ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A9E5DUJ0 | MRTHFRLQQFALSRLGYFGLALACSAWLSTGYYLERVAALTPCPLCIFQRFAYFAFAVLALLAALHAPRFTGQRIYSGLMLLCALAGLGVAGRQTWLQHLPADRLPACGPDLAFMVERYAPLDVLKRVLRGSGDCAVVDWTFLGFSIAEWSLGCFASLICACVLQLWATRRPEWR | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Subcellular Location: Cell inner membrane
Sequence Length: 175
Sequence Mass (Da): 19513
Location Topology: Multi-pass membrane protein
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A0A3B9JLR5 | MKPNFQPKDIEKTIKDLTEEGLKIANLASQGHDWESVVTPLDQMEFELGQHTSVNSHLNSVMFNEEFNAEYEKTLPLITNFYSEVSTNKTLYEAYKNLRNTSLNEQQRHIVKESIESFKLSGVGLEGEQSDRFKAIKERLSLLSNQFSKNALKATNEWKKTLTEAELEGYGENELAKVKTKDGYEISLQVPVYMDVMTYAKNQTLREEVYKAYISRASEVGITSTEFDNKAIMDEILSLRQEMATILGFGNYADLSIEGKMVESTEQVIDFLNDLVDRSKTQAQQELDELQLFAGVELMPWDLMYYSEQLKEKKFGFKKS... | Cofactor: Binds 1 zinc ion.
EC: 3.4.24.70
Catalytic Activity: Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-Pro-Ala is cleaved, but not Z-(Gly)(5).
Sequence Length: 466
... |
A0A661EKL4 | MQNLSWQRIEVFLQNSDFNKFLIAISGGVDSSVLLHLCHTLKTHNKKIQFRAVHINHQLQQNATIWDKHCEDECKKHDISFISQKITINTNTKKSPEEQARIQRYQAIKNIVKKDEQVLCAHHLNDQVETFFLRLLRGSGSVGLSGIKPRINIFNMSLARPFLNISQQQINDYATTHQIKYIVDDSNADIKFTRNYLRLKVMPSLDNINTAYLNNINKAINIIAENNNFIDETLLQKYKNIDFCSDKINSEVLNLAPNFEKKWVIRYWLSKKICFYPNQKHTEEIITQLINSNNDNKIEIKLDDNHSLKTYDNVIYLVQK... | 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)... |
A0A7C7W8W5 | MANTLDMRTIFREDIPLIDVRAPVEFDAGAFSQASNLPILDDMQREQVGICYSASGPESATSLGHDLVSGEDRDIKVAAWLAFLREHPDALLYCFRGGQRSRIACEWLKAEGYDVPRIEGGYKALRRCLLSTIENLPPLIIVAGKTGSGKTEFLQQFGQAIDLEGIANHRGSAFGRHISAQPTQLNFENELSIHFLKLAQHPSVFIEDEGRMIGKVHLPPPLQEKMQTAPIALLEDSIAMRADRIYQEYIELQWREYEAHFAGRAAEEFSRYLIEAVDAIRKRLGNTAHSEVRGSVLAALKHQEQVGSLEGHREWITLLL... | Function: Involved in the post-transcriptional modification of the uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Catalyzes the conversion of 2-thiouridine (S2U-RNA) to 2-selenouridine (Se2U-RNA). Acts in a two-step process involving geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiour... |
A0A8T7IB59 | MSHIIIKTAMLLAMLLALAGCQSSIFGDDCLRNKTLAQENYRPTPDSTQQNRNQEGIKQVAEPLAIAEPQYPRNAYQCGIEGWVQFEVTVKTDGYVKDINILDSSPDRTFVQEARKAVNKWRFKPAKNDKDEWVESTFIFAIEFKLPDPLQ | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
A0A7C7WDF7 | MNSTLVFGGTFDPVHRGHIESVCAVARLLGDVDVYLVPCQIPAHRPTPAASPEDRLKMLQLAVASQDRIFIDDCELRREGTSYTVDTLLGYRQRVGKSGPLLFLMGRDSWATYPGWHRWEALSDLAHLLILERPGTDQRSPDVLRKWLKTRQVQDPEEMMNSSSGKVCFLSLDQIDVSASGLREAIAKGSSIEGNVNPLVMNYIRQHNLYTGASLENKVPGKRMEH | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A2E8REX5 | MKNYDVLILGVNGMLGSTMMQFFKQQNKFTTCGTIRNEILSDKIRCFEQDIFQNVIAEDPTLLENLIISKKPKFIINCIGIIKQLDASNDASLSININSIFPHRLALLCKKHGVRLIHISTDCVFNGAKGMYVENDLPDAEDLYGKTKFLGEVTYDHCVTLRTSIIGHETSSSHSLLEWFLKQDGEVNGYQKAIFSGFPTFELSKIIHDIVLCEPSLSGLYHVSSEPINKYDLLKLFSEIYLKEIKINVDQGLIINRSLDSTKFRNITGFEPSSWESMVKKMREFG | Cofactor: Binds 1 Mg(2+) ion per monomer.
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NAD... |
A0A965HVI2 | MWCQDYRRDGEVLDTLKVFKERGAEAVFNLSASPWTWQKSDKRNRVVREILSASPLPFFYVNQVGAQNNGKNILVFDGDSTAYTSQGEATHRAQAWIDEILYSTERTVPPQPQSQTDAIFKGIITGLRHLDHIRGAKNKVLVAASGGIDSSVVLCLLEQAFGPERICAVNMPTRYNAQITQDNAHDLCRALKLDYLSCPIGDLYRAVSEKIQAVEFPHHEGVYTRLVDENIQARIRFADVLSGIAAKHGMLFTNNGNKTEVALGYATLYGDVSGAPAASYKNYMTKAGEARLRAELLQLLDVERPIVVEAV | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis.
EC: 6.3.1.5
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Length: 311
Sequence Mass (Da): 34518
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A0A965RCZ7 | MSEPPSPAQQPDPDSRRAPRLILIMGVSGCGKTSVGSRLAAELACRFVDADGYHPAANIEKMRAGRPLDDDDRAPWLDRLNALLRHSAARHESVVLACSALRARYRDRLADRLPGLAIVHLRGSAETISARLAPLRDFLLLFFFIALGATIDVSTLGGNAAYAVMLSLFVLIGKPLVVLIVMGAMGYRKRTGFLSGLTLAQISEFSLIFVAMGVSLGHVDQKALGLVTVVGLVTIAASTYLITYSHQLYLLCEPLLGRFERAGTPREPHDTTTPHQTSHPIILFGLGRFGTAIGRRLHQHGIEVLGIDFDPAAVNRWREL... | Pathway: Carbohydrate acid metabolism.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 424
Sequence Mass (Da): 46081
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A0A967GEI1 | AVFVDGLRVTTAEGLDVTEMVLSGLVNKDIVALVNQQGGRGVGISGKDGPTVLARRLQRQDGKDLGLVGEIEQVDPSLITLLLERGFIPVISPIGMGDDGTTYNINADSAAARIAAALKAEKMIFMTDVDGVLQDGTLVSALTAAEALHLIDQGVISGGMVPKVEAMLHCLGHGVGTATIINGGEHHAIIAELFTDTGVGTQITP | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
EC: 2.7.2.8
Subcellular Location: Cytoplasm... |
A0A2E8KXB3 | MRILINKIPSLLVHLFTSLGVVFGFLALVATLNHDIKTAFLWLGVALIVDGVDGSLARKYDVKANMPYIDGAVLDNIIDYFTYVIVPAFMVMEFKMVSEEWVYFVVVTILITSCYTFSNTKLKTDDFYFRGFPAAWNLVVLYIYILDLSHVTSLIWILFCAVFTFIPVKTLHPFXVEKFRKINLVTTSFWIVSIAMLIFNNSYSDIFYLIFIVTSIWFTLITLSRTIKGG | Function: Condenses choline with CDP-diglyceride to produce phosphatidylcholine and CMP.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + choline = a 1,2-diacyl-sn-glycero-3-phosphocholine + CMP + H(+)
EC: 2.7.8.24
Subcellular Location: Cell inner membrane
Sequence Length: 230
Sequence Mass (Da): 26385
Location Topol... |
A0A2E5RGE8 | MRQVFLDTETTGLSAESGHRVIEIGVVEVIDRRLTGNDFQTYLNPERKIDPATFPVHGITDDFVSDKPKFSEVLTEFIDYIEGSEVIMHNAPFDSSFINKELELLGYKDRLEDLCEIKDSLTIAREKHPGQRNSLDALINRYEVDGTSRDLHGALIDAKLLARVYLLMTGGQVGFFSKDDEKRHGVDSSSEKFDYSKRKIIHVSSSKDQKEAHKVYLEKLSKASNKKLNW | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)... |
A0A2G6KU65 | MKKMLINATHAEELRVAMVDGQRLYDLDIENRTRIQKKSNIYKGKITRVEPSLEAAFVEFGAERHGFLPLKEIAREYFYQNPKDVEGRAKIRDLVKEGTEIIVQVDKEERGNKGAALTSFISLAGRYMVLMPNNPRAGGISRRIEGEERAELKEAMADLDIPADMGVIVRTAGVGRSTEELQADLSYLVNLWQAVSKAAGEVASPALLLQESNVIIRTIRDYLRDDVGQVTLDSEEAYHQALDFVSQVMPQFKNRIRLYEDSIPMFNRFQIESQIETAFLREVRLPSGGSIVIDPTEALVSIDINSARATKGSDIEDTAL... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs.
EC: 3.1.26.12
Catalytic Activity: Endonucleolytic cleavage of single-stra... |
A0A0K1JPR7 | MERSRDFERFITFIDAIVAIAITLLVLPLVDIAGELNGGSVTDLVSDHSNEIWGFLLSFLVIARLWLSQHAVIRTVIAENAALTRLLLGWTLTIVVLPFPTALLAEPGAGDQAATKIFYIGTMAVSSALLAAICVVVGRDRSARDSDDKPDPTPLIQTTVAFVLALAISLTFPATSYYPLMLLMATDFPFRRLFSRAKAH | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 200
Sequence Mass (Da): 21774
Location Topology: Multi-pass membrane protein
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A0A534A2L4 | MSRLLALFYGFVCYLAFLATFLYAIAFVSGFAPKHIDNGATAPFVIALTLDLALLGLFAVQHSGMARPAFKRWWTRFVPESIERSTYVLVSSLALIVLFWQWRPLPQLLWQVDGELARAAMYALAALGWLLVLSSSFLINHFDLFGLRQVWSFANRRTAPDTPFVTRAFYRIVRHPLMLGFLIAFWATPTMSVGHLLFTLMTTGYIVVAVKFLEERDLVAQLGETYRDYQRRVPMLLPWPKRASAPPHGSAQSTPGIPR | Function: Catalyzes the methylation of methanethiol (MeSH) to yield dimethylsulphide (DMS).
Catalytic Activity: methanethiol + S-adenosyl-L-methionine = dimethyl sulfide + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.334
Subcellular Location: Membrane
Sequence Length: 259
Sequence Mass (Da): 29359
Location Topology: Mult... |
A0A962RH36 | MQIDWWTLALQTINFLVLVWLLTHFLYRPVRQVIAERKALAEQALVDAHEAERVAESRQQALDEAIADAARQRESMLKEHHQALEAERAAVLDKAHEEARALTEAGRHEIAQERRAAERALREQASELAVELAAALLRSCEHALPGEFFVQRVEQELGELPAHELERLSRDLTANGGRLGVVTATALDSTEQDHWKTRLLERLGCQAPVDFSIDAELLAGVELHFPHSVLRYSWADQLSQARARLLQDDLSE | 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: 252
Sequence Mass (Da): 28492
Location Topology: Single-pass membr... |
A0A2E5ZYN6 | MGSSLDMGFSGNACPSVRELTGRSAFGLLCGSGCVDQSMKYVLPLAGKGEQIPALWEAGNKAAALGRVSELTGVKVPAGFALTFPALEDSLEEAGARAAXESIQRMAEAGGPAEASTHATCLRELVLQVPFAEAFGKELVSVLLPWVDGRAISVRSSSNLEDAGNLSFAGQHDSLLNVRGEQDLREAVSAVWASAFTDRAVTYLLTLGRSLAELRMGVVIQEMVQARAAGVAFTVHPVTGARDVIHISAAFGLGEVTVSGEVTPDKAVVAREGFVTSSYTAVGETPVLDAANCATVAEAALLIERSAGGNPMDVEFAFDD... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 794
Sequence Mass (Da): 86328
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A0A3C0TCY5 | MHFSSVGLIAKTGSEQVLESLRRVQKFLKSQAVDIVLEADSAEMLGVEGSTCALAAMGDCCDLVIAVGGDGNILGAARALAPAGIPILGINRGRLGFLADVSPDEIEIQVGAVLKGDFATEDHFLLEGEVTGREEMHSALNEVLIHTASMPRMVEFDLFINDEEVYTQHSDGLIISTPTGSTAYALSAGGPIMHPSLDAVVLVPMFPHTLTSRPLVIPGDFEMKVQVASPGDVEARVSFDSQVEFNIQAGDELVVRKIKTPLKLIHPPGHSFYDVCRSKLDWASRVGDKQNGDG | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Loc... |
A0A356R225 | MHPLDPLGREELDRAVQIIRDQMNLPPDALFEQVRLKEPCKSAVNAFNSGNPSDITREAFAVVLDRSADEVCEIVVSLDENKITSRELIPGVRISFLSEESAEFRKIICEHPDFLAALERRGISDPEQVLVEGFAVANLAESDEKHLRHTRAHCFFREHPKDNAYARPIEGLVPVVDLNNRKVLRIEDNGVVPLPPDRGDYRSDRLDTRPPLAPLEITQPDGPDFRVNGYAVEWLNWRFHVGFTPKEGLVLHTLSFHDGEIDRPVVYRASLSELVVPYGDTAGDHYMNHSFDLGETIFGKQVNSLKLGCDCLGEIYYFDF... | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
Catalytic Activity: an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+)
EC: 1.4.3.-
Sequence Length: 628
Sequence Mass (Da): 70971
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A0A389M0M7 | MIGIIQKITNAYFSLLRLIMVICLAIMLCMVFTNVCLRYLGRGIDIAEELPRFLFIWMTFLGAIVGFKERAHIGVDFLIEIIPKYAKQISWLTVQLLILLCAVYILYGTYLTHDLLVGNVSTVMRLPEIYVFGVSYFTGASIILMSIGNILRFFIIGIDDQELIHKQITKNAH | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 173
Sequence Mass (Da): 19740
Location Topology: Multi-pass membrane protein
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A0A8T7C322 | MSRIAVIAAVAKNGVIGNAGKLPWRLRADLQWFKRCTVGHTVVMGRKTFDSIGRALPERQNIVLSRQQDLECAGCVVVHDLDAALDVATADRVFVIGGAELYRLALPRAEQLFLTVVEASITGDTWFPFVDLDDWLVLQRQFQDADADNQYACEMREYQKR | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tet... |
A0A8T7IPY4 | MIFSSLLAPIEVAINRVLATDSAAPEILAPLNERVIKLQFTDLERAVFVRFYQGRIDLYASYEGDVDLLLSGRAAQFAALARQKSSNALINSGVSATGKTAILVNLNEAVQALDIDFETLISSVMPPTGAHLLGQGFRAAVKQMTTMRNEAMRLTGEYATYEAQLAVPNEEVARFSGAVTQLRQDTDRFEAKLAALEATR | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Required for ubiquinone (coenzyme Q) biosynthesis. Binds hydrophobic ubiquinone biosynthetic intermediates via its SCP2 domain and is essential for the stability of the Ubi complex. May constitute a docking platform where Ubi enzymes assemble and access... |
A0A8X7T5H5 | MSEANSSFSSVLDSNPSFHRWLNACSTIFPSQDTLPFKRRRRTITSPFPNARIYSANEHFNKDEEPEEWKSGPETDEERKWRERAEAWAVQLAETSPMIRFLSRHLAMVSCNPYDKPDPSSPLAPDPEDPNRLPESPLGRIVFAACPPNRVGGFRPMDPPSESGILICSNRIARKADLERAMAHEMIHWWDTCRFRLNWNNLRHNACSEIRAAALSGDCKVMTEFGRISHGLRPGFLKQHQACTRRRAITSVVDAVALEHLEPDARLAAAERAVDEVWEACWNDTRPFDDIY | Function: Has a dual role in the assembly of mitochondrial ATPase.
EC: 3.4.24.-
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 292
Sequence Mass (Da): 33358
Location Topology: Peripheral membrane protein
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L7MI88 | RRCSSSAFVGSSAYGQASSARNYGFAGVWWWCCQAMSGDDGQWEVVPSYLDVLRGVYNVCHYGLYVTNGSESVSAAGPHRRPWPFIPLEDVFVVLVLAVLWTLVRRLLTDRVFKPLGWWLSLEPSNVAKLPESAWKLLYYGCVWLLTVYIVVLQGKYRFFQQPFSVWDGWSPEVTVPSDIWWIYAVQSSYYVHGMYAVLYQDLWRKDSAVMLVHHSLTLVLLGMSYAFRCHNIGVLVLVLHDFSDVLLEFSKLNVYLKVRAGRKHVVHDRIASAAFVCFAITWYLMRLHYYPCKVMYAASTGLFVKQVFPAHFLFFLGLL... | Pathway: Lipid metabolism; sphingolipid metabolism.
Subcellular Location: Membrane
Sequence Length: 416
Sequence Mass (Da): 47479
Location Topology: Multi-pass membrane protein
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A0A7C5PC00 | MSWLKKLFKYGLVATLVGALLAAAAVVGAYLYIEPDLPDIEALREIRLQVPLRIYSSEGKLIAEFGEKRRNPVRYDQLPPRLVQAITAAEDAHFFTHPGIDPRGLLRAGIKLILTGKRKQGGSTITMQVARNFYLSRKKTYLRKLYEIFLALRIEQELSKEEILELYLNKIYLGHRAYGVAAAARVYYGKDLDQLTLPEIAMIAGLPKAPSAYNPLSNPQRAVERRNYVLRRMRELGYISQEQFQEASAAPITARRYAPRIEVEAPYVAEMVRKRMVAEYGDAAYTSGLEVYTTIEGKAQTAANAALRRALHAYTERHGY... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-term... |
A0A6N8XJX0 | MLYDRRVLEVRTPRWRAYDAVLPFADIRPMHVPITESELTNGRGPSYMTNTNILPIDTRDATLEVVGGKGRSLAEMASAGLAVPGGFYVTTAAYRRFVADNDLQAKIIELAKPTIGEFTLSFDKASEAIQALFQSDAMSEAMAAEIAAAYQAIEGDNPAVAVRSSANAEDLPDMSFAGQQDTYLNVRGADEVVAAVRNCWASLWTPRAMAYRHEMGIEHDAVAMAVVVQLMVQSDVSGILFTANPATGERSEMIINASFGLGEAVVGGQVTPDTYTVDRETMQAKDTIIGAKEQKIVADGDQGTKLTDIAEDERGESSLS... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 593
Sequence Mass (Da): 65301
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A0A661EIH3 | MQKIIFIILLFLLLTLQYRFWFGKANYNQLQDLQERIETLNQQIETMNKQNREYGAKVQLLKKRLDAVEEYARYELHMKKKNEEFYPLDKNLAK | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
Subcellular Location: Cell inner membrane
Sequence Length: 94
Sequence Mass (Da): 11544
Location Topolog... |
A0A2E9ZM64 | MLDPLILRIISVGFALLFIFAAAHKFNNKLQFRGVLEAYKICPPGMLGLVVNVIPLFELMLGLAWAFIALLLIPISFVPLLSAMLLFTYAMAIAINLLRGRSYIDCGCGFYSMSESAQSGSSSGGIQQLSLALVLRNFVLTIVALLATVPLSSRDLIFMDFLNLLAASLALVLVYCAFNQLLANRNVIGAWLNSPGRNSNG | Pathway: One-carbon metabolism; methylamine degradation.
Function: May be specifically involved in the processing, transport, and/or maturation of the MADH beta-subunit.
Subcellular Location: Cell membrane
Sequence Length: 201
Sequence Mass (Da): 21775
Location Topology: Multi-pass membrane protein
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A0A2E5H4A1 | MIDPLXSQIVAYGFGLLFISSAWNKLSDIDQFSLILKDYQLLTIMPFKLLAIMIATFEXVLGCSWLLGYNTXMIGWCTAGILILYTLAITVNLVRGRVYIDCGCGFNNTLGDNSHLLSPILVVRNFILIVMVFFTLLPTSERDFVFLDYMVIFAALLTIILLYVGSVQLIQNRSAINTWRTGF | Pathway: One-carbon metabolism; methylamine degradation.
Function: May be specifically involved in the processing, transport, and/or maturation of the MADH beta-subunit.
Subcellular Location: Cell membrane
Sequence Length: 183
Sequence Mass (Da): 20601
Location Topology: Multi-pass membrane protein
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A0A2E6AB49 | MKNKIYIKKISIIGLGNLSQALIAGLDTAGYKGLIHIYDIDKKKKKYIKSKNMKFKTNIDESIIGSTIILIAVKPSNLKNVATKLKNLNINSIIISLMAGVKISQITKLTNKDLKIARIMTNINARHESAISFVYMNKKCTKIEDGVINELFEKFGSLYYATSENQLNKITALIGSGPAYFIHFAESIMKTFKSFGFTEAESMKYSLELFYTTAYSCIVDDRALGLIKKSIISKNGTTDAALKKMNQRNFQKNIKESILAAYKRSQELSREE | 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... |
A0A8T7IV69 | MPIKQLVTDHSVDLSTLTQRYDITEVSMPTEDMILRVSDGLVSLAFPTTKQGDVAVDFCSAASEYRRLHGGGYGQPIAKALSLSPKFQPAILDMTAGLGRDAFVMASLGARVTLFERHPIVACLLENGLKRAQESNSPAATVCQRMNLILGDSAERLAGSDRFDMVYLDPMFPSRSKSAAVKKDMAAFHELVGHDQDADKLLDIALDHAEYRVVVKRPKNAPFLADKSPSVSHKGKAGRFDIYSKRAIKQSEFISVVADE | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.242
Subcellular Location: Cytoplasm
Sequence Length: 260
Sequence Mass (Da): 28428... |
A0A8T7IZK4 | MNFLRNQTFVVASFVFIILFSLFCFSALADDQFLEVDQAFVFSSEHHSQGQSGVELMWNIADGYYLYKNKIQVLLDDQPITLNFLPEGTSHEDEYFGQQQVYKEKLRVELASVLLANGSKLTVRYQGCAEAGLCYTPITKHIQLTENAELNVNLPPPKSPEKVSPLSFEFMNSELGVSSFGMTLLMFFVLGLGLSFTPCVFPMYPILTGIIVGQNNKLTTRRAFALSFVYVQGMAVTYTAMGVIVAFVGMQFQAMFQHPVVLISLSVLFVFLALSMFGVFNLSLPSSLQQKLNNLSNNQTSGTYVGVALMGVISGLVASP... | Function: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction step... |
A0A8T7J018 | MTELKISSKKIRRRYILALIVVAILVTISELTISRAINLQENDANVINKAGAQRMLSQKIAYFAHTYDISIPAQQRLIVDKFQSAVNTFENNHEFLTQLPDLSEQLRKQYFEGSPPLNDEVAQYIVAAQRFIESPSQTNANYFNLIRTENILRRLNDTVSLFETEAKQQVLLVSQLKTVVWIITLVVLCIEALFIFYPMERLIVRSVNSLKEAADKAQKLQHKAEEANVAKSEFLASISHELRTPMNGMFGMMELALNDKANYKSYLKKAQLSGEQLLNLINDILDLSKIEANKLTIEHRSFNLIDMLDSVLSTYSTACV... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 726
Sequence Mass (Da): 81862
Location Topology: Multi-pass membrane protein
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S4VU65 | MQRTDDHCDPRQRHKDTDNGCADDRAHDDGRNREKNDHSRGRDNGDVAGCGGGDHPAQQRVRDKIDERPCAVVCAPRPQPPLADGRHFLVAEIHGCYRPAWRVFAMAAAVTAGACRGFVGRRVPAGTRIASAIAFHDPRRLCLDGASLRPALDAHPSFTFDRIVMVLSWPGGSNARDVKWVAASFGNASADVNGSDPARDHTVDGRSRVDPAVAGRGERCVDDGLARAIYRKALDQAARITRESLTAAVETLLNDRTFRKQHGQRESGDTMPIERWYKVCEPTLTKSVAACPDGTLKRACGHTTTNPSCAECDAVWTHSE... | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Cytoplasm
Sequence Length:... |
A0A351CZB5 | MIFRNGPNYFLYTLCISGILLCLSACVSPSKTSPGIGPAISWQKVPGWSQDKHADSIPGLLASCEKLHSQSNEWGQICSAANKTPLDDHLSAKVFYEYWFSPHIILNEQGNAEGLFTGYYEPLLNGSRKQSARYSTPAYAKPSNLIRVELANIYPELSGLRIRGQLDGDRLIPFPDRQGINSARLPNAEVLVWLDDPLDLFFLQIQGSGRVALDDGTTIRLGYADQNGHPYHAIGRELVERGEMEIDQVSMFRIRDWLELNPERADTILNTNPSYVFFVEREAAPDNPYSATGPIGSLNVSLSPERSLAVDPDVIKLGLP... | Function: Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division.
EC: 4.2.2.n1
Catalytic Activity: Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from eit... |
A0A7C1XSI8 | MVVETLLLLLPVAAFSGWLVGRRGHSAKTERGGIDIPSDYLKGMNYLLNEQPDKAIETFIQMLDVDSNTVETHLALGGLFRRRGEVDRAIRIHQNLIARPTLNKDERNQALFELGQDYMRAGLLDRAEILLSELLDSDPRHRSALKLLLDIYQQEKEWQDAIQVAKKYELRTGENLSTSIAQFYCELAEQVRAKDEPLRALKLLKKALAEERSCVRASLLEADIEIAVGNVKSALRAAQRVEQQDADFIPEALPLIKRCYQTLGRMDEFTRYLQRLLADHSCIAVVLELALLIYDAQGGKAAEEFITGFLKHTPSVFGIE... | Function: Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane.
Subcellular Location: Cell inner mem... |
A0A7C1YRJ7 | MDTLRWGLLLTGVIVFLLIYLFSRSKFSAKRERPVDRFSSDVVIDEEFGVANVDDDPRTLDTLARNIQLDAGNQVDDRLSDKQSDNITGSDKEKLIGFYLVEKEGNMLNGADIIDALEKVGLRYGDMKIFHYYGVDQQKTTRPVFSVASLVEPGWFDLISINSMTTPGLTLFMNLPGPLGSVAAFDGLLSVISQLKSLLPVTLKDRQHNNVSNQILTHMREEVVEFDRMRAIQGKG | 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: 2... |
A0A920L466 | MDLVVYSSVLPREGETVFGNSFETFLGGKGANQAVAASRLGSKVSFIGKVGTDSFGQILKEKLASENIDTSLLSVHEGESGVAMINVFESNSQNQIIVVPGANAHTKASQITDQSLSSFDILLSQMEVQANEVETLFLRAKERDCYRILNLAPAMKLSESLFSNTDLFVVNEIELESMSNISLLPDSIDSVRANIESISLNKNQSIIVTLGSTGVFINHANKQEFIEGHNVEAVDTTGSGDCFLGALASSLVKNENLFDAAAYANKAAALSVTKKGASASMPTHQDVLKFL | 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 ... |
A0A7C7WAC5 | MQLPSTAISRRIDPLITWVGESISWIWLLLLFTIVFNVVLRYAFEQGRIELEEIQWHLYSTGFLLGIGYTFQVDGHVRVDVVHERLSPRTQGWLELYGILLCVLPFTALILVFSAPFVASSYALSEVSVSPGGLPFRWVIKSMLFIGFFLLLLAVVSRFSRVWSFLFLSQAGDRHESQ | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 178
Sequence Mass (Da): 20371
Location Topology: Multi-pass membrane protein
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A0A962RPS4 | GMTVTAAYLFLAITLGPGLARAGLDPLAVHLFMLYWAMISFITPPVAIGAYAAATIARCSPLKTGIEAMRLGTIIYFVPFFFVLNPALIGRGSVLEVVTVCVAAVVGIVLIAAGLQGYLIGAGSLGRNHPLDWLLRLSLIAAGLVLCLPGGDLVGYSHAQLNLTALLLGAPAMLITWMLNRTRLPVTVKA | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 190
Sequence Mass (Da): 19897
Location Topology: Multi-pass membrane protein
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A0A6N9AX69 | MKRSKSRWILILSGTVVLMFGFGYALVPLYDLFCEITGVGGKPTVAVLQLPSDENPIDYSKEVTVEFTATGNNNIPWSIKPLVKKTKVHLGEVHVMNYLVTNTSSQQMIGQAIPSITPMQGARHMVKLECFCFNAQTLEPGEAREMPVRFYVNKDLPAEINTLTLSYSFFPINESVSISDDRSEVQQSSS | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Subcellular Location: Cell inner membrane
Sequence Length: 190
Sequence Mass (Da): 21154
Location Topology: Single-pass type II membrane protein
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A0A7L3U4N2 | SVSNLKMNSTHTEGEGRVPDDELECKICCQRFTIHSRKPKILNCLHRICARCLTKILHAGAGSPCISCPFCRHETELNEDEVEGLPSDTNIMSKLILKEKTAWNSDCKEVVLTPKNLAFSSFSHGSPNCLVITITEVQRDPPRPPRHSSASDYYADHGTESVSPSAPRQLNRDLFSKLCRHVPRILVWLLGFLYFSSIPLGIYLLVIQKVTLGVVCVTFVPSSLSVCLVYGFCHCLYHRARDGSSQ | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Cytoplasm
Sequence Length:... |
A0A1X6NIU4 | MLLGPLQLACWFWTGCALLNPLTTLPMVAYLLFIARGDPSVAAVRRYDRLRPSLRACGLLRLFTGYFPMVLVRTAALPPARRYVFGVHPHGVISMGAFSHFCTAATGWDALFPGVRPHLLTLAANVKVPFFRELLLALRVVDASRETCGAVLAGPPGAALAIVVGGAAEALDARPGTYVVHLQHRGFVRVAAAAGADLVPVLSFHENDLFRTLSPRRASPLRRAQEWVKRTFRWAPVLFHGRGAFNYYVGLLPYRRRVVTVVGAPIPVPRVAGDLRRDAECVALVDAVHRQYAAALRELFFAHADRYDPHRRADIDIRM | EC: 2.3.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 319
Sequence Mass (Da): 35216
Location Topology: Multi-pass membrane protein
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A0A920M9D2 | MEIIPTVKIVNRDGIKAVKNGQKANKFASIPAEKKPSWIRVKASFDPKYKLVKDQVASKKLNTVCEEAMCPNISECWSSGTATFMLMGSVCTRACKFCSVDTGNPKGWLDQEEPLKTAKAVRTMGLKYVVLTSVNRDDLEDGGAEHYAQTVQAIKDLNPNTAVEALTPDFKGIKSSIDTIVNSGIEVFAQNLETVKRLTHPVRDPRAGYQQTLDVLYESKEINKEVLTKTSLILGLAKQMKRLNKQWMTLLIIKLIS | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Function: Catalyzes the radical... |
A0A8T7C1P9 | MFGYGSLLWRPGFQYHECMTARICGWERRFWQGSPDHRGTPRRPGRVVTLVQAGDAGCTGKLYAVNEDHVEQVIRYLDHRESGGYQRLWVTAHDNCGRRFRALTYVALPGNPHYLGPAATVEMKAQIRASKGPSGTNVDYCRMLHSAMSALEVPDAEWHTLPLDGLLG | Function: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
EC: 4.3.2.7
Catalytic Activity: glutathione = 5-oxo-L-proline + L-cysteinylglycine
Sequence Length: 168
Sequence Mass (Da): 18871
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A0A3M1DRI8 | MPRSVFFVSDSTGITIENLGRALLAQFGDTGFHHQTYVFIDSPAKVDTVIAAIDYAAERDGERPLVFSTQADPALRRRLAGCRGLLLDPFDAFTGLLAEELGKEPQSRRGHLHGIFDRNRYDSRMAAVEFTLRHDDGALPGRYSEAELILVGPSRTGKTPTSLYLAIQYGIRVANYPLLDEELESLRLPPALLACRDRLYGLVVDPERLQEIRSARRPGDRDYASPARCRHEVEAAIALFRRNAIPWLNATSMSVEEIAAHIISDLGLHR | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation.
EC: 2.7.11.33
Catalytic Activity: [pyruvate, water dikinase] + ADP = [pyruvate, water dikinase]-phosphate + AMP + H(+)
Sequence Leng... |
B6JZQ7 | MHILIGIAIAVAVLCLYVQRRRCRSGKQVAILVLGDIGHSPRMQYHANSFAKHDWNVELIGYGDDNNEQELFKKDKRIRCIHIPKTPAWLTPSSKLQFLLFAPLKVTFLWLGLCSILFRVHAPSYLLVQNPPCIPTFVFALLMRFCFGSRIVIDWHNFGFSILALKLGKNHMLVKIMKAYELFLGRFAYKHLCVSNAMSEVLGNWGLKPTYVLYDRPPSHFKPLSKKPYNLLGTAFNPKTCKLLVSSTSWTPDEDIFVLYKALEEYDAQPNASPILAVITGKGPMKQDFLDHVKEHPLQHVRFLTPWLSTGDYPRLLACA... | Function: Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER.
EC: 2.4.1.142
Catalytic Activity: GDP-alpha-D-mannose + N,N'-diacetylchitobiosyl diphosphodolic... |
A0A3C1VQ71 | MSNKSISIAGITLANDQPFVLFGGLNVLESRELTLEVADHFKSVAAALDIPLVFKASFDKANRSSLDSFRGPGLEQGLEWLGGGQAGWGRVGGWGGVVCGGVLGGV | Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Catalytic Activity: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate
EC: 2.5.1.55
Subcellular Location: Cytoplasm
Sequence Length: 106
Sequence Mass (Da): 10946
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A0A8T7J6K5 | MNSSNSLRCFISTLSDCGYLADRQQRNLVVDPTNRPSAAAYEYLAPQGFRRNGNHLYRPYCPSCQACTPVRIVLDHFVPSRSHKRNLKRNSDLNVAFEATSSEDEFYELFIRYIQSRHDESSMKDMSREDYRAFLFCDWMGTRLLTTRLNGELMSATLVDFMPHGFSAVYTFYKPEESARGLGTFAILKMLEQAQEMGLHYVNLGYWIEQAPTMSYKTRFKGVELAFDGRWEPFDPNRQYTPDLTTQQLSPEQ | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-aspartyl-[protein] = H(+) + N-terminal L-leucyl-L-aspartyl-[protein] + ... |
A0A2E9NV56 | MEGLKKIDCLLGKIEEIAIALALGIASLLNVFQVGARYLFNVSFNTFDEISVYLMISVIFIGLVRADALRENISVDILHSLLSKSTAQKLFRISDGLLCVIAFSLTYFTADSVMFSKMIGETSVSSLGVMIWPIMAVMPISFCIVGIRAGLRSLEILNIHKGEQLETGARI | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 171
Sequence Mass (Da): 18736
Location Topology: Multi-pass membrane protein
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A0A2E3UTR8 | MLDNQFNKKSENSAGLHILLTGGGTAGHVMPHLALYPKMKELGWRVSYVGTKGMEKALVESKGIPFYVISAGKLRRYFSWQNFLDIFRLLLGLTQSAFIVFKIRPDIVFSKGGFVSVPISVAAWLFRIPVLTHESDLTPGLANKILARFSKSIFYSFPETASYLPRNKAIFTGLPIRQELFKGEKDFGLKLCDFKKDDQRPILLFMGGSQGAQRINSFVRENLGKILLNYRVLHLCGKGKIDQKLKLCGYWQKDFAGEELKHLLAISDYVISRAGANSIYEILALKKPMILIPLSVGSRGDQVLNAQSFKKQGLAEVIEE... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-t... |
A0A8T6C8A1 | MTANPVASHDSARSYEALPASMRADVRTLGSLLGEVIADDRGNELVDRIEEIRALAKRARGGGEEQWDELSACLKSLPEEDLVDVARGFNQFLNLANIAEQRYHASPEIYSPRREWARLLRETPEFDPSILEELRVELVLTAHPTEVLRRTMIRKYDAVDQTLQRKSDPAQLEILKRLIAEIWHTDEVRQRRPSPLDEAKWGFAVIENSLWDAVPRVMRAADEAATREGLAAIPPAVMPIRFASWMGGDRDGNPNVTAPITDTTLKLARWMSADLFLRDIQHLVESLSMAKATPELLKATGQSNEPYRVVLRSLRQRLHA... | Function: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
EC: 4.1.1.31
Catalytic Activity: oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
Sequence Length: 871
Sequence Mass (Da): 96988
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A0A534IWD2 | MKYRHGFHAGNFADVHKHVTQLALLAALERKDKGFLYLDTHAGRGSYDLSSPSPEAAAGVGRFVAAQHTAPELREYASLLARFRARPGHRHLYPGSPLIAALELRPQDRAVLIELAAAEAQPLKASVEALCAHVDADLAPTDLSSGHPGARRVHIERGDGFERMRAFLPPPERRALIFIDPPYEETRDDFGRVSLALAEGLRRFPTGVFAAWYPIKEERSTAAWLAHLSRALPAPALVSELWLYPRDSRVGLNGSGLLIANPPYLTLERTQVWLPELQRCLAAGPAGGTSVRVCQNPPHE | Function: Specifically methylates the adenine in position 2030 of 23S rRNA.
EC: 2.1.1.266
Catalytic Activity: adenosine(2030) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(2030) in 23S rRNA + S-adenosyl-L-homocysteine
Sequence Length: 300
Sequence Mass (Da): 32940
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A0A0X3P2X9 | LFWSATHKLLPTGGVFIPFLTYSMDPVEDTSDDLFASHRSLSTNLCSKLSSFWNSSSTRSPISSRTRYFCWNGLLCCKHPFRSKMRSRPGSLMNSTRFTFPNFSSYERHQLVTTGDDTDSLPSQKPTSSLMEQSSKKLERLDEDSPLRVSTEKSLPVVFSTPGPSFEPLTRSEVLLNGVQFTPIPFTDLTNSYGEVASQTASVCLSSRSSASPKSMASHTGDQQTALSPPENKSLTNTSPSPASVSPLNTAPTATALGKKSDARMKRRLTRQFRPSLPSLSESYIRVYKVGDALQILLKLAEQTDIGSFEHVFPRTRRGN... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Chromosome
Sequence Length: 668
Sequence Mass (Da): 74435
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A0A2E5JA40 | MLDEIIKNKEQEIVELMNQQQMNINDVLKKKIENRGFLKTIKKNIINNTISIIAEIKRASPSKGFLNENLNIEEIAIEYQQAGASCISVLTDQRFFKGSIADLIQVRNKTTLPILRKDFIIHESQLIQSKLIGADCILLIVAALKKDLFSRLYDLSLKLDLDVLVEVHDEKELQIALDKKCHLIGINNRNLKTFETSIQTSLDLIKSINDDVIVVSESGIRDSNDIKLLRNSGISTFLIGEMFVTSSNISKDLQGLII | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 258
Sequence Mass (Da): 29149
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A0A2E5M8B0 | MHISLIWAMSTNGVIGRGQRLPWRLPAEMQHFVRTTMGKPVIMGRKTFESMKAPLAGRTNIVISGDADYQREGIRVAQDLQGAIAIAEAQCLVDGRDEIIVAGGAQIYALALPVATRLYVTVVETDVEGDTHFPDVDFSQWEQLSSEQFAADQANSHAYTISVWERPGAAS | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tet... |
A0A2E5RHF9 | MNFQNYTNDMYKVLKLNNIAEEGLKVFNSERYHCGDDVTNPDAIILRSYDMHEMDIPKDLRAVGRAGSGVNNIPIDKYTEKAIPVFNAPGANSNAVKELVLASILIAARNIHSAIKYVELVKDSENLKSDIEHGKKAYVGFELPAKTLGVIGLGQIGVKVANAAYDLGMNVIGYDPLITVDNAINLQPGIQNVNDLKELLNDSNIVTIHIPHKKETENFIGDNEIKKLKEGSIIINLSREAIVDTNAILKNLETNKIKTYVTDFPSEEMIDHKDVLVMPHLGASTKEAEINCAVMVANSLKSYLESGNILNSVNFPDVKL... | 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... |
E5A0B2 | MYINTLVLAVLVPLNTVQAFNLTSTTPPPQHTPNSSHQTATTLLTWARSKLPSTTKRTSCPPVWSTISTALTAQFLADGQCTDAARAAIRAAFHDCFNGACDGSLILADECANAENSGLQQLCSALLNISIENQVGVADLIQFAAAHAIKTCPGGPTVPVVVGRRDASEANSQGVLPHGDALGGDLVTLFASKGLTPTDLTALIVRAVRRLPLPRMEILRGSHRRRGRGQLLQRARRRGTRRL | Cofactor: Binds 2 calcium ions per subunit.
EC: 1.11.1.-
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Length: 243
Sequence Mass (Da): 25904
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A0A962WNK7 | MSPSAVPHAAATADGTVAAFYRFAPLTDLPGLRAALLEQGRLLGVKGSILLAPEGVNGSLAGPRDRVAAMLECLCQRAGLDQLSARHDPVHDIPFRRFKVKLKREIVTLGIAELSPPPQSGRRVGPREWDALLRAPQVLVIDTRNDYEYRIGSFAGAVNPQTAHFRDFPRFVAAQLGDQRARPIAMFCTGGIRCEKASAYLLGQGFERVFQLDGGILRYLAETDPADSAWRGDCFVFDERVAVDHALNAAGYEQCPACRRPVAPSARGLPGYEAGVSCAACHAGLPAGRRRTLRERARQVRLAAARGESHLGAVMAVDD | Function: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
EC: 1.14.-.-
Catalytic Activity: AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA + A + H2O
Sequence Length: 319
Sequence Mass (Da): 34433
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A0A963F467 | VQEPGQEARFVINFQNCVDCKTCDIKDPAQNITWVTPEGGGGPNYPNM | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
EC: 1.5.5.1
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Length: 48
Sequence Mass (Da): 5283
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A0A1A8IGA0 | MNQSELSGFVFEQQFDQKRALEWMQENWSKSFMFCGLYATLVFAGQYFMRERPKLNLRWPLALWSLSLAIFSIIGAFRTGVYMLHVFSNRGFQQTVCDNYFFRAPVTKFWAYAFTISKVPELEMAFLPGRY | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 131
Sequence Mass (Da): 15536
Location Topology: Multi-pass membrane protein
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A0A849WJI0 | MYPFLVIGEIKIQTYFLIIAALAVISFYWVYLKSKKQHLNQVFMLDLTLVLSVSGFVFARLFHVIYESPELYWNQPVQIFYFWNGGFVFLGGFLGALLSGIFFVFIKNKKNMILYLCDFYSPLIAFDYAVGRIGCFMAGCCYGKFCNLPWAIEEKHPTQLYAFVWDIILFAILQLLPKLNGWQKKNCGKDGRIFSVFLIFHGVGRIINESFRADFRGPIFLLPLSTWLSLTMILASIILIIKNKET | Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,... |
A0A5D2QPP1 | MVTIVATADLILFFVFLVDFDHSWSYLAIVGSDVRVSQVGSIKTKWNCIKTLPDLSGTSRATCVKFGSDAKYLAVGSMDRNLCMFGVPEGDASMES | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin-protein ligase which is mainly involved pre-mRNA splicing and DNA repair. Required for pre-mRNA splicing as component of the spliceosome.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysin... |
A0A969XEJ7 | MLAAKPLLESLASRAAELLDAEGSLSRSELESRLKQMLHSQFARLDLVSRDEFDGQMLVLQRTRQRLEQLEQRVAQLEQQLASQDNHPPGH | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Required for efficient ubiquinone (coenzyme Q) biosynthesis. UbiK is probably an accessory factor of Ubi enzymes and facilitates ubiquinone biosynthesis by acting as an assembly factor, a targeting factor, or both.
Subcellular Location: Cytoplasm
Sequen... |
A0A1A8K337 | GKKQRYRYSELFGGSAAKKNAYPEKNTRKERLRYSLSTGGIFDNSGQYRVYKNLIKSDFTTNLIAGSDVNVLTLATHTTINNLHHLESLLERWQNPLSVAIFAHGEDVKFATALVYALSFFCPQIQALVDFHLVCLSGEIAIFPEQDHEHFAGLEDCASVFSRLETHKDKYKNYAINGNISYPNNLLRNVALGGTE | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: 3-O-[beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + UDP-alpha-D-glucuronate = 3-O-[beta-D-GlcA-(1->3)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(... |
A0A972KWF8 | MASRLLLYLCAALIVIMMLLVGYSVVTRYFFNNPQPWVDELTGYLMVGAALLGAAETLRRREHISVDLAAGRLGPVGKRVLEIFGLLAVLLLSLLMVISGVDMVVFSYSMDLYSIGYLELPIWIPQLVVPVSFSLLGLVAAIQLARMFSNAPGKST | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 156
Sequence Mass (Da): 17051
Location Topology: Multi-pass membrane protein
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A0A521W919 | AATGVAVPSVSPGSALRHFRKTECFCFAPQDFAAGEQRELPVRFIVDRELPAGVDRLTLSYAFYDAARAPSTADNRG | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Subcellular Location: Cell inner membrane
Sequence Length: 77
Sequence Mass (Da): 8316
Location Topology: Single-pass type II membrane protein
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A0A8T6EGA3 | MGSSDVDQAVNLLKQGGVIAHAAEGVWGLACDPWNEKAVNRILTVKNRSIDLGFIVIGSEPSAFHEELAALAPEIQQRVVASWPGHVTWILPSKRFPDWVTGNRTSVGARIPDHEQARTLTKLFGKPIISTSANVSGSEPAVTMEEVCREFGHLVDFVVPGKIGSAAGPSRILNALNEDTIR | 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. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosp... |
A0A0X3NMZ1 | MSATFLLLFLGGSIFFSRAEGRMMELQQQSKLKDTSSGISQKTNEDSEHEVFLRQLHNQSGIAGFLLEHEPGSILDDNWDASTVEEATQSAEDRNKDLVQPHEVNLEGVPVIISQPKKVYYAWEGRPAVFECVAEPVSHAVVLCADQKFPFMAPGTSDRLRVIQLDSTNRPTPGGSRWHIQLQVRAKDVEEWFGAYECTCEVWNQIPALKRVKKVFSENATIKEAYLEREFQLEPIPEQVTVGQRLLLSCQPPRGKPTPNLYWLKDGARVNHSTFPHIVINDYNQLIIEQVTVGDFGNYTCVADTLGIEKRYASAQVTEV... | Function: Receptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding.
Subcellular Location: Cell membrane
Sequence Length: 951
Sequence Mass (Da): 104683
Location Topology: Single-pass type I membrane protein
|
A0A2G6DYY4 | MRAWFEEFEQREQIALLLLVGAVLLFLLYRLAYLPLTGARDAVAQENARLQFVLSDVSGIASRINAAQKNQRTGNARKNITRIINQSTTRMQLPVSRLQPNSRGDVQVRLENVALEKVVKWLYFLEHDQQLVLSDVSLSQGSSAGVVSASVRVAEGE | 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: 157
Sequence Mass (Da): 17536
Location Topology: Single-pass membrane protei... |
A0A523LGW3 | MVRVTSSDSQSSNQEAIAEAVTALRAGGVIACPTEAVWGLSCDPFNQAAVERVLTLKGRSRDQGLVLIAASVAQIEALLGDLSTEQRNTVLDTWPGPVTWVVPGRASVPRWITGTHPGVALRVTAHPIASALCEAFGGPLVSTSANRTSGVAAQTEADLRANFPAGIDVIVPGTTGDNSAPTQIRDALSGEILRASP | 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. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosp... |
A0A8T7J3J8 | MNHVLDITNDHIKASFMALGATWLSCQVRIGGGWREVILGHADLALYQQKGPYFGATVGRFANRIAGGTFSIDGQHYQVDQNEAPNTLHGGRGGFSHQPWRVVEHTPTSLRFAIDSPDGDQGFPGHLHAEVEYCLSGAAIDIIYHATTDAPCPVGLTNHAYFNLDAEHDDISQHRLQLAATQVLEVDMALIPTGALLPVGGTAFDLNTPRRLAEVLSHRELQATQGYDHALVLEGSGFRHVGRLTASDESLAMDIHTDQPSIQLYSGNGLEGIKGRNGPYRAYAGYAIETQGYPDSPNHAHFPNCILRPSEQYQHRTRYA... | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-glucose = beta-D-glucose
Sequence Length: 324
Sequence Mass (Da): 35487
|
A0A3P7C4A2 | MTDGPPSISPRLLRGAILLRLALLVFSVWQDQTRWPDGQLRFTDVDYDVFSDAARAMVRGEDIYEARPTYRYSPLIAGLLAPGYFLLTHCPEQYPLLRAALTYLAVSMGKLLFITADILCALVQCRIISVEGRKYLLTSSRSELPQHTLNWLIGFCWLFNPVTASVSVRGNAESVLGLAVLCCLLCVLQERIFLSGILFGLCIHLKLYPVIYAPIIYLMLCQHRLLIAISTPRRAVEGKSPANIAHHRWKRLLRVILVPCVAHWLFALATLISLGGLTAAGYYFYGWPFLNQAYFYHFTRVDFWHNFAPHFYPIYLFEGI... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum mem... |
A0A661E5A6 | MHEVNSDQQQTRRLSLSLALVAVLMFGFGFALVPLYDTLCRILGINVKVEQVTLAQINAAADAQQVLARDVRIELVTTVSEQLDWSFYPLVKTLSATTGDSNKVLFYAKNNTDHAVTVQAIPSITPTPGAKYLRKIQCFCFERQTLQPGESVKMPVVFYVDPALPEQYQTLTLAYALFVVEDPPG | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Subcellular Location: Cell inner membrane
Sequence Length: 185
Sequence Mass (Da): 20526
Location Topology: Single-pass type II membrane protein
|
A0A3M1UHR0 | MTGYARGRLGAVGLCVLCLALAACGFRWRGAPALPPALHRVRIEGLPAYDPLRLRLARRLQGAGVVLVGSTGTPAARLQVLARDRVRRPLTVSQRGQVTEYALVRSVRFRVVDALGQVVVPEQSVQVRRVYLYDRTDPLGKSTEEQAIEEAMAQDLVTLILRRLEAH | Function: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 167
Sequence Mass (D... |
A0A2E6A553 | MRLFLLRACLIALVSGTSAAADGGTGQPMVLVDTSFGDFVITLETERAPRSVAHFLNLVAEKRYDGTIFHRVIPGFMVQGGGKWPDLTDIPEAPTVVSEAHNGLKNLDGTVALARFDDIDSASTEFFVNVGDNAHLDHTPESCTRADYAAQERAAARGLAKPLSCATYGYTVFGRVIDGMETVFDIELVETGLDDDRMDVPLEPVIIRSIRLIESTGAEEAASR | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 224
Sequence Mass (Da): 24161
|
A0A348ZIW2 | PFALGSLLALFEHQVYVQSIIWDINAFDQWGVELGKTLAKSMQGALTDPAQQQNLDASSRGLIKQIKSWNKQEQT | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
EC: 5.3.1.9
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Length: 75
Sequence Mass (Da): 8403
|
A0A8T7AVF6 | VLGIVKAYTTRVGSGPFPTELFDDMGKHLAKVGAEFGATTGRPRRCGWFDAVITRRAVLNSGITGLCVTKLDVMDGLDTVKICVGYRLDGELIDVPPLQVERYEECEPVYEEMPGWQQSTVGVTRREDLPAEAVAYLQRVSEALGVPVDLVSTGPDRDQNVIIRHPFD | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
EC: 6.3.4.4
Subcellular ... |
A0A2D8U1K0 | MRNLYDYPIGENSPDEFNVIIEVPHGSNNKYEYNSEYDIFQLDRVLFSSVHYPGCYGFIPQTLGGDGDPLDVIVLAGEPFSTGTVLKARPVGYLKMTDDKGQDEKILAVPVDDPRFNERHSLKDIRKHVLLEIEHFFQIYKDLENKFVDIDKWYDLDETKKLIVESNNNYKK | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
EC: 3.6.1.1
Subcellular Location: Cytoplasm
Sequence Length: 172
Sequence Mass (Da): 19982
|
A0A2D7F203 | MKFVSIIFVLSLLIGCGFQLRGTEQVVFLDLHSIYIETGDVHGDIHRILQDKFQQSKVEVSADPSEAQYTVLITDERNSRRAIAHSSSQIVTEYEIAQEVSLHLVNKEGDYLISQEKVSAERFYALNDQILDSSFQEERLLREEMQQDLSEQIFRRVNAGIQGYENKKN | Function: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 169
Sequence Mass (D... |
A0A410CSF1 | PPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMRIYNMNFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNINTSFFD | 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... |
A0A8T7IYV6 | MSEKNQISQVWQQFVDKWLELAKQNGFPEITADENWPSPCEFQQQEKTFWQPVKQDETLGFENVEHAIGYKLNDEFKTFFTLYYADNFDAKHSDGELQYLQAWSKPDFERLQQNLIGHLMMKGRLKQTPTLFFAVTDEEDLNIVVDNLTGKVALEYVGKEPHQTLANSLSAFIQQTTPVISQ | Function: Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function.
Subcellular Location: Cell inner membrane
Sequence Length: 182... |
A0A2J8Y040 | AAVGVGFYGNSETNDGAYQLMYSLDDANHTFSGIDALVSRTTQKMKVDLEQHLARLSEIFAARGDYMQTLKFIQQMAGSVVVQLSGLPVWREVTMELTKLSDQTGYVEYYRWLSYLLLFILDLVICLMACLGLAKRSKCLLASMLCCGALSLLLSWASLAADAAAAVATGDFCVAPDTFILNITEGQISTEVTRYYLYCSQSGSSPFQQILTTFQRALTTMQIQVAGLLQFAVPLFSTAETCLQSSSC | Function: Probable chloride channel.
Subcellular Location: Cell membrane
Sequence Length: 248
Sequence Mass (Da): 27131
Location Topology: Multi-pass membrane protein
|
A0A5Q4EWX0 | MPTESTFLLFALFMVAAAAGWAYARFLDRRARDNQEDEPPLSQGYLRGLNLLLDDETDKALEMFVRMIATDDEALDTHFALGSLFRRRGELDRAIRIHQNILARPDLSSTQRHTALFALGEDYLRAGLMDRAESLFRQVAEQAEDPEPALGRLVGILESLGEWEQAITVRRELEKVSGERQDGPVAHYYCELAERALSNGESRLARAWLKKAQRARRALPRGAMLRARLAEHEGDGALAWRLLSEVVRSSPALLPEVLPDLHRLASRRDDLASLDALLRPLLMTRESSGVAYAAITCDLLDPPVLEEALVGLLTGDDTLA... | Function: Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane.
Subcellular Location: Cell inner mem... |
A0A661E4P7 | MRKNNVKLCGSLFYILLAGYLILALSACGFQLRGSSALPEEMSVTFIKFKKPYGSLLDDFTEALRAHHVTVTDVRDEATAVLTIRNNERDRDVLSVNSAGKVLEIQLRQSFQFSVTTTDNRPLVELQSMTLTRDYLYSSTDVLSKDREEVVVRRTLQQELVHLAMLRITAAR | Function: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 172
Sequence Mass (D... |
A0A0H5R0S2 | MRKSVMRLRRHNRFSCVTNSAMSPQSPPYPFYCGADPVGFANPTVNQRWPIILSQIAERISSDRNGADTDSQHAVEGIKSILDDIKHERSLQALLPDNIPDWNQWNKAIAQFFPHATFYSASWLFAECYLYRRVYNVLRRSKGYENYDPFLVQKRESLLNSIDTMKDLVSRPVAVISSFHPELLRELFLLSLWGNATDLSMFAGMSSKEMGEMKQGSGESNIIANDLEDVCRYISTCSNVRIDFILDNSGFELFGDLLLADYLHRTGLAGKTVFHCKTIPWFVSDTMPSDFHELLDLLEGSAKLSQHNVNCFETIVSRWR... | Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function... |
A0A8X7N476 | LQGGDPTGTGRGGESIWGQPFRDELDEAGAYRHTERGILSMANKGPGTNGSQFFITYRATPHLDKKHTVFGHLVNSTDSELSTLERVPTDPTTNRPLRSIRILEASVFEDPFERYKDALGRKVARENMSAGEREEKERKRKWREEDRVTWLGTNLGSKEVSEGTTAGASAGPTGLSRASQLFESTGPANGGGKSSTTAAASSVGKYLSGAGKKLDGDVPVPTARPTPGKLAQQQQQPPPSKKKKKGGFGDFEGW | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 254
Sequence Mass (Da): 27344
|
A0A3D1S4U0 | MIEQIMERSINGVLALNAVSLEKMQPLIGKVITLQISDLNRIVHVLPGKDGVQVRRESKQPADVTISGHFGDYLQGTAASIRSSFQQDATLQVSGDPETAEQLRVVLGSLDLEEALSQVVGDTPARKIATGFRDVAGWLNQAGESIAATFGETLKEEKRLLVTGPRLERFLNEVARLRESTDRLEQRVHGLERQTPGD | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Required for ubiquinone (coenzyme Q) biosynthesis. Binds hydrophobic ubiquinone biosynthetic intermediates via its SCP2 domain and is essential for the stability of the Ubi complex. May constitute a docking platform where Ubi enzymes assemble and access... |
A0A2E5J811 | MYMNSVKIKLCGITNTEDAKLIVDLDFDFIGLIFVESSPRYVSLSVAKEIYSICKGRKKIVGIFQNQNIDFINNIVKSIKLDFLQFHGNEDISICENFSLPYIKTISVNQNGSLSHNIHDYNSSNALLFDTKIDNQSGGTGKTFDWELLHKNEGFHLFAKTNPFFISGGLNPDNVSKLILNYKPWGIDVSSGLEYNAGKKDITLVKKFLENVRIAENSCEKD | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Length: 222
Sequence Mass (Da): 25046
|
A0A8T7DDF7 | MVVKFYLQRRWWLLLVSSMLLFELTALYFQYRLELDPCVLCVFQRTAVMGVLVAGLVGVINPLNRWLRFTAYSIWGACSIWGAYTASKHAGLQLGFIEQSITCEYTAPTWFMLDKWVPWMFEPTSIYCDEIKWSFFGFSMPQVMLAIFVLLLLTLLYICVIEIRDGLKKTGMSV | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Subcellular Location: Cell inner membrane
Sequence Length: 174
Sequence Mass (Da): 20214
Location Topology: Multi-pass membrane protein
|
A0A660LEA6 | MRSAVGALIRKDLLLQRRTPEAVPAMVLFSIGTFVLFHFALDEREVSGNLASGILWVTLLFAAVLGINRLFVSEREEGGFDGFLLAPVDRTSMLVAKAILLFLFLSVVEVFVLAAFAILLLGPSPWGPLPELAVVLALANAGIAVIGTLVAALAIQTRARDLLVPLLALPLSVPLVIAAARACAPLLTEGGAGALEARWLAILGLYDLVFGLLAYAIFDFLLEE | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 224
Sequence Mass (Da): 23817
Location Topology: Multi-pass membrane protein
|
A0A2E3QKP4 | MEASVIKKINRKRMSFLVFLTCALLLCFAFYLELVEGLDPCPLCTLQRACIAVGGSFALIASMHNPGRVGFLCYAVLQVLFFSIGGALAGRQIYLQSLPTDLVPSCGPDLDYLLEIFPIFEVLRMIILNDGSCSEVLWRFLGFSIPQWTILAFLLLTVMCLLQISNKLENEIASKS | Function: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Subcellular Location: Cell inner membrane
Sequence Length: 176
Sequence Mass (Da): 19550
Location Topology: Multi-pass membrane protein
|
A0A2E8L7Y2 | MLRIKPFHIIAVFCLFSGLYYLLRLSVYDAISKDQIREDRFVIMERKPFWGITTPSMVITLALGFWVLYENWSHFMAWRWMHVKLAMVAMLVAYHVVCWWHVVQLRDERSVRSQIFLRIFNDLSVLLLVSVVILIVVKPTL | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Function: Catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX.
EC: 1.3.99.-
Subcellular Lo... |
A0A2E2YUZ6 | MELDGGLKTDQIMLKVALALLPAIAASVLVFGPWVLVGLSTAVIACLVAEAVFFQYVRILQDYSALVTGLLIALALPPTTPIYISVLAAVCAIGLGKKSFGGLGKNIFNPAMVGYAIVLVSFPFDIGAWDATTGATSLDKISHRFGATLQEIESDPAFGSFGAAGFEWVNVFAGAGGLFLIYRKIIGWRLPMATLIGLCLPAVLAYDGGSSASFGSPLMHCFSGGTMLAAFFIVTDPVTSPSSVRGQWLFGLIVGALIFVIRAWGSYPDGIAFSVLLANALVPLLDRKHSVKTVSGK | 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: 297
Sequence Mass (Da): 31096
Location Topology: Multi-pass membrane protein
|
A0A3C0TBS1 | PLLIREQAVGFAIGRAEVEEIDRINILQATMLAMQRAVEGLRIPLDFVLVDGNRTPVFSCPSDCLIKGDAKFDAIKAASIIAKVARDTEMIELDEVYPDYGLANHKGYATRFHLQALKKLGPSPIHRMSFGPCRQRELF | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 139
Sequence Mass (Da): 15511
|
A0A523M2E2 | MPALDTRHRLRIADVRRRFDQAASGFDAADFVHTVTRDGLFERMAPAVIDARVVLDLGCATGSATHTLAKRFRGATILAVDLSLPMLELCRAKQGWFSKTSAVQADASALPFADQSVDVVFANLLLPWVNEPAEVTLEVSRVLRKDGLFVFASLGPDSLLEIRNAWAGVDDCSHVNRFLDMHDVGDLMVRAGLSDPVLDVDRLTVSYKDADDLFRDLTAAGARNSLQNRNRSLVGRQRFGAMRQRLENTGSDGTIELDLELVYGHCWGGRPPLPEGDVRIDASAIAVRKR | Pathway: Cofactor biosynthesis; biotin biosynthesis.
Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
EC: 2.1.1.197
Catalytic Activity: malony... |
A0A0X3PRE2 | MIIQKFFPRLARGILALFVRRKQFVLLSLLAFVTVNISLICLIDRHHKSYPPSVTAPLKSCQELIIAQKHDGFFRRLHHLTNSCPLQAGMNSPPTRLGCFTHNPTKPPLSVVRYTSPQNNSPAFCVASCRSAGFAYAGLQGGVHCWCDRTLPSSPPLTAGHCHLPCPDTSSGEAANYPSCGAALAVDVYNTGAAERIYKTLTSLNTDPWQLDETSDVRVVYVLVLTGRSWRHIQRSFRLLYHSSNYYYVHVDKKSEYLYSKFQKVAQLLPNNVYVTSNRRNPVWGAPELLSLMLNIMQDLLTNFPSWKWDFLINLSETDI... | Pathway: Glycan metabolism; chondroitin sulfate biosynthesis.
Catalytic Activity: L-seryl-[protein] + UDP-alpha-D-xylose = 3-O-(beta-D-xylosyl)-L-seryl-[protein] + H(+) + UDP
EC: 2.4.2.26
Subcellular Location: Golgi apparatus membrane
Sequence Length: 587
Sequence Mass (Da): 66024
Location Topology: Single-pass type II... |
A0A833IPY2 | MVAIPIEALLKSGLWPLEQALNRLLGLDPETEARLRPLAGRHLQVELEGAPQPLQVHFSPQGLSLLPGAAERPEATLRSSPGALIGLALRRGELRSGDLSFQGDVGLVQGVQKLFGELDIDWEEQLAGLTGDVLAHQIGRGVREGFAWLARSRASLTQSLGEYLSEEARYTPPRLELEGFYADVDRLREGADRLAARLVRLERRRGAE | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Required for ubiquinone (coenzyme Q) biosynthesis. Binds hydrophobic ubiquinone biosynthetic intermediates via its SCP2 domain and is essential for the stability of the Ubi complex. May constitute a docking platform where Ubi enzymes assemble and access... |
A0A967HC13 | MLMSRTNRYIIKEILTPTLICLLVFTMVLLVGRLMKLVDLVVNKGVSISDIFILFGTMLPTFLNITLPLAFLMGIMIGLSRMSADSETVALKAAGIGLGQIARPVIALAIVFSLLTGIAGMWLKPWGYRAFRNQVFAITMQKATIGFQKQVFMKQFDNLILYANDIDGRSGLMSGLFIVEKKPESSMMIFADQGNILTDESEESISIQLRDGTIHRRQKDTDSAYQLIHFQNYNVQPNFGESGNQA | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Subcellular Location: Membrane
Sequence Length: 246
Sequence Mass (Da): 27410
Location Topology: Multi-pass membrane protein
|
A0A661DGN9 | MTAWNFEMSWPPSVNGYWRAVVNKRTGTVSQILSKRGRQYVESSAVDLMLAGMKGMHITARLEITMHLHPPTARKYDVDNFTKAVFDSLTKARFFMDDEQVDILHVYKKHIIRRAGLVRLTVNEVA | Function: Endonuclease that resolves Holliday junction intermediates made during homologous genetic recombination and DNA repair. Exhibits sequence and structure-selective cleavage of four-way DNA junctions, where it introduces symmetrical nicks in two strands of the same polarity at the 5' side of CC dinucleotides. Co... |
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