNAQLSGVQFIQEDYVVKVAVETEGLDESAAQVMATNMWNLGYDGSGITIGIIDTGIDASHPDLQGKVIGWVDFVNGKTTPYDDNGHGTHVASIAAGTGAASNGKYKGMAPGAKLVGIKVLNGQGSGSISDIINGVDWAVQNKDKYGIKVINLSLGSSQSSDGTDSLSQAVNNAWDAGLVVVVAAGNSGPNKYTVGSPAAASKVITVGAVDKYDVITDFSSRGPTADNRLKPEVVAPGNWIIAARASGTSMGQPINDYYTAAPGTSMATPHVAGIAALLLQAHPSWTPDKVKTALIETADIVKPDEIADIAYGAGRVNAYKAAYYDNYAKLTFTGYVSNKGSQSHQFTISGAGFVTATLYWDNSGSDLDLYLYDPNGNQVDYSYTAYYGFEKVGYYNPTAGTWTIKVVSYSGSANYQVDVVSDGSLGQPSGGGSEPSPSPSPEPTVDEKTFTGTVHDYYDKSDTFTMTVNSGATKITGDLYFDTSYHDLDLYLYDPNQNLVDRSESSNSYEHVEYNNPAPGTWYFLVYAYDTYGYADYQLDAKVYYG
Serine protease with a broad substrate specificity.
Q5JIZ5
Q03Z95
NAGB_LEUMM
Glucosamine-6-phosphate isomerase
Leuconostoc
MNIIRVKDVEQSAEKALEIYQNAVQHGAKVLGLATGSTPIPLYQKLATSQINFSELVSINLDEYLGLDGEDEQSYRYFMTKHLFQYKPFKHSYVPDGKSEDHEAAIKAYDRIIVEHPIDLQLLGIGRNGHIGFNEPGTSFDSTTHIVNLTQSTVAANARFFEKESDVPTQAISMGIASVMSAKKILLIATGESKAEAVAATINGPITEDVPASILQKHSDVTIIIDEAAASKL
Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Q03Z95
Q9PAN6
CCME_XYLFA
Heme chaperone CcmE
Xylella
MNARRRLWSLLMLILAVGTAATLTIMALRRNLTYLYMPSEVLRGDTAQQTHFRLGGIVEKGSFQRTSGTLHTRFIVTDGNARLQVRYARILPDLFREGQAVVATGQMQHGIFIAENILARHNETYTPRTLTNKMQPTPTQHTHLDTPIAQTTP
Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
Q9PAN6
Q99NG9
K199B_MOUSE
Keratin-associated protein 16-10b
Mus
MSYYYGNYYGGLGYGLGGFGGFGGLGYGYGSSYGLGGYGGYGYFSPSFYGGYLSSGFY
In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Q99NG9
A4WEI4
HLDE_ENT38
D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase
Enterobacter
MKVTLPEFERAGVMVVGDVMLDRYWYGPTSRISPEAPVPVVKVDTIEERPGGAANVAMNIASLGAHSRLVGLTGIDDAARALSKTLADVNVKCDFVSVPTHPTITKLRVLSRNQQLIRLDFEEGFEGVDPEPMHERIAQALGSIGALVLSDYAKGALASVQQMIQLARKAGVPVLIDPKGTEFERYRGATLLTPNLSEFEAVAGKCKNEEEIVERGMKIIADFDFSALLVTRSEQGMTLLQPGKPPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACYFANAAAGVVVGKLGTSTVSPIELENAVRGRADTGFGVMREDELKVAVAAARKRGEKVVMTNGVFDILHAGHVSYLANARKLGDRLIVAVNSDASTKRLKGETRPVNPLEQRMIVLGALEAVDWVVSFEEDTPQRLIAGILPDLLVKGGDYKPEQIAGSEEVWANGGDVMVLNFEDGCSTTNIIKKIQKDSQ
Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.
A4WEI4
A6TBU4
GLPB_KLEP7
Anaerobic glycerol-3-phosphate dehydrogenase subunit B
Klebsiella
MKFDCAIIGGGLAGLLCGLALNQHGLRSVIISRGQSALHFSSASLDLLSALPNGDHVTDVAQGLQQLAEQLPEHPYSRLGAEAVLKYATQTEALLAACGAVMQGDARRPHRRVTPLGTLRPAWLSPLEVPVAPLPSQGACLVGISGFADFQPHLAAAALGQHGVTAAAVEIELPLLDVLRDNPTEFRAANIARVLDDENMWPALHAALLPLAQQYDLLIMPACFGLADDRLYHWLQARLPCPLRLLPTLPPSVPGMRLHSQLQRQFIREGGAWLAGDEVVKISHRQDAVEAVWTRNHGDIALRPRFTVLASGSFFSNGLVATRDSVREPILGLDLHQTLPRESWYQRDFFASQPWQRFGVKTDALLRPLLGGQPFHNLFAIGSLLGGFDAIQLGCGGGVCAVTALHAARQIHALAGGRP
Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor.
A6TBU4
Q9JJK3
PEX3_CRILO
Peroxisomal assembly protein PEX3
Cricetulus
MLRSMWNFLKRHKKKCIFLGTVLGGVYILGKYGQKKIREIQEREAAEYIAQARRQYHFESNQRTCNMTVLSMLPTLREALMQQLNSESLTALLKNRPSNKLEIWEDLKIISFTRSIVAVYSTCMLVVLLRVQLNIIGGYIYLDNATVGKNGTTVLAPPDVQQQYLSSIQHLLGDGLTELVTVIKQAVQRILGSVSLKHSLSLLDLEQKLKEIRILVEQHRSPSWIDKDVSKSSLCQYMMPDEETPLAAQAYGLSPRDITTIKLLNETRDMLESPDFSTVLNTCLNRGFSRLLDNMAEFFRPTEQDLQHGNSINSLSSVSLPLAKIIPIVNGQIHSVCSDTPSHFVQDLLMMEQVKDFAANVYEAFSTPQQLEK
Involved in peroxisome biosynthesis and integrity. Assembles membrane vesicles before the matrix proteins are translocated. As a docking factor for PEX19, is necessary for the import of peroxisomal membrane proteins in the peroxisomes.
Q9JJK3
B2XWK8
NDHK_FAGEA
NADH-plastoquinone oxidoreductase subunit K
Fagopyrum
MNSVEFLPLDRITPNSVISTTSNDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAVIDAITKLRKKISWEIYEDRIQSQRKNRYFTIKHKFRVGRRIHTGNYNQGLLSKSPSISEIPPEKFFKYRSSVSSHEFVN
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
B2XWK8
Q10588
BST1_HUMAN
Cyclic ADP-ribose hydrolase 2
Homo
MAAQGCAASRLLQLLLQLLLLLLLLAAGGARARWRGEGTSAHLRDIFLGRCAEYRALLSPEQRNKNCTAIWEAFKVALDKDPCSVLPSDYDLFINLSRHSIPRDKSLFWENSHLLVNSFADNTRRFMPLSDVLYGRVADFLSWCRQKNDSGLDYQSCPTSEDCENNPVDSFWKRASIQYSKDSSGVIHVMLNGSEPTGAYPIKGFFADYEIPNLQKEKITRIEIWVMHEIGGPNVESCGEGSMKVLEKRLKDMGFQYSCINDYRPVKLLQCVDHSTHPDCALKSAAAATQRKAPSLYTEQRAGLIIPLFLVLASRTQL
Catalyzes both the synthesis of cyclic ADP-beta-D-ribose (cADPR) from NAD(+), and its hydrolysis to ADP-D-ribose (ADPR) . Cyclic ADPR is known to serve as an endogenous second messenger that elicits calcium release from intracellular stores, and thus regulates the mobilization of intracellular calcium (Probable). May be involved in pre-B-cell growth (Probable).
Q10588
A3Q695
MSHD_MYCSJ
Mycothiol synthase
unclassified Mycobacterium
MTSIDWRSALTDDEQGSIRDIVAAATRHDGVAPVGDQVLRELPADRTRHLVAVDPDAGAVVGYLNLAPASDTAPPMAELVVHPDFRRRGTGAAMARAGLAEGGTHARIWAHGNLEAARATARTLGLQVVRELLQMRRPLTDLPPVTVADGVRLATYSGPGDDPELLRVNNSAFAWHPEQGGWTDADIAERRAEAWFDPAGLFMAFDDASGKLLGFHWTKVHGPDLGEVYVVGVDPAAQGRGLGATLTLTGLHHLAERLSNSPQPTVMLYVEADNGAAVKTYRRLGFDVSSVDAAYAAVAD
Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
A3Q695
P22549
IPDE_DICDI
Cyclic nucleotide phosphodiesterase inhibitor
Dictyostelium
MAKIIISLILLLSLFSFSYGAYNCNKLNCSSKNTKCRTFSCTSVVGCYYTDKCTSPDLCHNSACNASTGNCTLTTISCNDNNPCTDDFCHPGYGCYSVPNSCDPGVICQQNCNDNDPCTYDFCDALNICRHSETYCNDGDACTLNTCGVNGCNFTKISCDDNDPCTADYCSTLYGCYHEPIECSIKVPCNIDSDCNRNNGCETFTCNLSTNTCDYYAKNCGGWPCINNQCTTGSISN
PDI acts by binding stoichiometrically to cyclic nucleotide phosphodiesterase, changing the KM of the enzyme for cAMP from 10 uM to 2 mM.
P22549
P25269
TRBP2_ARATH
Tryptophan synthase beta chain 2, chloroplastic
Arabidopsis
MATASTAATFRPSSVSASSELTHLRSPSKLPKFTPLPSARSRSSSSFSVSCTIAKDPAVVMADSEKIKAAGSDPTMWQRPDSFGRFGKFGGKYVPETLMHALSELETAFYSLATDEDFQRELAEILKDYVGRESPLYFAERLTEHYRRENGEGPLIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLQCIIYMGAQDMERQALNVFRMRLLGAEVRGVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHAVIGKETRKQAMEKWGGKPDVLVACVGGGSNAMGLFHEFVDDTEVRMIGVEAAGFGLDSGKHAATLTKGDVGVLHGAMSYLLQDDDGQIIEPHSISAGLDYPGVGPEHSFLKDVGRAEYFSVTDEEALEAFKRVSRLEGIIPALETSHALAHLEKLCPTLPDGARVVLNFSGRGDKDVQTAIKYLEV
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
P25269
P12706
INS1_XENLA
Insulin-1 A chain
Xenopus
MALWMQCLPLVLVLFFSTPNTEALVNQHLCGSHLVEALYLVCGDRGFFYYPKVKRDMEQALVSGPQDNELDGMQLQPQEYQKMKRGIVEQCCHSTCSLFQLESYCN
Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
P12706
Q8CPW3
NAGD_STAES
Acid sugar phosphatase
Staphylococcus
MKHYQAYLIDLDGTMYKGTDEIDGAAQFIDYLNNNHIPHLYVTNNSTKTPVQVTEKLREMHIDAKPDEVVTSALATADYISEQHPNATVYMIGGHGLKTALTDAGLSIKNDEHVDYVVIGLDEKVTYEKLSIATLAVRNGAKFISTNPDVSIPKERGFLPGNGAITSVVSVSTGIQPEFIGKPEPIIMSKSLDILGLEKSEVAMVGDLYDTDIMSGINVGIDTIHVQTGVSTYEDIQSKEIPPTYSFKDLNVAIAELEK
Catalyzes the dephosphorylation of 2-6 carbon acid sugars in vitro.
Q8CPW3