ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A0S7YCF7 | MLYWLLYPLKDVFGPFRLFGYITFRSAYAAVVAILIVLIFGPRFITFLKKKSAGQRIRSEVPESHHMKEGTPSMGGFIILLSILVASLLFCDLNNQNIIILFSATIWFGLLGIWDDYIKIYKNKPRGLSIKTKLVLQIVYGIGLGLFLYFFSPGEYATKTNLIFVKNYVINFGILYPLFVTLVVVGSSNGVNLTDGLDGLAVGLIGIAAVAYAALAYACGHVVISDYLNIIFITNGGEVTVYCASILGASLGFLWFNTHPAQVFMGDTGALSLGAIIGTAAILIKQEILLVLVGGVFVIEALSVLLQVIYFHRTGGKRLF... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yield... |
A0A8J6YMV5 | MRDKLRVARSFSQASPAYDARAGLQTVVGAALLDLLETGCSRAPEVLIDLGCGTGARTALLMDLHPGARAFGLDLAQGMARHAASRAPGAFYVTGDMEALPFAPRVADLLYSSLAIQWCEDPASVLREAHRVLRPGGRFVFSTLLAGTLWQLEEGWRQVDSHVHVNRFRTGGDYRSLAENAGFRITAWREETRIETFPDVLALMRSVKGIGARNLNTGRRPGLTAPARIAALARAFEPLRTLEGLPLTYRVLYVGLEKPA | 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... |
A0A8C7CS59 | MNDKIWFRTPALQLGELGKGAGKGGGGGGSVREAGGALGKKQAAEEEMYFRRKEQEQLAALKQHHQEEIDHHKKEISRLQSEIDRHKGKIRKLKHDD | Function: Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase e... |
A0A8C7CWW7 | MSVIYILCYMAVLLLCVGGNMLVSLVVLRNRNMRSVTNLFILNLAISDLLIGVFCVPTTLIDSLISGEKVEGCEKVWSEKADFQSTCC | Function: Receptor for NPAF (A-18-F-amide) and NPFF (F-8-F-amide) neuropeptides, also known as morphine-modulating peptides. Can also be activated by a variety of naturally occurring or synthetic FMRF-amide like ligands. This receptor mediates its action by association with G proteins that activate a phosphatidylinosit... |
C7MDK0 | MSTVVLPGSFDPFTLGHLDLTRRAAALGHHVIIAVSHNPSKQGTLDLETRKAAITTTLEQEDLSGAVEVRTLPRGLLVDFCREVGATAVIRGLRSQLDLAYEEPMARMNHHLADVDTVFLLTDSAWSHISSSLVREVHGLGGDVSDMLPGPSLDALRAAAAVS | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
... |
A0A3Q9XV31 | MRYSFSKLFRLRKRYQFQKFTHSSKRLIGRWITIEIVPNPLQMTRLGITVTKRYGKAHDRNRFKRITREAFRYCQSSLPLGQDLNVKPRVNAKQATSLDIYMDLIKLLSTNHHERGT | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
A0A3Q9XZ61 | MNLEETLFNFLNIYANHQQPVLLGLSGGSDSLALFYLLIKYRNLKALNFAAAHVDHGWRAESKEEARQLQHLAASMHVPIYLKNLNIAQLFGNMEEACRHERLAFFKNLCNQHGYQAVILGHHLNDQAETVLKKVLEGGSLPYLGGMAPVTDYQTLKLWRPFLTCSKSQIKQWLVCKNYKFFEDKTNEDEKFLRARFRKTIIPHLASTFGKKIEESLCRLGYEAQELKKYLDNHLQGYLKDIIKGPFGSSLNFQPHGKCTDFEMRYLIRKVCESEGLKLSRHLIEEACKKIHSKAANCQLLAKDTWVYIDRERLFVMSKP... | 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)... |
A0A0B7JQR9 | MSSVSSADVAVDSEPIPPTGSLISIFEGGRGEGGGGDPVKKTPVRGKRSVDETVAFRREPPVDEGVASRAAEKRPFKTEPKSQATPPRLDHLMSKDRIDTRESDLEASPSSSRQRQRALQAASAVELSRPEVKASRSPPRLKNLVSQNTSDRKRPEVEERRASPTYTSPVQTAVPRITNKYNSPQTSNPPQFSPLTPPPQSAGISPLQPGAVKPPPKPKRAPTQTTRPPTPPESRPSAPPPKPKPSVDKPTPGVSSKQRSGQAAPLGEDAARVSKLVAKSSAPPTPPKPRKPQSTSNLKQNQAPEDQRRPIPSKTKGNRG... | Function: Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma mem... |
A0A5D0MNP6 | MKFYIETYGCQMNEYDTDILIYEFLKEGYEQTEDIKDADIVIFNTCAVRQSAENRVHGQLGHMKREKENNSFILGVMGCMAQKEAEKLKETHPHIDFVLGTDFLHRVIPAIKYLDKNRKESIVKTENDKPFLEFEDIGRKEPQLQEFVSIMRGCDNFCTYCIVPYVRGRERSRDYSKIVKEIEYLVKNGTVEVTLLGQNVNSYQYKDVDFLKLVKKISKIEGLKRIRFTTSHPKDMTPEILTELMSIPKVCDHYHLPLQAGSNKILSKMNRKYTKEHYKKLVKTIRDNSRFASITTDMIVGFTDETEEDFQETLELAKYS... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
A0A7Y3P2I3 | MSEREELDGLLAAAGVAEAYRERLSAFGASLLEANRRFNLTGAKSPAALAPHILDALTLLPEIEGRTLDVGSGGGFPGIPLLLAGATVDFLESNAKKCGFLREQIAAFGLEAEVYCGRAEVLGRDTNLRERYDRAVARALSSATTVAEYLIPFLRVGGVALMPRGRAEEGEEAAIADASLVLGAEPLEDIRLEGDRRIVRLIKRKPTSDRFPRRTGIPTSKPLCR | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 225
Sequence Mass (Da): 24201
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A0A924KVN0 | MNKNLARAAIFATITLVCLVFSLRISASSPLAQALPKSGTAYASAEIRALQADDASNPGMLWVANGETLWNAIAGEQTKSCAQCHGAASVSMKAVATRYPQMIPTATVPTLINLEGRINLCRVKHQRTTPLVYESPDLLALSTFVSHQSRGLVRRLTISDGNRAHYQRGGALYQQRMGQLNIACTHCHDQNAGKTLLAEKISEGHPNGYPIYRLEWQGVGSLHRRFRSCLSGVRAEPFVPGGDEYLSLELYLAIRAFGLEFETPAVRR | Cofactor: Binds 2 heme groups per subunit.
Catalytic Activity: 2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]
EC: 2.8.5.2
Subcellular Location: Periplasm
Sequence Length: 268
Sequence Mass (Da): 29309
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A0A418VQ88 | MPLSLTLHGGALALVVLLGAEKPPPPPAAAVAFLLELESPPSPPAPPGPPVEAHPAPTPEPPVEPTPEPERAAVAPVPELLALEPQPVEPPPTEPAMIPVAEAPPPEVRLLEVPPVAPEPPPPVEAAAVVEPPPPAPPQPAPPPTPTPPPRQPVKRTTPAKPQTVSAPVAPARVTPTPTAPPSVPIPPQPTHAAAPSAPPPDYLAAIQARLARYKVYPRAAQTAREEGTVLLRFVIGQDGTILRWTIVQGSGHESLDQAAESMIERASPLPPIPADLGRDRLEVTLPVRFALR | 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... |
A0A8S0Q443 | MSSTRMIELKSSDGEIFEVEEAVALESETIKHMLEADCADTFFPLPNVTSKILAKVIEYCKRHVEAVAAKPAEGVLVAADKMTDEELKAFDADFVKVDQGTLFDLILAANYLNIKSLLDLTCQTVADMIKGKTPEEIRKTFNIKDDSTPEEEEEVRRENAWAFE | Pathway: Protein modification; protein ubiquitination.
Function: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein... |
A0A140LAS0 | MTKYKREDLVNLLPYKPAKVKEAIRLHANESPYDLPEDLKESIFDRVRKESFNYYYDPNCDELREALSGYLGIQPEKIFVGSGADEIIYDIVLAFAGPGREVIIPVPSFPSYETFSVISGAKVVRVPLLLEEDSADCCWKLDVPKIKSQFKKDAPQVMFICYPNNPTGDYFREPDVFELIKDFNGIVAVDEAYFEFGGKTFIKRLSQFPNLVIIRTFSKVFSLAGLRIGYAVADENIIEELYKVKPPYNVNLFSQIAAVEVLKHMDWVEEVKKKIIKAREELKNKLKELPGITVYPSSTNFLLCKFKVPRDLVYQKLLEK... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 362
Sequence Mass (Da): 41572
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A0A5D0MJ98 | MIWVHNINPVILHIYKNIAIRWYPLAYILGFIAAFIWIHYLIKNNYLDLNKKELDDFIFYLFLGVLLGGRIFYMIFYQFELLLKKPFELFMVWHGGMSFHGGFIGILFFTYLFSKKYNKNLWKLYGSLAVVAPVGLFFGRIANFINGELWGKPTNGEWGIIFPEAGPLPRHPSQLYEAFLEGLILFIILFIIFKSTRKLKYLGPYFGMGYSTFRIIVELFREPDRQLGYLILKPITMGQILSLIMFLFSVYIFYIIRKKEGF | 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,... |
A0A5D0MAG8 | MRLLSNQEKVDMDKYTIEDLKVPSIILMENAAQSVFNVIKKEIKKNDKILVLTGKGNNGGDGFALARILKIKSYNVELYKIYEPKTKDARKNSKLCKIYSVESVDSKNLNIEEYDVFIDAVFGTGFKGILEDRIQNVFNKINNSSGLEISIDIPSGISGDNNEISPNCFNADKTITFEYPVLAHCLYPGKKFVGKLFVEPIGLKYNKELKKEVLEEKDLYLKPLKYDVHKYSRGQVSVIDGIRKYSGATYLTLKAALKAGAGYVRLITDGENRFKNILFEIVIKNISSYEKIKLNSKIAKGILVAGPGMGRKSDKLTLLN... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A956SY90 | MMEVNVSHEGVDDDEPPSCEWIEKVVQSTLESARFDSPCEVSVLLTDDHRMRELNRDYRGKDKPTDVLSFAFEEGESLVLPPGAPRMLGDVILSLPTIRRQADGHGQTYARECAWALCHGTLHLLGYDHQTDSEDEAMRGLENEVLSGLGEEFLSW | 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: 156
Sequence Mass (Da): 17532
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A0A5F8A9S9 | MAASMVRRLWPLLTRRGLRPHRGWISNGSPRRSFATEKRNRNLLYEYAREGYSALPQLDIEWFCACPEEAARALELRKGELRSADLPAIISTWQELRQLREEIRRLEEEKEAVTEAVRALLANQDSGEVQQDPRYQSLRARGREMRKQLFPLYPREAQLEEQFYLQALKLPNQTHPDVPVGDESQAQVLHVVGDKPAFSFQPRGHLEIGEKLDIIRQKRLSHVSGHRSYYLRGAGALLQHGLVNFTFNKLLRRGFTPMTVPDLLRGAVFEGCGMTPNANPSHIYNIDPARFEDLNLAGTAEVGLAGYFMDHAVAFRDLPV... | Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
EC: 6.1.1.11
Catalytic Activity: ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-seryl-tRNA(Sec)
Sequence Length: 539
Sequence Mass (Da): 60807
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A0A2M7F7K1 | MTIPMPSLPNLTAMTPELMVLFSALAVLIIDFAWPRVNKGFLAFLGAFGLAAAGILSYQSLALNIPTHIAGLSADAYAQFFKIIFCAAGIMVMGISVRFLALEGYNYGEFYAIVLLAVLGQMIMASGTNLLVIYVGLELMAISLYILAGLFKRNDKSNEASLKYYLLGSFSSGFFLYGVMMTYGLTGSLDLATIGGLVAGGHFSGLLLLAVIMMAAGFAFKIAAVPFHFWSPDVYEGAPTSVTAFMSVGPKAAAFAALIRVFTVAFGSLRPDWVTLFICLSIATMITGNFIALRQTNIKRMLAYSSIAHAGYLMIGFIVG... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
A0A2W5X8X3 | MTDQIISASSPEDGFAIVAGITTNLVIQAQARHALSPTASAAVGRLMTGGALLGVSLKGKERLSLQVAGAGCLRGVVADVMLMTDGSVGVRGYAKNPGAEVPLNPRGKFDVGAAVGKGHMQVTRSYEVGQPYVGVVPLVSGEIGDDLASYLANSQQIPSVVALGVLANPSGVIAAGGVIGQVLPGAGERAVAHLEHAVASMSPVTQQIANGAGAADLLASLAGDAKIKHQRVIGVQFACRCTKSKVEIALLGLGRDELLKLADEQVRTEATCEFCKKTYVLSSNEVNALAARL | PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive.
Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversi... |
A0A1V5LWA6 | MSAIGNGATIETDTRVKAAAKAASQSAGKAPNQASGNKTSGDRTSGKQAAGKEIAKEPGKEPGKSAGKERKTSGKSKRGLRSGNLIVITGPSGVGKGTLVKKLMAQMDRLKYSVSVTTRPIRPGEVEGTSYFFRSVAEFEEMIGQGAFMEYAKFAGNYYGTPRGWVSEEQESGVDVILEIEVQGAKQIYSQYPEAVMIFISPPSFEELEARLRGRQTESLDKINLRLEKAREELQEKNIFHYEVVNDKIEDAVNNLEHIVYAERCRIDKRR | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
EC: 2.7.4.8
Subcellular Location: Cytoplasm
Sequence Length: 271
Sequence Mass (Da): 29786
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A0A7S3A548 | MAVERKQIFRFLRAVILPIFFGGFMALVFEPERYDAERVKGKNRIFFCGRTLAGADWWRNLYTLLLIISVSVLYAVFGGGWTTGNNPGLGIFLLVVTKVLVTMTISAWILAALSDPGIIPRSNTPPEDLPQDLPPGHVALKEVVINSVTVGLIYCGTCQIWRPPRSSHCRICDNCVEVFDHHCTWLGNCIGSRNYGWFYLFVLYTDLLAAFTLWGSILFLVGFSNETAAERGVSGVEGLNIILSETPASVSRPFIASLSPRPAPAVEI | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 268
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 29630
Location Topology: Multi-pass membrane protein
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A0A2W5YRP9 | MPADRFFVAGVHECGDRVHVGGADARKIRTVLRKRTGDRVEIVDSGGRCFRATLMLHARRVEAELVEVLATRADAGEGLVITVAQSVPKGTKMDFVVEKLTELGVSQIVPLLSQRVIARAEGAKIARWRRLARVAAQQSGGLSVPVVADAITTHELAQTFSRYDRVLLAWELADPVALRDVLPDLLKSAQSVLAIIGPEGGFSADEGDEFLAHGATAISLGTRILRTETAALVLASILRYIR | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A950XH26 | MASTLWRARVYGAQNVPATGPLIVACNHISYFDPPFMGCFCPRRIRYMAKKELFEIPVLGAVITGLGAYAVDRHGSAAAAIKRSLHVLKEGGAIGIFPEGTRNLTGSVAPQTGVALLAALSQAPVVPACIHGTDRALRLARVDVAFGAPLSPPGAGRKATREELAKFTAEIMKAIEELAGSIGGNS | 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: 186
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):... |
R7FP99 | MAKTMKLTIITPNGTILDREGVTYLEVKGTEGMLGIMPGHSPFVTTLAPSPIMFKTEMHKYDMAMSEGIIYVDFSKVTILADAAFFKNQIDFKLVKELLANAKERLAVAKEKEEAKKIEDEINIQEIKLSLENLAGRERLKK | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 142
Sequence Mass (Da): 15963
Location Topology: Peripheral membrane protein
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A0A6P8B6C3 | MLSRIGTTAAHAPARVELCLRIKPTCLASSSSSSSSSSSSSSSSLPRRGSKSRLGHASNAFAVWAVPRRGYASSSSSSSVITKDKPDAKIAVLGGGLTGLSTALFLSIFAPRARITLYEANERLGGWVHTVDSSAEDAQGRPQSVKFERGPRVVQLKEGDANSRLYVLLLHQLGIADQAWALGQDSELARRYIYHPDHLIDLTGPSNSDSRLIKSASLARFAGRMLKNALTEPALKGLLPALAHMLSNRKPLGAEEYCRRLVDIEDESIGSCLTRLFGGRSSVADNLASAMTHGIYGGDIWKLSIQSTLFARAQMFPYRL... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
EC: 1.3.3.4
Catalytic Activity: 3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyr... |
A0A950XHW0 | MPRRCAPSFAPRRRVASPSIFSIATRLRKIPRIPENEIAVGRIAGAFGVRGELKCDPTGAGRTVISAGAELRCRQPELPSAIRVESARTHKNRLLIRIAGVNDPAAAAAYAGAVLFANRKEIPLQAGEYFDDDLIGCAVYGEDGTAYGSVARVEHYPASDMLVIDGHMVPMVGAIVTAIDLDDRRIVIDPPEGLFE | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A0A924XYT7 | MPVNLPNLITLLRILLIPLIVGIFYLPSDWLGYGDKNRLATAIFIFAAITDWLDGYLARKLNQMSAFGAFFDPVADKLVVVAALIVLLYLNRVDMVVALIIIGRELAISALREWMARVGQSKSVAVAFIGKLKTVL | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 136
Sequence Mass (Da): 15031
Location Topology: Multi-pass membrane protein
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A0A1V5M660 | MSIKTCAVIGLGRFGALFAEILSANFSVVTFDIDASRRKFTPARTTFVDELSTALSADAIFYAVPISSFESVLEEHVKDHRDLLCGKLLVDLLSVKVHPAAVFARLLPALPGARALCMHPMFGPDSVERQAGSLSIRDLKIVMDASMAPSDAAQLKEVFAAQGAKVLDLSCDEHDRQAAESQGLTHFVGRILDEFNMKATAIDTAGATGLLRIREQVSRDSWQLFVDLQTYNPYTIPMRVKLSAAQDKVFNKLLPNRIFKDRLVIGIQGGAGSFNEEAATHYMSRYPEQPYELIYLHTTENVLKALHEGRVDRGQFAMHN... | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Length: 453
Sequence Mass (Da): 49884
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A0A2X2HZU3 | MSACICILGVAWLGDTFVSNNIDWIKDTAGEVIQGHPWLLAVIFFFASALLYLQAATAKALMPMALALNVSPLTAVASFAAVSGLFILPTYPTLVAAVTDG | Catalytic Activity: (S)-malate(in) + succinate(out) = (S)-malate(out) + succinate(in)
Subcellular Location: Cell inner membrane
Sequence Length: 101
Sequence Mass (Da): 10574
Location Topology: Multi-pass membrane protein
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C7MCC4 | MTDTVPTRARIDALRRTHIAEYPDFPTPGVLFRDITPLLRDAAALREIIQHWKTLLPEGVEYIVGTEARGFVLGAPLAYEIGAGFIPVRKAGKLPGRPAALRYDLEYGSAEIEIPENSLPAGARTLLVDDLLATGGTAAATLELTRRFGVEVLGATFLLELAGLGGREQLPDVPLSAVWTIEN | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.
Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
EC: 2.4... |
A0A3A6NKV6 | MTMKTTSLHDKHLGLHAKMIEYAGFHMPVSYTGITEEHLAVRTGMGIFDVSHMGEFLIEGADALSYVNHLVTNLITPDTTKVTYSLMCDEKGFVVDDLLVYVIKEDQILLVVNAGNIDKDFAWVSEQAKAFHVTTRNLSDQYGQVAIQGPLVSANVKTMLGLDGSDLSFMTYKVVPYQDGYVIFSRTGYTGEDGFEIYGKPHLIDDVWDKAIAYGVTPCGLGARDTLRFEANLPLYGHEISESINPVEAGLNFAVKLDKSFIGRDAIVAYKEAPKRKIVGLELLERNIPRHGYKVFIGEKEIGSVTTGYLLPTLETPIAN... | Function: The glycine cleavage system catalyzes the degradation of glycine.
EC: 2.1.2.10
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Length: 359
... |
A0A3D3SUA4 | MTQAIATEASVVKVRVWRGKEQGEYQAYEVPRQPSQTVLDIVTYIQREIDPSLSYRFACRVGVCGSCAMVVNGQARWTCRTHVDKVAQDGEIEIAPLRNLPVVKDLVTDMAPFFDKWAKAKGQFQGDTTRHDEFARVEPESKQRQAVDLAIECIGCGVCYSSCDVVSWRPDYLGPAALNRAWTLMNDVRDT | Cofactor: Binds 1 [2Fe-2S] cluster.
EC: 1.3.5.1
Catalytic Activity: a quinone + succinate = a quinol + fumarate
Sequence Length: 191
Sequence Mass (Da): 21463
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A0A8J4V0R3 | MYFGKFISPIFQKGLYFKPNNKISVFGQPNFYIGNRKLCSFRSTKNLKTSLILSKQDIKESFVKKFPVSARPYVQLSRIDRPIGTWLFLIPSYWGLFLASPTPDLKLLSVFAVGSLVVRSAVCIINDMADYKFDKQVERTKTRPLASGQVTHKKAFVFLGAHFASLYAMTLPILNNQTILLCLSSLPLAVLYPFMKRFSYYPQAVLGLFINWGVLAGYYAIAGPIGLTAVIPLYISSFLWTIVYDTVYAHQDKNDDRMIGVKSTALKFAENTKPILSVLSVATIGGMALTGSLLSMPLVYYLGTGVCATHLFYKLYRVNL... | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, ge... |
A0A418W121 | MFAQAGRHGTAPPSAVRLLGIDPGLRHTGWGVIDVVGNRLTHVADGAVHSDANCTLAERLVQLHDALSAVLERYAPDEAAVEETFVNANAASTLKLGQARAVALLVPALAGLAVAEYANNMVKKAVVGQGRADKAQVQAMIRLLLPGCAITTADAADALAVAICHAHHRSSWTMWRRGGGVFPVKRSLSPERAEARVLETLSPRGEGWVRGTRRGSSRVRPAPPPHPNPLPGGERG | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
A0A142XKB9 | MSATVIVDYGMANLRSVQKAFEQVGHSATITSDPKHLAHAAKIVLPGVGAFRDAITRLRETGIDDVVRRHIESGRPFLGICLGMQMLFTRSHEDGTHEGLGVFSGDVVRFPSVPGLKVPHMGWNTLRLTRPGGPLFAGLPADPAVYFVHSYLARPNPAAGNIISAEADYPTPFCAAVWKDNIFATQFHPEKSQRVGLQMLRNFAAL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthe... |
A0A7Y3KG79 | MHLDRVVSAVAPGSGLAFAAVVATRSVAEMRDRHDSSPTATAAMGRLLAASALFGISLAPREWVTLRISGDGPLGTLGADSRLLDEGTLGARGYAAHPLADLPPNALGKADVAGIVGSGTLHVTKSYAIGQPYNGVVPLMTGEIAEDVAFYLANSEQIPSVVALGVLMGPEGVRAAGGVMAQVLPGANRRSVDRLEERARSLRPVARSISEGADAWGLLAMLAGEEALRSKHELALRFACPCTLERVERALVGLGEETLVEMAASGESTEAFCDFCRERYLIEPSAIARLLRER | PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive.
Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversi... |
A0A956PGQ9 | MNYVSTRGDNKKRTFSQAVLEGLADDGGLLVPESLPDFSREWPKWKNLPYNELAFRVLEPLATDMPEEALRQCCDSAYGPSYGGPVAPLREVGPFHLLELFHGPTLAFKDVALQLLGRLFGVILEQKNQELNIVAATSGDTGSAAIYGLKDVPRVRLFVTHPEGRIADLQRLQMSTVMNDSVFNIAVDGTFDDCQHMVKQLSSDLEFKRNHSIGAVNSINFARIAAQIVYYFAAYLQTPRAAEQVPAVVAVPTGNFGNILAAEYARRMGLPLACTVLASNENDILPTFFKTGMYKRGAPRATHSPAMDIQVASNFERYLY... | Pathway: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 5/5.
EC: 4.2.3.1
Catalytic Activity: H2O + O-phospho-L-homoserine = L-threonine + phosphate
Sequence Length: 480
Sequence Mass (Da): 53193
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A0A8J7CW90 | MRYDVIVIGAGLAGLVAGLRVLEGGRSCALVNAGQSALHFSSGAFDFLGHLPDGTPVSRAPDALEALADQAPDHPYALLGRQRTLELGQRAEAFLRDRGLALDGSLAAGNRLRITPLGTTVPTWLGASEALGLDPATGALPWKRLLVATVEGFLDLGADVLSSHLAATGATTEAAIRSASLRLPVLDRLRTNPSEFRSVNIARVLDHPEALATLAAELAPLARDVDAVVLPACLGFRSNEPVATLSRQIGVPVRVVPTLPPSLIGARFSRILLNRFLADGGVCMNGDRVTGHDWNGPSLARIYTASHEDIPLEADDFVLA... | Pathway: Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route): step 1/1.
Function: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor.
EC: 1.1.5.3
Catalytic Activity: a quinone + sn-glyc... |
Q2JV26 | MSSTPLQRTPLFPLHQALGARFVSFAGWEMPLQYQGVVAEHRAVRERAGVFDISHMGKFDLWGPELGSHLSRLVPSDLGAVAVGSARYTVLLNPLGGIVDDVIFYRHPPEGELEHWSLIVNAATRQKDWEWLHQQGIPGLELQDHTESQVLLAVQGPAAEEVLQPFLAGSLRALRRFQHGQFATRKERSSGAGVFVARTGYTGEDGFELLLGPADGLWLWEQLVQAGVQPCGLGCRDTLRLEAAFCLYGQDIDESTTPLEADLGWLVSNPGDYIGKPALESQRQQGIPRRLVGFRLLERAIPRRGYAIYAPNSPEPIGRV... | Function: The glycine cleavage system catalyzes the degradation of glycine.
EC: 2.1.2.10
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Length: 378
... |
A0A8I3W821 | MNPQIGNPMERMYRGTFYYNFENEPVLPGRSYSWLCYEVKINKDPSKLPWDTGVFRGQVYLKPQHHAEMRFLHWFRKWKLHSDQEYEVTWFVSWSPCPVCARNVAEFLTEDGKVTLTIFVARLYYFWIPRYREELRRLCQRRDSPHATMKIMSYGEFQHCWDKFVDNKTETFAPWNELPKNYTLLRITLGEVLRDLMDPDTFTYNFNNDPLVLGRHQTYLCYEVEHLHSGTWVPLHQHRGFILNEASNSLSFPEGRHAELCLLDLILFWKLDPAQRYRVTCFISWSPCFCCAQEVAEFLQENPHVNLRIFAARIYDYRPG... | Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-se... |
A0A1D5RDB9 | MTQYPACTSGTLATSSRWNLTMSPRHQVGSMQTPGEGRVGYGLFNSTCADCSSALSSLCESALSSLRESALSSLRESALSSLRESALSSGKLGLVQLSEVVPGISGGPLENHYRLKQFHFHWGAVNEAGSEHTVDGHAYPAELHLVHWNSVKYQNYQEAVVGENGLAVIGVFLKLGAHHQTLQRLVDILPEIKHKDARAAVGPFNPSSLLPACRDYWTYSGSLTTPPLTESVTWIIQKEPVEVALSQLSAFRSLLFSALGEEEKMMVNNYRPLQPLMNRKVWASFQTTNEGTRSLRR | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 297
Sequence Mass (Da): 32574
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A0A0Q9SGR9 | MLLEKLFLNILIVLAPVLLQSVFGERWRNDPSPIVMGLLHGTASSLCLLFSYYELDLYWDLRYVPLVISSIYWGPLAGLINYMMILLMRTYLGGDALIFGYISMTLSFIIPFVASYKIKGLSGNSRIKAALLVALSPLLVMLLILMSYVSLYKGFESFDFATIPAVLSFGILLVLGTWLSAILQEIHEERFRMKVQIQKAEKMKTLGELAASIAHEVRNPLTVVQGFLQLMRPNEQGKNQQYLNIAMEELARAESIINDYLNFSKPKLNKLESFSFSDVLNNIIVLLTPMAMKNCVEITVNLEDHIYIFSDRGQLQQALV... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 414
Sequence Mass (Da): 46238
Location Topology: Multi-pass membrane protein
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A0A8C6B1F4 | MALSQGRVKRYFKAFCKGFFVAVPVAVTFLDRVACVARVEGASMQPSLNPGGSQSSDVVLLNHWKVRNFEVQRGDIVSLVSPKNPEQKIIKRVIALEGDIVKDGGRWKRM | Function: Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO.
EC: 3.4.21.-
Subcellular Location: Membrane
Sequence Length: 110
Sequence Mass (Da): 12... |
A0A1I6MZD9 | MVWAPNAGPFRGAEMNCAYMVMGVSGCGKSTVGAAFADRIGAVFLDGDDYHPQQNVDHMAAGHALTDEMRWPWLDRLAAEVIVRQRDETVVFACSALKRSYRMHLRDRIPRLEVVYLEADRDLIAKRLGARHDHFMPASLLDSQFATLEAPETCFARIDIGQPVTKIIDQLERLV | Pathway: Carbohydrate acid metabolism.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 175
Sequence Mass (Da): 19644
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A0A6P1U794 | MRETLYFRLRGLDTPSSVAYCIAGDSAAVSFDVAHAPLETVLEQAAGRRVVGFIPGADVHLTCMELPARQRSKALLAAPFALEDQLADDVDALHFAIGSKQPSGWPLAAIRQSTLAAYVERLAQYGVRADALIPDLLALPVPGDEQMVLLVEAQDVLLRTSAYQGLSCLRDDLPLCLQLSDPDKQRTLRVIVPRNQTFDPSTLDATVEPLSGFSDPLEVLLQNYTPETAINLLQGDFAPGQDGIKWLKPWLPAAALLAGVGLMGAALYGVQAHQLKQQVRSQTAANQKRYQQIFPAETRIVDLDAQLGQQMALLSNGTAQ... | 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: 400
Sequence Mass (Da): 43127
Location Topology: Single-pass membrane protei... |
A0A074WJ95 | MSLYRKNEPITVITAHDFPSAHVADQAGIDIVLVGDSLAMVALGMDDTSEVLMEEMLLHCRSVARGAKSAFLVGDLPMGTYEISPDQALQSAITMIKTGRVHAIKLEGGAEMAPTIKKITSAGIPVLAHVGLTPQRQNSLGGFRVQGKTTASALKLLQDARAVQEAGAFATVVEAVPAEIATLVTKKLRIPTIGIGAGNGCSGQVLVQVDMLGNFPPGRFLPKFVKKYGDVWGESSRAIQQYKEEVKTRAYPAVEHTYAMPQAELAEFEKLMAEDKEETSV | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
EC: 2.1.2.11
Catalytic Activity... |
A0A3G2Z7E7 | MSSSLFFFIFVPILAFVLLLINFIFAPHNPYIEKRSVFECGYHSFLGQNRTQFSISFFIFALLFLLFDLEILLVYPYIVSAYTNGVYGLFIMLMFFIALTIGLGFE | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NA... |
A0A1V5M2Y7 | MQPSLTKPAKNNSLRWGASITLVILVTILIQIFHLDRGFANVSLLYLLLVFLLSIYVGRSAAILSAVLAFFAFNWFFVEPRYTFAVKSANEWLTLCMLLTVSIITGHLTARLKSSEEEARRKQLETETLASASWAVSSQITTEEALTEVLKQIAKLTVVDVAAVASREKEGMVIRACLGEDRENLIAEMNSELEPRKDENKVTLQTGQGAIYLKLAQGQKLDESKRTVLDALLNHAAVILQREELSRKQSKLEAIAEADTLKTALLSMVTHDFRSPLTGIKAAVSVLQEESTTLRPVESNEMKLLLQGIEQETDRLNRMI... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 489
Sequence Mass (Da): 54232
Location Topology: Multi-pass membrane protein
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A0A4R1RE94 | MLWIKTVIVLAVAYFIGSITSGDIVARIKKVDLRSLGSGNIGATNTFRVLGSFYGAVVLAGDIVKGILAVLLGHYVLGSFHGFDMAILTGVFAVIGHNWPVHAGFKGGKGIATSAGVMIGLTPVSILAALPVWLAVFLLSGYVSLASIVAAIAYPVSVFLFYHDDPYKQFLALIIAVLAIYRHHSNIKRLLRGEEHRILYKHRGGDKS | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl pho... |
A0A554L0W2 | MTAKTETKHTTLYRAYRPRTFGETHGQEHIVKVLEAEIKQKKPAHAYLFVGSRGTGKTTFARILARELGVTDKDLYEMDAASHTGVENIRELREGANVMPFESPYKFYIIDEAHMLSKGAWNAFLKTLEEPPPHVIFVLATTDRDKVPDTIQSRCEIYSFKQPTREVLAQVVSDVAKKEGYSLESSASELVALLAEGSFRDALSILQKVLAVSKDPSETGKLSHGAGKKVTVAEVEEVSGAPRGELVRRLLKGLSEKNAKDSLSAIQEAVDENLDARTLAKLLIHRMRVVLLLRYAPDLAGSFSKELTDADLALAKEISK... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 360
Seq... |
A0A397VQ38 | MTESNEFVPILSLNSIEQPTLLKRCKTLIEKFKSLYNNSPDFIARAPGRVNLIGEHIDYAGFGVLPMAISNDVIIAVNFSNKKGYTNVRLSNIIDDKYKQKSWDFEGKDKIVEIIVEAGVSEWSNYFKCGYKGILRHLGIDNPVGMDCLVDGIVPIGAGLSSSSSFVCCAALATSHANNAKLTKKQITEISIECERFAGMNSGGMDQTASIFSQFGHALYVEFLPTLNATPTKLPTTNSPITFVVANSLVKADKVITAPIHYNLRVVETKLAAYHLGQLLFGEGCENLKHLCDLYSKSTKVTIDNLEKLSDYVDQVYKKN... | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 2.7.1.6
Catalytic Activity: alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate + H(+)
Sequence Length: 496
Sequence Mass (Da): 55193
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A0A077FLF7 | MVTLITRPKAEAELLQQKLHSMNIYSVIESLFTVVHIHVDINDLNNILGTNKLQFIIFTSINAIKAFAELSNIRDILVLTVGSSTARQAKTIGFKQVITVNKDATELLHYIRRNFIPSKGMVLYPHGKIISLDIMAILKKDGFDVRDRVVYDTLPVKCLSNHLIDMINSRYITSALFFSAETARIFISLVRQADIGQMFNSITAFSLSANITKILESLPWKSIYTSSRPTENSLLQLLEDKL | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
A0A916MET6 | MTLAIPDSLRATARTLASTPIAALFARDPSRVERLTFEWEGFRVDLAKERITPEALAELCAHAGGAGLGRWIAALFAGEKVNVSEARPALHPALRDPSTTPLSVDGADLRRDIRVSRERIGAIADAIRRGDRCGATGKPIRHLVHMGIGGSDLGPRLVVDALSPGTPVEGPGVSFVANVDPVALDRALAPLDPASTAFVVASKSFSTQETLVNANAALAWLAAALPPSADTHAHLIAATARPQAAAEFGVPADAILPFHESVGGRFSLWSSVGVTIAAALGNRVHAELLAGAHAMDRHFATAPFAANLPVVLALAGLWNA... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
EC: 5.3.1.9
Subcellular Location: Cytoplasm
Sequence Length: 548
Sequence Mass (Da): 57143
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A0A924KRN1 | MRVICLTGGIGSGKSAAADFFIARGVRVVDTDKISHRLTAKDGAAMPEIAGAFGFQALDNTGAMNRAVMRELAFADPAARTRLEAILHPRILADANLEIERLAGDDGYSQSYILLAIPLLFERMTYRQNLWRTLVIDCAVALQVARAAKRSGVLAVDVMRVVKAQIPREVRLQLSDDLIWNGGDLLQLESSVDAQHRIYARPPTE | 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... |
A0A0A0M3K9 | EAPAAVARDTPEPETRPLPRGRERIEHDMEMARLAAEIHLRSEQYAKRPSRKFVSASTTEYAWAGYLREWVDRVERVGNLNYPDEARRRRLSGEVVISVAIRRDGSVEQSRILRSSGIPLLDDSALRIAALAEPYPPLPRTEEDPDILHVTRTWAFLAGGELVDR | 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... |
A0A1X7LA18 | MQVFKFGGASIKDSEAVCNMSEILKRFPGEKILIVVSAMGKTTNALEEILHLRLNSLSTTTAIRTLFQYHQSIVTKLFKENEAAVSHLLEEIFHELNAQLSDIKKTRYDESYDSIISFGEIISSSILLHYLQKEGFTISKIDAKDCIKTDESFRDALVNWETTKDLINKTTQAEFHKNQLVITQGFLGGTADGKITTLGREGSDFSAAIFASCLHAKAVTIWKDVPGILNGDPKKIKDAVLYQELSYQEAAEMTYYGASVIHPKTIKPLANAGIPMHVRSFSSPEKGGTIIHECETVHQIPCIIIKERQSLITFKLNDFT... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
EC: 2.7.2.4
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Sequence Length: 424
Sequence Mass (Da): 47907
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A0A1C6UT90 | MARPWRVAIVGGGITGLAAAVRLRDRAPTGTEITVYEQSGRLGGKLRTGELAGGPVEFGAESFLMRDPAGGESAAVSLIRRLGLAGSIVHPTVGQAALVVDGGLRPVPGGTLVGVPGDLDKVAAVARPAAAADRDGGAPLLPADADVSVGALVRDRLGDEVVDRLVDPMLGGVYAGRADDLSLVTTMPALARAARVEHTLVGAVRAAQAAAPRAPGAPVFGTLAGGLSTLVEAAARESGATIRRDAAVRELRPTPTGWRLTVGPTRDPDDGSRSRRGGRRAELESSQVEADAVLLAVPARPAARLLAGPAPEVATAVGGL... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.
Catalytic Activity: coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2
EC: 1.3.3.15
Subcellular... |
A0A1X7MHT3 | MDIFQAIALAVLQGLTEFLPISSSAHLILLPVLAGWQDQGLAFDVAVHVGTLTAVVMYYRKDLAKLIMSWCG | Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Membrane
Sequence Length: 72
Sequence Mass (Da): 7832
Location Topology: Multi-pass membrane protein
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A0A950UV46 | MSELLPPTEAIHAGNPQLDRLPTTELIDVLLRDQFDAIEAVRSQSAAIAHAVDEIAARLARGGRLHYVGAGTSGRIATLDAAEMPPTFGAPPELVHAHIAGGDAALVRAIEGAEDDSKAGAAQMRDVEPGDAVVALSASGGARFVIAAAEEAKARDAYTVAVTSVESSRLARVADHAIVAATAAEALTGSTRLKAGTAQKIVLNAISTAVMVRLGKVYGNLMVDVVATNDKLRHRALRLIADLAEVERERARELLDAAEGRVKVAIVMERKRCSAAAARGLLDRRGGSLRAVLE | Pathway: Amino-sugar metabolism; N-acetylmuramate degradation.
Function: Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate.
EC: 4.2.1.126
Catalytic Activity: H2O + N-acetyl-D-muramate 6-phosphate = (R)-lactate + N-acetyl-D-glucosamine... |
A0A2W5YLY0 | MINTLRAALLVPDIRQRIGFVFGAFAVFVFMVHIQLPNVNEQAWQQQLQSGTFFNFLGFLSGGALQKLSIIAMGITPYINASIIMQLMTVVLPQLEEMAKKGGEEGRKKISQYTRWLTIILATVQSFFMTRFMSQAGVFYDHSLAFQLFAVLMFVAGTMFLMWLGEQITDRGIGNGISLIIFIGIVLRFPTQIANTVSSAAGGGINIFNLVMFILIALVTIVSIIFLYQGQRRVPVQQARRVVGRKMFAGRSTYIPLRLNNAGVISIIFAISLLLLPQQALSWFGRGTQSGFAGNISAFLTAYFSPNEWLYNVVYFLLVV... | Function: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring compos... |
A0A401SMT0 | MRISVFVLLLPTCLSLVWAEHNAKNEKERHDAKTQKVKKPKIKENQSVLVLNKGNFDRALKESAFLLVNFYAPLSGASLALLTEFEKAAEQLKSEKQVNLCKVDVSVEKDLAKEFGTQDYPVLKFFIKGDRKNPLTCTGVRTASSIITWLRRRIGPSATRLLNMTHIETFIASEDVVVVGFFKDLKENNTKTFYETAKDIPDIPFGVTNSAKHFVKYSISTDTVILFRKFEEERLDFKIANGSTLEKDKLTKFIKVNELHLVTEYNQMTSNKIFDVGIDSHLLLFVDKTSKEFNEIYENFKAAAADLRAQIIFILVDTDE... | Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
EC: 5.3.4.1
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 521
Sequence Mass (Da): 59691
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A0A0G1U331 | MNPLPSNYEILISVLGKNRVKLDEPLGKHTYFKLGGPADLFYTAENVDELIGSVQSAINFQVPYFVLGGGSNVIISDKGIRGLVIKNRTGGIKLKGFTGSALKGKLNLKDVLVEVDSGVPSNRLIRFTLDQGLAGLEKMLGLPGSIGGAVYNNSHHLDILIGDYISEVKVIGKDGNIKTYQNKDLKFAYDYSILHDTKEVVLSASFKLEHGDKAALWEVATSAVKRRASTQPLGAPSSGCIFRNIPLSDAMRLGTPDHTTSAGYVIDKAGLKGERVGGAVVSSRHANFIVNDGSATTKDVMDLVSVIKQKVKAKFGVDLT... | 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: 329
Sequence Mass (Da): 35307
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A0A8I3W3Z6 | MAVLWRLSALCCAQGGRALLLRTSVVRPAHISAFLQNQPTPEWCGMQHIHLSPSHHSGSKAASLHWTSERVVSVLLLGLLPAAYLNPCSAMDYSLAATLTLHGALDKLLLTMFMGMPRRKLPRQGFWPFQL | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Subcellular Location: Membrane
Sequence Length: 131
Sequence Mass (Da): 14471
Locati... |
A0A5F8ATE3 | MVCTRKTKTLVSTCVILSGMTNIICLLYVGWVTNYIASVYVRGQEPAPDKKLEEDKGDTLKIIERLDHLENVIKQHIQEAPAKPEEAEAEPFTDSSLFAHWGQELSPEGRRVALKQFQYYGYNAYLSDRLPLDRPLPDLRPSGCRNLSFPDSLPEVSIVFIFVNEALSVLLRSIHSAIERTPPHLLKEIILVDDNSSNEELKEKLTEYVDKVNSQKPGFIKVVRHSKQEGLIRSRVSGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFDNIKYDNFEIEEYPLAAQGFDWELWCRYLNPPKAWWKLEN... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 674
Sequence Mass (Da): 76711
Location Topology: Single-pass type II membrane protein
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A0A6A1WNQ1 | MAVSNSLSFLFPPPPIIFVTAMSVISFTSLAYTGFSEIRGKHLQYSKFWNVASPKASKTKQIKLSSRTGMLLLYTPAFLAGLASFVLFPSQDLRFLLLDSALTLHFFKRIFEVLFIHKFSGGMVLDSAIPISLSYFLSTATMIYAQNLTQGIPEPSVDLKYPGILLFLIGISGNFYHHYRLSKLRGEGDKEYRIPKGGLFDLVICPHYLFEIIGFLGISSISQTLYAFSFTLGTVFYLMGRSYATRRWYFSKFEDFNEDVKALIPLFYDVKEQQEEQKNRKRKDKSMIDRRLMDRLNGSASLMIVSDLDSTMVDHSDPAN... | Pathway: Glycan biosynthesis; sucrose biosynthesis; sucrose from D-fructose 6-phosphate and UDP-alpha-D-glucose: step 2/2.
Function: Catalyzes the final step of sucrose synthesis.
Catalytic Activity: H2O + sucrose 6(F)-phosphate = phosphate + sucrose
EC: 3.1.3.24
Subcellular Location: Membrane
Sequence Length: 717
Sequ... |
A0A7S2ZZE5 | MSCLAGREFCAGKTYIDEFEMNFLRYMSSGRVLNGVKHAKLSEQSVLVKEGVRPRQKILEDSFGRKHTYLRISLTERCNLRCMYCMPEEGIELSPSNELLTASEIERISKVFLSYGVDKIRLTGGEPLVRKDFDDIVQRIGAYRRDPRYNLKTIAITTNGITLKKKLKTLVDNGLSAVNISLDTLVPQKFELITRRRGHERVIEAIDACLDANFGPVKVNCVLMRGVNDDELLDFCRMTEHKDLDIRFIEYMPFDGNRWSDKKFMSYAEAIEKITAEFGALSKVVDDKNDTSKHYKISGFAGRIGFITSMTSHFCGTCNR... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.1.99.22
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Length: 391
Sequence Mass (Da): 44291
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A0A3D5NAP6 | MIKVLVFGKNGQLAQSLAWRSSAFAGLSVQFLDRNDCDVAQSDNITKAVDLHRPDIILNATAYTAVDLAENEPELARRVNCDAVRTMAENAARHSVPFVHISTDYVFDGEGKKPYRETDPVAPLGVYGSTKLAGEEAIRAITNQHLIFRTSWVYSPFGKNFVKTMLGLLGDKTHISVVDDQQGCPTSALDLATAILRIIPDIIRRDFDQFGTYHLVSDAEMTWCAFSREIQAKAIKIFGGQWPGATCQIKAVTSTKFPTVAKRPSYSVMSTEKFMTNFGFGLPDFDQSLMEVLQKLAEGDAHA | Cofactor: Binds 1 Mg(2+) ion per monomer.
Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose 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(+) + NADPH
Seque... |
A0A0A2TAP0 | MDNKWKLLFSNRGLTLIEVLASITILSIIIVTFLSVFTQTARTNQYSETIMDATYVAQTHMENVYNVSTTNTFEYGMKTLKQIGYTQESTSENRFTFSKNSKKYFVVITVEDKGDLTDVKVEVFNDSSLSDIEAQMQTLLTWEEA | Function: Required for transformation and DNA binding.
Subcellular Location: Cell membrane
Sequence Length: 145
Sequence Mass (Da): 16600
Location Topology: Single-pass membrane protein
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A0A849TS57 | MGSMSVWHWLILLVIGLLVFGGKGKISSIMGDMAEGIKSFKKGMAEDETSKEAEDKKKLEMQKTVDNVSTGTKTS | 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: 75
Sequenc... |
A0A950BXE7 | MWLALGLLCAYLVGSIPFGIVVGRGIFGVDPRTVGSGNIGAANAMRALGPTGAALVLLGDVIKGVVPTALATYWLGYGHWGVAATGLATIVGHNWSIFLGFRGGKGVATGLGVLVVLSWQATIVFAIVWFVTVAVTRYSSLGSILASAAVPVSLGLMHAPLPYEIYAIIALVFVVWRHAANISRLMAGTELRIGMSKEKNGPP | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl pho... |
A0A7S2ZQM4 | MSAEAFLEQLGVPGIGLKLVGLFFVSVFILFWPGIAELSDSVITYIAESKTGQLTRRVYRTIAVPHRGEEPGILQEVAINQEELNSGVLRLQTWIPARVEKGVQCENDSAKFNSSLPPRPPSLDAVGRNDGAPSLLNRSIFSSQLKAVSSSSSIVSLGSGSSNSLKLLEDEQVLAKLRSGEMSMHALEKTLGDTARAVRIRREYFSQQNMMNFEGVPFEGYDYDAVFGSCCEVVVGYLPIPLGVVGPLHIDGEVLHVPMATTEGTLVASTNRGCKAISLSGGVETTLVADGITRAPCVQLPSVREAAIVKRWLDDPMNIA... | Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
Catalytic Activity: (R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH
EC: 1.1.1.34
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 581
Sequence... |
A0A961ZAV5 | RQAQVKRMRPDLEVIGFRGNVQTRLRKLEDGVAGATFLAVAGLNRLGLADRITRAVPTEEMLPAVAQAAIGIEIREGDEKTAALIAPLDHAATHTCVIAERAFLRRLEGSCRTPIGGLARLGEDGQMTFRGEILTPDGKVAHATQRVGSPADADTLGDAAARELLARAGSGFFSVAS | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobil... |
A0A961Z6L7 | DVLNMNVATSSVTKGETLIDTAVTLNAMQPDIIVVRHHAAGAVELLSQKVDCSVVNAGDGAHQHPTQALLDALTIRRAKGRVSGLTVAICGDILHSRVARSNINVLNTLGANVRIIAPSTLLPAGSDRLGATVFTDMNAGIADADVVMMLRLQRERMEGSFVPSTREYFHFFGLDHEKLARAKPDALIMHPGPMNRGVEIASTVADHSRSVIREQVEMGVAVRMAVLEALAGNLPSE | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Length: 237
Sequence Mass (Da): 25299
|
M3H0W3 | METKPDLSKNEGTKKWKKEFVLHDGPPYANGNFHLGHALNKILKDTIIKSKSLAGFYADMIPGWDCHGLPIEVQVLKNLGKKVRETGPEELRQLCRKYAEEFVGKQGDDLSRFLCFWDEGRIYKTMSPDFEAKIVEVFGELFKKGYVYRGKKPVYWSIDLATAHAEAEIEYYPHISPSIYVKFPIIGEKKRFCLIWTTTPWTLPANLAICFNRKIEYSIFKTKSGEELILADALAENVTITTGVALTKLKPITSEELAALKFQHPFVDRISVSLFGDHVTLEAGTGCVHTAPGHGQDDYKVGLAAGLEPFSPVDDYGRYT... | Function: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves ... |
R5JNC5 | MIIGSAALTRKMDEMCMDTFKIPSIVLMENAASAATKRIEEILDSQGLCGQRLFTILSGAGNNGGDGLVIARKLSIMGHRVRVIFIGQEEKMTESTRTNMDIIRSMGIEILSFEHGDYHMNDTKMTGILKQTDYLIDSLFGVGLNRDLDFSYIGLIGMVNRAREMYSFKTIAIDTPSGIDPTSGQIMGDAIEADYTITFEYFKEGFLNYSIEDYLGQVFVEPIGIPDKVYNYIERQDRTKFGASIDQSADRRDFISGRFVEIDYINDILKDRKPSSNKSDLGKVLIYAGSKGYYGAAYLASRAASKTGSGLVTLVSDEDT... | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that... |
A0A077FMM7 | MIINSTISLTPTASEQGLRVDKFIAERLKYLSRTRIKTLITSGYLTIDNCIIEDCNTSVKLGSTYILTIPPPVETYIKPNESLKINIIYEDKFLLVINKQAGLTVHPGAGNHQDTLVNALLAYYGDSLSAIGGRLRPGIVHRLDKDTSGLMVVAKDDPTHHSLTKQLASRTLTRIYLAVVFGVPKPLQGTITGNIGRHNQDRKKMSILKTGGKEAITNYSVQQIFYNNIASLIECKLVTGRTHQIRVHFSHYGHSLIGDQTYGNNKRKLSKLFSEEIQEKIYNFNRQALHAISIGFIHPITKEHMQFTTELPDDLQNLVQ... | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 326
Sequence Mass (Da): 36493
|
A0A140LD53 | MGAYVIVGGSKLSGRLKVQGSKNASLPIMAATILNRSKNRIRNVPDIKDVHVMIDILKVLGAEVSFSGNELAVDSSKVSIWEVPENLMRKMRSSIILMGPLLGRYKKVKVSYPGGCEIGPRPIDLHLKGFVALGANISESHGFIYAEADKLKGANIHLDFPSVGATENLMLAAVLAEGRTTIRNAAKEPEIVDLQNYLNKMGCHVKGAGTDTIKIEGCSIEDLKEVDDYSVIPDRIAAGTYLAATAATRGNIVLENVIIEHIEPVLAKLREMGCDIKTLEDKVQLWVEKPLRALDSLRTLPYPGFPTDMQAPMMALLSTV... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
Catalytic Activity: phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 2.5.1.7
Subcellular Location: Cytoplas... |
A0A1D5QM19 | MIRALGCLSVRTTALSDCRHRECAARGRLLTARRRQVALCAGRRPKAPNGRGPAELPYSPHVRAARKLGHPATASGGRGAGRRWRGGAPAARAGRGRGALRGPGRPWAPPPSAPRPAAGLAPPPTRSLSPPLRPAVLPSRRRLFLGEALFQRAGSMAAVETRVCETDGCSSEAKLQCPTCIKLGIQGSYFCSQECFKGSWATHKLLHKKAKDEKAKREVSSWTVEGDINTDPWAGYRYTGKLRPHYPLMPTRPVPSYIQRPDYADHPLGMSESEQALKGTSQIKLLSSEDIEGMRLVCRLAREVLDIAAGMIKPGVTTEE... | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
A0A1G1NC61 | MRGLSRSHVDIFLSLFTVATIVLADRVTKIFFSDLLSLGESLPLIRNVIHMTLVHNTGIAFGLFKNHGIVFIIIPIIAVILLVFNIFYYRNNKELSRLYIGGFSLILGGAIGNLIDRIAYGYVIDFIDLRVWPVFNIADSAITVGACIIAVKCLRLSAK | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, ... |
A0A2H9LEE2 | MEQNTEIKEKQKDYKEIEKDIWLFWQKEQIFKYDPNSTNPVFSIDTPPPTVSGKMHLGHAYSYVLPDFIARYKRKKGFNVFYPFGLDDNGIPTEILVEKLANVRAKDIGKSKFVELCVKHTKESEEELYTDFKSLGISCDWSLLYRTISPEVVRVAQYSFLDLYKKGKIYREKGPILWCTKCQTAISQAELVDVEKETYFNDIIFKLDNGENITIATTRPEFLSACVGIFVHPDDDRYKHLIGKHATVPLFNFKVKIRKDKRVDQNKGTGIVMCCTFGDQTDMEWYKTYKLELKEAITVDGHMSNICGKYAGMKIEDARK... | Function: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Catalytic Activity: ATP + ... |
A0A7V1DII3 | MEKKFLIGITGASGVVYAYYLLKELKKLKYPAEVIITRAGEMVWNYELEKPVEEILKFAEKLYREDEISAPPASGSNEYSGMVIIPCTMGTLSAIACGSARNLLQRSADVMLKERKPLILVIRETPFNLIHIRNMKTCSEAGAIIFPAMPSFYHKPKNLEELINQFVRRILQFLGLSPEGLKTWQEVELE | Function: Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.... |
A0A7V5K1M1 | MLPVLLEGLRRLEYRGYDSAGVVFLEDGKISVIKVKGRVFDLEEKIFNNLPQKPKAPGLGHTRWATHGEPSDENAHPHIDCKGMLALVHNGIIENYYELKRELQEKGHKFNSATDTEVIVHLVEDYVNQGLDLKKAFFSALKRLKGAYAIGLISKENPDFIMVARNLSPVVIGLGEGENFLASDIPALLPFTKRVLFLNDGEVAILSKDKVKIFDLEGNEIERNSIVISWDLASAEKGGFPHFLLKEIYEQPEAIKHTLLGRVDLDREDIDFSKEGLEKEFFDNIEKIFIVACGTSYHAGLVAKHLIEKNLKIPVEVDLA... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
EC: 2.6.1.16
Subcellular Location: Cytoplasm
Sequence Length: 602
Sequence Mass... |
A0A950FU95 | DVEIGALELVSGASVPGVVQRVTRYGAEPAADGAKVVFVAHALTGSSRVVEWWDGLVGRDGLFDLERWCVVGVNVLGGCYGSTGPSSLAPDGRRWGPRFPVVAVADIVEAQRSALRAAFGIERVAIAIGGSLGGQQALQWARAHDELVDHAIVVGTFDHLRAQGIAQNGVAREAIRLDPRFKGGWYDEPPADGLRLARAIATLTYKSEDLFERRYANRADRAGGDPTRTLDARFDVEGYLAHQGDVFVKRFDANSYLVLTRAMDLFDLRGHERPAGRTRLTFVGIEGDQLYSPQFVWSCAARWAEAGWDSSYRHLPSDHG... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
EC: 2.3.1.31
S... |
A0A2W5Y816 | MEHRPQTTQRLHHGGILLREFPIHAAVRMRLQPYQICAPPLAASASESKTRPGEGRTHIGLRDGPRRWAAAMADTTSPLETTESTENLTDEGQRCKGRKANAPMSLSSPPSQTGKGAFVREMFAEIAPRYDAANRVMTAGLDEGWRRRAIALLAPPRGGSVIDLCCGTGDLSFHLVRKDPTLHVTGVDFCEPMLAGARTRAQREARGRGVTFIEGDVMALAFPDASFDGATMGFSLRNVVDIDATLREIRRVLRPGSRFVNLDVSKAPNLLFKRLFDLYFYHLVPLLGGLIGGSRAAYTYLPHSLTNHPNARDLQTRFER... | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
EC: 2.1.1.163
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquino... |
A0A2W5XCN6 | MARGFAAFLFRGNVVDLAVAVVIGAAAGSVITAFVKDIFAPTMGAIFGRHESVAHAKWSLRGNELQYGDFLSNLLSFLIVAIVVYFLVIVPVQKLAANEKLVPLDRDDRKCPECLSDIPRKARRCAFCTTAVDPLA | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Subcellular Location: Cell membrane
Sequence Length: 136
Sequence Mass (Da): 14739
Location Topology: Multi-pass membrane protein
|
A0A956TFK4 | MRDRLFASQDAGYESFEFNTPVAQVFDDMVRRSVPHYEAVQDLMARLALAQAGDQVIYDLGCSTGNTMVGLLELAERPLRLVGIDRSEAMLDLCALKLAPMKGDHQVELLRADIETPDFSQGPPGVVILSLVAQFLRPVRRLALLEQIRAQLTAPGCLIMLEKVIVPGRLTNTLFIEEHHRFKRESGYSVDEIRRKREALENRLIPFEPAENLAMLDRAGFDEVSIFYSWLNFQGYLALKHEQEDADQSHQHARGLSPRDPLTQG | Function: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
EC: 2.1.3.-
Catalytic Activity: prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O
Sequence Length: 265
Sequence Mass (Da): 29942
|
A0A926C1K6 | DTDVQWSAWEGVLGYYKAKEAYLQDQLGNPEGPDSPNKKYYDPRVWLRKSEETMVKRLTVAFEDLNCINRLA | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Length: 72
Sequence Mass (Da): 8411
|
A0A2N9L9P7 | MRTPFRTAAVFVKTRTESNRTALLQALHAILAIVERAGLHILLDGETCAVLDQSQHRGNSLAAIGEQADVAIVLGGDGTMLSIARELAAYDVPLIGINFGRLGFITDIALHQMPEVLEQMLGGKFEADRRTLLEGEVLHAGALMLRTHALNDVVISHGVAGGLVEFTVRVDGVNMYNQRADGVILATPTGSTAYALSANGPILHPSLAGLVLVPVAPHTLSNRPIALPDDVEIEIELTEVRDASAYFDMQSYSTLAPNDLVRVRRSKRVATLLHPAGYNYFATLRQKLHWNVMSSEQHGRA | 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... |
A0A7K2Q252 | MSAISPTSATSATSSTSATSENSRSDHPGPRPSTAAAATVISARPVVLPAPSGRGEDLQVSVCAPATGGDLPVIVFSHGFGWSMDGYAPLADHWAAEGFVVVRPTHLDSRTLAIPHEDPRTPRIWRTRVEDLTLVLDGLGVLEASVPGLAGRVDHGRIAVAGHSWGAQTASTLLGARVLDADGVPGEDMSDPRVTAGVLLALPGLGDSLTPFAAENLPFMKPSFDTMTAPALIVAGDRDDSALSTRGPDWFTDAYTHSPGRKSLLTLFGAEHSLGGVPGTEVAETTDESPERVALIRRLSTAYLRGALSPADTDWREAVT... | Catalytic Activity: (ethylene terephthalate)(n) + H2O = (ethylene terephthalate)(n-1) + 4-[(2-hydroxyethoxy)carbonyl]benzoate + H(+)
EC: 3.1.1.101
Subcellular Location: Periplasm
Sequence Length: 335
Sequence Mass (Da): 34950
|
A0A1E3BK05 | MIASKLKLLASLSILSLANAASIQQPRSPPSSSKEPFAQTHGTDLNIHDPSIVRDGDTYYSYGVDTHIPIHSAPSLDGPWTRLGNALDADSVIPKGDRTAPWAPNTIALNGKFYIYYGVSQAGCRDSAIGVAVSDHPGPGNWKDHGPIIQTGTGKGSGKYPFGTSNAIDPSVVISGGKPYLNFGSYWSGIWQVPLNDDLISLGDNVKSDSRHLAAEPKAMFPGGNNPDPNCRDDSGSHPIEGAFISYHFPYYYLWYSHGKCCDLDPNALPKPGDEYSIRVGRSSNPQGPYTDKSGKDLVDGGGELVYGSNRDVYAPGGQA... | Pathway: Glycan metabolism; L-arabinan degradation.
EC: 3.2.1.99
Catalytic Activity: Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.
Sequence Length: 364
Sequence Mass (Da): 39290
|
A6YCJ1 | MMAYKVLHFVVISLGLVTLVASRCDFNYYNQRAWLSCPGSQCGGNRQSPINIDTEKTKANNSLIALRFNDYDDPVDGDFENLGTTVEFVPETKDATLTNHLGTYDLLQFHFHWGRDSSEGSEHRIDDEQYSAEIHFVHLKQGASPSDTAGDTFSVVAVLCEAADIPIRGVWAKLSPVPTGHEDSHSVSDLVYTDLLPRNRDYYHYEGSLTTPLCDETVQWFVLKNTIKIPKAFLTMLRRVESDEDGTLLTFNFRNLQRLNGRQVFEFPPDVDNGEDKKRKRRNNRHGRDHHG | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 292
Sequence Mass (Da): 33238
|
F7NNK4 | MRFYGLLGETLSHSLSPEIHGYLFRRLNIEAAYVLFPVAADKLAEAVNGLRLLGAGGVNVTIPYKISIVPLLDELSVEARMLGAVNTVLFRDGRAIGYNTDYDGFGLMLQQHGIAAAGKTAVVLGTGGAARTAAYWLRDHGAAAVKLVSRRPAGTEPFETLPYDRLKVLPPTDLLVNATPVGTYPHTEETPLDRDLLSRFANLVDLIYNPPETRLLREARQQGIPAVNGLTMLAAQAVAAEEIWQGRSLAGELLEPLGDFLAGLPERTPNLVLIGMPGSGKSTLGVWPRTG | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydr... |
A0A7L8GE15 | YPFMFWYIDVLMKLNYLDMMLMMTIQKIIPLYLYMNLWNSSVINLVYIHTAINMIIPSVMIFNFLNVKKILSYSSVSKI | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
A0A924WHD6 | MKGETKSFASIYAVSFVIILAIALIAQTLGWHWRSWLPGAEGVESLNDGVKVAVYNFMSYLL | Function: Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Subcellular Location: Cell inner membrane
Sequence Length: 62
Sequence Mass (Da): 6864
Location Topology: Single-pass type II membrane protein
|
A0A0A2THL9 | MLPLSGKRILVTREATKAHTITRLIEQQGGISIEIPLLHFQGIYSDENEKIMKQLPSYDWVFFTSTNGIHFFFELMKHYNNTYEQAAKLKFAVIGEKTEEVLNDFGYEAHFIPNTYTGEHLGKEFNEFTSKCCSILVVQGNLAKQSVVQELSTRDHVISTAEMYETRVNVRMKEALKKSLQGTRLDIITFTSPSTVQAFVKLAEEEWREELMSIPCVCIGPSTQAEAIKKGFNYTMIPEYYTVEGMIEVASAYFNKKG | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
A0A8H7NPL1 | MHLKYNVAQSLDGFIAPRDESTSWIVPDESIDFDALHESFDYYIMGRRTWDVMCTLEPNPCLKKTPGSVIVISRTLKQQDHPNITILRDGYIDVIQQLKKRHGKGIWLMGGGWLAAECLEAKLLDAVDVAVMPVLLGDGFKMVDGGLSGSCYKLELQSSERLCSSGILMTKYQVVYE | Function: Catalyzes an early step in riboflavin biosynthesis, the NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.
EC: 1.1.1.302
Catalytic Activity: 2,5-diamino-6-(1-D-ribitylamino)pyrim... |
C7MA29 | MSPAEERPQIAMIWAQARGGVIGAGGTMPWHLPEDLKHFSRTTTGSPVVMGRRTWESFPPKYRPLPGRTNIVITRDDELELPGAVRARSLPEALELAASVAGPGTTTWVIGGGAIYADAIGVAEQLVVTEIDLAVDGDTLAPRIPEDFTLAGADPAEGWHEGAGGLRYRILTYRR | 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... |
A0A8H7N8K0 | MDDFKFDHAWDMKGDYNWKTLIDNYNECYHCSVAHPGIAAMTDLKTYNVETVGGQVQHFAKDKPGMDSGLEVAPTFMFPNASITMTTKYFYLMRVVPVSPNETSMQYEVYRHKDATDEEFEEVDKFFKQVESEDKALCNAAQKNLNSGTYITGDLHSFNEKGVLHFQQHLKKILVAHHEKEEREGGEIWPARQRVIRNGLDEEIKFCEGLACGADGKKIDW | Pathway: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (monooxygenase route): step 1/1.
Function: Catalyzes the first step of the osmoprotectant glycine betaine synthesis.
EC: 1.14.15.7
Catalytic Activity: choline + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin... |
A0A4V2QDQ8 | MNGKNIVFIGMPGSGKSTLGVLLAKHLGMAFLDTDLIIQQREGRLLQSIIDQDGVVEFLQIEAAVVQQIRVADTVIATGGSVIYSAPAIEQLRRDSILVYLQLSYPAIEQRIQNMASRGIALAEGQQLVDLYHERIPLYEANADLTMPCDGLSVDELIFKISDLLKPLLASQDPTRP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
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