ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A1I7XVP4 | MLMECALFKTDYFCDSEERKYNSYGYPPISSNTVVFCNCHYNCIIYLRNTHLLGNNAAKRDEGYQWNAFSHGVTRCGFAVQFGIVLLAITGMLVWVEYFPSVDYLGVACMTFNIINFGAPLAGLGVVLRRRCCDTLPLPMCIVNLLVSSQWFLYGNIVHDPYVMAPNGIGMGLAVLQLSLFVIFPRKERGKSLLSRIIEQCISNKSEEEKGYDTNVEGFMPNNET | Function: Mediates sugar transport across membranes.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 225
Sequence Mass (Da): 25368
Location Topology: Multi-pass membrane protein
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A0A3B1E4W8 | MWLLNSEIFIDLITNSAINKRSYSRHNLPSWLATVTSWAQSVTVDYKIPKELARFCQSELIDKTSTGSVPQHEVFLAIDNLLRQSLTLRDLIISKAIIDVRQTIAKEKKQRGEIGFDDLLSNLDKALHAESGERLANTIRHRYPVVMVDEFQDTDPQQYRIFQRIYQGSNNYGLLFIGDPKQAIYAFRGADIFTYLQAKNQIESHYTLDINWRSSPNMVAAVNQLFSLAKNPFLFEQIPFKTVKSAYSNSNQHLAFVHKKATLSALNFYYLDKETVSILDYQQTMAYQCAHQICDWLKESENGKTWLYRDDVTRPVKTAD... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) s... |
A0A419DEA7 | MVSEKSSKKEEKKEKVNLEAGKVFTKEFIKTIVLITGLIIFIRFFVIQPFIVKGGSMEPNFHDNNYIFVNELSYRFTDPKRGDVVIFKHPEKECTEFVNKSFINRIFLQGPCTNFIKRVIGLPGETVVIKDGKVIIKNTGNPDGFTLSESYIPASDNFKLRGNISKTLGKDEYFVLGDNRQPNASLDSREWGALPENHITGKALIRVLPFNDFGFIRHPKY | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 221
Sequence Mass (Da): 25225
Location Topology: Single-pass type II membrane protein
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A0A7C6P3W8 | MFDVIIVAAGSSTRFGENKILLDIHSKPLIIHTIEIFKDLEDLKQIILVIKKEDQKEIEKILKEYDLDLVVTFGGKTRSESVVNGLKKVTSDYVLVHDGARCITLPSDVLKVLEEMKKHQAAFLMSFVSDSLYYEGKLIDRSKAYFSETPQGFKTEILKEAFSLMKKEYPDEVSLVQDVLNIEAKKIKSNNFNIKITEPKDYTFVMERFVKRNLIGESLDIHPFEFGKSLYIGGIKIPYHSGAKAHSDGDVLLHAISEAILGALGKGDLGSNFPDTDPKYKDISSIYFLERVKEILGKERTQIVNIDATIYLEAPQINSY... | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP... |
A0A089LVT4 | MRRQGITFKLFVMTVIFFLCFYGMVTLGQLLFFDGFYQHQKESRVEKHLKGFGASYTSEQWNGSRLSQELVRFMLRNKTQLAIVKLDGKMNSDDPYHMKLRTKDGRELVVSLSMFMSEYGDALRAADIKEEDSLTLEGELFEEEGSAQDLIYPVSITFGGRTIGMHEEGMTRLSGTVTEIVLPDLKLWNPRQGILLEALEEWFPLTSKQKADLEQLEMQKQEWTAPWSGIRNSVIILPVRQAGGEIELLFTVTSLQDVKDSNEALRWFFLYLGLGGFALILILSLFFSKMVTRPLIKLNNIAKRMVLLDFTGDNSIRQKD... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 582
Sequence Mass (Da): 66183
Location Topology: Multi-pass membrane protein
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A0A947DP98 | MIDLYGWSDALQTDFATYAARGLLPARVTAQHRGLWRIVSPLGEAAGRLTGRFLSTAAPGDHPVVGDWLAVDVNADNGDALIHAVLPRRTLFARRAAGGTGEIQNVAANVDVAFLVAALNGDLNLRRLERYLVAARDSGAMPVVVLTKCDLLDDPARAAEPVVAIAGGAPVVTLSANTGAGVEGLAPWLRAGVTVALLGSSGAGKSTLLNALAGRALMDTGAIRESDDRGRHTTTHRELFRLPEGALMVDTPGMRELGLLAVDKALDASFEDVTALFATCRFGNCTHVSEPGCAIQGAIAEGALSVARWRAYLKLQRELD... | Cofactor: Binds 1 zinc ion per subunit.
Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyz... |
A0A452XIB2 | MHQRKAEMGRQSDAFIALPGGYGTLEELLEVITWAQLRIHDKPVGLLNVDGYYNALLSFIDKAMEEGFIAPTARHIIVLGTTASELLDKLQEYSPRHGEMKGEVEQLSSRKNCDMDGLKEGSSQGPDAA | Function: Cytokinin-activating enzyme working in the direct activation pathway. Phosphoribohydrolase that converts inactive cytokinin nucleotides to the biologically active free-base forms.
EC: 3.2.2.n1
Catalytic Activity: 9-ribosyl-trans-zeatin 5'-phosphate + H2O = D-ribose 5-phosphate + trans-zeatin
Sequence Length: ... |
A0A947DS18 | MTSSATNPEASPLPMALTIARFAAAPIVAGLLLGGSQALFTEGRDLSLVLYALALVVFVLAALTDWLDGMLARKLNATSALGAALDHSADKALTTATLVILAATALPIDLIVAAAILVTRDVAVGGLREGLALSGRKLPVDSIGKVKTVVLMIGIGAAIAFQVAALTIPAGGGPFSPLDAIQWLTRAALWGAVVLALWSAAEYFGAAFKKT | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 211
Sequence Mass (Da): 21443
Location Topology: Multi-pass membrane protein
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A0A1F8V2R5 | MTVGRIFIFDENPGQIITVSGSDMHHIKNVLRMKLGDTIIVCNSQGNEYRTTITEMNSNIKLNVEEINKTNSELPVCVTLYQAFPKGDKMDIIIQKCTELGINRIVPVMSDRCVVKLDSKSVENKKARFIRIAESAAKQSGRSIIPEVTLPVTFGQAISEIKTANLGFVCYEGEVTTQLHNVLTGFKSTGFELNPFDKKSIAFFIGPEGGLSLDEADTAKNSGLIITGLGKRILRTETAPIFVMSAISFMFQ | 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... |
A0A419DCJ7 | MKKVEILTFPNPILRKKAKEVEKIDKKVESIIERMILALESSEIEGLAIAAPQIGESIRLILVRVREQRDKDGNIIQKEIPLTAYINPEITKFSKEKTIMEEGCLSYPNHYGPVERPKKIRFEATLINGKGVKKSASGILAKIIQHEVDHLDGILFIDKLTDKSKLKKVEPKNDEKSKKQP | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
A0A1F3VIJ0 | MRKKILIKFGGEIVENEKSLENLALSLAKLFADGHQIILVHGGGPLATALSKRLNIEPKMVGGRRVTCKETLEVMKMTLPGIINSNILAMLKKHKLPAVAVSAISFINASLRPPKRVSGSNNEVVDFGFVGDIKSVDPALINFYLEKKLIPVISPLCADDKGNILNINADTVATATAEALEVDSLVMVTQVGGIFEDIKNPSSKMTLLSMSEASKKIAEGIISGGMIPKVEECNKLFEKQLSAVHIVGVNSPDDIANEIAHPGSVGTTIVKK | 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... |
H9U9Z7 | MASKISEFTKGIIKENPTYVQVLGMCPTLATTTSAKNGFGMGLAATAVLVMSNIVISAIRKTVPEKIRIPIFITVIATFVTIVDLVMHAFTYDLWKTLGLFIPLIVVNCIIMGRAEAYASKHGVVDSLLDGLGMGVGFTLSLTLLGSIRELLGNGTIFDIEVWGKAFNMFVMILPPGAYLTLGLLAALFAAISINRQEKAKKKAQAQQAQQTQQIQQAQQKVGETK | 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: 226
Sequence Mass (Da): 24393
Location Topology: Multi-pass membrane protein
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A0A8J5IMR7 | MTEGVAGYDLAVNQSYHIPPYGQAMLNTGISIKVPKGTYARIAPRSSYAMRGMIIGGGVLDPDYRGEIKIFVYNYSDDDMDFAKGEKIAQFILECYRTPPIIQVHGFDKTKRQDKSFGSTSQQYPCTINRANPLCDGCPNCDDGTESATPYEYYVAPHPDYIDDREYIEYQPPKLGVAIQHTIDEDCQARIQARKALIHDETLDEPE | Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA... |
A0A7G6DZ51 | MEETGLTAHVYVDVVFLVNLIMDFFILWATGKIGKIRMKMVRIFLGALFGAFYSLVIFFPEWPALTSLLVKVLCSLVMVFIAFAPLPLGSFIRSLGYLYLVSFAMGGAVMGVIYLTNNSPGYVQAWNGAAVIIGNIHYSWLSVAIGMAIFLGVGGLSYVRKNWLQENLMSQIILTFGSDKVSLQALLDTGNQLVDPLTQKPVIVAEVKALHKLIPREVVNIVNSGEEIHLPELTSLIDPQWSSRLRIIPFNSVGRSNGLMLGFRPDAVEIRYHGKMRKTGDVIVGLVNKKLSNQGRYQALLHPELLE | Function: Probable aspartic protease that is responsible for the proteolytic cleavage of the RNA polymerase sigma E factor (SigE/spoIIGB) to yield the active peptide in the mother cell during sporulation. Responds to a signal from the forespore that is triggered by the extracellular signal protein SpoIIR.
EC: 3.4.23.-
... |
A0A8J5LP93 | MAELPPAMYSAIIRQHRNQFSLPWTEDVKVLGVLLSPFVIRVLIALRLKRVEYELVEVRFLEPNLPALTIALRVEMKATKVTKLASQFRQVLGLLEEAFTECGKGKGFFGGDAVGYLDIALGSGLGWIMAVEKGKSVKLLDAEELPRLAGWAKRFLVEESVKGLVPDGDEYLKFSAATTARTSSTPEDIMRSKLGFVGQEFP | Function: Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
EC: 2.5.1.18
Subcellular Location: Cytoplasm
Sequence Length: 202
Sequence Mass (Da): 22358
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A0A970IY97 | MDILNFEVLKKEENLTILEWLENFHLSNKTLRDIQANNLLKLNGEIVDFNTKISEYDIISIDISSFEENNFEPFSKELDILYEDEDVLAVNKPRNILVHPDGNTNQTLGNIISNYYLSQGLNRKVRVIQRLDYETTGVIIYPKHYLAHSFLDYELRNQNIKRIYLAICEGKISPRQDTIDKPIGKDRHHNNRYIVYEKGKEARTNYFSLQYKKNYTLVMLSLGTGRTHQIRVHLSHLGHPILGDELYGS | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 249
Sequence Mass (Da): 29128
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D5EGA4 | MLGQRNEDDIVDKKLNVAVLYGGDGPEREVSLKSGAAVVSALEEAGFKVVPFDITDLGQLSDLRKTGHIDSVFIALHGSWGEDGRVQSALDALRLPYSGSGSLACCLSMDKAATKGLLNLFGVPTPEGVLVLKGSSFSLEKARHFAERHHSVVVKPCNGGSTLGVTVVHNSQGLSDAFNEAWKYDSRCVIEKYIDGVDLAVTVWKQKGYLEALPEVMICPEKGFYDYDSKYTPGKTRYIVPAPFDPSIRSDIHQMACRAFEALSCEGYARVDFRVEEKGTPWVLEVNTAPGMTGTSLTPKAAAAAGYDFPAFLSHVVCLS... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 328
Sequence Mass (Da): 35... |
A0A378I406 | MVKILKFGGSSITTAERMKQAANIILNLRGEDQIILVVSALRNTTDKLLSCVSLAASGEDKYKEIYYYIARRHIETLEKLLDKPKDPAAYQALEQLLDDLDKILQSIKYLREQGPHALDLVASFGEQLSAIIFSAYLNQLKPACYVDARQFIKTDDRYTQAQILYEESSLAIRNYFENLFLRKGETVIPVVTGFIGMTETKHTTTLGRDGSNYTAATIGAALHARIIEIWSDVNGVYSADPKLIPTCVAHANLSYAEAEELSNFRVKVVRSAITPQVIAQTIPVLVKNTLQPEAQGTQISLHTKHYHIKNVSIIHELVLV... | 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: 467
Sequence Mass (Da): 51923
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A0A7G6E0U8 | MQNRRLAMSYLVKIVTLGCPKNTVDSEQILGQLFRHGHQPVDDPSKADVIVINTCGFIESAKRESIETILELAQQKIEGKCQYLIVTGCLVQKYADELKAELPEVDLFLGTGDIHLLPQLLASLKPGVRIAQVGDPDNYLFDDEIPLVPGHIKHYAYVKIAEGCNNCCTYCVIPSMRGKYRSRSLESIVHEVSKLTENGVKEAILVAQDITLYGYDKYGKYMLPALLQELVKLKNLQWIRLLYCYPNRLTDELLLTIKEEHKICRYLDIPLQHISDPVLKAMGRPMGKQDTIDLLKKIRKLLPGVTLRSTFIIGFPGESE... | 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 an aspartic acid residue of ribosomal protein uS12.
EC: 2.8.4.4
Catalytic Activity: [sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein uS1... |
U7UDH1 | MKLVLIRHGQSQWNKLNLFTGWKDVDLSEEGIEEAIRAGEKIKNENILFDIAFTSMLTRAIKTCNLVLEHSDQLYVPTFKTWRLNERHYGALQGLNKKETAEKYGDEQVHIWRRSYTTPPPALDKDDERSAHRDPRYRNVPQEIIPDFESLELTLKRTLPYWMDQIAPKIIEGKNVLVAAHGNSIRAITKHIENISDDQITSLEIATGQPIVYEMDKNLKIISKKIL | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
EC: 5.4.2.11
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 227
Sequence Mass (Da): 26291
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A0A3A6P4K1 | MPANSSPETGLIQPSEADWSQQALAQARQKIDEIDRSLQELLNQRAQQAQAIAQYKAAGDQPLFVPEREAQVLEALGQDNGGPLAAESLRHIFREIISACRQVQEPLRVAFLGPEHTFSHQAALSHFGRSCEYDPQESIAEVFAEVEANRSPLGVVPVENSSQGGVNETLDTLMTSRLNVCGEIYARVGHVLMSREAELAYVTRVHSHPQALHQCRGWLRRRLPQAELREAASTAAAALLAAQEPGGAAVGSALTAQHYQLNMLAADIQDSPLNTTRFLILGRRPCPPTGQDKTSLFFGLDHRPGALCRSLGHLARRGVN... | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
Function: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
EC... |
A0A1I7XG71 | MTIDSPEISLRDLRTEAFKFIQDTYPDSSCESLQDHILLYKHDLRSINILQLVTTSADITEGTLIEIVISSCPQHERLVVHPHTLYVHSYKAPTFCDFCGELLFGLVKQGLKCHVLVASKFLIHCTGCGLNYHKRCASKIPNNCNGSRQRRPSAIPLSPSRSPCGSMENLRMCSVPYDTDQSAGTNDERDDELSPRTHKKAQNTPSAPLQGSDGGFNGQTSPDDDMIHTESQEIPLNEVLDLKTMDHETLKTTPTHFFEIKTQDCTYYIGSMLLDTAYLAAYDLPLVHFSSQKKIHDSMLVVHDIEVPSTSRGQCSLKPD... | Catalytic Activity: ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]
EC: 2.7.11.13
Subcellular Location: Membrane
Sequence Length: 495
Sequence Mass (Da): 55303
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A0A453F3Q0 | DLVSCYRTDGIGLSAPQVGVNVQLMVFNPAGVKGEGEEIVLVNPVVYKFSKRLSVYEEGCLSFPGIYANVLRPDTVKIDAQDASGAKIKVKLSELSARVFQHEFDHLQGILFFD | Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
EC: 3.5.1.88
Subcellular Location: Plastid
Sequence Length: 114
Sequence Mass (Da): 12504
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A0A0T5ZTF4 | MNVEEVLVKGASELGVQLTSHQVTLFLEYLTKIKSWSEKINITGITDERGIVINHFLDSISTLAFISEYSKVLDIGSGGGFPGIPVKIVRPSLEMTLLDSVQKKVFFMRDVIRRLGLKEIKAIWGRAEDISNGIPRAYFDFVVTRAVGKVDEILKLCIPYLSEGGKIILMRGKKGVEEWKERKDKTTRNFRLVNSKMFSLPFSPHQRVILIIAPEQ | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 216
Sequence Mass (Da): 24423
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A0A1F7JIH2 | MQKDFNDGYSEHIPVLLDEVLDYLQVRPGKKYIDATFGFGGHSQAIIKKGGTVLGIERDEQTIREAKKRLHISKQEQKRLTIVHGSYEHIDTIAVREGFGTVHGILFDLGYSSWQLDKSGRGFRFTGNEPLDMRYEPNLQHRTAAEVINRNSREALTELIMTYAEEEQARRVADALVKNRPITTNTHLVSVLESVFGVHQRRNIARVFQAMRIAVNNELQVLTTALPKARSLLDVGGRLAVITFHSLEDRVVKRYMVRTESVEFSIVTKKPVTASYAETVRNSRAKSAKLRVAQKI | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.199
Subcellular Location: Cytoplasm
Sequence Length: 296
Seque... |
A0A1I0SQH2 | MSRIRVAGAVAELCGDEMAAVMWQMVTTELVHPFLEIEIDRYDLSLASRDRTHDRVTVAAGHAVLEHGVGVKCATITPTVAQADEYGLAERWRSPNATLRTMLGGTIFRSPIIMESIPRLVPGWREPIVIARHAFGDQYLAGEITVPGPGTVTLTYTPDDGSAPVERTVARFAEPDGGGVVLGQHNTTRSIEEFARATFRYALVVSYPVYLTTKNTVLATYDGHFTDVFARVFRTEFAAEFTERGLTYEHRLIDDMVAAALRWPGGYVWACKNYDGDVHSDVVAQGFGSPGLMSSVLLTPDGRTCLTEAAHGTVTRHYRR... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
EC: 1.1.1.42
Catalytic Activity: D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH
Sequence Length: 417
Sequence Mass (Da): 45869
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A0A7W0XXY4 | MRVTRSVAELSDVRDELTTGQPLPTVAFVPTMGALHAGHRSLFRIAKNIADIVVVSIFVNPLQFGPDEDYARYPRALDDDLAACRSDDVDIVFTPSVAELYPAGRQVSVSAGPLGTILEGRSRPGHFDGVLTIVSKLFHIVRPDKAVFGQKDAQQLACIRRMVADLNCDIDIVAAPTIREDDGLARSSRNRYLLAHERTSALALSSALRVAARHDTAAAALEGAGRVLALAEADPTFR | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
EC: 6.3.2.1
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Length: 238
Sequence Mass (Da): 25682
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A0A8J5HPN2 | MATAAAASSPAVFPLRSFARNGPSRDPRVSFNVSLIRSPRFTVSSRKQHRAVCCSWSSPEAGSCAPRKGIWSIRDDLVMPSTPYFLAEVQGGQGPPPAVQENFQSVVSQLFQHRIVRCGGQVDDDMATVLVAHLLYLDSVDPTKDIVMYINSPGGSVTAGMAIFDTMRHVRPDVSTVCVGLAASMGAFLLSAGTKGKRYSLPNARIMIHQPLGGAQGSQTDIEVQTNEMLHHKANLSGYLASHTGQSLEKIYQDTDRDYFMSAKEAKEYGLIDGVIMNPFKALPPRRRSIMENRDKALIAVGFEGSANKIGVGIVALDGS... | Cofactor: Binds 1 divalent metal cation per subunit.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu... |
A0A7G6E2A0 | MGDGDTIEHRKKGKMQIVNNQVLQYKSVEEGFQQSLSLLRATLESTADGILVVDRNRKIVSFNQKFLDMWQVPEYLVKDFPDNTQLLAYVSKQLKDPDAFYKKVMDMYQQPEIICFDLLERKDGRVYERYSIPQRIGEEIVGRVWSFRDVTEQKKVERALRESEERYRELVEYSPDSIVIHCEGRIVFANSAALKLLGAGAMDDIYGKPVLDFIHEDYKKLVLQRIGEVEQGKVVPILEEKLIRLDGKVLDCEILITPFQHQGKPAVLVIVRDITEQKQMEQELLKADRLEALRLLAGGIAHDFNNILTIILGNISLAKI... | Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporula... |
A0A847YMD1 | MTQSERQISGHTLLYAVIGDPVKHSLSPLLMNRAFAANQIDAVYVALTVKETAARLAMDMVRTFGLGGVNVTMPLKQAIIPWLDQLSPAAELVGAANCVINRDGVLIGHNTDCTGFRLSLANDFPQVPTAAFLMGAGGAARAIASELVRWGCRTLFITNRSRDKAEELAEILRSRGRTDIRVLDWRSPAWPAALATTKLLVNATSIGMGGVGNLAELLPWECLDQTTVIYETVYNPLETSFLRQARQCGFQVLRGTELLLWQAVAGFELWTGTTAPRDVMQESLLSTLNN | 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... |
A0A1F3V4J4 | MRSVYLPQLCPEGESVIITEREQLHHLSTVVRLRPCEKILALNGAGLKVFCTATSIEKNAITLTINSHEVVAPLSQLDLLLAPPKRPALEEIVRQSTELGIGNIFLLQSQFAQEVEIGEGKSRFLKIIESAMIQSNNPFFTKFEQTIPFADLEIFLKQAKYEKIFYFTSLASTAAFPSPALPLTKKDKTLFIIGPEGGFSTEEESYFSNNPQISKHHLNSYILKAQTAVVAAAGFLLGSQSNE | 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... |
H3NJ29 | MFSFIKNALSSRDVRRRILFTLFILAIFRLGSHIPVPGVNAKVLDKIATSGLLGLLNTFGGGALRRYSLFAIGVSPYITSSIIVQLLQMDIIPKFTEWAKQGEVGRRKLNQWTIYLAIVIGYIQSLGLSFGMNQMSGLGLIKNPTTATYMTIALVLTAGTMFLVWLGEQITRNGIGNGLSMLIMAGIVAQVPSEVTAFTKKMLIGAGDKFTQNALIGLGIVLALLIMTVIVVLMERAQRRIPIHHSKKVSGARHMAHLPLKINSAGVIPVIFASSFITTPQTLIGLFNPNPDGAAMQFISKLFNIQHPYGAILYTILLIA... | 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... |
Q0C7I8 | MDAGTADDRWKELVQIVPQRTEVLRFFQFYRQLAYPFNPILVDIDRFELDLCTYLNAYAAGVFEAHSRSEKWATDQSIAHISLLLATLSAGAHFSDLDLPQRSNISHDLGNTLQNHGQSDAAWAQLGTTVRLAQTMGLHTERSIAYLPLYIQSKAKALWLGIDVTTADRDAQETAFYVNMLNHVDEVYQRALPHLTSRANCKSMHEHLEHLALKMHLSLLIGVLTRPALKQPQTQDLSYGILRERAKTSMIDASRAFLDFQALSVIPLRTWSMVHTALTSTLLLSTWEETRNDPESRDLQQRVIELFSAVSSVGQPGDSA... | Function: Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for the ferulic acid decarboxylase FDC1. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.
Catalytic Activit... |
A0A7X6ZZ42 | MIDFEKLVLEKLNYQLSETQLNQFNDYYEFLVQYNENVNLTRITEKEEVYIKHFYDSIQITCEVQFGNQKVCDMGSGAGFPGIPIKILFPDLELTIVDASLKRLTFLNLLIKKLNLKNVVTIHARVEQYQNENPNYFDIVTARALSTLDNLVKWSFPILKTNGCLIAYKAKNFLEELELIEKKHHSKIASINVINQDLPDKQGERNNIIIKKA | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 213
Sequence Mass (Da): 24731
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A0A7X7UNZ7 | MIKKPKVLAFLIYYFVFTVLGIIFRGKINFIWMQLLFHFFCILIIILMLFKIRRKIFYVLSFLSSFVCFLFGTLFIIMICYGNSMAPNHYNKAILFFWQQDFKVERNDVVAVKYPENWDLDYQINFKRIIGVPGDEVRFEGNYILINGRKLWYWEGAYFGIIKGIEEGRIKEDYYYIKGDAHNSFDSNYIGLVHRSRILGKLLFIIHKGEKPAEEIPDLYKKPLLH | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 226
Sequence Mass (Da): 26993
Location Topology: Single-pass type II membrane protein
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A0A383WQC3 | MADDEQPVRFSGKGKANHEGSSSSTAAGALVPHPNTALQQPAGAQPIQQQQRPAVRQQVPDSILNNAALTAAMSVLPANYNFEIHKTVWRIQQAGASQVALQFPEGLLMYACAIADILQEFAGELACSSSSGSSISLFLHCLCAIADILQEFAGVEHCYVMGDVTYGACCIDDYSAAALGAQLLVHYGHSCLVPVDVTCIPCLYVFVDIQVDVDHLVDTIRLNFPPLPAGAAAGAQQQQQQQQQDPAGEQQQLQSLSLSTAANDSSQQQEPQEQQQQQQQQQASSQQQQQQQTQPQQLVLAGTIQFSSALQVTRQRLASE... | Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
EC: 2.5.1.108
Catalytic Activity: L-histidyl-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + H(+) + S-methyl-5'-thioadenosine
Sequence Length: 577
Sequence Mass (... |
A0A8I6RNE3 | MTRNVCPLFVICVISSLVQLGWGLDCYKCSTIYYEDCNDLQDISKAEVELCPQNGGQRNFCAKYTFSYDNKKMTQRSCATVDDCNLGLEMLKSMYSIDVLKSCDFCTGKLCNSATNVDVTVTYVVALLTTVCMLL | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excita... |
A0A650BVZ6 | PDYEVKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEAVIGEDNQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYRRAVYECLHGG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 170
Sequence Mass (Da): 18791
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A0A1V4QNB3 | MGLFSKRQYTSQTTRLMAYERRRRRARLVGRIFIGLFLVVLLAAAGLAGYVYYHFSQDLPDYTAIRDFRPHLITRVYAKDGRVIGEFYAERRIEVPYSRLPWHLVAAFVAAEDARFFEHPGVDFFGIVRAFIRNLQAGEIVQGGSTITQQIVKSILLTSEKSYSRKIREAILAYRIDNYLSKEQIINLYLNHIYLGHGAYGVEAAAQEYFGKHVEDLDLAEAALLAGLPKAPSRYSPYLNPLRAQERQVYVLNRMVEAGFIRPEEARQALNQPLTLKSRHHNRGNETGYYAEYVRQYLENKYGRNPLYQAGFRVYTPADV... | Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
EC: 2.4.1.129
Subcellular Location: Cell inner membrane
Sequence Length: 775
Sequence Mass (Da): 87521
Location Topology: Single-pass type II membrane protei... |
A0A0T5ZLH4 | MDHTLFKIRKLSLRVSEEAKSLVSDYLLGLDAMGVAEDVIEGEGFDVSAYFSIEMDLNPIMVSLKDYLLFLENNLLGFRAGNITIEEIDRTNWEVWKNELKTVRASGRIVIRPPWEEYLPKEGEHVIEINPSMAFGTGHHETTRLCIQAMEEIIENSKVKNVLDVGCGSGILAISAVKLGAYEAIGLDIDPVAVEEAKKNIARNSVSHKVKLLCGYLEGVKGKYDLIVANIFAEAILLMKKELYTRLKDKGVLLVSGIPVSRRDELISGLERAGFIFTRELKEGEWIAVVFCIDKNSN | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 298
Sequence Mass (Da): 33290
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D5ECU4 | MLEFTKIQGNGNDFIVIDNREGSMTSPDLSRLAASICERRQSVGADGLLVVEMSERENFTMRLFNNDGSEGEMCGNGARCIARYAWEKKIAGEKMSFETLAGPIHGVVTAPFVELDMGETNLSQGFWGQSLKVEGETFPFVYLVVGVPHCVLFVDNLEDFSHDSLRDIGRTVRYDTHRFPKGTNVNFVQRSGERTLKVVTYERGVEDLTLSCGTGSTASAIAASIVWEMAAPIQVQNPGGDNWVTVSFNETRSICKTYLTGKTVMIAEGRLYDEALPKDIE | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacte... |
A0A453C6R8 | MQYEGGAMEGGRGPSIWDNFTHQHPDKIADRSNGDVAVDSYHLYKEDVRLMKDMGMDAYRFSISWTRILPDGTLRGGVNREGVEYYNNLINELLSRGVQPFVTLFHWDSPQALEDKYGGFLNPNIINDYKDYAEVCFREFGDRVKHWITFNEPWAVSVAGYAMGVLAPGRCSPWEMGKCSAGDSASEPYTVSHHQLLAHAAAVKLYRKKYKVVQKGKIGITLVSAWFVPFSHSDSDSDAAKRAIDFMFGWFMDPLTRGDYPLSMRRMVRDRLPRFTKQQSKLVKGAFDFIGINYYTANYADNLPPSNGLKSYNTDARANL... | Catalytic Activity: DIBOA beta-D-glucoside + H2O = D-glucose + DIBOA
EC: 3.2.1.182
Subcellular Location: Plastid
Sequence Length: 346
Sequence Mass (Da): 39348
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A0A971EAH0 | MKIIGVTGGIASGKSTVTAYLRKQNIPVFDADASAHDAVRLGSPCLAKIHEIFGDEILMKTGELDRKALATLVFSNKEALKKLENIIHGYVWAKAQEFIAAQKKEKIIVLDVPLLIECGWYTSVDAVWLIKISEEEQIKRAIKRNNITEGEVRARIKAQMPFSEKQKYATTILDNSGSISSLEKQVSVALRTI | 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... |
A0A2T2XGG1 | MIDPRTRSGILDLVQNRGLGPYKPLGQHFLVNLAMIQRIVDLLPQGSRQAVEIGPGPGGLTLTLLEQDWRVVAIELDHRWVRFLSETWGKQFYGRLSVVEADALALNWAALPQQFGLAAPLTFIGNLPYYITGPLLAKFAGESVPWHTAVVMVQKEVADRLTTPPGSRQSNALGVILRYNATIEREFTIAPSHFYPVPEVDSAVIKLTHGTQLPVGFPEFHWVVHSGFTHRRKMLRQALAIGENSPYPAEQWESLMRGVGLNPTARAENLTIEEWVVLARLLPSQTR | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) +... |
A0A2G9XQB7 | MPKKYPIFFPTVFLVVALDQLAKSYITAGMLLHESFTVVEGFLNITYVRNPGAAFGFLAHASPMLRFAFFMAITVLTSGFILYYVVKSDGEEPRLIFALSLILGGAMGNLVDRLRFGEVVDFIDVYFKTYHWPAFNIADSAISIGTFFMVLEILQRRKESDGQV | 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-, ... |
A0A8J5IGU2 | MERNLSSLFNAKIVDHENGVRVYEPSGSASVTPMSQGVTGWSSSVTHQFHAVAGSGGGGVYPGNSSGESFKRKRGRPRKYGTDGTPVLGVSPLSTSPAAPPPSTGIFSPATHVAATVAAEGAKRARGRPRGSTNKRPIKALGKLLAGSTGTGFMPHVIAVETGEVSPVCFVELELVLTAIESTESNY | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Subcellular Location: Nucleus
Sequence Length: 187
Domain: The PPC domain mediates interactions between AHL proteins.
Sequence Mass (Da): 19293
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A0A933Z547 | MADKKSNPAPSKAAAVKPGAKAVALPGKATKAAVKDEPSKGLGYWVEQGVQFLREVKTELKKVTWPPRKQTVASTGVVLGLVAIISLFLGLVDYVLTHFVRFLIS | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 105
Sequence Mass (Da): 11230
Location Topology: Single-pass membrane protein
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A0A7X8X071 | MENYLIGKIMNTHGVKGELLVKPLTDFDRFVKDKEVFTLEPFIKFKIKKVRHHNKGLLVSFYDYDNINLVVNLKGLLLYTNEKPTLLEDEYHFNELIGLEVYNQDNILRGIVKEVIEVPQGHLLRIEVGETLKLVPFNKQFVKEVKDNHLIINEIEGLL | 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 ... |
A5WCA8 | MPASTLATTTTTTTTIPASSPSSCRHLETDAYPRHACATRPIQIYLGGSFDPVHNSHLAVLAHVYQHLHIAKPSSKLSAYFMPTSRSPLKDNSSRPEHRMAMLQLAIDEMTAAKAQTAISPADFGICDHEIWQTPPTYSIDTLRALRQANPEASLVFVIGADNVQSLPQWRDGDRLIEFAHLWVIPRDHLQTHQHIANLLPNKLKSALTEHIEDLKYAAKGHIYIDSHRVDPISSSAIRQAITEGSFDIAKSALPRSVYSYIMKNNLYHSY | 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... |
A0A453LK85 | ARRYLGIWYNGMSGPRTVVWVGNREAPAAGSPTLALANDSSLVVSDADGRVLWRTPGSGGSSSSSSSPPPALLTNEGNLVVRSPNGTVVWQSFDHPTDTFVPGMKVRLSHLTGEGNRIVSWKSPGDPAAGSFSYGLDPGTSLQLLMWNGTRPYWRTPVWKGYAVASMYLSAGTVLYTAIVDTEEEISIAFTLSGGAAPTRYVVTSSGRFQLLSWNSTVSAWATLLSWPSSGCSTYKRCGAYGYCDVTAAPAACRCLDGFEPASPTEWGAGRFEQGCRRKEALPPCGGGMGVGFVAMPTMKVPDKFSLDAGNRSAEECAAR... | Function: Involved in sporophytic self-incompatibility system (the inability of flowering plants to achieve self-fertilization).
Subcellular Location: Membrane
Sequence Length: 417
Sequence Mass (Da): 44256
Location Topology: Single-pass type I membrane protein
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A0A847YLV7 | MKAIEGRLQLSGRGFGFLIPSDPDEPDIYIPRANMNDAMHGDQVLVRLTERAELYGRKPEGWVVKIIERANARIVGTYDNRHGISVMHPADVKIAADILVPKKFSAGARAGDQIIVEITRWPNAGAPAEGRIVEILGHTGEVGVDVLTIMAAHQLPRDFPPKVAHAAERVPTTITPDEIHGRRDLRELPIVTIDSEDAKDLDDAVHVEQLANGQFRLGVHIADVSHYVTENSPLDLEARQRGTSVYLVDRVIPMLPHRLSNGICSLNQGEDRLTLSVSMDIDQDGRVKRYEIYSSVIRVRTRLSYRIVRRILAEADAELR... | Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.13.1
Subcellular Location: Cytoplasm
Sequence Length: 698
Sequence Mass (Da): 788... |
A0A9D0ZVE4 | MTKQNKGLKGILGVLVLAAAILFLLNYVVQPTEVEGLSMYPTLSGGEYLLLDKVSYRFRSPRRYELVVFPSRYQEDTYYIKRVIALPGETVEIRDGTVYIDGEPLEENYGYEPIEDAGLAGEAFVLGTDEYFVLGDNRNDSMDSRFAEIGNVTAQEIVGRAFFRIWPFEKAGAL | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Cell membrane
Sequence Length: 174
Sequence Mass (Da): 19582
Location Topology: Single-pass type II membrane protein
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A0A9D1XER4 | MSDKYLNVAFIGNPNCGKTTLFNAYTGANLKVANWPGVTVEKVEGSFKFQDYKMKLVDLPGTYSLTSYTMEEKVSREYILSDAVDVIIDVADASALERNLYLTLQLIELGKPVVLALNMMDIVEKRGMEIDLHRLPEMLGIPVVPVSARKRRGLDILMHAAVHHQDPSEKTPVIHHHGNRQSRHPHDHHREFAMVYSDEIEDKIDVIKDRLKEKYPDMFNHRWHALKILEGDEEITKKYPIELPEGFVCNYEQQIINEKYDFIEEIMDEVVVHREEKAAATDRVDAILTNQWLGLPIFLVIMGVVFFLTFTIGDWLKDYM... | Function: Probable transporter of a GTP-driven Fe(2+) uptake system.
Subcellular Location: Cell membrane
Sequence Length: 527
Sequence Mass (Da): 59405
Location Topology: Multi-pass membrane protein
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A0A0E3ZHI9 | MAKTLFDKIWDNHVVRSLPGGQDVFYIDRHLIHEVTSPQAFDELGRRELPLFRKNQIVATADHNVPTRNQHLPIEEPLSRSQVDKLTENCSKYGVELFGLGHEHQGIVHVIGPELGITQPGMTMVCGDSHTSTHGAFGTIAFGIGTSQVAQVMASQCLLLSRPKRMRINVTGSLRKGVSAKDMILYIIAQLGTGGATGYFVEYAGQAVSELSMEGRMTVCNMSIEMGARGGLVAPDQTTLNYLKGRKYAPKGEQWEKAVAYWSTLYSDKNATFDVEYTFKAEDMTPMITYGTNPAMGMAVQEAIPVSTAEVDEQGMLKSL... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
EC: 4.2.1.33
Catalytic Activity: (2R... |
A0A7X7UPL6 | MKILVTNDDSIRSKGLWELVRLSKKYGEVKVLAPAREQSGKSHGINIRSGLKLEKFDLGDVEAYSLDSTPADCVRAARFGFGWDFDIVFSGINRGLNLGEDILYSGTCAAATEAALLGKKGLAFSTVWHTFDTIVSEFDAIMEFILSEGLLEKGDLYNVNVPEETKGIKLTFQGNNHYDTRFDLSPKGFFFQKGKHHREREENVGSDVWAIHNGYISVTPLNFDRTDYGLLRKLNS | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
EC: 3.1.3.5
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 236
Sequence Mass (Da): 26408
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A0A8J5LIM3 | MLGLRFPRPKRSPWELLRSALFSCALVLISQFALASVPWLFPSISLLAMLPIAALVMAVTILLGRFWRRLFDVSASAPALVLFNLLFMWGVYITVIRKAVPSLLDAVLNAECALLLYGLYRIFSSDPGAVSFSSSTVESGQNEFDTLNVQFENSPTLSRVRYCKNCKTGIKGFDHHCPAFGNCIGHKNHRLFIILLAGFLIAESSYTMSSTKFLTKSADAQRMEVSSA | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 228
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 25237
Location Topology: Multi-pass membrane protein
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A0A8J5GDV0 | MLLHFLCPFSFCASTLTSFSILRKINSLTCQNCFCVCVFSNFSINLYPCVIIIYLISDCLVLFLDALGTMLATHLDKHRAYIGCMKSGEVFSDKNQMWFEPEWWKFGDGKLYFQHASGEMFVVSRALAQFVSINRFVFLFQVMS | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 144
Sequence Mass (Da): 16596
Location Topology: Single-pass type II membrane protein
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H3NIR1 | MKIILLYGGKSAEHEISLLSAHSILQAIMYSVYTVQPIYITKDGRWIKGEVLDQPSLGDQQLILRSSDQMGWSDANTPSQGIEIAPGAIQEKDAIVFPVLHGPNGEDGTIQGFLEVLDMPYVGAGITASATGMDKIITKALFNQAGIPQVPYVAFTDSEWKLQQEALIQKVEGTLLYPLFVKPANMGSSVGISKVQDKKCLIEAVTEALKFDRRIVVEQGIQAEECEVAVLGNADIHVSTVGHLVKKQDFYDYNEKYVNNTIEMEIPAHLPENVIDQIQNYAKRAYLAIDGAGLARADFFVTSNYDIYINELNTMPGFTQ... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 362
Sequence Mass (Da): 40... |
A0A8X6J2H0 | MNAQFKTTRKCLLAAFFLLGCVASPVRSEENFTDLHGPIKCREGLLLPIWLPQENLSDGDRVARGIVYFVALAYLFVGVSIVADRFMASIEVITSKEKEVVIKKPNGETQTISVRIWNETVSNLTLMALGSSAPEILLSIIEVYAQDFDAGELGPGTIVGSAAFNMFVIIAICVWSVPSTENRRIKHLRVFFVTMTWSVFAYIWLYLILTMSSPGVIDVWEGLVTFMFFPATVLTAYIADRQFLIYKYMTKKYRMNKRNMIVGGEGGEDVEMGMTKTNHIVDGNVKNYEEEPSDDIREFEEHRMQYIQILRELRRKHPDA... | Catalytic Activity: Ca(2+)(in) + 3 Na(+)(out) = Ca(2+)(out) + 3 Na(+)(in)
Subcellular Location: Cell membrane
Sequence Length: 926
Sequence Mass (Da): 103962
Location Topology: Multi-pass membrane protein
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A0A420WKZ6 | MKHYPVMLPEVLDALDIRAGETYVDGTFGNGGYSEAFLRGGDCHVVGLDRDPNVAPRAAALSAQYAGRFRLIETPFSKLDSVGLPPVEAVVLDIGVSSMQLDEGERGFSFMRDGPLDMRMSQNGPSAADAVRLLSQVELEQIFRVYGEEARARHAAKMIIEAREVSPITTTAQLADILEKALGRRGKTHPATKVFQALRIYINDELGELCQALVAAEHQLAPQGRLIIVTFHSLEDKIVKAFFRERAGEVEGGSRYAPVVERTGPEASFALPKRSVTKPSKAEVAENARSRSAKMRVAIRTAAPAWPESARRALRVPSLS... | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.199
Subcellular Location: Cytoplasm
Sequence Length: 326
Seque... |
A0A1H8UKP6 | MDTLRWILLAVGVLVIAGLFGYYKWQERQGSKGRRSTSKSAGVRRSVRGDRDVEAALRDMDDFLLDDGIDEAADLPDLEAEPDDAPVGRARVRTSHHETVDNDSSVGPVRVRSVADDVGAADFSDALDEEPADAWNDDFEPEYDEAPDAYEDESDHEREEGGWNLGPVRIPRPSWVKDAGWLGGDHGSRADSDAQEDDQASYEDAVAQAVGEKIIVLHVHAGEGMCFTADGVSDALEQVGLRLGQHEIFHRHVETRRGEEPMFSVASMVKPGTLDPSQPETLETPGLALFMQLPGPFDGLSGFEQMLETARRLADQLDGH... | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 3... |
A0A1H9LRU8 | MKRELIFLGIKISAIVFVLVLVFTFVFGIARCSDNMMSPACKDGDIIFFYRLRKNYEENELVIVNKDDKVQIRRIIGRPGDIIEITDAGLIINGYQQQELEIFKQTQPYLDGIKFPLELKNDEYFVLADNREGAKDSRIYGPIKEQEVKGSAMILIRRRGL | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Cell membrane
Sequence Length: 161
Sequence Mass (Da): 18595
Location Topology: Single-pass type II membrane protein
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A0A520JYU1 | MHILVYGAGAIGSLVGALLSKEHEVILLGRKEHMQAIRKDGLRVTGLTRMHIYLETTTTLGEVNGKIDLVILTVKSYDTHSAANELAKNLKPSQLLSIQNGLNNANILERYLGKTRLVFGTTSQGVTFVKPGEVRHAGLGRTVVGCMRNEDFETATQVCDLLSSCGLKTELTDNIIGEIWAKAIVNACINPLTVILRCENGRLLGLPEVMSVMKKCSDECEAVAKAKGIMLPTPDMYRYTVDVASQTASNHSSMLQDIEKGKPTEINGITGVIVSAGKKFKVQTPVNFTLLQLVKGIEALNKKVHNAFDCNQSATNVKSY... | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NAD(+) = 2-dehydropantoate + H(+) + NADH
Sequence Length: 322
Sequence Mass (Da): 34989
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A0A8I6RJS8 | MKFIFKNVPMSSARHGVLSSFSKFPEKIFETPLLLVSTKGGSVPHITHEVLQLITKDSHIMQFPLPSTMLSHETVKEYAKGLAHFCGLKDYLTYCTVQDPSCLTPVGYNKTTVVSVWTNIGRVSVNAEKYMKTMEAFQPDMYQILANTDTNLDSTRKKALKTLRSCQIIFDECIKRHQESEKLKNSGVIGVISGGIDLDVRKDHVKYMLEKPVSGFSIEGLHNNGADVEKMDYEKCNMVLEEILNILPEDKLRIVPGCWKPQQVLKMVELGVDMFDSSFPFIVTERMCALTFSWKSIPLDVSEVPSQNVEEEINLRDIRY... | Cofactor: Binds 1 zinc ion per subunit.
Function: Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hype... |
A0A970IYU3 | MNGVSLKGFKFKIISLIISSVIIIFFQRFRRFNFDFLKRTYVLIIVALTLILIITSVLVLLYVPDLNYKVKKLLYNTLDFFQTLTFALVLFLCIFTFWFFPATVQGRSMMPTLVENNRVLISVGNKKLSRFDIVVIDATELLEVHSEDDLIIKRIIGLPGDNFYYQDGKLYLYVDGIPTLIEEPYLVDEEGNFLKNGILYDTETEDFTLSDFCIIGSNLDNQCEINGEIKIPGDYFFVMGDNRGRNKSVDSRTFGLIHRSKIVGKAKYIRQGLFKWKKLK | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 280
Sequence Mass (Da): 32421
Location Topology: Single-pass type II membrane protein
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A0A8J5HHJ0 | MQYIHLGVLQVRIQILHRQHEGTMALIVFRDNWWQGDQAILATMEVDLTRGSQMIYVIPEVMMTIGDFYRNIQISILARGYEARQNSEANLLITRGMVGRLSNTPNVGFAYEVQGVVDYLTSHGVNALPGRKFSTNNLQGLNWVINPTQVSIPMQPSEVNSQTMMDGRISVSFSSYAAARPTEQPTFNNKDEEVYETLAVLIETKPGVFTNYDAKPRSPEEKQARETSSERYSSITEPHILINKISPDTVTPTRHTEGSAVLDIAASHAAVIEPYGRDLIHTGLQIEIPYGYYGRLASRSGLAWKTGIEVGAGVIDSDYR... | Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA... |
A0A2M7Y1N5 | MKIKTFRAKTFGEALALVKREMGEDAVVLSTEEKKGPRPSVEVSAAVDYEAGEAASPKAAIPSWATPIPSPAVPPPPVREQEEIRQLKNTLIEFKTEVGSIRELIEDTRTEAKTARLPAGKRDVLRFLKKRGVREEHARGICDTANNVKEIPRAMAAGVAVRGGGMGGKKAIVLIGPTGVGKTTTVAKLAAAAIKARKRVAIVSLDSYRIGAIEQVRIYAKIMGVPLEVVPDAGRVKACLARHADKDVVFIDTTGRNPLGDAVLSELAPLYESGVPVETHLLVSATSDYDFLDRAWKSYGRLPVDCVGVTKVDEAVRYGA... | Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 372
Sequence Mass (Da): 39887
Location Topology: Peripheral membrane protein
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A0A2M7GUS2 | MNIRPLMRLNLSSALAILGFAAVLVVADGARAQDAQALSQRLERLERDIQTLSKMVVRGPGAVPAAEVPAAARPAEPMPNLPQNAVARIGVRLDTLENELRDVTGRIEQLTYNIDQLTARVDRLVADVDFRLSGLEQQSRPMGQTPGAAGPQQANAAPGPADVRIVGAPPRSLGQIEADRVESGQSPAKPAAGSSKPSGAGTAVESAPVQPQAEAAAVPQASTTPGPALPDGTAEEQYQFAFGLLRKHQFDQAETAFKEFLSKHEGGALASNARYWLGETHYARAEYVKAAEVFLQGFEKDPKGGKAPDSLLKLAMSLGQ... | Function: Mediates coordination of peptidoglycan synthesis and outer membrane constriction during cell division.
Subcellular Location: Membrane
Sequence Length: 360
Sequence Mass (Da): 38260
Location Topology: Peripheral membrane protein
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A0A453C754 | MKDMGMDAYRFSISWTRILPDGTLKGGVNREGIKYYNNLIDELLSKGVQPFVTLFHWDSPQGLEDKYGGFLSPNIINDYKDYAEVCFREFGDRVKHWITFNEPWSFCVTGYERGVFAPGRCSPWEKANCSAGDSGREPYTAAHHQILAHAAAARLYKQKYKAEQKGKIGISLVSNWFLDPLARGDYPESMKELVGNRLPQFTKKQSELVKDSFDFIGINYYTTNYAGSLPLSNGLRNSYSTDARVRNGVPIGPQAASPWLYVYPKGFRDLLLYLKEKYRNPIVYITENGVDEANNKSLPLEEALKDDARIEYHHMHLDAL... | Catalytic Activity: DIBOA beta-D-glucoside + H2O = D-glucose + DIBOA
EC: 3.2.1.182
Subcellular Location: Plastid
Sequence Length: 380
Sequence Mass (Da): 43681
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A0A7X7C5F6 | IVTISALKGTGIDDLISVIIKGFGKEDKPKIFSEDIEAKLGEIIEDKKHSRFLSVKLLERDLLVRNLESPELDATIRSLEVSYQSSLEEVIANKRYEWIDKVKAEAVIQKTRKVNWTDRLDKIFLNKYLGIPIFVIIMFLVYFLSVGLVGGATVSLIDNGVERLAHVTDRWLTDLGASSWSRSLLIDGVLSGVGAVLNFIPQLMMLFLCIALLETSGYMSRISFLLDKLLRRFGLSGKALVPFIVGSGCSVPGIMTTRTVEDSREREMLLTLTPFIPCSAKLPIIAFMAGFFFESYLGLITASLYFLSIIIILFSAVLMK... | Function: Probable transporter of a GTP-driven Fe(2+) uptake system.
Subcellular Location: Cell inner membrane
Sequence Length: 522
Sequence Mass (Da): 58148
Location Topology: Multi-pass membrane protein
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A0A0E3ZEY3 | MSGEDIASFIDHTLLRPDATVEQVHQLCDEARSYGFAAVCVPPCYVQEANTRLGVGAQVKIATVVGFPLGYHHHKVKFLETHQAIEDGATEIDVVMNISYFKSGRYKEVENELSDLAKFCHMKEAELKVIIETALLTEDEIVKACSICTSAGADYVKTSTGFAAKGATVEHIKLMRRVLPSRMKIKASGGIRTAPEAEALIRAGADRLGCSASIQIVTYEQNS | Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Ca... |
A0A1F8UYY7 | MLYPSIQQLTEGKINRYALVMGTAKCARHVTDEIIREKEFAATSMVKESKSDITSDTMNEKAVTIAIRRISQGKYKIKMSE | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 81
Sequence Mass (Da): 9185
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A0A8X6LI40 | MTLATCSKDCIPSARVVLLKEYSKEGFVFFTSVNSQKGKELTENPKAALVFHWIEFSRQVRIEGEVKLLNSKKADEYFSSRALGSQISAWCSKQSSVLKNWQDFEQAIKLKEKEFYNTQVPRPNFWVGFCVIPKVIEFWQEGEYRRHTRFRYTLIEESNWKVEQLYP | Pathway: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
EC: 1.4.3.5
Sequence Length: 167
Sequence Mass (D... |
A0A453SCS7 | NDYAAYAETCFKAFGDRVKRWITFNEPHTVAVQGYDSGIHAPGRCSVLRHLCCKQGSSGTEPYIVAHNIILAHATVSDIYRKKYKAEQNGEVGMSLDVIWYEPVSNSTANVEAAKRAQEFQLGWFADPFFFGDYPATMRSRVGERLPRFMTKEAHLVKGSLDFVGINHYTTFYTKEDHSTVIKYLLNDTLADSGSVSLPFRNGKAIGDKANSIWLYIVPGSMRRLMNYVKDRYNTPTVYITENGMDDSNSPFISLKKALKDSKRINYHNDYLTNLADSIRC | Catalytic Activity: DIBOA beta-D-glucoside + H2O = D-glucose + DIBOA
EC: 3.2.1.182
Subcellular Location: Plastid
Sequence Length: 281
Sequence Mass (Da): 31833
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A0A969TZF3 | MGETKFLLSTYESHDLNCPLHLLCALSTIFLVGCGGAVTSREDRSTQAAVDAAVAPENRAIAIFAGGCFWCMEKPFDVVPGILSTTSGYSGGIVDNPSYESVTRGITGHYEVVQVEYDKTRVTYQQLLDIYWRQIDPFDARGQFCDKGQSYLAAIFPKTPEEAAAAQASKAAVERKFPGQTITVNILPAKRFWPAEDYHQDYYLKNPLQYGYYRTACGRDNRLRTIWGPPVR | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
EC: 1.8.4.11
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionin... |
A0A174BZE7 | MEVYIDIYIFENIVINLFLLLLTFKLLRFSFNKKNICIAAVLGGLYGLVIFCNVNLLNSIAFKLLIPAIMIYISLESKKFKYVLKSILVFFMLAFMLGGICFGALQMQNTYMIGQAFVVENNSIKYIVLSVAIVFIFINRIVDLLKDRALVKNFLYDIYITEGTRTVLVKGFLDTGNELREPVTNLPCVIVENNYFNQFDIPDDKKFIIKYDTINEVGEVKGFKGNIMIKNEDSNSWTRVDAIVCGCERKLSKEDEFQALLSRGIV | Function: Probable aspartic protease that is responsible for the proteolytic cleavage of the RNA polymerase sigma E factor (SigE/spoIIGB) to yield the active peptide in the mother cell during sporulation. Responds to a signal from the forespore that is triggered by the extracellular signal protein SpoIIR.
EC: 3.4.23.-
... |
A0A970LKS4 | MRIFIGVALPEKIKEKLYELQRCWLDTAIRKRPTLFNNFHLTIKYIGELSLEEVELLTYSLEKQLANFKSFEAKIANIGAFNKGSGQIIWVGFTAGNDLLNALNKEVVKAIKAIKIELKKERYTPHITLARNVYFNDYKADLPLVNETIEINKVTVFQSHRIKGELTYTPLYEIDLQ | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 177
Sequence Mass (Da): 20479
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A0A9D5JM41 | GPAPPKVKICGLTRTGDVEVAVHFGADYVGFVVEAESQRRLGVDEAARISRPARGMASIVAVTVNAGDALISSIFDRIQPDYIQLHGDESPDRVRFVSRNFGAKTIKAIAVNTRAHVEAARAFEDVTDIIVFDARPPKPDRNTDAKGGHGLSFDWDIVECNEMRQTWALAGGLTPENVTEAVHRTSAPILDVSSGVEYEPGKKDPAKIRRFITQAKQQKLDPAI | 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: 224
Sequence Mass (Da): 24342
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A0A383VZN7 | MMGPLGAMRALSGAVAKCFMLAQQQHSNSSQRVLLPCISSLVRQAHTAQIKPVTEKEQAALSKIRNIGISAHIDSGKTTTTERILFYTGKIKDIHEVRGKDGVGAKMDSMELEREKGITIQSAATYCTWKDKQINIIDTPGHVDFTIEVERALRVLDGAVLLLCGVGGVQSQSITVDRQMRRYSVPRVVFVNKLDRVGANPWKVIQQARDKLKLNAGAVQIPIGVEEFHEGVVDIVKRRAITFGGAKGLDVVEGPVPADLAEEVEARRAELIERVSEVDDQLAEQFLLEEPIEAEQLAAAIRRATLANKFAPVFMGSAYK... | Pathway: Protein biosynthesis; polypeptide chain elongation.
Function: Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed ... |
A0A1X1Q7E2 | MQGLFGGYMKIIVGITGASGSIYGLRLIEVLKDAGHQVHVVLTDSGNKVVRFECPELYERILASADMLHDVHNVGASIASGSFRADAMVVVPASMKTVACIATGVTDNLLTRAADVILKEGRRLIVVPRETPMHAGHLENLLKMSRLGAMVIPASPGFYHQPKTLMDLVDMLVGKICDSLNVENNLFKHWDGNM | 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.... |
A0A2X0V670 | MDRTEIKVLEFDEELAKKLFYIDCLCHTHPWTYDGIKESFNDNSKVIGIYHDKELIGFSVISLLFDECELFTIGIVPAMQGRGFGSKLLAFSLSLAYSLGGRRCFLEVRVSNEKAIALYKAYNFEIMGVRRGYYSAYKGQKAEDAYTMSCEIKP | Function: Acetylates the N-terminal alanine of ribosomal protein bS18.
Catalytic Activity: acetyl-CoA + N-terminal L-alanyl-[ribosomal protein bS18] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[ribosomal protein bS18]
EC: 2.3.1.266
Subcellular Location: Cytoplasm
Sequence Length: 154
Sequence Mass (Da): 17602
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T0JC49 | MKDDKNLIGIIDYGGSNLKSVFNAFNKLNIVCEICDDYSKLDKYDKLILPGVGAFELASKQLKANGFFNKIIDKVNSGTPILGICLGMQLLLNSSEEYGYSKGMGLIDGEVKSFKNIGVNPHIHMGWNDIKITNNSNILGEGNETYYFVHGYYCDIKEQEFVAAKVHHGLSFDVAYERNNIFAVQFHPEKSQKNGLSLLKKFANL | 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... |
A0A8H5LKR2 | MAATSKFQWLLCCILLSFQTSLGAVVFHNVDDLPQDTQYDFIVAGGGTGGSLVATRLAENPNWKVLVIEAGGSNEDFWQTRVPAFWPMLWKTPMDWNYTTVPQPGLNNRAVDYPRGKVLGGCSSHNAMIYTRGAKSEWDRYAELGGNDGLKWDNVLPLLMKAEKWSQAPGGLSDAGHYDPAFHGTHGELAVSAPYSEHPFNDMLMQSSQELSDEFPFNQDWNDGTPVGTAWDEFTIDAHGQRSNAATAFLSQTGNNVHVLLSTYVTRVVPATSGGTDFRVVEVGTEAGGELKQIVAHKEVIVSGGIFGTPQILLHSGIGN... | Function: Catalyzes the single-oxidation or sequential double oxidation reaction of carbohydrates primarily at carbon-2 and/or carbon-3 with the concomitant reduction of the flavin. The enzyme exhibits a broad sugar substrate specificity, oxidizing different aldopyranoses to the corresponding C-1, C-2, C-3 or C-1,2, C-... |
A0A2M8GHD9 | MSTEDCFMSQPIQKMFTEVPQTYRLLNHLLTLGQDIVWRRRAAEIAASGGGTRWLDACGGTGEMATCLSHLATDGTSIVVADFSPPMMSKAMEKPEAKGIAFTLADVSRLPFRDNSFDVITISFATRNLNISQDNLLKCLREFHRVLKPSKRFVNLETSQPRFAPIRWMFHLYVRATVSPIGRLVSSSDTAYTYLSHSMRHFYSPEELAEIIRQAGFCEVSFNRMLFGAVAIHKAIKREGS | 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... |
A0A7V6GNW8 | MRIVFMGTPDFSVPILKNLIKHYEVILVVTQPDKPVGRKRVLTASPVKDVAIEHGIEVFQPIKIRNDFQKIIDLKPDYIVTAAYGQILPRGLIDNVHSINIHASLLPLYRGGAPIQKSIMNLDKETGISIMKMEYKMDSGDVYYQESIPIKDVDTTTSLTKKLSILGSEMILEYLNNPKKYPPVSQDESKATFAYNITFDDQIINWNQKSSVIEAHIRAMQDEPGAITYIGDHILKIYEARKSDIISNGTPGVVTNLDKKLLISTADYDLEILKLQPAGKRAMLTKDFLNGQTILKLYDKLGKEVLL | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A964GDU3 | ASRVQAVLLDDEVGALMVLFPQSHLLDLNRLAAPTGRAAERMAESLRNAVQQLPRLGVDAALCAQLPTTGTTLHRLLGVIPDSPRFRHHADNPLAYDTIVVDEASMIDLPLMAKLVEAVASGTRLVLLGDPDQLPSVEAGDVLGAILRAAGDGTRIAPDDAQALQGLLGALPAASIAPPATGFAGTRVQLQRGYRQSEALQLAPLAAAMRGGDAARALSLLRDAQLPGVHFHENEDDPLQTWREPLQRYWEALAAAQTPAQALALAGRLRLLTAVREGPQGARGLNARIEELLGGTTPRGGAPAHFHGRLLLVTENSYRH... | Function: A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA ... |
A0A419DB13 | MKKTKIIATLGPSSDDPKIMEKLIDAGANVFRINFSHATQEEKDHRIKSLREIEKRRKRPIAILQDLQGPKIRVGVIAEGIELKTGEEIVMTVSGVNKGEIPVQYKGIVGDVNVGDKILLADGRFELKVLSKRHPKIKCKVITGGFLTSKKGINLPTSSISLPALSAKDKEDVAYGLANDVDYIALSFVKSRKDILDLKKIIKKAGKDTKVIAKIERHEAVDNIDEIIEEADAVMVARGDLGIEVSLADVPLLQKDIIKKCNARGKPVIVATQMLDSMVRNPISTRAETSDIANAILDGADAVMLSDETSVGKYPVNAVK... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 467
Sequence Mass (Da): 50904
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A0A8T8I764 | MKFIKNVIAEMKAVTWPKFSGLVRTTGLVVLSIALLAIFFGTIDTGIGALIRSLLSL | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 57
Sequence Mass (Da): 6137
Location Topology: Single-pass membrane protein
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A0A432R3W4 | EAEDGRKPVFLLPVASTLSQEEVLASGVNEFAGNLDLKLITENRYDMMAACDAALAVSGTVTLELALLDTPMVVFYKVSQTTYRLGRLFLNKDLKYFSLVNLVADDSVVAELSQENVTAANLYKELSPLLSDSRKRREMLQGLALVRARMGTAGASQKSASLALSLLD | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.4.1.182
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydrox... |
A0A5C0B0G2 | MRAWFWTFILVVAAVGLAIAVRDYSGNVALLVPPYRVEVSLTLAVLFLVVLFAATYVLLRALAWTTGLPTRVRAWREQRVQAQQQTILEQGWIHLLQGRFARSERDMAQVADQSKTPVRQVLALLSSAQATHAMQEFARRDALLVRVRGVAEGDPALMSAVSIVEAELLLEQQRPAEALALLEPLHEGGQRHVHSLRLALRAHRELGNWAEVLKLARTLAKRNALHAAASHRMIAAAATERLRSTSDDVVRRDLWKDLKDDERIVPEVALAAAASFEEGGDPVRARAILEAAIQANPTRELWQAYARTVPAEVKPRLEKA... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in a late step of protoheme IX synthesis.
Subcellular Location: Cell inner membrane
Sequence Length: 425
Sequence Mass (Da): 47037
Location Topology: Multi-pass membrane protein
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K6ASC2 | MRPNLNNLSGEKEALSLLELNTRIRGALSRAFPETCWVRAEMSDVRVNTSSGHCYLEFVEKNVQTGQLVAKVRGSIWAKTFRMLKPYFEMETGQMFASGLKVLVKVSVEFHELYGLSLTVLDIDPAYTLGDMVRKRMEIIRQLQEEGVFTLNKELPFPLLPRRIAIITSPTAAGYEDFMNQLTRNKGGYPFYTKLFPALMQGERTEASVIAALDRIYQHQDLFDVVVIIRGGGATSDLNSFDSYLLAANCAQFPLPIITGIGHERDDTVVDLVAHTRMKTPTAVAEFLISRMDSVGEELESLRQDVSLLAMDILSRQKNY... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A1F9BFY0 | MTRQNRILQGIPASPGIVLGRAKVLADREAQPFYCLLYSPEEINGELDRFLKAVEQAEADLISLKDSLPPEYQEHAHLLDLQILMLKERMIFQETQRLIQEERYNAEWALFQAWQKVMELFRGIGDPYIKGRIQDVEEVYRRLQSNLTGKETWSLSSQEPVILVARDLSPAEATQMSRSQVLGFITERGGRTSHTAIIAQSLEITAVVGVDFATREIATGDAVIMDGLSGQIILDPDEAMSASYQVRKKEFEAFKEEVAQSGSLPATTIDEYATQVLANIELPEEVELGLKNGADGVGLYRTEFLYLRLRRLPTEDELFE... | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfer... |
S5ZMB2 | MKTETKEKKVHKIFETISDRYDKANNRISIYMHKKWKMNLVNKIIKGSSKGNNILDVCCGTGDIAIWTAKKRRDISVTGIDFSSSMLQKARQKSIKIKNITWQQADALKLPFPDNTFDSADISFGLRNTSEYEKVLFEMKRVVKKGSNIYCLDSFIPENKFIRPFHKFYFKHIVPVLGGGIHCHKEYLWLYESTSKFLGKKDLMKLYSKIGLANTACYSYFFGCCALICGQK | 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... |
A0A0V1M759 | LDCCKLGHFFWKHRPTVLSDCSSILLNIAYILFFSCWLVGWLKMSVMFSQIKLPPGITFDELIDSAKDWAQIHGLCIRPPGKYENSDEVQLAPFTLLPSPFSKSCFDTAINLHQAMMAVYHQIAFDYDFMEEALSPVMLSDVFVSKLFAIYRAVMKHGNMTSRLVLNIQRCDYMMQEEEANSSYSLKQVEVNHVAASFAGLGVRCRQWHWLMLNQMVENGKLDLLPENHALATVALGLLSAWRAYGRSEAIILIMVEDELRNFADQRLVEYKIQSLAEFQHVPMKRFRLSDCPGNIATDGRGRLMLNGVEVAVVYYRTGY... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.
EC: 6.3.2.3
Catalytic Activity: ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + glutathione + H(+) + phosphate
Sequence Length: 545
Sequence Mass (Da): 61560
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A0A2P5P5P9 | MDENQSEYLPNAILLLGPTGSGKTPLGDLLENEGLAGRKCFHFDFGAQLRGYAANPTDLLSEVELEIVKISLGSGALLTDSQFGIAEKLLGEFIEKNRIGSGDLIIMNGMPRHAGQAAGLERIIKMKAVVVLGCDAATVRERICTNAGGDREGRVDDTKEDVVRKLAIFAEKTLPLLKFYEGYGIPVIHIDVGTNDSAIKSRGALVVKITNIFD | Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence Length: 214
Sequence Mass (Da): 23029
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A0A1B2EV71 | MAVTIVVFLILGSVLEGLPAIVLMAPLMFPIATSLGINDVHYAMILVTAMNIGLMAPPIGMGFYLACKIGNVPPDEAIGAVWPYLVALLVGLIIIALVPWISIGFL | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 106
Sequence Mass (Da): 11146
Location Topology: Multi-pass membrane protein
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A0A380BXV1 | MAMKIKCVSKYILLIVLSATLFAGCHSPKAEKISFEHLPSQPRNSEHDTATFAAGCFWCIEAQFKELKGVEQVLSGYSGGHVKDPTYTQVSLGGTGHAEVIQVVYNPHIVSYDQLLQGFFLAHDPTQLNRQGNDVGEQYRSAIFVHDKIQLDKVRYYIRKMTDEKLYDKPIVTQVEPFTVFYKAEDYHQNYYANNPDEAYCQYVIKPKLEKFKHIFSTNLKHTP | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
EC: 1.8.4.11
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionin... |
T0KPT7 | MTKQIDFAKFSSIKIGGVHEVFILEDASDFSDDFFLIGSCNNVIVGTQPPKLMKLSKKYDYIKIENDTLKVGAATPSGKLASYCKKNNIANFEFVSHLPGTLGGLVYMNAGLKEHEIFNTLLSVTTTKGELKKKSIDYGYRCTNIKEPILEASFTLVYGYSVEKAELFKQMRANQPHEHSAGSCFKNPNGDFAGRLIEAVGLKGKRVGAMEFSTKHANFLLNHGGGVFEDAITLIKEAQKRVFDEFGISLECEVVILDERYLKTKH | 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: 266
Sequence Mass (Da): 29567
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A0A926G9Q7 | MTRLQQGLEALLLGGPASAPGRERGLFLGFAGLAALALVTAAAVAADVGYGTAVLGYLLVVLLFSLAANFLLSACLSAVALACLDFFFVEPRFTFQIDYARDLTSLLFFVAAALVVTSLVSRIRALALAQAEQARLLDLTHDCILVRDCDDTITYWNPAAEQLYGWSRQEALGRKTHELLKTRFPAPLKDIQAIVQETGRWEGELVHFHRDGTALHVASRWSLHRDATGRIAGTLETNNNITERLAAEQALRQIEAAQYDEAQRLSATGSFVWHAGTGETFWSDEARRIYGIVGSASPEMATLLIGVAPEDVTVLREWIE... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 646
Sequence Mass (Da): 69090
Location Topology: Multi-pass membrane protein
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A0A8J5LLX9 | MGKAAVLVVSAVVLVACVATVGVVTVSNRQAADSSKPQMAELSTSQKNIQQFCQPTDYRQTCETTLSSVAGDNTDPKDLVELVFNITIDHIKKAFDHSSTIQEAAKDPRTSEALENCRELLDYAIGDLRTSVDRLEDFSMEKIDKFIDDLKVWISATITYQETCLDGFEGADTDAAASMRKALNSSAELTSNVLAIVTSFGDTLEKFELGNLNRKLLAVDAESFPSWVSGGKRRLLQQSPAELKPDVTVAQDGSGDVTTIADALLRVPQNSAKIVVMYIKEGVYNEKVEIGRSYTNLMMVGDGPTKTKITGSLNFIDGVA... | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) ... |
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