ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A2D9XV03 | MQLIIVSGLIGSGKTTVSKLLKKKKFHYLNADGIAKDLLKTNKEIKEXLFDAFGKXINLGKNLSLKKIKEKLXVSKKNKIIIDKIIHPIFFSHINLLLKKMRKSSVVLELPLIETSXNISMPFKILTXDCSFXNRLERSLKNKKISKLEFTKLNXMQSNRXFYINNSNFILSNNGTISTLKNKFEELYLRKLLIK | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
A0A2E0GNF3 | MNVLVYSINPSKNKILLPAINEYSKRIKYFVNFKFIEVKSLKLEHIKKFKNKFIFALDEEGELLNSLEFANKIRDFMEDNLDIVFIXGDANGLPSDVIKNSNMVLSLSKLTLPHLLARVVLIEQLYRSFSIINNIPYHKG | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.177
Subcellular Location: Cytoplasm
Sequence Length: 140
S... |
Q2PYQ5 | HIELAKPVFHAGFLVKIKKVLETVCCSCGEIKLDDTNEAFKRALRMTDRKKRFNAVWKLCASKKECEGSSEDDDFMADADNNQEGRGKKKNSTHGGCGASQPTFRKKGLSLEMVERQTKDSEGGDLAGKGRVIAPGEVKQLFESISDDDAEAMGFSPDYSRPEWMVISILPVPPMAVRPSVHQEGLGRSEDDLTHKLMDILKANNTLKKNEQDGAPQQIIREFEALLQYQVATLMDNDLAGVPQSLQKSRRPIKSIRARLKGKEGRLRGNLMGKRVDFSARTVITGDPNLSIDQVGVPRSIAKNMTFPEKVTPFNIEVLT... | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 808
Sequence Mass (Da): 89684
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A0A2G6EUV2 | MTDSLQFIYFFRQAAPYIHQHRDKTFVFCIQDDETTQSVLKSLLHDIAILHSLRVRVVIVFGARYTLNQQLKDQRFHQNRRITDAKALQQMQSIVGALGIQVQAILSMGLANSPMQGASIQTGSGNFVIAKPLGVRDGVDFGLTGEIRKVRSEAIRHRLDSGEIVVIPPLGYSSTGEVFNLTTEAVAGAVASALKADKLLFFNDAVVKFADTRDEGKVVTSAEANALADNNADEVILSTVLKESAAACKQGVSRVHIIPKQTDGAVLAELFTRDGFGLMVTNEAYDRIEQATFDNRNRLF | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
EC: 2.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 300
Sequence Mass (Da): 32957
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A0A2G6KP55 | MASLEKLLARIEDAPDGPQITAIFDFDGTLIAGFSATVFLREQLRRGDLSPRDFVAVAAAMTNFGLGNIGFSALMVVTAQFMRGIAEDDYQALGQQLYEDHIARLIYPESRALVEAHQRKGHTVAVISSATPYQVEPAAKDMNIDHVLCTKLEVEEGKFTGSVIHPTCFGEGKVTAALELNDKVGADIEDSFFYTDSTDDLQLLARVGKPCALNPSNKLLRFARKQKWPTAHFGSRGRPTVMQFIRSVTATGSLVTSFLAGLPISALTGSRRDANNFSLSLFADTASALVGLRLNVTGEENLWKNRPAVFIFNHQSKADV... | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 553
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da):... |
A0A2E3UW34 | MLNDQNKSKIFIVDFSGNEKRVDLWLKEKLQEISRSKIQDLIESKMILLNNKPCQTSTRLSPGDVIAIKKISHKNQDMLSPVKMNLDIIFEDEHLLVINKAAGLSVHPGAGKASETTLVNGIIYHTQGQLSTVNKSENGNRPGIVHRLDKDTTGLIVCAKSNKVHENLAKQFRLKTSQREYIALIDGEMKMKTQNCESYLSRDPNNRLRYTSFSNQELLCKYKEKQAFPKKYRLAKTKIEKVCIYAGRFTLIKATLETGRTHQIRVHTAKIMGFPILGDPLYSVKKTLPKIFNKDLAMKIKRINRQLLHAQKLSFYHPIK... | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 350
Sequence Mass (Da): 39989
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A0A947C3N9 | MSVTYADWVSKAQSKLTSISESARLDSQLILAHALNKDMTHLLTWPDKSIPENLIHALQALLGRRLAGEPMAYILGQCEFWGLTLDVNSDVLIPRADTEVVIETILKVVNDLGLEQPRILDLGTGSGAIAIALASELPIAKVTAVDVSSAALTVAQLNANKHRLKNISFVVSNWFDAITGQAFDIIVSNPPYIAEADPHLASLVYEPEIALTAKDAGYADLALLIQQAPDYAASGWLFLEHGYNQSEKVRHIMQQCDYQQVVSVKDLAGHERCTFGKIPNHG | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A963AZP7 | MPEYLFISDLHLSPERPGTTSLLLRFLRERAVHGSSLFILGDLFDAWVGDDDRRPPIPEILAAMKQLTDVGTRLFFIAGNRDFLVGDAFVKATGCHLLPDTHLIELAGTQALLMHGDLLCSDDRDYQQLRGQLRSPAFIGEFLSKPLEQRIALATEYRKRSGEAVSLKAADIVDANQSTVENYLRDAQALLLIHGHTHRPANHRFRLDGADAVRVVLPEWQAYCGGYLSVCGNSISRHVFV | Cofactor: Binds 2 Mn(2+) ions per subunit in a binuclear metal center.
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 4/6.
Function: Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine ... |
A0A534B2A5 | MRRATAVRRGRGGFTLIEVLVALAIVAIGMAAVLGALSSAANTTAYLRDKTFAEWVALNQIATLRLKMQTAPPATGNTAGEVDFAGRSWHWRQEVSAT | PTM: Cleaved by prepilin peptidase.
Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 98
Sequence Mass (Da): 10472
Location Topology: Single-... |
A0A9C9YW42 | LDQDPEAVAAARERFGADERFAIWRANFADIDRLPIPDADRFDGVLMDLGVSSPQLDQPGRGFSFRADGPLDMRMDTTRGETAAEYLRRVSERELKRILKVYGEERYAGRVASAISRAARRGALQTTAQLADVVRSAIPGRPGEKDKATRSFQAIRIAVNREMEALATGLEKMVQRLDKGARLVAITFHSLEDRLVKQAFRRLSSPAPLPRKLPVPAADFKPSFQVVGKPLKPSAEEISANPRARSATLRVLEKLA | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.199
Subcellular Location: Cytoplasm
Sequence Length: 256
Seque... |
A0A2E3UTB4 | MYKGVKMEKILITGKIHPSAIQQFKSLKSYQVIYEPDVRRERLEDLISDCLVIVTRSETKLDNKLIDRAQKLKIIARAAVGVSNIDIDYATEKGILVINTPGKNTNSAAEHTMGLMLSMMRKIPQAFIKMKSGGWDRHLFSGFELKDKCIGLLGLGNVGHRVAKFAKGFDMQVYAYDPYIAPKLFTRHGVVPSQSPYDLASQVSILSCHVPLNKETKGMIDRKVLEKLPEGSYIVNTSRGGVVNENDLLKELDKGKILGCAFDTWEDEPLPKRELVEHPLVWCSPHIGASTLEAQKKIGQTIFEQVHKALGGGVVDFPVN... | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
Function: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydrox... |
A0A1G9REL6 | MKKWGFFVARQAHKKKRGKRWRWLVWLGGVLLVVMIAAAGYGIYLYDKLQDTVKEIHEPLNDEQQSEETESNGQTANDQNAERQSSYSDGTDIDDKQKTLNFLLLGVDERSNDQGRSDTMILVSANPNTNSMLMMSIPRDMYTDIPGKGMDKINHAYAFGGTSLAVKTVKQTFDVPIDFYIKVNMEGFRDGIDALNGVTVENSFAFTQDGKTFPEGEINLNGEEALAYTRMRKKDPQGDLGRNERQRQVIQAALDQAANFSNFTKIGRILDIVGGNVRTNMKLENMRNVYSHYRQTRKTIHSLQIDGSGKILEDGIWYYM... | Pathway: Cell wall biogenesis.
Function: May catalyze the final step in cell wall teichoic acid biosynthesis, the transfer of the anionic cell wall polymers (APs) from their lipid-linked precursor to the cell wall peptidoglycan (PG).
EC: 2.7.8.-
Subcellular Location: Cell membrane
Sequence Length: 340
Sequence Mass (Da... |
A0A9D8J5Z6 | MLHKLLHLAVIMDGNGRWATERNLPRSEGHLKGIDPVKMLIRRAVQHPDIQFLTLFVYSLENLKRPLQETQYIQDLLINCLQSDLEELEQERVFVRIIGDVAGIDLPVRYVSNPKLVVNLCFRYSGRWHISNIVNRLLAQNQPCTPDSIQSMMVADLGPDPDVIIRTGNEMRLSNFLLWNLAYSELFFLPVLWPDFSESHFDQVVTSYLKRHRRYGTLGVDDG | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in ... |
A0A9D8A322 | MNDDKIMNLWLAIALGGASGAMSRYWLMSYTISVLGKTFPYATLFVNVSGSFVLGFLSVVLWSKWSLPEELKLAIIVGFLGSFTTFSTFSLDVLNSFLAGHYVRLFIYIIASVSLSIVAVGLGYLAAKVVV | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 131
Sequence Mass (Da): 14261
Location Topology: Multi-pass membrane protein
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A0A3D5AXZ3 | MASAAVAGAAXTDQPAFINAVCELDTELTAPDLMAALLDIERAHGRVRDQPGGPRTLDLDLLWYDGQVVQDPALTLPHPRLHERAFVLYPLYEIAPGLEIPGRGRVEELLPACRGQGIERLAEQTG | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step ... |
E4ZS85 | MRRGLERSDHRRARPVGHAAKSGTSTRKAGVQFSTHQPLSSPAQRAAVSQLLDAPSLAFEVRGGRWCSLSYSFRTGSKYIWRRGMLWKPVIDQPNRGKTRLAKWYAPYSDEEKVKLKGEVHRLIAPRDQKHQSNFVEFRNMSKIVYRRYAGLFFCACVDTNDNELAYLEAIHFFVEVLDAFFGNVCELDLVFNFYKVYAILDEVFLAGEIEETSKQVVLTRLQLQGILQLQGLPRVAGDVKVEQMQAALCNAPQKYPKTKYPN | Function: Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration.
Subcellular Location: Cell membrane
Sequence Length: 263
Sequenc... |
A0A1M7FX59 | MTEVRYNWTKEEIAEIYHRPLLDLVYEAASVHRENKDYSEVQISSLISIKTGGCPEDCAYCPQAARYNTGVDVHAIMPKEEVVAVAQKAKDGGASRLCMGAAWREVRDNRDFDKVIDMVKAVNELDMEVCCTLGMLTEAQAQRLADAGLYAYNHNLDTSEDDYKRIITTRTYDDRLKTLEHVRKAKITVCSGGIIGLGETVEDRISMLKTLSTLPKHPESVPINALVPVQGTPLADQPRVSVWDMVRMIATTRIIMPKTVVRLSAGRTEMSLVEQAFCFMAGANSIFAGEKLLTTPNPSFDTDMAMFDLLGLTPRKAFKN... | Cofactor: Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.
Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2.
Function: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a ra... |
A0A9D1PUS9 | MDINFSLKDKSSEIKRNAFIENLTFFRERAKVSNFFEPSSVNELKSVLEKAREENLEISIIADGTHSIISECGIDGLLISTRKLKGMTIKGNLITASAGERLNDVINTAIEHNLTALEELGGIPGTIGGALYLDAHYQNVRLSDYVFYADYMDYDGNIYRKPHYMDYFSQEGVPSGKNEIILSVSLALKPNSRTAEARKRKEDFVALQFVPPCMNMCGLVFDLDESLYSTLDECASSFDSPCSIRMNSLFTFPETRASEIKEFIEKVIKEMKMKYGISVKETLSFLGKF | 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: 289
Sequence Mass (Da): 32555
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A0A7C3D3K4 | MARLVLLAVILCAQIAACSTSPKQIDLNQTQRNAAWIKHKSELDSIKHWQLQGRFSAQNETESWHGSIQWSQDQNQFAIHISGPLNSGSFSLHGNARSATLELAKDKIFQAPDPELLLETYTNLRLPVKNLRYWVIGLPSPDSDTRSTLNKNGLLGHLSQKNWEISFKNYQKINNLRLPNKIFLENHEFDVRLVIKNWQISS | Function: Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Subcellular Location: Cell outer membrane
Sequence Length: 202
Sequence Mass (Da): 23097
Location Topology: Lipid-anchor
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A0A7C7WGE7 | MDFDLRQWLLILGPVFIICVLLHGYFRMRSGNNEIKMKLDRSFVSRQGEDHVVDDLSLFKAELPNGGARLVDSKAGAVNPGDDVPLLMDAVELPSMRATSSVDLPKTDPLPAFTPEPIAEPIAGPEEPAIDHSVDVAPAKAPPARKAPKIEEDQSAEETAAPIRKPEMFVVIYVLALDEPFLGQGLVEVLLNSGMTFGEMDIFHQLDDRGAQLFSLASAVEPGTFNLSSLDQFSTPGVSLFMRVHELAAPLQVLDSMLSVANMVAQELNGEVRDETRSVMTPQTIEHCRQSLTEFLYKHSA | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 3... |
A0A9E5DUB1 | MPLDGKKIKLLALDVDGTLTDGGIYVLESGEQFRKFNAKDGLGVRRAVAQGLEVGIISHSLAAGMIIKRAEMMGVARCYVGQAPKLDVLREWCRELLITVDQVAYIGDDINDLAVIQAVGLSACPADASAPVLAACDVVLTKTGGEGCVREFLDRFLWRD | Function: Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate.
EC: 3.1.3.45
Catalytic Activity: 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate
Sequence Length: 160
Sequenc... |
A0A9E2B9H3 | MSEKELLLPDIGDFDSVEIIEMHVVAGDTVKVEDPLLTLESDKATMDIPSPFAGTIKQVDVAVGDKVSEGSKLGVIESSEKSTGSAPPAKAEKTDASAKPPAKTQKSAPAASKGGADIDTEVVVLGAGPGGYTAAFRAADLGKKVVLIERYEALGGVCLNVGCIPSKALLHTAEIINEADHMKANGVTFGKPKIDLAGVNDFKNKVVGKLTGGLSGLAKQRKVTVVHGVAEFIDQNNIQVDKGGEKTRVKFDDCIIAAGSQPTEIPSFPNDDPRLVDSTGALELSNVPKKLLIVGGGIIGLEMATVYDALGSEITVVEFM... | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.4
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH
Sequence Length: 585
Sequence Mass (Da): 61630
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A0A6L9SFW0 | MTQNRLRALTELGQAVWVDNLTRQMLNDGTLERMIADDGLSGVTSNPTTFDKAISDTDDYDDTLRRVAGETDDPTEAFFQLAYRDIRDAADLLRPTWERTEGQDGLVSFELPPDLAYDAQGSIDAAKRFRSEIDRENILIKVPGTREGVQAFEELTAAGVSINVTLLFAVRRYEEIAEAYLRGLERRVRDGEPIDGIVSVASFFVSRVDTKVDNALDELNRPELKGKAAVANAKIAYESFQRLFTGDRWDALRKRGANVQRPLWASTSSKDPDYPETYYVDQLIGPDTVNTMKEKTLDAARENAEVSVSLTQGVQEARDT... | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic... |
A0A2E0GQ62 | MSGFKSFVDTTXINISNDRTGVVGPNGCGKSNIIDAVKWVMGDTSKHIRGGSLEDVIFNGTDTRKPNDYAFVELIFSNTENKIGGEFAKYDEISIKREASRDGNSKYFLNNSHCRRRDIIDIFLGTGLGPKSYAIINQGTASKLIESKPEEFRVFIEEVAGISKYRERKKETESKLLDSKSNLDRVEDILKEINKRLFELKKQSEDADKFKKLNEEYEKIRAEVIAISIKNHLDKAERIKIENSKIETQIEKLNSEMLKKSNEIESITNEYDSKNQNYNEIQKKYYELMTEAGKIEKSLEYEQKSEKEKEEQTKNKKESV... | Function: Required for chromosome condensation and partitioning.
Subcellular Location: Cytoplasm
Sequence Length: 923
Domain: Contains large globular domains required for ATP hydrolysis at each terminus and a third globular domain forming a flexible hinge near the middle of the molecule. These domains are separated by ... |
A0A2E2YNU7 | MTPGPWELLIILAIVLLIFGPRRLKSLGSDLGNAIKGFRSAMSEKEDPSQPAEDPRIIPNESNSSASADSTTEQETAKQKQDV | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 83
Sequenc... |
A0A2E3YJH0 | MTEGRKVYTVSALNREARQVVSNHFGLVWVEGEISNLVKHSSGHFYWSIKDESAQLDCAMFRQKNRFLKFSPENGQQILAQGRLDIYEARGRFQLKVDYLEEAGEGLLRRRFEELKSKLALEGLFEADRKRVPPKLPSKIGVITSPSGAAIQDVLSVLSRRFPAIPVLIYPTAVQGDGASDEIAHTLTLANQRKECDLLILTRGGGSLEDLWSFNEEIVARAISSIKIPVISGIGHEIDFTIADFVADVRAPTPSGAAELAVPDKTQWLNTLTTISGQLSRTINQQLSATRRLLDSIGHRMNQSHPGVQLSQSSQKLDEM... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A6L7VJ83 | MSLTSIDRSQIPRINGGLVAIVESKWHANLVGVMAFKCKGVLISHGVTQVDSYRVPGTLEIPLAVKALAEDKVPKYDAFVCLSVVEKGSTAHFDMIVHATTQTLQQLSVDLKVPVINEILAVYDLNDAIARASNDEYNKGIEAAAAALEMMHLIERLE | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This ... |
A0A933R0V1 | MPLAEFSLIDRFFAAHAMRRADVALGIGDDAAVVDVPAGEQLIVAVDTLVAGVHFPDSATAADIGHKALEFARGFFALAERFQVELIGGDTTRGPLCVSVQILGTLPRGRSMLRTGVRVGDHVFVSGNLGDAGLALRLLQTQGSCADDVRTAVDARLHRPEPRVALGERLRSLASAAIDVSDGLLADLGHILERSGVGAMVWVDRLPRSTAFQSCVSPQTPEWFELPLAAGDDYEICFTAAPEQTAALQTLARELDVPITAVGVIEAEPGLRCCTDDGRDFQPTRRGSEPFD | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
EC: 2.7.4.16
Catalytic Activity: ATP + thi... |
A0A2E5M8J0 | MASQSDLLYLRTAIEHAAKGIYTTTPNPRVGCLVVRDGEVLGRGYHVRPGEGHAEVNALADAGRPVVGATAYVSLEPCAFEGRTPPCAKALIEARVERVVAAMIDPHPKVSGQGMAMLRAAGILAELVELPEAQALNAGYVSRVTTGRPYVRLKTAISLDGRTGMASGESQWITGEAARADVQEWRARSCALISGSGTVMADDARLTVRDERFSVDGVIRQPLRAIADSKLQLPSSAAVLQPPGEVLIVHAGINAPTVEGVEHICLPGSGVPPKVDLAALLDELGARGCNEVLVEAGAALLGAFLDADLWDELLVYMAPK... | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino... |
A0A938Q642 | MTNKIQESSGYYVPHSSWWPFATSIILGLTMAGFAEMLHGHMWFGALLSASSFFIGVYVIGRWFKDVVTESLAKLYNQKMYQTFRMGMIWFIFSECCFFAGLLAALIYIRLVSVPMLGGAEGYHISTREFLYPEFQAQWPLLDNPVNTSFHPPIAGVGPWGWPLINTAILLISALTLTFAHHFLLKGKNKITAFFIFLTSLLGSIFLVGQAIEYLHAYEALKLTLGSGVYASIFYFITGFHGLHVLIGTIFLFIIGIRLLKNHFTTESHFAFEAAAWYWHFVDMVWWCVFVMIYCL | EC: 7.1.1.9
Subcellular Location: Cell membrane
Sequence Length: 296
Sequence Mass (Da): 33749
Location Topology: Multi-pass membrane protein
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I4AGC7 | MKFTDFSDTIIALSTPAGRGAIALVRLSGKDAILHTQTFFRGKNLLEQKTHTVHFGTIRNLENEILDEVVVTIFKTPNSFTKENVVEISCHGSPFIVKRIIQNFLDNSPVRYAKAGEFTQRAFLNGRFDLAQAEAVADLIAVDSAASHKVAISQLRGGFSSQIKELRQQLLDFVSLIELELDFGEEDVEFAEREKLTQLVKTIQTVIEQLLSSFELGNAIKNGVPTVIAGKPNAGKSTLLNALLNEEKAIVSEIAGTTRDFIEDEISIEGIAFRFIDTAGLRQTDDKVESIGVERARKKMTEASLILYVIDLAELFNQNT... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
EC: 3.6.-.-
Subcellular Location: Cytoplasm
Sequence Length: 474
S... |
A0A8T7CRT7 | EPTGLLAELLRIEARMGRQRGAEKWGPRRIDLDLLMHGDNVMQSESLTLPHPGLAQRAFVLQPLAEVAPGLQLPDGRWVRDLLQKCDCTMLEPLAKQEEK | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step ... |
A0A921NCC9 | MSESVTFSNALASLEEVVRQLESGEASLEEAVALYSKGMQLAQVCQEKLQVAENQVAKIIDDNGQVQAFKEE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A1F8SHD9 | MPTSSGIWINIAGYYYRRSLDYPIVPIKSTKEIEFFTQVAYISIFFLLIGLILFIVAIRRKRLAGIPSGRLIYSDTNQWGKVEKPLYDPALRLTGKPDYLVKQGNQVIPIEIKSRSSPRAPYDSHIYQLAAYCLLVQHEYGNRPNYGIIHYRNQTFAIDFTPTLEETIKATLREMQDKTILSHVDRSHNNPRNCQNCGYRSICDQSLRI | Cofactor: Mg(2+) or Mn(2+) required for ssDNA cleavage activity.
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences ... |
A0A1G1YKV3 | MTKTIDYLKASRQELKKVVWPSRKEVIQHTILVIAVSLGVAFFLGGIDFILTLLIEAII | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 59
Sequence Mass (Da): 6641
Location Topology: Single-pass membrane protein
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A0A939B1F3 | MTGTISDRDDTIVAPATPPGRGGIGIVRISGPATRGIATAMLGAVPAARHAALTTFSDAGGESIDSGIALFFPAPHSFTGEDVLELHGHGGPVVMDRLVARAIGLGARNARPGEFSERAFLNGKLDLAQAEAIADLIAAGSEEAARAALRLLSGEFSRAIGELAARIMELRVLVEAAIDFPDEEVEFLGEAAVRERAGDISTRFEQISRLAGQGRLLRDGLRVVIAGRPNAGKSSLLNALAGHEAAIVTPIPGTTRDALREHIQIDGLPLHVVDTAGLRETSDVVESEGVRRTLGEIRGADLVLYVVDAAAGLDPAERAH... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
EC: 3.6.-.-
Subcellular Location: Cytoplasm
Sequence Length: 450
S... |
A0A2E1PMA5 | MXIDQAEKDKFNKIAEXWWDPSGKFAPLXKIXPXRSNXINXKKXVNNLEVLDVACGGGLLAEALYDFGAXVTGVDISEVAIETAKLHASKNNKDISXILGEAESLLLXKKAFDVVSCLEAXEHVPDPELLVKTCSDLCKPGGEVFFSTINRNPKSFLFAIIGAXXILXLLPKGTHDFNKFIKPSELHXFMTXSGLEVKEXIGMSXNPLSGNYWLGDDVTVNYLVHAHKPQ | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalytic Activity: a 3-(all-trans-polyprenyl)benzene-1,2-diol + S-adenosyl-L-methionine = a 2-methoxy-6-(all-trans-polyprenyl)phenol + H(+) + S-adenosy... |
A0A920AQ31 | MDLKAPDIIVRNEKRMLQESVDALFDNGRRGRVITGTGKRPLKSLAEMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPDLKLHECGLPKKMALELFKPFLYARLNKLGLASTIKQAKKLVEKETNAVWDALELIVREHPVLLNRAPTLHRLGVQAFEPKLIEGDAN | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 165
Sequence Mass (Da): 18575
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A0A5Q4F134 | MDTNALARHYPEHVARCQAVATEALAAAEADHLVICAGLEHYAFLDDQTYPFRANPLFKAWLPLHRHPGCWLIHTPGERPVLLYHQPRDFWHQPPADPEGYWTEAFDIRVIRDPAEIGQHLPGPPERRVLLGEGVEALVPGAKVNPERALNVLHWHRAVKTGYELACMRAANERAAPAHRAAREAFLAGAPEYEIHLAYLRACGHTDDELPYHSIVAVNEHAAVLHYQHREREAAPRRTLLVDAGADVAGYASDITRTWTAGDGEFADLVGAMDDLQRGLCAEVRAGVAFGDLHRTAHQRIGQLLKAAGVIRMDGEAAAA... | Cofactor: Binds 2 manganese ions per subunit.
Function: Splits dipeptides with a prolyl residue in the C-terminal position.
EC: 3.4.13.9
Sequence Length: 437
Sequence Mass (Da): 48412
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A0A920V5H8 | MANFLVLNGPNLNLLGEREPELYGETSLDKL | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Catalyzes a trans-dehydration via an enolate intermediate.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 31
Sequence... |
A0A8T6HTN9 | MALWRYLVFAGVIALGALYAAPNLFPPDFALQITADNSGRPVDQGLIDDLTILVEDGGIGVVGSELLAEGGLIRVANADDQLRASALLQDRLNPPGEERQYVVAFNLASTTPDWLTGIGAQPMTLGLDLRGGAHFLLQVDMVEALSKRLADEAEKVKDMLREERIRYRSTDIVIEGQTMRFAFATPQLRDLAVAVIEDEFREPDYTLESVDVGNRAGFLITVQSDKIREIESNAVEQNLTGLRNRINQLGVAEPLVQRLGGNRIVIDLPGVQDSADAKRKINKFANLEFRLEAQANDRPSEIDRWPYGGSVVELNKRVIL... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 617
Sequence Mass (Da): 67234
Location... |
A0A0H3VDC4 | AELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG | 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... |
A0A9E1U1K9 | MSICFIADLHLSADRPEIAQRFLHFLQQEATQHRTLYILGDLFEVWLGDDLSSQVHANILYALKRVTETGTAIYVQHGNRDFLLGRQFEELSGCQLLEDPYLIDLESEQILLMHGDQLCSDDLSYQKYRKWVRNRFSLWVLRHLPKSVRRRVGTTLRQRSEYGKQQKSVEIMDVTQDTVEAVTRQWNSTHLVHGHTHRPGYETFRLENRLIYRLVLGDWGASQKENVWVFSEGEFSQRHY | Cofactor: Binds 2 Mn(2+) ions per subunit in a binuclear metal center.
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 4/6.
Function: Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine ... |
A0A2D7G4G1 | MTERVGFENATAELEDAIGYQFKSMRLLVLAMTHRSFSKDNNERLEFLGDAILGAVVSSILFESNPNYQEDQLSLMRAELVKGRSLATLGRSVGIPEMLRLSTGEAKQGGADRESIIADAFEALIGAVYLDAGIEVVEEIVRRLFADRLEKAEFANLKDSKTELQEQVQSEGENLPRYSVVRAIGPDHNKTYEIKCELSWLKLETVAVSGSKKEGEKLAAQKMLGLLQETAV | 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... |
A0A920UYH8 | MSGAFTGQINAGLLLDQGCRYAIVGHSERRTLYGEGDEWVAQKGVSSPVSGFVADRVCWGNP | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 62
Sequence Mass (Da): 6615
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A0A344U8Z9 | MRIILLGPPGAGKGTQGMYLKRILGVPKVQIGDLMRENISQGTSSGLLAKQIMDRGDLIPDGVFMDMLRHRLSREDVSDGFLLDGLPRTVEQSQMLDSLVDERGHKIDIALHLDISRDEAVRRISGRRICKKDSSHVAHVLYAPPQGYDACRVCGGGFVARADDSRHVVKNRWAVWEAYTEPTAALYGARGQLVKVSGYGSVDEVTERAVDALAAFFG | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Function: 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.
Catalytic Activity: AMP + ATP = 2 ADP
EC... |
A0A6L7VSD6 | MNMIIESTTSVAVQFAEQVPDISGSDVTEWVESARGDRVGEVCVRFMGLDEARMLNRQFKEIDKPTNVLAFQSDVQGMLGDLAICVPLAVQEAQEQGKALSSHVAHLVIHGTLHLCGLDHQNEQEARRMESLESDLMQRLGFPNPYQDYG | 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: 150
Sequence Mass (Da): 16674
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A0A9C9FZE6 | MKLRYLLLLTSILLTPFNQVAHSQMLDGVYAIVNDDIITRQEFESAKRAVVSQLNSRKTPLPAAKILDRQILERLIIERLQLQVAQRRGIRVSDEQLNQAITSIATRNKITLSQLQKRLAEQGRDYTEFRRGIRRKLIIQNLLNLAIRNRLRITAEEIDDFLAKERQQGDLNLEYDLSHISISIAQDASADEIQKARNKAETALKALQNGEKFGRVSAQFSDASNALEGGRLGWLPAGQLPLLFTKALRRMKTGDISYLIRAANGFHILKLNAQRGARHQLVNQTHLRHILMLPDKLLPVKEMLARLRQIRQRILNGEKF... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
A0A9C9KNQ5 | MASYRTVRDLATTVEQLLVTAHNNRHRATLVLTGAPEWARNTALQLSNAFTTPVRYWISNQRLPDVRTIAPHQVDSILGSECDLLIVDALDGLNPDALAGASGTLRSGGLFLLLIPPLQNCVGVIQENDGNSNPVRAGYFLQYLAAMLGTSEVTIRTQSQTRDSTIRGLQIPVSSQTATNSSLACTDDQQAAIHTVRQVVLGQRKKPALLIADRGRGKSAAMGLAAASLLQQGVRHILVTASHYAAVQSLFHHARQRLPALRIAGRTLKLENQHISFMMPDRISQELPATDLLLVDEAASIPVAVLTSWLHHYSRIAFAT... | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Catalytic Activity: acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O = ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) + phosphate... |
A0A661EG03 | MIATLTGLIASKNPPFLILNVMGVGYEVQAPLSSFGKWEKVVKNESITILTVHIVREDSQDLYGFATDDEKNLFKTLIKVNGIGPKIAIGILSASGVDGFIANINSANIDNLVCLPGIGKKTAQRLIIEMKDKLTSKAGNSKQEANFLDKNSQVISALTNLGFKSSVAQRMLAGIDSNNKTIDEILRLALKNN | 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 ... |
A0A949UGY1 | MKPASGGVHNLRAPSIIQIKERISLKERHTFGLPATARFFCEIENESSLLALLKSPTFRDNEHVFLGEGSNSLFMRDYPGIVVCLRNKGVRILSENDEAVCLRVSAGENWHEFVQYTLTHGYFGLENLSLIPGSVGAAPVQNIGAYGVEVNDFITHVEAIDVESAEVRTFKNKECGFSYRDSCFKSSLKNRYVITAVFFRLLKQPHLVLGYAGLREGLDSRGINNPTALDVSALVCEVRRTKLPDPKETGNAGSFFKHPTITESHYLKLKEIFPDIKSFELDHGRYKIPAGWLIERCGFKGRSIGPVGIYKKQALVLVNN... | 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: 354
Sequence Mass (Da): 39370
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A0A2E2WTT6 | MLNVFMSICINLYMRMKEISMIRIGHGYDSHRYEDGDYIVIGGVKIMSKRSIVAHSDGDILIHAICDALLGASGNGDMGKYYDNTEKYKNMDSSIFLKDVMKIINDDNFSIINIDSTIITEKPSISKHSKKIEESISKILNIKCEQINVKSKSNDKLGFIGRHEGIVAHVVLLIEKI | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP... |
A0A6P1MCP2 | MKPIVVVGSSNTDLVANVERLPGEGETVMGTSMSKFAGGKGANQAVAAVRTGAKVAFVGAVGTDAFGDETVQAFEEDGLDLRFLKRTEEAPSGTALICVDQNGRNQIVVVPGANGLVGTEQIDSVDFSEFGIAVFQHEIPHEAVWHGLKKAHAAGCITILNPAPAAEVPAEILTMLDYLVPNEHELKIISEKGGSFEEMVEEMLSKGVKNLIVTLGAEGAACFSRDGNVAVPAPDVAVKDTVGAGDCFVGVFAASLYKGCDLEQSLRYAAAGASLSVTKVGAQASYVGWDEIEILAARAVVS | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step ... |
A0A6P2BI53 | MTSARREGGFTLLEILVALAIFAVMSITVYGRVGDVLMQTGSLEARTFATWIAQNSLTRLQLELPPGELPATGRTVENVSMTNRDWELVTEISNTGEPGLRRVEIRVHQVGEGGTRGDDAIASLTGFVGRY | PTM: Cleaved by prepilin peptidase.
Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 131
Sequence Mass (Da): 14237
Location Topology: Single... |
A0A0S8JS18 | MTTLLATLLVLSVLIVIHEFGHLLAAKRLGIKVLRFSIGFGPRLFGIEVGGTEYRLSSLPFGGYVRMAGEEGLAEPGVETETEGRFSAKPVWARSIVVLAGPMGNLVFAGIILFGIVYTLGIETYKPVVGQIEEGSPAASAGLLPGDRIISADGRSVQFWSDLVDAVAECDGSEMRLIVDRDGQRIEKALVPRYDETIDRWRVGVGPWVGTEVGTVRRGSPAAAAGIRRGDRITEVGGEPVELWHEMVEHIRGKAGTPVVIEWEHAGERRRAEIVPERVKSATPDGDVEEVGVIGVVAEQPRRRISLFQAVSAAAQQVWW... | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 440
Sequence Mass (Da): 48239
Location Topology: Multi-pass membrane protein
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A0A0S8JI72 | MHAVHTITEEDIVPFVSQVRGTIAKHSMFGRGDTVVVGVSGGVDSMALLHVLVELRDEYALQLHVAHLNHGFRGEEADADAALVEAAAGDLRIPATVQKFDVPGFASRMRLGAQEAARNARYEFLEGVASRIGADKVATGHTASDQAETVLINLLRGSGALGLGGIPPVRGRVVRPLIEVTKDEVWEFARRGGIACREDSSNAKSVYLRNLIRSRLLPLLAAEFNPQIVSVLARTAELLREDERHLQNDSEAALQKVVVSVEPGEKIAVDLGALLSYDISLRRRILRELVIMFRGDPRGPSFEEIENLMRLTRRPGGSAR... | 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)... |
A0A7C7JCT0 | MKIVFAGTTSFSAFHLDLLIKSKNEIAAVLTQPDRKSGRGKKIKLSPVKIFAEKEGIQVIQPKSLKDNLETIEDLRAMNPDLILVVAYGLILPAEIINLPKFGCINIHASLLPRWRGAAPIERSILEGDSKGGITYMKMDEGLDTGPIMKLLPCPFDEDEDSESLEIKYQNLSQIELINFLEDLAGGRVKEVNQDSELATFAKKIKKQETEIFWEHEPAEHIERKVRALFPKYGAFTFFGDKRIKILNSTKAKISKVLSPGELSASGGDALYVGCQNHQSLRLQSLQIEGKRPVSAEDFMKGNRENIFRVKKFSSSLEN | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A368D6T1 | MEELHKQVDPEGITPRPNPGMDNEPLEEGLHKGLVVESTGIWTQVKLVDDDSVVSSRLPGRQRLEDSDYAHPIAVGDWVNIRLEEDGSGMIQYIYPRKNGLPRQSTHTRRQSQLLLANLDFLWLVQSARQPRVNTRFIDRCLVACEAYDIPVGIIINKLDLARRTDKEHLQRVIDIYAEIGVPTYTCSVLQEDGLEPIKEQMGGKVSAFFGPSGVGKSSLLNALDPELELNTAPISSSTGKGTHTTTYALMVEPKGFPEGTMIADTPGIRELGLVGIPVEELSHYFPEMTEPRSRCKYSDCSHLHEPGCGVQEAVKRGKI... | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyz... |
A0A7C7JDA0 | MNPDFIVLAAGNGKRMLGSSPKVLLPIGGKPMAQHILDTISGIEKSRPILVVGDQAKEVKNSLQFKRNTKIVTQRKQLGTAHAVKTALAQLRPGSVTVVLYGDVPLIEGKTLKRLIRDASKGALAILTFNKDRPQGYGRVVRGAKNQVEAIVEEKDATKEEKSINEVNSGILAIKSILIKKLLPEIKNNNAANEYYLTDIVSLSKKHGIKVQPLLLEDPDEALGANTPLELQDLERACQRIRAKKLVNSGVNIADIDRIDSRGSLAVGRGSFIDVNNVFEGRVEIGKNTKIGPNCYIKDSVIGNEVTLQASTVIEDSRVG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl c... |
A0A060JLX1 | MYLVGLTGGIASGKSTVASAWVELGGIEIDADQLAREVVEPGTPGLAAVKAAFGDSVISNGALDRSALGQLVFANTDKRKQLEAIVHPLVRELAAKKIAELPNDSIVIYNVPLLVEAAVDLDFDKVVTVEAPSEKQIERLVSIRKMNREEAERRVAAQASPAQRANAADVILNSNQDLHLLLKDARRLWQQIEHEAAQRGSN | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
A0A661BJ72 | MGQRPEPIREQTMKHDLPDSDGHFGPYGGRFVAETLMGALQELQSAYERYIQDEQFLRELDEDLRDYVGRPTPLYFAQGWSKKLGGAKLFLKREDLNHTGAHKVNNTVGQALLAKRMGKQRIIAETGAGQHGVATATGAARLGLECVVYMGSEDIQRQAINVYRMKLLGATVVPVESGSRTLKDALDEALRDWVTNVDSTFYIIGTVAGPHPYPAMVRDFQAVIGRETRVQALETIGTLPTALVACVGGGSNAIGLFHPFLDDSDVAMYGVEAGGHGLEVDNGHASSMSGGRPGVLHGNRTYLWQDGEGQIREGHSISAG... | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phospha... |
A0A946YEC7 | EQYLPKQSGGKLPTTPVGITLALADRLDTLVGIFAIGKIPTGLKDPYGLRRAALAVLRIIIETPLNIDLSECLEKAATFFPDKLNADKAVGDVHEYINERYRAYFSDRDIPVDVIDSVLANHPTHPSDVAAKIDALMSFRKLPNAESLAAANKRIRNILKKIDRDNIGEVDISLFKENAENTLHSALESLSDDVESLFKDNQYEQALSKLADLRQPVDNFFDGVMVMDKDEKLKANRIALLSRIDSLFMHVADFSRLQS | Catalytic Activity: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
EC: 6.1.1.14
Subcellular Location: Cytoplasm
Sequence Length: 259
Sequence Mass (Da): 28864
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A0A6L8EL77 | MAHVFIGVGSNREREKHIRAGIRELKAEFGNLRISTIYENRAVGFDGADFYNFVVSCETGLEVEEVFDRLRRIEDDYGHDRSGSCFSSITLDLDLLLYDDLVISHESFQLPRSDIDRYAFVLCPLAELAPELRHPVSGKTYARLWSEFDRSAQELRRVGFDPDAE | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step ... |
A0A9C9DCN1 | MTNSQITIQQAVCNCQQRLIENSDSPQLEVEVLLAHVLQSNRTYLRTWPEKLLTTQQLAQLEGFIERRNNGEPIAYITGEREFWGMSLHVSPDTLIPRPETETLVELALERIPRDAEWQIADLGTGSGAIALAIARERPRCLVLATDISPAALAMARHNATRLGLDNLRFADGAWCTALGNERLEMILSNPPYVAPGDPHLQQGDLRFEPPAALASA | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A1H9QE36 | MGIRVWRVVGVVTGVLGAFVVAAVVAVAVLAIPITGGSMEPTFHDGDRVLPHPFLGPDDVERGDVVATRFSADGPLVVKRVIAVAGDRVRIDPGPVVRVLPAGESEWRAIPTAADWGAKPVECCGPDGKAAPVAADALVPAGKLFLLGDNPGGSDDSRASGWAPRDLVRAIVWTTVWPIGG | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 181
Sequence Mass (Da): 18667
Location Topology: Single-pass type II membrane protein
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A0A2E2HAV4 | MKLIAKTVLLAACLLLANCGDAPAEQMLQLSGNTMGTTYTLSVVSESTVSADAISSLLESIENSMSTYRDDSELMRLNRAELNTWLEVSPALFEVISLSQEISQLSDGAFDISVGPLVNLWGFGPPIPANDLLPEAVEIDTLLPNIGYQHIRLDPQQQAVMKTRDVALDLSAVAKGYAVDRIADLLETAGIDNYLVEIGGELRTAGLNLERNPWRIAIENPESELSARQVQRIIAVGDAAIASSGDYRNFFTLNGERYSHTIDPRTGWPVSHDLVSVTVITENAARADALATAFSVMGENAAMLLAEENMIAAYFLRDSG... | 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: 343
Sequence Mass (Da): 37149
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A0A2E2YSI4 | MHLYIRXLDRXSSQTSEQDFVIEWLVDPHSEPGLSRDVKQLTELVRLHEELRDPANVTVIVPTEDALWVQCKVPGRSVAQVRRALPFAVEEFVADEIENIHIAYGAITRGESVDCIAISKEVXRSWXEFLAVXDVIPGRVVVDGMLVPNDSGKGTLVVDSESVLLRTETQLVVVNRADLASIXDLIPDIDGRDDEITVFADSKNVLGEIGLTAESVRFKNVENPLMPFLIDRIDDHVINVLQSEFSPASSYTDQWMKWRSVLGLAVFWVALTIVLMFGEGFWARGEFADVRANTTDLYRSIYGEQRVPGNPASTMRRRVG... | Function: Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 410
Sequence Mass (Da): 45736
Location Topology: Single-pass membrane protei... |
A0A352KR70 | MHMGEPSNHSLKVSHQPRKVRSFVRRTGRLTRGQKQSLDYLFPKFGLAMDAPLPDNWQPGQVVVEIGFGMGDALHQLASAYPQFNFIGIDVHRPGIGHLLNRIESSGIKNLRLIEGDAMEWLNQTQWHQSLHAVLLWFPDPWPKKRHHKRRIVQTEFLQHLSEVLKPGGYWHFASDWIPYADAVKERIGRQHQLQLIPPEQIQTEVLRRPTTKFEQRGMALGHQITDLYCLKPTC | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
EC: 2.1.1.33
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 235
S... |
A0A2E9AT53 | MFNLLNTYIYMDGNGLYVWACFTLLLIVLSLNIILAVFRKKRLTKIIKRK | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 50
Sequence Mass (Da): 5936
Location Topology: Single-pass membrane protein
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A0A3C1TZB8 | MAKETISVNIDPKEIEKFESLAQRWWDPNSEFRTLHHINPTRLNYINDKANLKNKTVIDIGCGGGILTQSMAELGAKATGLDPAKASITVAKLHALETGMDKHIRYIQDDPDEFAKNQSEKFDIVTALEILEHVPDYAQLVKTIAHIVKPGGKIFFSTINRHPKAYLLAILGAEYLMNILPRGTHEFQKFIKPSELSKAIREAGLIMKELVGFSYNPLTGRSGLSESVDVNYLIFAEKPN | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalytic Activity: a 3-(all-trans-polyprenyl)benzene-1,2-diol + S-adenosyl-L-methionine = a 2-methoxy-6-(all-trans-polyprenyl)phenol + H(+) + S-adenosy... |
A0A8T7BP39 | MLSAIRVTYREEMQEIQKKFDAIVIGLGMTGMSFVRHLSEKTTRLGVVDTRHNPPQLDTLLKEYPDIPFIAGKFDQDLLSSADLLLVSPGVTLSSPAIQAAIHSGAAISGDIELFLNEAQAPVIAVTGSNGKSTVAKLVSEMIAGSGRKVLLGGNYGVPALALLESDVPDFYVLELSSFQLETLNNVNIAVSTILNISEDHMDRYRNFQEYVSVKGKIFKGEGIKIINLDDPVVCNLVRTDDNVISFTHEKPEEGSFGVCQVGDIEWICFGNQRILKVSELQITGRHNLTNSLASLALGNAIGLEIESMAESLKQFKGLP... | 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-... |
A0A8T7D381 | IGIDTELLLMFAARAEHLATVITPALRAGQWVVCSRFTDATYAYQGAGRGIPDTRIAILEDWVQGDLRPDLTLILDIPVEEGLNRVRNRGGGVDRFERERVEFFHRVRGAYLARAQAYPHRYHVIDARAPIETVKEQILDVMRKVVAP | 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: 148
Sequence Mass (Da): 16750
|
A0A8T7BJZ8 | AIEKAVTELNNISQLYENKLPEADRLLFDAYALIASDKELQKVTIQRIHEGNWAPGALRETIEEYAGQFESMEIEYMRERANDMRDIGNRILGYLQAEAETDRDYPDKVILVGENLGPLDLSKVPGDKLAGIVSGHGSGYSHVAILAHALNIPAVLGFSGHIPLSKLDGNQLIIDGYSGQLIVAPSVAEFKAYQEIIASEAELITDLTGLNDKTAETPDGYRIRLYTNMGLLTRVKHLIDVATEGIGLYRTELPFMVKDNFPSEEEQYTIYRQVIEAYTPRPVTLRTLDAGGDKVLPYFKIKEPNPFLGWRGIRVTLDHP... | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfer... |
A0A2E8KAG4 | MSTSSRHQVFLSIGSNIDAEANIRSVLIRLRDIDREMTSSRVYRSEAMGFNGPPFLNLVTGIRTGKSLQDLSSHLKAIEREHGRAEGLQKNSSRTLDIDILLYDDLAGQHSGIELPRPEIRLNAYVLRPFAELKPLLKLPGTGDTLEAMWQSFDQSSQPLIEVSVE | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step ... |
A0A661ECG1 | MCFVLKKMKQNKANLSLSYVTTKQITAYNFQYRNKKTPTNVLSFTADLPADIADKLEYKPIGDIVICPQIINMEAKKQKKITDYHHKHIIIHSLLHLLGYDHITNNDAKIMESIEIKLLSKVGIKNPYEC | 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: 130
Sequence Mass (Da): 14991
|
A0A6L7VN78 | MRMTRTHRKLRKQNHRMVQKRPQDSSFFVGLLAEQARSDAQAAPFELSDLISQLRYLTPQQIKEVRAACKFAEQAHEGQTRKTGHSYITHPLAVAGILAELEADHDTIMAGVLHDVIEDCDVSKESLETRFGSTVANIVDGVTKLAEFTTSQEFHATNIQNIALATVKDPRVIVVKLADRLHNMRTLAVMDKSKRLPIATETLEIYAPIAHRLGIYIVKNELEDLAFATKHSFRHDHISHAVQRFESANETIVRLVQSRIQARFNEIGLDASIGYHPQHLYEIYRKMKFGPMTFDDAMAFLNFKVLTDSIEDCYRALGAI... | Pathway: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step 1/1.
Function: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance.
EC: 3.1.7.2
Catalytic Activity: gua... |
A0A3C0L480 | MEQLQAQLGYVFTDVTGLKLALTHRSAAGLHNERLEFLGDAVLELVVTHRLYHQFPGVDEGRLSRFRAQLVRKESLASKARELGVGRHLILGPGERQSGGWERDSILADSLEAILGAIYLEAGVQTVTELITDWFEDQFNRLDARRVIKDSKTALQEFLQAEGMPLPTYALLQTTGLGHQQRFTVTCTCQLLATPAVAEGDSIKQAEQKAAETCLAQLHREKPNG | 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... |
A0A8T3RWG8 | MIKTDDLPELRFRGLLDYEPAWREMQAFTNERDADTRDEIWFLEHPPVFTLGLNGSPAHVLAPGDIPVIPIDRGGQVTYHGPGQLVVYPLLDLKRLGLGIRGLVSGLEQAVIDTVAAYGVEAHARREAPGVYVDGRKLASIGLRVRRGCSYHGLAFNIAMDLEPFGRINPCGFAGLEVTQLSALGGPADLERVARDLSGHLLENFGYGSAMGPSPAASAARKAASRSGVPTSNQRPA | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-A... |
A0A967ZFF3 | MRYSAETGSALQTDSSICYVLERDQLFDKLVLRDLCAKETWPRAGAKLPDGAGALWSVRTFRGLLVRHLVPNATDRLSRAIAWLEAHPDKDIQLVPVAVFWGRSPAKERSWLKLLLAEDWAASGRVRRFFSMLVHGRQVLVKVARPVSLRQLVSEGLGVERTTRKAARLLRVHFRRQRAATIGPDLSHRRLLLDEVLASPGVREAVKREIQSSQRSERRVNKRAHKIATEIAAHYSHSVVRVVERSLARLWNRLYDGIEIQHFDSLGDIAVGAEVVYVPCHRSHIDYLLLSYVIYQRGLVPPHVAAGINLNLPLIGPILR... | Pathway: Lipid metabolism.
EC: 2.3.1.15
Catalytic Activity: an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA
Sequence Length: 479
Sequence Mass (Da): 54657
|
A0A8T4AM55 | MIASNMAKTGIALAIFALVCTALLAVTNEATKDRIAEEERLFTLRTLSEMVPATLYDNDLVTDSFQLIAPNYLGNANPKTIYRARNNDAPVAAVISATAPNGYSGPIELLVAVNTHGKLMGVRVVKHKETPGLGDGIEIQRNDWITDFDGRSLSNPGHRGWAVKKDHGVFDQLTGATITPRAVVKAVHLCLQYFEKQQSLIFSAESGKTIDATE | 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: 214
Sequence Mass (Da): 23195
Location Topology: Single-pass membrane protein
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A0A4Q5Q308 | MNITIQRNLDGAGNASVFIGRFFKELFSFPFEGSEFVRQCFAIGYKSLPLVGITGFIMGLVLTIQSRPTLAEFGAESWLPGMVALSLIREIAPVITGLICAGKIASGIGAELGSMKVTEQIDAMEVSGINPFKYLVVTRILATTLMVPILVVFADGVGILGGFVGINIHGDVNMVRYSSQVLESLDFIDIVPATIKTFFFGFFIGMIGCFKGYTAASGTESVGKAANAAVVVASLSIFIIDMLAVQITDLFY | Function: Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Probably responsible for the translocation of the substrate across t... |
A0A2E0GEF6 | MIKGIGIDLVENNRIKKLYTKYGSRFAEKILSKTELIEFENSSEPIAYLAKHFASKEAFSKAVGTGLYRNGIYPSKISIGHLKTGQPYILDSKAIIEILKINSLKSVFISISDTKQHSVAVVAVQ | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 125
Sequence Mass (Da): 13861
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A0A7C3D8R9 | MNVSAGGVRPWVVQRLSAIYMLLVLCFFSLTLMFAGFDNFADWKAWFGSPFLSTIVIIFWLAVFLHAWVGVRDVIMDYVHHDGLRFAMLAIYGFYLIAMTVWMMRIIMRVVTG | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 113
Sequence Mass (Da): 13065
Location Topology: Multi-pass membrane protein
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A0A2E3UV73 | MKTENLWTIKSNFQPHGGLKELSKFEKKGSFYSANVLLSDIKGLSSLEELCQEFHQEGNFIGIKPYGFQPQAFFFDMDGTCIKEESLVEIAECAGAKNKVEKITEQAMAGKIDFSTSLRQRVKYLKGLDEKKLFEVSSKLKLEKGMDVFAKKCVSQNVPLYLISGGFYPLIDVVGKKVQCKSYVANRFEINSGYLTGELDGNIVDKEFKCQWMKDVCNKKGYDLSSVVAVGDGANDKAMLDAAGLAVGFKSKNVLSKSIQVYNGVGDHNLLNDFLTQDNLFN | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
Catalytic Activity: H2O + O-phospho-D-serine = D-serine + phosphate
Sequence Length: 282
Sequence Mass (Da): 31378
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A0A8T3S045 | MVAVIQSSPLDIRAMTADDVTQIMSIENASYPYPWTTSIFTECLRVGYVCRVLCEQQHILGYVVLSVAVQECHILNVCVADHARDQGNGRLLIRYVIEQATRLQLNTIYLEVRPTNTHAIGLYHSLGFQRIGVRKDYYPADNGREDAWVMALNMSPQW | Function: Acetylates the N-terminal alanine of ribosomal protein bS18.
Catalytic Activity: acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]
EC: 2.3.1.266
Subcellular Location: Cytoplasm
Sequence Length: 158
Sequence Mass (Da): 17975
|
A0A8T7BHX4 | MSLHIQQNVSLQSFNTMAVPAQADYLTTVTSVPEMHDALSLARRQNLPVLVLGEGSNTLFEHDYKGLVILNRLRGMDVVEELGDLIRVKVGAGENWHRWVAHSLKQGWSGLENLALIPGLVGAAPMQNIGAYGVELEQYLHSVELLYVDSGEIGELSREQCEFGYRDSVFKHRHAPRAIITAVTFELNTYFEPQITYPAVKEYLQTRMRPSQELTALHVFDAICHIRRSKLPSPREIPNSGSFFKNPVVSEEKLASLREHYPEIVSYEHRGQIKLAAAWLIERAGWKRRQRDGVQVHKDQALVITNPGRASGASVMSLAR... | 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: 341
Sequence Mass (Da): 38556
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A0A661EDH9 | MKIWIIKIGSSLIAKADLPINIKNIQKWAGQIDKLRDYGISVVLVSSGAISAGVQKLNWQKRPHRVHKLQAAAAVGQTALIQNYESVFYDKYKIRTAQILLTHQDLSNRKSYLNAKRTIQTLLDFNVMPIINENDTVATSEIRFGDNDTLAALSANLLQAEKLIIMTDQDGLFDDNPQNNPNAKLIKTADANDKNLLKYATGRGSEFSTGGMMTKITAATKAANSGCMTIICNGNNETALLDIYNNKQVGTTLKADKKQKNAFKVFIKNNLKAQGKIILDSGAIEVITKSGKSLLPVGVLQATGDFQRGDLVVCCDEKNT... | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2.
Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
EC: 2.7.2.11
Subcellular Location: Cyt... |
A0A2H0KEW3 | MLNTNYRTYSHASSPPTVYKYGRIRSMAITIEEIEKLASLSRIELTEAEKGEMQGEFDAILGYVASVNKVAEGHSSDAQSSTSTLNILREDDTAHESGIHTETLLSSAPKREGQYVKVKKILGS | 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 ... |
A0A523MAH7 | MRHAISVLLENEVGALTRVTGMFSSRGYNIDSLNVAATDNPMISRVTLVV | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
Function: Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine.
EC: 2.2.1.6
Cata... |
A0A9D0NWM6 | MLHVDVYGDGPDLVLVHGWGMHGGLWQSWATELGRSFRVHVVDLPGHGHSVQEKVPQTLDAWAEQVGDVVPADACWLGWSLGGQVALAAAGNGQPVRSLVLLASTPRFVTAADWQTAVAADVFDQFAEQLENDIERTLGRFLALQVRTAEHGGETLRRLRAAWGSRPAPALQALRTGLEFLRECDLRSTLAELSMPVYWLLGERDTLVPPAVASAFPEVHTALVPGAGHAPFLSHPGHCNGQLQRWLPGNKQVQHAAG | Pathway: Cofactor biosynthesis; biotin biosynthesis.
Function: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.... |
A0A2E1PHM5 | MDNDIYKSDYFYDLPQDLIAKYPLKERTMSKLLCLDKSDYRIVNFPDIVKKIDRNDLLVINETKVFQARLELNKKTGGRVEILIVEKINKFTANCLTRGLNKKLLKQRLFSAKFPLDIKIITSSDNKFTRIEFSQSIDKICSTIGSMPIPPYLKRQGEQIDEERYQSVFSNNKYNNSVAAPTASLHFDKELLIKLSEETTIAKISLDVGYGTFQPIKSNKIPIESTLHTENFYIPKNINKEIKKCRSNGGRVIALGTTTLRALESAYNVVKKEMNTGHQSTDIFIKDGYKFKVVDSLITNFHLPESSLLILVCAFGDKSN... | Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxy... |
A0A946M6Z6 | MKNIDEQLKIIRHGASEIIQEDDLIEKLKSKKKLIIKAGLDPTMPDMHLGHTVVLNKLKQFQDLGHEVVFLIGDYTASIGDPSGRDITRPPLDSTTIKKNGHVFQKEIYKILSKDETRIEFNSKWLGKLSGKDLINLASSYTVARMLERDDFDKRYKSKKPISIHEFLYPLLQAYDSVHLKADIELGGTDQKFNLLLGRKLQEQNGIKPQVCIMMPLLEGLDGIKKMSKSYDNYISISDEQNDMFGKVMSISDDLMWKYFDLLSSSSLDEIKSLKDSSDRDDMNPRDIKLKLAQELVSRFYTKSIGEECADNFINRFSRN... | Function: 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).
Catalytic Activity: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr)
EC: 6.1.1.1
Subcellular Location... |
A0A349X2X5 | TGSEMAAQFRESIWSLSLPFGIILGLRFGLFTPTEAGAMAVLASVLIGIFVYKELEVAHIKSILLDTIYGTGTVVLIIVSASVFGYYLNWERIPQELTATLLEFTSNKYVMLAVINVFLLIIGMFLEGGAALIIIAPLLVPVVIELGIDPIHFGMIMIVNIMIGGVTPPFGSMMFTTCSVTKVPVGDFMREIWPFIIALLIALLIVTYAPGLVMFLPGLM | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 220
Sequence Mass (Da): 23906
Location Topology: Multi-pass membrane protein
|
A0A3M2EBH6 | MTDLLISDLHLQPDREDLTRLFNHFITGPAYEGDRLFILGDFFEYWIGDDFSHPWLSDIEQKLRNYTATGRTLVIMHGNRDFLIGQTFCERVGAKLLAEPSVETIGGIPSLITHGDELCTDDLEYQAFRRKVRDPEWQAAFLSQPLASRIAFAEDARSHSRQKQAEYNESITDVNPDAVLAAFRTYDVHRMIHGHTHRQAIHQIECDGRLAERIVLGDWGKTGCYCQCHNGHRQLINFVAP | Cofactor: Binds 2 Mn(2+) ions per subunit in a binuclear metal center.
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 4/6.
Function: Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine ... |
A0A2E1GVF5 | MIFISPAKINRGFNVLKKRSDGFHDIETNFQFLEWGDEITFNFDTSTSQVTCPKVKEKNNLAYKAIHLLKKTYKINKEVSLKIKKNIPIGSGLGGGSSNAATVLLVLNKYWKLNLNNNVLKDLGSSLGSDVPIFIEGVARKANGKGEIFSKTLLKEEIIFLVMPKCNISTAKAFQEIEISDFKNLKNSKDFNFFEKWARKNYKEVDDSFIWLESIKKGNLTGTGSALYAIFNSFEEASKIIDNAPKNNNYFVTRSLNESPLLKELNKNGV | 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... |
A0A2D5PQH6 | MIQRKLTLVMENKPGALARVVGLFHQRGYNIDSLHVDPIEDFGPFRFIEDELGIKFQVGEVSRLTIRTTVGDKLMRQILRQINKLIEVIAVSDEESTYLKGILRNENLL | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
Function: Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine.
EC: 2.2.1.6
Cata... |
A0A2D8DKZ2 | MIDRKKRKKFGQNYLIDPVTIHKIIKSIGLDHQLPYLEIGPGHGAITDGFIGAINNYSAVEIDHENIEFLLKKYGDQQINLISQDILSFNFESLPENVKIIGNLPYNIASQIIIKILTSKVNPKDLHFMVQKEFADRLCAKPGDKSWSKISIKSQVLFFNESLFEIDPIAFDIKPKVTSSFIRMTPLKNPIVKKADFNSFSKFIDVCFQSKRKSLKNNLKDLLIDADFGLEHFKKRPEEITLDQYKELFKMIK | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) +... |
A0A2E4HS19 | MNFNYTLIGQLLAFVLFVWFCMRFIWPQLLQVLEEREKEISDGLSAAAEGKRELEEASNKKEEILNDAKKEASELLGQANQRAGQLVEDAKSEARTEAEKIKISAQKDLEQASKRAREELRSEVATLAVAGAEKILGSEVDEKKNAQILEEITKEL | 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: Cell membrane
Sequence Length: 156
Sequence Mass (Da): 17566
Location Topology: Single-pass membr... |
A0A7C3GIH4 | MKQTGINLTYSLITSFEQLSSLCQKLSQSSVIAVDTEFKRETTYFPIPCLFQIATDELTACIDPFKIDDLTPLKDLLGNENILKIFHAGRQDLEIFYYLFKQLPKPIFDTQVAAAILGFPAQVGYAKLVSDYIGIELDKSLTRADWEKRPLPEKQLEYAANDVIYLLQVYKKQQQALAELNRLDWPTNDCNALLNEELYQANPSTAWTRIKNYPFLTTREKRVASALSKWRETLAIERNRPRKYIFDNPVISELSAKQPTSLEALNQLKNIPTHVGRKYGKQIVEIIKEAINSNEPLDDKGYQRLTDEQNKLVKQMQQLV... | Function: Exonuclease involved in the 3' processing of various precursor tRNAs. Initiates hydrolysis at the 3'-terminus of an RNA molecule and releases 5'-mononucleotides.
Catalytic Activity: Exonucleolytic cleavage that removes extra residues from the 3'-terminus of tRNA to produce 5'-mononucleotides.
EC: 3.1.13.5
Sub... |
A0A2D8QNF8 | MQGRTKMTEHIIEISRSVXPFDGEPNDGQXAAWLESALNKLVKERMELSLRIVSEHEMTALNSDXRNHHSPTNVLSFPSGVRTEECCFLGDIVVCADVILKEAQEFEKSFAERYAHMLIHGLLHLLGYDHVDARQREAMESLEKTLLISFGIDNPYEXLDGSRXXVQ | 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: 167
Sequence Mass (Da): 18950
|
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