ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A2K2Z204 | MTEPKKIWTEIPDIELFSDGGAEPNPGKGGFGIILSYKGKQKEFFKGYELTTNNRMELMGVIFGLEQLKTKSNVQVFTDSKYVINGITKGWAEKWKKNGWKRKKNIPAVNSDLWDRLLNAISEHNVEFNWVKGHSGHIENERCDTLANNGINSKELIEDIGYEPKEVDNDQSSSANTTFTKKVR | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subcellular Location: Cytoplasm
Sequence... |
A0A1F3V2E5 | MNKLRINAIYLATEGEGLLIGRVQIFVRFQGCLLGCKNCDSKDTWNVSNGSFMSEDEVIAAIEAKWPSPNVPIKTVSITGGDPLNLQNIEAVRSLVVRLKASGYTLSLEAAGDVIDQDIFQRLDFINFDFKTPSSGVQSDLEKIIFMQQNFTGKFQVKSVVEDKNDFDYIWQNYQKFLARLFKIDFIWVITPAYNLKEKFPLTRFVEIINWNQIAGGPFRVIGQQHKWIFGPDKKLV | Cofactor: Binds 1 S-adenosyl-L-methionine per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
Function: Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of a... |
A0A380MTX1 | MSQSETIARPYAKAIFEQTVNKQSQIQWQEFLTAAADFCQSEIVLARLFAPGFYDEFVNWLEQYLVSTRDSKLTKEERNLLHILRENDRLSVLPEIALKYDQLLNESEGMLEATVYSAKSLTSDEEKKISLFLEKKTNKKIVLKVKEQPSLLAGLRIEYDGLVIDQSTRGRIEQFARKLDDLRN | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A0A926NHN1 | MHAKRIAGEKATDFVESGMVVGLGTGTTVYWTIKRLGEMIKKDNFHIKVICTSIETEVLASKFGLDITSFGEVNSIDLTIDGADEINQNLHIIKGGGGALFREKIVASSSKFNITVVDESKSVSVLGKFPLPVEVLSFGWEVTSKKINDLGTVSVRREGLNGKPFITDNGNYILDCHFGEINDPRFLHKNLKMITGVIETGLFFDTTNIALIGNPSGSVKVISNTIS | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.
Function: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
EC: 5.3.1.6
Catalytic Activity: aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosph... |
H8WBK1 | MQCSHFAETGVAAEKEGDLVGFISGYIPPQQPETVFVWQVAVHEKGRGQGLAKRMLKEIVGRDACSNVTHLETTITEDNEASWALFRSFARDLGAELTYHEHFEKETHFGGKHDSEFLLRIGPFTNPV | Pathway: Amine and polyamine biosynthesis; ectoine biosynthesis; L-ectoine from L-aspartate 4-semialdehyde: step 2/3.
Function: Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl coenzyme A.
EC: 2.3.1.178
Catalytic Activity: acetyl-CoA + L-2,4... |
E4WSF7 | MKKLLFVLSLVVLAVNNSEYYEKLGVEKSATSKDIRKAFKKLALTMHPDKSKEPDAHEKFMELNKIYEVLKDDETRKKYDRWGEKGLEDGFNGGGRYESWSFFEEEFGLYDEDPEIHVFDAVELQAAMASDDVWMIKFYSERCSHCHDMAPAWREAAIQLEGIVKLGAISCRDYRQTCMNVGITGYPTVMVFEQGAQRYQIYHGGKYVRRGKKLPGQKTVENFVEFGVKSVSHRVREILGIVSLPNFIKKPCVYILSDSDGEFNYPKIPFEYQLSVGFGQDAFALKVDCTKDVLPDLCKRKSSTEETMFIFPPGVSPVDS... | Function: Plays an important role in regulating the size of autophagosomes during the formation process.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 807
Sequence Mass (Da): 92628
Location Topology: Single-pass type IV membrane protein
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A0A4U0VRM9 | MAVSKSRSLLRSAAYTALALSTAVLADNYTLPYSTYFSRPDLQAPSLDIAISDSSPTTGFTPGYIFIAPYQVTQNGPYIYDKFGNLIWDGSSAVGPGNAHDFKVCQYKGSDHLCLYIGNQQEGYAHGIALILDSNYRIVQSVQTGNNVPASDMHDFQLLHDGQSALLTAYQSVPADLSNRNITGGQGWILEGVFQEVNVTDGSAIFEWMSLNHVDPSASYVAPNTTDTSGNGLSASTAWDYFHINSVDKSPSGNYLVSARHTSSIYYVNGTDRSTIWTLSAGGASTFACTNFNFSFQHDARISSENDTTTVISMFDNASN... | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Seque... |
A0A1Z8LD56 | MLNFFIFVLILVINIFFELFFKDLVLSNKERIIIERGMGISEVSDLLKNNNVIKSKLAFKIWIKVNFSEKKIKFGEYEFEEEISVNKIVRKLKNGDFFFRKITIVEGTTKFDLLKKIKEIYPDQEIDINELSDFFIADTYHYNITENANKLIENISKSSSEILNKFWSQRNPDLPLSNIEDIFILSSIIEKETSLDYEKSKVAGVFYNRLKKGMRLQSDPTVIFSITEGKTKFNRKLLRKDLKYKSSYNTYLNKGLPPSPICXPGIKSXEATVNPXKNEYFYFVADPKINGHIFSKHYHQHLKNIKKIKEYKIND | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell inner membrane
Sequence Length: 315
Sequence Mass (Da): 37014
Location Topology: Single-pass membrane protein
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A0A088MFA2 | AYSSIAHMGWMTAILAYNPTMTLLNLTLYILMTATTFMLFMFSSSTTTLSLSRSWNKMPLITTSILAMMLSLGGLPPLTGFLPKWMIIQELTKNDSIIMPTLMAITALLNLYFYMRLAYSTSLTMFPSTNNTKIKWQFEPAKRMPCLAPMIVISTLALPLAPMLS | Function: 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. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 ... |
A0A1H0DJE5 | MNECRIEAPAKINLTLDITGVRHDGYHILRTVMQTVTLCDYLLLRKTPSGGIQLKCDHEELCCDETNLACRAASAFFAYTDIPPVGVQIVIEKNIPLEAGLAGGSADAAAVLMGLNVLFDTGLSDRTLCELGLPLGADVPFCIMGGTMQGEGIGEILEPLPSLPKCYFVIAKPESGVNTKEAYALFDRENPIRRPDNDMMVAALAAGSLEHIGNQLCNVLEGVCPLPEVSRIKQTMLECGALGAAMSGSGSAVFGLFENKGDARHCLSILNDHYGAVFLAKPCPHGAAIVE | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
A0A0A2MM36 | MIKTIRIGTRDSELALWQAHTVEKKLNDLGYATEIVAVKSTGDLILDVPLYELGITGIFTKTLDIAMIRGEVDIAVHSMKDVPTALPKGIVQAAVLERADSRDILVHKGNTNFFTDAATIATGSLRRQAQWLNRYPNHNVVDLRGNVNTRLKKLEDNDWEGAVFAAAGLERINLTPTNHIMLDWMIPAPAQGAMVVVAMENDPFCREALAQLNHKPTELATFIERQFLKKLEGGCTAPIGALATYIDDEIRFEGVLLSIDGSEKLHIEKVVALNDDIANFGNACAEEILQNGGTELMEQIKSQLKK | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Length: 306
Sequence Mass (Da): 33726
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A0A3D5ZZA5 | MRLQESQTDITEGAGYAAEAAFPPFDPTYFASQLFWLAISFAILYFLLSRWLLPRIGSAIEERKDRIADDLDAAAGLKLQADEAVKAYEKSLADARAKAQAVGV | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
Subcellular Location: Membrane
Sequence Length: 104
Sequence Mass (Da): 11427
Location Topology: Single-pass membrane p... |
E4XZD1 | MSVSPKQNPENENGAEEVGKLQDARKRAQRLILLEHLCNTLADRMWLYAAGLLLIDTIAKLDENSSSIVTASLYGVVLASVKILFAPLIGSLIESSRRLHGAMTSLIFQNTTVALSCLTMFWIIYSENVDISAWAVFAIVTAFSCFAILASVGLQNAISRDWVVEITTPEELTTMNAWMRSIDQATMVLSTALSGFSISLNQAWGAVAVASFNILAMIIQAICLVKTYNLIPALSQKKTKKEPDDSDEMKIVDKIKEALKTFFDGWALLFTSKVAIPGLALATLYVNILGLSFPLQGYGRENCLSEATISIIYIGSAVSG... | Function: May be involved in iron transport and iron homeostasis.
Subcellular Location: Basolateral cell membrane
Sequence Length: 507
Sequence Mass (Da): 55692
Location Topology: Multi-pass membrane protein
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A0A424NYZ7 | MFIKKINPKSFERTASNFLKIRIEALLKAKAVVHIALPGGSTPMPILKLLANENLDWARVCFYQTDERIVHTNNKENNYSLLNEVFFSHINALSFPMYTGEYSPEESCESYIKKLEKLETHNNIPRFDLIVLGMGKDGHIASLFPNSSILAESNKWAAVDQEKRKGTYRMTLCFPVLLNAHETVLLIIGPNKIKLIEDKAARKNLPIEILINQNQNLTVLCSKGQ | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequen... |
A0A8D2DCI4 | EGRRSWGRRVLGAPDTALTLLSCVPTAFESRALVSSWLGGEKRSPLQVLYDLDRAPRSPLAEVHRQRRDLLRRACSRHTRRQRLLRPEDLRHVLVDDTHGLLYCYVPKVACTNWKRVLLALSGRARGDPRSIPAHEAHAPGRLPSLADFSPAEINRRLRAYLAFLFVREPFERLASAYRNKFAAPTRSATRAACATTSWASSRRWRRTRLSCWAWWAPRQPSGCRSHLTTLEAAHLRWHLSKPLEGARAL | EC: 2.8.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 250
Sequence Mass (Da): 28565
Location Topology: Single-pass type II membrane protein
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A0A8D2B7D8 | KGEMALGALLLLFSGSLSLTEAWTGSHSMRYFNTIMYYPGREEPRFFSVGFVDDTQFVSFDSYAENPRQEPRAWWMEQEGQEDWDSNTQICKIVAKNYEVEFNTMLGYYNHSKGGSHTLQRMFGCDLGPDGHFLRGFTQYAYDGEDYLALNEDLSSWTAADSGAQLTQRKWEEARVAEYWKTTLEGECVESLARHLENGKETLLRLDPPKTQVTRHTNPEGDVTLRCWALGFYPKEITLMWQRDGEDLTQDMELVETRPAGDGNFQKWAAVVVSAGEEQRYTCHVHHEGLPEPLALRWGKEGRLSGDPEQEPPPQPTIPI... | Function: Involved in the presentation of foreign antigens to the immune system.
Subcellular Location: Membrane
Sequence Length: 372
Sequence Mass (Da): 41979
Location Topology: Single-pass type I membrane protein
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A0A1H0DJD3 | MSYINLYDSHTHSDNSPDGRESVTYMCENAIAKGLRGISITDHCEMDNFEGGRYNISTKQSYFESLKAKSVFRGSLIVSSGVEIGQPLYNLKLTRQTLASFEYDFVLASMHNMIDGSDYFYVDYSDMGEEEIDCILKNYFKDLLDICNWNEFDCLAHLTYPLRYITGTHGIPVELSRYNDIIDEILKTLARNGKALEINTSGFRQGLETALPPLKYIKRFKELGGEHVTIGSDGHRSEDVGKDIEKGMELAKEAGFEQFTIYLSRTPMLIDIK | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 273
Sequence Mass (Da): 31021
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A0A2A5X4J4 | MIGFLNSIIDPLKKNRYISLSMRKLLFPLAWIYGLLLLIRHTLFDLKLLSQKRVAIKTLGVGNLALGGTGKSVVVDYLLEQFKKTTHLAVLSRGYKRKTKGYIQAQQNVTAALIGDEPFQFHKKHPEVIVAVCEKRVVGIQHLMALEKGPSVVVLDDVMQHRWLVIDKLIMTTTYDNLYSSDALFPVGALRDRKKEAQRAAILLITKCPQQMTLEQTEQIKKRIKPKQNQAVFFTSIEYASKIIGCSKTINLKELKGITILVVTGIADPKPLYTFLEETQVQFDHLAFPDHHSFSDHDVKKIENHQAELILTTEKDFGRL... | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form te... |
A0A2A9NYY6 | MLPQLNLKVDFESVTRNFKINNNFNWKRQLLNTRATIVPYAREFLGTFFIVIFGNGANCQVNLSSSPAVALQPKGNWTSLSFGWAAGVAMGFWVSNGGHINPAVTLALATYRDFSWRKVPAYILLQVLGSFSAAAVLYGNYYHAIDQFEGGDGSRTSNTSGLFGTHALDYMTNIGCFFNEFLSTTVFLIGLLTLLDKRNRVPSGLIPVGVFILVFGIAACLGMQTGFAINPARDLGPRLLTSIVGYGRQVYNYRNQYWIWCPILGPIMGAQAGTIIYDTFVYTGRDSLISKFLLPVPQPSCDMEENFQSHELHDGVCPGN... | Catalytic Activity: H2O(in) = H2O(out)
Subcellular Location: Membrane
Sequence Length: 354
Sequence Mass (Da): 38804
Location Topology: Multi-pass membrane protein
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A0A6A6UUE4 | REPFKFPFVLDNPHPSHVEWIEESSERIESEKAVYRVLMQHRRPNIVDGILIASEGIFMRRENMTLETRLQASSSVAPNKQVQWIRQLASALAWIEQLGYVHGDVRPENILLDTNENIRLGDFDAAVKIGDQVAVASEPYIRLGENYELPIAGPASEQYALASCMYYIRFGHIPYHELEPQARGRRLDRGDFPSTAPDAVFGGLIQDCWNGCYGSMRLVEQKIAALMRDHGVVQDSFLGQTERTTDDLLYALRAECEVYLAKERSSNARD | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N... |
H8WDT2 | MLAVKPQVMGDVCRDIAPVVQNTRPLMVSIAAGLTADTLDTWLGGGLPLVRVMPNTPSLVGKGAAGLFANSQVKDDQRKAVQKVFESIGSALWVDDENLLHSVTALSGSGPAYFFLMLEALESAATEAGIESETARALAIQTMAGAAEMAARSEDDPGQLKRNVMSPGGTTERAINTFEEGGLRDLVKKAYSAAFERSREMSRELADKQ | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm... |
A0A1V4ZM74 | MAGTIVFEPDDRYNAFLSTATAGPQGSGTLSGVMVAVKDNISTRGIETTCASKILKGYVPPYDAHVVGLLKAAGATIAGKTNLDEFGMGTTTENSAFGPTLNPRDTSRVPGGSSGGSAAAVAAGMVKVALGTDTGGSIRCPAAFCGIVGLKPSYGRVSRYGLIAYSNSLEQIGPLGRTVSDVSTLMGVIAGYDRHDSTSQNKPYNHTPKADIKGLKIGIPAEYFGKGVDPDVAAVVKKAIGRLEELGATTVPCSIPSMEYALAAYYVTCTSEASSNLARFDGVRYGPAPDWKKSWHDAFQDVRGSAFGAEVRRRIMLGTF... | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
EC: 6.3.5.7
Catalytic Activity: AT... |
A0A0A0EZF8 | MTWRTMTTWVLLVAAIASGWMLWRQRAPETAPAKAQFRPDYVLNDLELIALDDHGREAFTLRAPHLTRDPSAKSMDIQTPLFMIPPSPGKAGTPWAVRSATAWVAPKGDEIRLRGQVKADSQDAQGRPVNITTEELNVFPNTKRATSTAKVAMTQPGFILNGRGLDAQLDAKRIVLQSDVKARYERTAR | Function: Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA.
Subcellular Location: Cell inner membrane
Sequen... |
C0WHA6 | MLPAHHKLTSPPQFRRTMKGSRRQGTRTVVVHARDTMSANSNGTMDNPAEVAATGPRFGLIVSKAVGNAVVRHRTSRRLRHVCMTLIPKLPAGVDVVIRALPASATATSEQLEKDITKALRKQWDM | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
I5AQR5 | MEPILRADQHKEADIRTSENGIPSLVLMERAALAVVDVLEEEEFDLSDVLVICGTGNNAGDGAAIARILTERGYGATVFAAGDEKKYSEQMKTQMMVLTHYPVKVLRGDFPVEGYTLIVDALFGIGMHRPVTGNYAEVIEAVNDSDLPVVAVDMPSGIHTDTGAVCGVAVRADLTVTFTTGKAGLYLYPGAAYAGRVLVRKIGIPVEKDMLRECPLFSLDETDLKLLPARNESGNKGTFGKVLVIAGSEEICGAAYLSAAAALKSGAGMVKIYTDEKNRTALATLLPEALLSVYTSKGWKPESLLENLKWADAVLIGPGL... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
U5TU35 | MLIMSFIMMLIILFSIILIIMNFFIMFKINFSREKSSPFECGFDPFSSPRLPFSINFFLISIIFLIFDIEISIILPMIINYKYSQIFYWMFLNFIFMLILIFSLLIEWVDGSINWMF | Function: 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. Essential for the catalytic activity of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NA... |
A0A3B8UBW9 | RLEGPVRVDPAVHTAADVGDEPLMLAQGSPAWIARDRVEGARAAAADGAAVLVLDDAHQNPSLKKTLSLIVVDGETRGDEWPFGDGSVFPSGPMREPLKAGLARADAVVVLLPADLAEVDPELIEVFGGLPVFIARLEAAAPPPPGPQVGFAGIAKPWKVERSLLAAGCDLRDFVPFPDHAELSDRDFAFLNDRASVYGAGLVTTEKDWVRLSPERRARVSPWPVVARFEDEAAFAAFLLDRLKPQS | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form te... |
A0A0W0XNC0 | MLTNTSTMTSRYLEEIRAEQAYLLDQTNLPVGKKYTGKVRDSYDLGEYLLLITTDRLTAFDRPLALIPCKGQVLNLTSAWWFEQTKDIVPNHLVAIPDPNAVIAKKCQVFPIEFVMRGYITGTTDTSLWTQYNKGVRNYCGISFPEGLKKNQILEEPVLTPTTKEKIHDRPISPEEIISEGWMKEEHWHQASVLAKKLYARGVEIARKHGLILVDTKYEFGLDSSGKVIVVDEIHTPDSSRYWLGNTYEQRIAEGLEPENIDKEFLRLWFAKNCDPYKDNDLPKAPQELVEQLSLRYIQLYEMITGRPFEFQKHHETAEK... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(... |
A0A1Z8L5X1 | MMNLKKVKALEXNTFLKKKMIEIDFHQKLNYEEIEIKNYIFSSVKKCFETLKKNQEDYYLSIFLTNNYDIKKLNNKFRKINKPTNVLSFIQDEKLCLNGSKHVXLLGDIVISLEKISSEAKNLGKKFSDHXIHMCIHGLLHLFGYNHKKDSEAKVMQEKEISILKKLSIPSPY | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 173
Sequence Mass (Da): 20320
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A0A0A2N2H4 | MENLKKAYIAGGCFWGMEDLFRVLPGVKDTEVGYLGGQNENPTYQDHPGHAEGLEITYDPQVITYKELLDYFYRVHDPTTVDRQGNDRGASYRSALFIQNEEEEQTAKEVIDIVDASKRWPGTVVTTLEPFTKFWTAEGYHQDYLVKNPNGYTCHFERFGTFL | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
EC: 1.8.4.11
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionin... |
A0A0G1JSB1 | MRVLGIDPGTGRVGWSIVSKEKGVESLVECGCFETPKNSPLPSRLKLIYDFLTKLIKEHEPDEFAAENLFFSTNAKTAFDVGAARGVILLAAENAGLPIFQYTPLQVKSSLTGYGAADKKQVQFMITRILHLKVTPKPDDAADAVAIALTHLFTQKHPIKIRN | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
A0A5C3DZS3 | MTTSAFQPLQNEDIPRPAKSSKLTHPTTTTATMSSSPLRLLVQRHPAHPLAKLPTRGSALAAGYDLYSAEKVVLPRGGRKVVQTGICLAIPTGHYGRVAPRSGLASKHGIDTGAGVIDEDYRGLLGVLLFNFGDADFTINAGDRIAQLIIEKISTPDVQEVESLDETLRGAGGFGSTGGFGAATATTAADATAAAVAADLPAEVGKSSS | Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA... |
A1ZJN6 | MNKPSNIQTSLTQKASVPILLVSVFIIAICGILYELLISSISSYFLGSSVLHFSLTIGLFLSFMGLGAYLSKFIPDKHLLDRFIMIEVWLGIIGGASGALLYVSYAITENYYLIAFLLLGSIGTLVGIEIPILTRIIRGYFNLKDTLAQVLSFDYLGALIASILFPLFLLPYLGLTRTSFFIGLLNLSVGIFNMLVFKKQLVRFKRKLTFTLLITALYIIGFFSAFTISGYFEQFLYQDDIVFTKQSRYQRLVVTQWKNDTRLYIDGNLQFSSVDEYRYHEPLVHIPLALAKKPESVLFLGAGDGLAIREILKHPHIQQI... | Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putre... |
A0A1F2RCZ2 | MAKRVGILTGGGDCPGLNAVIRAVVRKADALGWESLGIMEGWRGLLENNVEPLDLIRVSGILYRGGTILRTSRTNPLKRPDGLTRLRENIELHGMDALIAVGGDDTMSVADRLFQQGVSVVGVPKTIDNDLYGTDYCFGFDTAVNIATEAIDRLHTTAEAHNRVMVIEVMGRDSGWIAVASGMAGGADVILIPERPVDIEQVCSLIRRRSERGKDFSIVVVAEGARLPSGEEGGGGMQIHQSRIVDEFGHVQLGGVSNFLAREIEARTGFETRVVVLGHIQRGGSPTAFDRILATRFGVAAMTLAHQGDFGKMVALRGNQ... | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-depe... |
A0A519HMU0 | MIGVIDYGMGNLRSVANAFYENGLEVEVISEPDRLEDYSHLVLPGVGHFGKAVKNIDERGFRGPLAALAAAGRPMLGLCVGMQLLAEVGTEGGESRGLGLVAGRVTAIPPAPGKRIPHVGWNELNIQRDHPVFNGLKQGRDFYFVHSYQFDVADPDNLLGSTDYEGQVTAVVGRANVIGFQFHPEKSQVNGAKLLENFADWDGVC | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthe... |
A0A7C8QJ80 | MANADFLGSRKVPITTVLFPYGCNDSSCGYCDVTIGNKSYMMMASVDRPGETFLGITPNDYKTLLDRGWRRSGNIIYKPDMRGSCCQEYTIRLKSSLFKPKIHNDEASEGGFKRFLCANPFKPPYSVDKKGRKIGAYHQCYYLDGRLIAMAVLDLLPDCVSGVYFMYHTDFSQWSFGKLSAVREIALAEEAGYEYYYMGYYIHSCPKMRYKCEYQPAEVLDPECYDWHSFDNNFRKILDVKPYYSPSLERILTAEGSERSMTLLNNYHINTKKGVITNLDDDTVFSTDMSGVVKLEDIEPVIDDIRILVGRKLAIAEMIS... | Function: Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway.
EC: 2.3.2.8
Catalytic Activity: an N-terminal L-alpha-aminoacyl-[protein] + L-arginyl-tRNA(Arg) = H(+) + N-t... |
A0A1F2RGY2 | METWGARFAPEQPLREHTSLGVGGPADLIVIQRLEALEPVTEGLRQRGIAWGLLGGGTNVLAADEPHQKVYLRLAPNSHDIEFRGNTVRVPAAAELGRSVMECAKRNLGGMEGLVGVPGSVGGALRMNAGAYGTEIGPLVRSITVFRGSTGRREELVPQGGVSFQYRKSSFASDDIMLGVTLELKERPFREILDHVKLLNQRRRGSQPLKEKSAGCIFKNPPGLSTGKLIDELGMKGTGVGGAVVSERHANFLVNRHSATASDFFRLMDLIRERVLRAYGVELEEEVIVWKN | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 292
Sequence Mass (Da): 31803
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A0A7G3I2P0 | TETKASVGFKAGVKDYRLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVIGEAEQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 190
Sequence Mass (Da): 21041
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A0A8D2JNX5 | SFHVIFWDDRKLKPQKRHLFNNICFTFLSEPQAMCYVATANLDGETNLKIRQALLETAGTQKEEQLVNLAGKIECEGPHRQFNNFVGTLYLRGKSPVSLGPDQMLLRGTQLKNTLWIIGIVIYTGFETKLMQNAVKSPLKRSKVEKVTNLQILVLLLLLFLMSAVSCVGALIWNKIYLENIWYMGNNDNPSHNFVFDLVVFIILYHNLVPISLLLTLETVKFIQAQFINWDEDMHYDQNNLYAMARTSNLNEELGQVKYLFSDKTGTLTCNSMTFKKCTIAGVIYGNFWSKVIFFILPHSQSSFCEFNDPKLLENFENGH... | Catalytic Activity: ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.
EC: 7.6.2.1
Subcellular Location: Membrane
Sequence Length: 622
Sequence Mass (Da): 71254
Location Topology: Multi-pass membrane protein
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A0A177W711 | MTQSLLDQRVLVIGAGSSGLVALKECLAEGFSNVVCYEALANLGGLWQYEPVQPNQKVHSSVYKNTVIDTSKQMMAFSDFPIPHHWPIYLHNKSVVKYYHMYAEKFDLINHIEFNTQVTAIDPLKSTTNDLQASKPYNGQWRVEYMQDGNQLTAVFDKVIIASGHHWKPKMPEFPGMNEFKGEMMHSHYYREANPFKDRQCLVVGLGNSAVDVAVELSYHAKQAYVSSRRSAWLMSRFSLNGRPLDQTVSRFYTMLPIFIRNILVRFTTWVQLGDIAQFGLFPKHEPFSAHPTISSELPGRISTGTIVMKPNVKRFYRLA... | Catalytic Activity: (2E)-geranial + H(+) + NADPH + O2 = (1E)-2,6-dimethylhepta-1,5-dien-1-yl formate + H2O + NADP(+)
EC: 1.6.3.1
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 527
Sequence Mass (Da): 59987
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A0A9D0KW56 | MKFIKKVEGFIWFIPILTVALFFKLRDLKYFSLDNVLSCYDCFWFARLSEDFLNSKFSNIDYLSNVPDYMVVPLSLIVVFPAVVSKLTGIELNKIFLYAPPVMGTLFVIPMFYWIRQFAPVHVFVGASFLGLFNYVYYYRTSLGRYDTDFLILFFVFLILFLISKSVFDKEKSYLYIILAGIFSQIFMWWYYKPILLIFISFGLLLGLIVQKEDLKDIFKKVIFYTLLCNPVYIYEGLNSFGRYFFGYFLRKTETFPISIASTIVELQPVNLDRFLYMTVDHLGILILGIVGLVLLFVFKFRYMIIALPIISIGLTVFTA... | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 659
Sequence Mass (Da): 77880
Location Topology: Multi-pass membrane protein
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A0A1S6IQ16 | MKKPFISFQNFTFTYSDQVTPVLNELNVTINEGEKILVVGPSGSGKSTFARCLSGVLPNKDNNDYMGRIVYGREGTTPTISNFLPNELAISMAASMAALNEKNRDSNNQTAVQPFQTYLEKKKLAGMDWFLSRTPDLKESFSKLTDNQFEKIHSAGFFIDDKPVLILDEPLANLDPKSGDAAMKFIDELANQTNTTIIIIEHRLEDALVYPVERLILFSDGRIMADGAPSDILKTEVLSEIGIREPLYITAMRYAGVNLDEVNHLDLVHKLNGPNLKEKMEQWLSYLPQFEYPVQSTALLELQDISFKYPWNVRPILNQV... | Function: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system.
Subcellular Location: Cell membrane
Sequence Length: 567
Sequence Mass (Da): 63994
Location Topology: Peripheral membrane protein
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A0A9D9DLV4 | MTEEKQIRPNSFRAWVLALRPKTLSAAAAPVLIAVSLAFCDSRFAFAPALLALLFASGMQIAANFINDLLDYTKGTDSKGERIGPKRVCAEGWIDIKHMKRGIAVAVTLSSLIGLSLLFYAGYELVFIGIACILFAYLYSGGPYPLSYIGMGDLLVLLFFGIVPVTVTYYILAGYITSTAAITALSCGLIVDTILVMNNYRDFHGDRESNKKTLVVLLGSQKAGRRLFLLTGLAGALLPLYGLGTGYCCAALLPMLYIPLHFTVWRKMKTKSGRALNPIFGETSRNVVIFTFLQCAGFILDSYL | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
Function: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK).
Catalytic Activity: 1,4-dihydroxy-2-naphthoate + an all-trans-polyprenyl diphosphate + H(+) = a 2-demethylmenaquinol... |
F6KMV3 | RSRESIPGFGLISHMICLESGKKETFGMLGMIYAMVSIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMVIAIPTGIKVFSWLATINGMKMKLTPTMLWIIGFIFLFTIEGLTGIILSNSSIDIILHDTYYVVAHFHYVLS | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A075MPW4 | MKATFGMGCFWCSEDVFGRVKGVKSTTVGYMGGKIEHPTYEQVCTDRTGHAEVVQIEYDPAQVSYEEILSVFWANHDPTIPNRQGWDVGTQYRSAVFYHSPEQKAAAEAIKQKLQDSGAFKRKIVTEVSPASAFWKAEEYHQKYYQKCGLKMHGYGTFW | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
EC: 1.8.4.11
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionin... |
B3PCM4 | MMRPIALSSLAYFMLSQKLPNALKPQLKGGDAMFTRVSTDTRTLDAGDLFIALRGERFDAHDFLAQAEARQPCAMVVEKFNPAIQLPQLVVADSTLALGQVAALNRSLFTGPLVAITGSSGKTTVKTLVASILGECGETLATRGNLNNHIGVPLTLLELEERHQFAVIEMGASGPSEIAYACSLAKPQVAMINNVMPAHIEGFGSIAGVANAKSEIYGGLVTGGIAVVNIDDAFAPQWIQQLAGKKTLTVSLANPDANCRAEAIEYASEHLAFDLLIHRQRLRIILNAQGEHSVRNALMAAACAYALGASMEQIQRGLAR... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-d... |
A0A7Z2SHJ2 | MRSFFITIEGMDGSGKSTIIPELAERLEKTYSGQNVVATKEPGGTTIGDDIRKILLNVKNNKIDIRTEVLLFAASRRQHVVEKIIPTLKSGGIVISDRFLDSSIVYQGAGRGIGMQDVAELNEFAVEGLRPDITLYLKINPVEGLKRIKTNRKDDIDRMDREQQNFYFRVSHAYNQVIEKDSERFVIVNADQPIERVVDEAWDKLVNRMNTIEKNIGICGGNHEL | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 225
Sequence Mass (Da): 25435
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A0A9D8TRT5 | MHNDLNNDTSYMNDSRAVSPQVHGWNRSWDYPYSKEATSGNEGSENSESSAPATPKDESLGHRLAEKLSFKTGSWGEKITELSWIFIIFMISRCVLFSIIYLGNYHYPSEVNYIHEPLFSNVVGDTMNIMCQFDCAWFETVSRDGYAPVPQNLTTGHAANWAFLPGYPMLAGVVSFVLGGNYLLGLMTVSNLSFLLALFLWNNYLKLHNLSRSVREASTVILCFLPYSIYFMAPYSESLFLVFSILAFTFIAKKNFLMAGLVAMGMSATRNVGVMFVFPLLLAGIMEYGFRNLFTFNRNNLKLILGIMLVPLPMFIYQNY... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 454
Sequence Mass (Da): 51695
Location Topology: Multi-pass membrane protein
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A0A7C5Y3X4 | MGNEAIARGALEAGICFAAAYPGTPSTEIVEVLSEVARECGIYVEWSVNEKVAFEAAYGAAIAGVRSLTAMKHVGLNVAADILMSSAYAGVEEGFVVVTADDPSAHSSQNEQDNRWYGLLAHLPVLEPSNAREAYKLVKEAFNLSAKYKIPVIFRSTTRISHTRMPVELEEDIPATKKCKGEFIRDYERWVLIPAHTRKRKLELIKTWEALRGEDRFVTVYNPGGEKAIVASGLAYTYVKESLSILSLLDKVTLVKVNMPVPLPRRPLLRVLEHAKEVLVVEELDPVVEMQLKDLVATSGFSVSVRGKDLVPESYELTLE... | Cofactor: Binds 2 [4Fe-4S] clusters. In this family the first cluster has a non-standard and varying [4Fe-4S] binding motif CX(2)CX(2)CX(4-5)CP.
Function: Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates.
EC: 1.2.7.11
Catalytic Activity: CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferred... |
A0A6A6V4Q1 | MNSRFVRPLTRALRQPAFFRPNAVARPALAASQSKLQKESPQQMLVLKSAMPQLIPFFFVNETTMAFILIPSLIYVMSKYILPQKVRLFAARLFISKL | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... |
E4WZB3 | MRQFFNRGFNGFRNQFRAGRRFNSEQADNSFKAWRDYFFSTHFWGPAANWGIPIAAIADCQKSPEIISLSPGGPLELMLLRAFAFDDSPNF | Function: Mediates the uptake of pyruvate into mitochondria.
Subcellular Location: Membrane
Sequence Length: 91
Sequence Mass (Da): 10471
Location Topology: Multi-pass membrane protein
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G9LVZ3 | RAWAGMIGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTAINMKPPAITQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHL | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A7L5Z5B0 | MARLLARLDPGASYPLAVAFSGGGDSVALLDLVASWARTYRRSIVALTVDHRLHPDSPEWTRKAQALAHRLGCQWQGLTWERPTPGVGLTARARAARHALLADAAWRGARVLLFAQTRDDRLEADWMRSQEGASIGNLREWSPSPAWPQGRGMMLFRPLLXRGREALRRHLRLRSLDWIEDPANADLRFGRSRARQALAGREGHPLSVPVSDDLGSLPEVDDWGLVTVSRQVQSRVLASALVVASGGQRLPRRQQVERLRSRLQTGEVFSATLLGSRLTATDKAVQIGRQWAPRSGQVPPDPVPLDPEVPVFWDGRFEVW... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A0W0XZX5 | MDIHRFENCEILHEEFANRLIEILNEAIAVRGEAYLAVSGGKTPAALFEVMAAKDLNWNAVSVILVDERWNTQDRDSNEWLVKNCLLKNKAAAATFINLYTQNSTIEEAVGEAEAKLARIPLFDAVILGMGEDGHTASLFPGSRELEYGLSNCAKDVIALTPMHAPFQRITLTKPRLLRTRKLFLQLVGENKMRVFQEALADNDVLTMPIRAFLNQPATRLQVMFAPS | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequen... |
A0A0X9VQL8 | MTHINESVILNQITKIIGSNLKILVAFSGGLDSTVLLHALTVLRNTTIPNLNIRAAYINHGLNNKSNSWGVHCKHICLNLKVAFCSYDIHIYKSKKGIEAAARDARYKTLRRILLQNEIIVTAQHLNDQAETFLLALKRGSGPAGLSAMPVSIEFGHTYLVRPLLLFSRQELTMYAQKNNLTWIDDDSNYNQIYDRNFLRLTIMPCFNIRWPYFLKSVARSANLCAEQEKLVNELLEDYLSKLLTTDGSLKLDPLVEFSEKKRNAILRSWFRLYKILMPTRVQLKQIWQDVICARSDAEPKFILADNVIRRYKKELWLLP... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A0X9VLS7 | MFNIFQKFKFNKKKLFDILNKIYPFKIKKKINLAPLRILPLADEFIIPIQQHVGTSGDIIVKPGDYVLKGQPLTIGCKYKIPVHATTSGTIIEIVEYITEQYSGPKELCIRLKPDNKDKWCELKPLTNYSQYSIKVVLSHIEQAGIVELGNLCFPTAIKLKNNNKVISTLIINAVEYVKNVIANDQLIQEYTDEIIDGILILKYITKPKRILIVIADSNIASILSLKKAIYSYKYYIKLIVIKSKYPVFENKVLIKILTGKKILSGINHSASNIMIQDISTVVAIKQAIIDGKPLIERVVTLIRGDIAKNSINYLIRFGT... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell inner membrane
Sequence Length: 539
Sequence Mass (Da): 61790
Location Topology: Peripheral membrane protein
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A0A932YHV3 | MSGKKLSDKPDFECPPGVRTWIELDANACRRNVRTFRRLVGPKVKLWAVVKSNAYGHGLSTFSKVIDSTDIDGFCVDSILEGLRLRKDGIRKPILVLGFTLPAFFEKAASNDIAVTISSFDSLRAFDRTKRKPFFHLKIDTGMHRQGFQEEEMRRAIDFLKKRKLRPEGAYSHLAFPESKKSSLNQQKVFERCLEFFKSGGIRLKWIHLSGTGGVCERRPFYNMVRVGFGLYGYFRRPFRNKFLHPVMKWKTVVTEVKRTKKGGRIGYDFTERFKRDSTIAILPVGYWHGVDRGLSGVGEVLVRGCRARIMGRVSMDMIA... | Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
EC: 5.1.1.1
Catalytic Activity: L-alanine = D-alanine
Sequence Length: 375
Sequence Mass (Da): 42770
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R9PJG0 | MMTSLTASELNGEAKLFYLVGPSGSGKDSIINGLRSQLRADSNLLIAHRYITRAVDDSGENHIALSVPEFTHRKHSGLFAMDWQANGCNYAVGNEVNTWLSMGFSVLFNGSRQQIPLAEELFGERLRIIALEVDPSILAERLRKRGRESEHDISARLRRSEQYQASLPEECWRLDNNRNLDSTVSKLLKYIETETTELYIQ | Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II): step 3/3.
Function: Catalyzes the phosphorylation of ribose 1,5-bisphosphate to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP).
EC: 2.7.4.23
Cat... |
A0A926RVT3 | MSLSRKLVLTVAGNRLITSLVSKYGMKLGASRFVAGETLGTALEGIKKINDQGLMVTLDHLGESVYKKKEATAATEAALKLFDAIHERKINSNVSVKLTQLGLDIDPTFCYENINRIVAKAKEYNNFVRIDMEDTPRLEITLDILNRLLDQHGHEHVGTVIQSYLYRSANDCKELAKRDVNLRIVKGAYKEPTEVAFPDKKDVDQNYIKLVQQHLSGGHYTAIATHDEALINDLKSWFDTQKIDKARYEFQMLYGVRSKLQKQLVEEGYRVRVYVPYGKDWYPYFTRRIAERPANALFVLKSFFQK | Cofactor: Binds 1 FAD per subunit.
Pathway: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2.
EC: 1.5.5.2
Catalytic Activity: a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+)
Sequence Length: 306
Sequence Mass (Da): 35028
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A0A2D9KUT1 | MSSKYVLTDFQHLRDEMVRKQLINRDISSSKVLEAMSAVPREQFLPLEMRGFAYEDSPLPIAEGQTISQPYIVALMIDALNLQGGERVLEIGVGSGYASAVLAEIADQVIGIERIPTLSDQAKTVLKQLGYNNIKIINANGTIGYVEAAPYDAILVSAGGPEIPTTLKKQLKIGGRLVIPIGNRLYQRLLRVTRIDENQFDEEVISQVHFVPLIGREGWSDDLNTSSTKRSSSASLSAGKDQSENAVRHKTQTIEALIAEAAQPIDTIETVDLSPLLDRIGESRLVLLGEATHGTSEFYRFRARLTQQLIEQKGFNMVAV... | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-m... |
A0A0Q0AFB7 | MKFSEQWLRGWVSPQVSRDELVARLSMAGLEVDSVTLAAGVFSGVVVGEVLSTEQHPDADKLRVCQVSNGSETFQVVCGAPNVRPGLKIPFAMIGAELPGDFKIKKAKLRGVESNGMLCSAAELQAGEGNDGLMELAADAPVGQDIRVYLSLDDASIEVDLTPNRGDCLSVAGLAREVGALYAAEVTRPQVAAVSAVHDEVRPVEVLAPAACPRYLGRVIRNVDLSRPTPLWMVERLRRSDVRSIDAAVDITNYVMLELGQPLHAFDLAEINGGIRVRMAEEGEKLVLLDGQEVSLRADTLVIADHQRALAIAGVMGGEH... | Cofactor: Binds 2 magnesium ions per tetramer.
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 612
Sequence Mass (Da): 66472
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A0A9D8TN38 | MNVRVLIVDDSYFFRRRLSEAIDGKKGIEVVGFASNGKEAIELVQNLHPDVVTLDIEMPHINGLEALKAIMKKAPVPVLMFSALTTVGADITMKALEFGALDFLPKNFNELAARREDVIEIVTNKILALSRARHVVRIRAGDGESPVRENRSSDMSSSDISRGKVQRGQTAANEYSSLSKQISRNTSDLFMKTEKPAARGFSDKKVGVMAGIDVEQAVSKKENKAAAVDDLKWKDVSFSSFARDLQRKTELRKNSSDFHNFQNSFNEDGKTRQQAHAGKFSQKMIPGKSEILKTADEKLSDAVTKLDVGIMSRDELSSLM... | PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate resi... |
A0A850MKR7 | MCEISELEPLIVTSHDKGPKRGIALYFGINEINELEKNGLSLKEDRRFLVQLTTDNKLILIPFSNLDFLLNIEDKLDTIIDLDKEEKEEFTEELLAIISEKKVEIGNKERYSVFQFTKGHYTRYNIRNTIRVGLRVDKKATLNLIKKYIEKKRANKMIDEKLIEEFSYLSGNDKEDLRDELIDLIVEKNVDMSQQEKSAMFQFVKGHYNKNILSKVLYLVNKTDPNKIKQLSTTFLKDKTKISPPKPLKADINREELLNRIKTFSSTIQEDFVEDILSILSKDELKNLNLAPREKTDIFQLIKGHYNPARLFNAVQVAIR... | Function: Catalyzes the oxidation of methyl-H(4)MPT to methylene-H(4)MPT.
Catalytic Activity: 5-methyl-5,6,7,8-tetrahydromethanopterin + H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n) = 5,10-methylenetetrahydromethanopterin + reduced coenzyme F420-(gamma-L-Glu)(n)
EC: 1.5.98.2
Subcellular Location: Cytoplasm
Sequence L... |
A0A0G1Z3Z3 | MNFEIQKKLKGALGRTGILSTAHGNIETPAFVAVGTKATVKSLTPEEIRATHAQIVLGNTYHLYLEPGEKIVHEAGGIGAFMGWGGPTMTDSGGFQVFSLGAAFNRASRSKISTHKEHTNKLEIVGMSTARGKEIPPAKIDEDGVTFKSPKDGSAHRFTPERSIEVQHALGADIIFAFDECTSPDAPYTYQKEAMERTHRWAKRSLERHCELKQGSTLPARQSLGAGGNREKGRTLFQQQLFGIVQGGQFEDLRIESAKTIGQMEFDGFGIGGSFDKEDVGNAVRWVNELLPEERPRHLLGIGDPTDLFDAVENGCDLFD... | Cofactor: Binds 1 zinc ion per subunit.
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His ... |
A0A5Q4C5E0 | MRFSPFISTLVFTFSNLTRVRAAQFVRAQAPYAAARPLRASMSSIPSLGALFGSSASQKDTMSYPDNRSADEWRAVLNKEQFRILREKGTEPPGSGKFDKHYPEEGVYTCAGCSAPLYKATHKFKSGCGWPAYFDSLPGAVVRHEDRAFGMARTEIVCANCGGHLGHVFKGEGFDTPTDERHCVNSVSLSFSTDEKKAGEGSGEGAKGESKV | Cofactor: Binds 1 zinc ion per subunit.
EC: 1.8.4.12
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Length: 212
Sequence Mass (Da): 23018
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A0A2M7T3C1 | MVAIALYQPEIPQNTGTLMRLAACFDLDFHIIEPCGFLWNDKKLSRSAMDYKKMCTLIRHLSWDHFQHYIKDTQKRIVLIEVDGKKTCWNFKFQENDVLLLGSESVGVPHTVHTLSHESLHIPQKQGRSLNLAVAASIVIGQALSQQ | Function: Methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH of the wobble nucleotide.
Catalytic Activity: 5-carboxymethylaminomethyluridine(34) in tRNA(Leu) + S-adeno... |
A0A1G2BFT6 | MNKKFEIIIGLEVHVRLKTCSKLFCACNNIDEGIAPNKNVCPTCFGSVGTLPLLNKEAFLLGIRASKALKCSIAKKCKWDRKQYFYPDLPKGYQISQYDMPFAKNGELEFFLDEKNLKKILINRVHLEEDAAKLLHTKKDSLVDFNRSGVPLIEIVTEPDLRSASEAKQALKEIHRIVRNFEISDADMEKGQLRCDASVSLRPYGNKKLYPRTEIKNLNSFRMVEMALQYEIDKQTKEWLEDNFQKTQRTVLWNSVAKKTEFMRGKETEADYRYFPEPDVPEVEIESQLITESCGDSFVLPIEKVKKYLAIGLYFSIANI... | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
A0A1G2BD67 | MQELNKKLFGGYIKILVYTEHPDTEKILQKTYTEGLRLQKIFNFYDPESELSQLNQNKKAKVSPELLSVIKTALNYCIQTQGAYDITLGKVIAKRKKGLIVKTHCSYKDVAIQENTVIFNNPEVQIDLGSIAKGFVVDCLIEYLQKNGIAESLIDARGDIRVCGMINHVLGIQHPRQEGIVGSLKLNNQAVATSGDYEQFVGSFQNSHIVNQQELASVTVVAKTLQEADVFATALFVTPRSQREKLLKENSQLQTLTVDVKEQVRTYNQFEKTLTYEN | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 278
Sequence Mass (Da): 31332
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A0A1H1UCT2 | MSLITTDKQRIIVGLGATGLSVARYLAGRDLPFAVCDTRAEPPGLDKLKRFAPMADLYLGELDAELLSGAGELIVSPGIALSTPAIKSAIDAGVSVVGDIELFAREADAPIIAITGSNAKTTVTTLVGAMVEQVGKRVAVGGNIGTPTLDLLDEKADLYVLELSSFQLETTQTLNAAVAVVLNVSEDHMDRYTGLAAYHLAKHRIFRGAQQVVFNRDDALTRPLVADQLPCWNFGLSRPDFKGFGLIEKGGQSWLAFEFEALMPTAELKIRGAHNQANALAALALGHAVGLPMPAMLAALREFAGLPHRCQWLGQYAGVD... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
K1K0G2 | MSEATKVVGLVCAAGVGSRMGLGSPKQYMKFGSEAMLVHTVRALRAVERMGEIVVVVSPTDPYIDDVARHFPENVRVLRCGGRERAESVVNGLLNAGFDRDAWVLVHDAARPCLKPSEAARLIDEVLADGGVSGGILAVPVADTIKRADKSRMILETVPRSDLWRAATPQMFRVHDLVEALSGDLAGITDEASAMERLGRPVRIVPGRTTNIKVTEPADGVLASLILGDGAVVPFRVGQGYDSHRLVEGRPLILGGVQIPFELGLDGHSDADVLLHAVTDAVLGAAALGDIGQHFPPSDPKWKGADSRVLLRAVVALARQ... | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (... |
R7QXZ4 | MAKEYAKEEDLILLCGHYEGIDERVLEEIVTDYVSIGDYVLTGGELPAMVMVDAISRMVPGVLSNQESGSTESFEGSLLEYPQYSRPEEWHGKKVPPILLSGDHAKVDAWRREQSILRTKERRPDLLKRAELSEKERKNL | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.228
Subcellular Location: Cytoplasm
Sequence Length: 140
Sequence Mass (Da): 15962
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D3R0I0 | MKPTNSAPEAITANRKIDPVGSVTQLAGVSAKRAALMARLNINTCRDLLNYWPRRYEDWATLSTLADIEPEQEVTVLARCITMPHLQYKGKLSYLRVGLADASDQLGVIWFNQPYLETQLDIDKVYLFHGTISKNRPLSLQNPAFTPVPELAEAPLNTIKPSALANTFIRPVYPLTAGLTQGVLRNLIRQCLTAMREQLEREDYLPLKMRQRQHLTTYVYAVEHIHFPTCLEDYTIARERLVFEELFFMQLGLQLLKKRRLNGQTAPIINLDKTAETKYQAVVNALPYRLTKAQIAALQDISTDLAVGIPMDRLVQGDVG... | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA).
EC: 3.6.4.12
Catalytic Activity: ATP + ... |
A0A8D2CPW0 | GGERPGGTSGPGPLPRPPAARSGAAAREPAPRCAGAAHNPSSSPGLRVSEAQTFLLPLTPAHHPGSARVGQAFAGPLRREHHVPPPADPAGGPKWRRAPGPGAEEGPLGQSPGRVGGSAPATAVHADVRRDRGLQRAAAYDRAGYLGGDETPSPAPSQPRGRGLARDSPQAWGTVPGFWGLGLASAAGCPESDLAGGVWTTWHAPGPLGLAGGAAAHPAASHSHLRPEEIRYRLQHYFKFLFVRDPLERLLSAYRNKFGEIREYQQRYGAEIVRRYRAGAGPSPAGDDVTFPEFLRYLVDEDPERMNEHWMPVYHLCQPC... | EC: 2.8.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 407
Sequence Mass (Da): 44106
Location Topology: Single-pass type II membrane protein
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A0A1G1KKT5 | MIFYSLMTDKQKGVIFAPLKASLYLLSLIYSMAIFFRRIFYKLHIFKTHNAPLKVISVGNIALGGTGKTPFTITLAKILESSLKRNVCVLIRGYGWDEQEMLKRNLSDVPVVVGQDRARSSYKAIKLYGSDTAILDDGFQHWELARDLNIVLIDSRNPFGNGRLFPRGILREPKRALARADIIVFTKASEKSCDINKIKQEISSIKNGLIFLEAVHTPMHFYEGRAKHIFDLSYISGKKVILLSSIGDPLYFEDTARGLGANIIEHIKFQDHHDYRKSDIDHVIRRCNERNFDFVLTTEKDIVKLNRLGLNLCPYTVLTL... | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form te... |
A0A2M6YPL1 | MIRKIITIPHPLLRQKSKPVRKIDKKIEKVIVDLLETVKNASEPEGLGLSAIQIAQTLRIFVAKTGKNFEVFINPKITFSSKKTLKEVLKKEQQFFEGCLSIPGIYGFVDRPYQIKMEWQDEKGKKKVKEFKNRLAICLQHELDHLNGILFIDRLLKQKGSPRGEAGKIYELKKNQKGEDLFEEVEL | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
A0A2S6MV33 | MAKLRTLLAGAFAATLLAAPLAVPLAAPAFAQDEATMPNESWSFENPFGTFDLAAAQRGLQIYGQVCSNCHSLKFLHYRDLAGIGLTPEQIKAFAAQFTVPLGLDDQGNPKEGPALPASEFRSPYPNATAAAAVFNGAVPPDLSVMVNAREGGPNYVYGILTGFVNAPAGFKLQPGQYYNTMYPGHRIAMPPPLQDGTVQYTDGTKATLHQEAHDVVTFLAWAANPEMVERKQMGVRIVLFLIFMTGLTYAVKRKVWANVEH | Cofactor: Binds 1 heme c group covalently per subunit.
Subcellular Location: Membrane
Sequence Length: 262
Sequence Mass (Da): 28284
Location Topology: Single-pass membrane protein
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A0A1Z8WU72 | MSKKTSSKWINRQTKDPFVKRRNQLSARSRAFFKLVEINDKQRFIKKGYKVIDMGAAPGGWSEAASEVIGSHGHILSVDSSDFKSVRNGTSLKINCLDPRLKGKITGVFVPGSVDVVMSDMAPNLSGIKARDEANWLDLVDVSLSIADLFLQKNGTFLVKFFQFRDTASAYNRIQNSFRMVKRLKPQSSRAESSEFYVLAKGKKNSDQEVLN | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.166
Subc... |
A0A7J2KB10 | MGTRIADRDVLSKAITLLLKYPLCENCLGRLFGGLGRGLSNYERGRALKIVVLMDIYRRFIEGSMNKEEFITIASNIGSIAKQSVLELGFPISEDRSRCIICGFSSLEEKLVEWAQRIVKYIKEYNARSFLVGVVKGSSIEKREEELAREIELKYYENIRNEVKREVGKKVQELIDIKPNFTRPDVVLIVDIDNDAITVKPMPIYIKGRYWKLGRRISQAKWILWNGSKKYPLSIEEVLEPMGEIVGAKEVILHASGREDVDVRMLGTGRPFIVELKEPKTYNFDLKTLEEKANSVSRYVRFTLECETSRKDIRLIKIER... | Function: Responsible for synthesis of pseudouridine from uracil-54 and uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(54) in tRNA = pseudouridine(54) in tRNA
Sequence Length: 435
Sequence Mass (Da): 50249
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A0A380MQB6 | MSNIQAIAFDLDGTLIHSLPDLAASVNQMRAHYGLAPLPESTIETYIGDGALELVHRSLTGDRNGRDNERVDEAFTLHRDYYYDHLTVHTTLYPHVAQTLEKLYQKGIPLALVTNKPEKHAKNLLNHFNIAQYFTTIYGGDTLPVHKPDPAQILAAAKDMNVEPTALLMVGDSPNDILSGKAAGAKTLLVTYGYADIPAMLANPNTTPDYQAKQIDELLNYI | Pathway: Organic acid metabolism; glycolate biosynthesis; glycolate from 2-phosphoglycolate: step 1/1.
Function: Specifically catalyzes the dephosphorylation of 2-phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major ... |
A0A0A7FY69 | MILVLNLNASVDKKYKMNDLSKGLVMRALDVHNTPGGKGIHVANVISILKEDCLATGFLGGKTGEFIENKLKEYNINQDFVKIQGDTRECLAIITDDLVQTEILEPGPTVTNEEQEEFLNKYKALIKNCNIIVASGSVPKNIPKYFYKTLIDIAKSENKKFLLDTSGELLENGIKAKPFFIKPNKDEIEALTGRKISNVKDAINEIKEFHKKGIELVVISLGKDGSIAGFNGKFYKVTVPKVNAVNPVGSGDSYVAGIALGLQKDFSIVDVLKYASACGTANAIEEETGFVNKEVVENLFNKITVDIIEE | Pathway: Carbohydrate metabolism; D-tagatose 6-phosphate degradation; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate: step 1/2.
Function: Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
EC: 2.7.1.144
Catalytic Activity: ATP + D-tagatofu... |
A0A177W9C0 | MPPLMPIYTSLDSSNCPGSAAEDLELGQISTTEYTAIEVKKNGQRRFCSKCNLLKPDRCHHCSACERCILKMDHHCPWHPCP | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 82
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 9246
Location Topology: Multi-pass membrane protein
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R9PQW4 | MSVVSSIQSDVDLSPYNTFALAAKAKHFVELKHAEDIKELIAWVGSKQLPWMVIGGGSNLLLLEDFSGLVIVNKLRGIEVSDDAETYTIKAAAGEDWHQFVQWTVKQGMPGLENLALIPGTVGASPVQNIGAYGIELANVCSEVEFYSLLTNSMQTLSSKQCKFAYRDSIFKAQLKDQVVISKVTFKLSKSWLAKRDYGGLQQLAEDVSAQTVFEEVCRMRISKLPDPKVLGNAGSFFKNPLVSQQHLSSLLSRYPEMPNYPASKGQTKLAAGWLIDKLGLKGYSIGGAAVHQDQALVLVNKANAKASDLLALCRHIRQQ... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 355
Sequence Mass (Da): 38909
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A0A1Z8LC98 | MSLIVKLKGKIDNYSENFIDIDVKDIVYRILMTNSNIEFFKEITTEVEIFIYEIIKEDSRTFVGFKDFQEREVFSDLLTVQGVGSKMAINIMSSLECSEIIASIKADEISRLTKISGVGQKLAKRILNELKEKLXKKFELSDFKISEKDQKXKNDLISCXINLGYPXKISESTAIEVISKNESXDLESLIPIALKMLTHPS | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A1ZNE2 | MTYLYIFIGGGLGALSRFAVSNLVNKLSQVSFPYGTLTANVLGSFLIGLVVAWFESKTQTFTHWKPLLVTGFLGGFTTFSSFSYETMQLFKTQGIAQGLANAGGNVVLCIVCVYLGYSLAKAA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 123
Sequence Mass (Da): 13184
Location Topology: Multi-pass membrane protein
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A0A8D2E0Q6 | MQGPPAPAPGPGPGSPRGSPRGSPGLFRKLLVNQSIRLQRRFTVAHPLCFDLENGLSCGRPVLEPQSGPSLGRGVQAPAPHSQRRESFLYRSDSDYELSPKATSRNASVASDLFRSLPHLTTSHRQVLASLRTVRSNVAALAHRIRGPGSPRREDTGQKLALETLEELDWCLDQLETLQTRHSVGEMASNKFKRMLNRELTHLSETSRSGNQVSEYISRTFLDQPTEVELPRVTPEEPQRPVSEISGLRGLPHSTSLSAATVPRFGVQTDQEGQLAKELEDTNKWGLDVFKVAELSGHRPLTAIVFSIFQERDLFKTFQI... | Cofactor: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Pathway: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.
EC: 3.1.4.-
Catalytic Activity: 3',5'-cyclic AMP + H2O = AMP +... |
A0A8D2DR99 | MAQRLLRQYTDIADGTECHRKAYASTSIGGAVGLIWSAYSVTLRPPDSILEGVARTGRYTFTAAAIGAVFGITSCVSAQVREKPDDPLNYFLGGCAGGLTLGVRTHSYGTAAAGCVYMGTVAALFKMGQLEGWELFSKPKV | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
R7YJP2 | MDHHCPWTVNCVSHITFPHFIRFLFYAVAAMVYLEYFLYIRAAVLWKDRKMPSYLGPSALQLAHLFVLVVANSTTLFALSILLVQSIWGLASNTTTIERWEIERHEALLRRARHLGGFLDGPDGQRVRIIRQEFPYDIGIWKNIKQGMGSGNAYPSVTWPPPDPDRIPRVRREFNPEEAFIHKEGYVDTYNEVEAFRQRQQEDLQRWKRPSNEVQRRRPFHERLEKSVAAEVEDGYSSPDEQDGAPGEEAWRNSEGERLADFGVEEDVDFYDEDEVPLADLLRRRKAASVKGQ | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 293
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 34075
Location Topology: Multi-pass membrane protein
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A0A1F9WAW1 | MQKNSFTWKLILPVITASVLGILFSGFLAYNIARREILRSVNREINLTAQEVASQLSAFFAQRSSDLESFSEVPLIQDYFNNRDFGLNEEAAAYLAGFKQFSSVFINRTGVHQAAGLMDRSGTELCRVEKREPAPRFGPGAGKSVGPQFFEQARAAGPSGRYISSVLNAAGRPPFMVYARPIYNPAGELRGVAYLEADLTFMAETLHRLTVGASGFSFVSDSDNKVVLGASQQASGSILKTGRDIPGTDLSITVIAELSDFLKPLSQIRAATFGFVIFFGLSVGLFIYRKIRLSLSPIKALVSAAGHFSKGELDYMVEVG... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 1014
Sequence Mass (Da): 110350
Location Topology: Multi-pass membrane protein
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R9PF02 | MHVLVFDSGVGGLSVLEQLQQRNPNMQYSYLFDNLYFPYGELDDQQLITRVVELLTKAVNKFNPDLVVVACNSASTLSLPSLRETLSIPIVGVVPAIKSAANKSITRHFGVLATPGTVERSYTEQLIADFAKDCRVELLGSTLLVQLAEQKLAGESIALEDVKQALASWLLFDDLDCVVLGCTHFPLLKDEIQQVLGERVCLVDSGAAIANRVHSLLSTNEALNLSQKKAEAHAYCTMHPANSSLLKQLQAYQLSSLQLFT | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
EC: 5.1.1.3
Catalytic Activity: L-glutamate = D-glutamate
Sequence Length: 261
Sequence Mass (Da): 28590
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A0A2Z4FR28 | MAGIFLVFLLLPLIAIGTTTTPAEILTALKDPLVWPAVRISIVTTAISFGITLAFGTPLSWLLARSRSRWARACESLLELPIVLPPAVIGVALLLAYGRRGWLGGVFESLGWSPGFSLSAVIFAQLVVAAPFFIQSATAAFRQVDDELLIVARTLGASPMRTFLRVAVPLALPGLLNGAALMWARALGEFGATLFFAGNLSGRTQTMPLAIYAALESDLRVAQAMSVLLVAVAILLLSALRGPIAAKFGPYRHNGELQ | Function: Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 258
Sequence Mass (Da): 27380
Location Topology: Multi-pass membrane protein
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A0A6A6V7R8 | MPAVSPHSGLNVIPHKHQVSHDFEFIPPTDERSADPLERWKGYPIFRWGLGGTVVTSFPKQIPRYGGGASQPKLKCTPGEVKLPTVKEFLPLPEETVKFPGPLKAKSKKKDVSAWLGRGIEAVENQLKAPGFDHLMTPSDVKRLHEKVLLWKILQVMVDNDGVLEGNPTVEGAIRRILAPEGLISDSEPNASIPIAADLVGGMAKSQTTAQPEPIDPKAVEELRSLLTKGDREKAVWHAVDQRLWGHAMLLSSTLDKNVWRQVVQEFVQKEVKKAGPNNQALAVLYEIFAGNWEDCIDELVPASARAGFQMVSTDGAGAP... | Function: Involved in the initiation of assembly of the COPII coat required for the formation of transport vesicles from the endoplasmic reticulum (ER) and the selection of cargo molecules. Also involved in autophagy.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 556
Sequence Mass (Da): 60210
Lo... |
A0A9J6P481 | MNEYVIGIDIGSSKIYAAVGKIDSEENLQIMGISSSKCEGLNKGIVIDIESTAKSIEKCKGQLQKMVEQDFNSAYLVVPGGICDLIESKGVVAVSALENTVTHKDKDRAIEASKFISITSDKEIIGVIPQDYVIDECDKIKDPVGMCGNKLEANVKVVTARSSVINNLIKSVEAAGLTVKGLELKPIAAASVVLSQEEKKFGAALVDVGAETIDLSVFSNGKLCYTSIIPFGGKAITNDLSVGLKVSMDEAENMKLKYGTLKKDVSNETFTCNNISGEFIEVKHGFLVDIIEARVSELLEFIKAELEKSGYEKSIERVIL... | Function: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular Location: Cell membrane
Sequence Length: 418
Sequence Mass (Da): 45284
Location Topology: Peripheral membrane protein
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A0A850LXU3 | MKDVIIPNGRPYVILNAAMSLDGKISTCSGGAEYSDEQDWKRVHKLRADVDGILIGIGTILKDDPKLRVKYFSGNPTRIIVDSKCRIPLDAKVINFEREKYPAIIATTEQAPKEKIEALKKLNVEILICGPGPQVDLDDLMHKLRKKGFQSVMLEGGGTLNFGMFEKNLIDEVRICMAPVIVGGEEAVSLVDGKGFPDLNDAVNLKLVRIEELGKNLILFYKVVE | Pathway: Cofactor biosynthesis; riboflavin biosynthesis.
EC: 1.1.1.302
Catalytic Activity: 2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-phosphate + NAD(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-one 5'-phosphate + H(+) + NADH
Sequence Length: 225
Sequence Mass (Da): 24923
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A0A1Z8L8N1 | MXNSSKNIVLIGMAGVGKTTVGRVLSKKIQRKFXDXDQEFEDQTKIRIXDFFXIXGEKXFRKIERRIINDVLTKNKXLVVSAGGGIFSXDEIRDLIIKKSITFFLDSSIETLXERLKKNFSXRPLLNKGNLXXNIEKLYQKRIKDYMMANHIILVDDLSVEDVVLNIIKRI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
A0A7U3US75 | MGDHITRPENDFIPALRWEEPPEGPVLVLLDQTRLPQEEVELACTDVQGLVGAIGSLAVRGAPLLGLAGAYGVALAAARGYDVEEAAELLARARPTAVNLAYGVHRALGAYREAEPEHAAAAALAEARALHAEDAEASAAMAGHGKQLLAELVPGGGYRVLTHCNTGALVSGGQGTALGVVLAAHRAGELRRLWVDETRPLLQGARLTAYEAARAGMPYTLLTDNAAGSLFTAGEVDAVLVGADRIAADGSTANKVGTYPLSVLARYHHVPFVVVAPTTTIDLGTPDGPSIEVEQRSGAEVTDLAPSPLGTQAYNPAFDV... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6.
Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
EC: 5.3.1.23
Catalytic Activity: S-me... |
E4XY39 | MPAIAGMVTANGAEILLSIFASCKAWEVFPGKNTFYCDGRFLTANDKTVLCITSTLITMTTALFIFNDYRATLKDQAYGIYMLACSLLLYSFVMLMLFRTSFCDPGIIPRASSSQSAQVERQLIDADVRKNGYSGYKPPPRVQEIEINGVTMKQKYCFTCKIFRPPRSSHCSICDNCVDRFDHHCPWVGNCIGRRNYRYFYLFLASLSGRCLCLLIFSCSLMNLLILSKEKHNGEILAALQESWPSAFEIFVSFFSIWSVVGLTCFHTYLTSTNTTTNEDIKGSWKKNRAARNPFSRGSCLLNCIHVLCAPLPVRSFNPR... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 352
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 39979
Location Topology: Multi-pass membrane protein
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K1KK77 | MQDLSILEERIGYKFADRKLLERAVTHRSFAAQHNERLEFLGDSVLNCVVGYALFQRDKHFTEGDLSRVRANLVCERTLAVIAKQIDVSAFLRMGEGEMKTGGAHRPSITADAMEAIFGAVFAESGFEAAQKVILGLFEPILAAPTAEQLGKDSKTRLQEYLQGRHLPLPQYVVVSVTGAAHAQHFNCECRILSLEITTQGHAASRRSAEQEAATAALEILKNRESTNGRSRHE | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
A0A9D0KW51 | AREHTRNIIPVLDRAVKEAGVDLNSVDAVAVTVAPGLIVSLVIGISAGKSLKWALKKPLIPVHHIEAHIFAVFLSEDVQFPFISLVVSGGHTELYVIRKFEDYTFLGGTLDDAAGEAYDKVARMLDLGYPGGPVIDKLAKEGKEVIKLPRPLLNDKGKNRFNFSFSGLKSAVMREVEKGVYKKEDIARSFQEAVVDVLVGKTVDAVNEFGIKNIVVSGGVSANSRLRERFFEEAEKNSFSVHFPPLYLCTDNGAMVAYTGYRRFKETGRTIGYDFEGKARLRLDRFVEYISRR | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, togeth... |
A0A2V2XS05 | MSGLGVDLKPVEDENIHLTLRFLGDVEDSLIPSIYRAVDELSSFGSFVMRVRGLGAFPNTKNPRVVWVGVADGSEILRSMRSALDRGLRGLRVHEDEHAFHPHITIARVRGRSNLDILSRYIEENIDLEFGLSPVTKVVLKKSTLTPRGPIYSDLRVVALSSPR | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 164
Sequence Mass (Da): 18273
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Q0W7F4 | MYSLFGNNLKSAYNNLSKMVPEEIRYILLLFILSRFILIIIGCYSRLRYCGSDFFHFTDFIWLNVWGVYDSGWYVSIANNWYSSHLSTYPTTLNQGNYAFFPLYPLLMKLIGSIIGSTFIAGLIISNITLLIACFFLYKLILIENDPTIAKKAIKYTFLFPVAFIYSGVFTESLYLALLIMCFYYARKEQWHIVGLLGLFLSLTRSLGVFVIFPMLLEYLAIRDYKVTKVKSNVLYLLLIPVGLAIFSVYNFYFTGDFFAFIHIQSAWGRHLDNPLNYLLHGLFSNHAEEFFWAFFTVVFTVLLIAGSSLIRPSYLLVGV... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 384
Sequence Mass (Da): 44188
Location Topology: Multi-pass membrane protein
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