ids
stringlengths 6
10
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stringlengths 16
1.02k
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stringlengths 117
4.4k
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A0A6A6W2V5
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MPEITPSYKDHYGILNLRLSESDPVPRGITAKDIKNAYHKALLEHHPDKKQLDHDPVSDLASARATKSSNITIDDIIEAFEILKCEGTRKEYDRSLCLTRQTHNLESRGSHSTHDSHIFCGSASISAPEYEDVSEGIVYKQVDLHDLKEEETTTGDQVWSTNCRCGMDRGYVVTEEELKRESREGLAEAWVQCGGCSLWLGVEFGIEESNYDG
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Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Function: Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2.
Subcellular Location: Cytoplasm
Sequence Length: 213
Sequence Mass (Da): 23946
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A0A2A5DXQ5
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MAGKFPPWLRRPWASGETFGLTKGIVDDLKLHTVCQSAHCPNIGECWANGTATVMVLGNTCTRNCTFCSVPSGKPVFDDPSEPKNVAQAVKRMGLNHAVVTTVVRDDLPDGGAKHIAETIRHIHAVNPRTTVEILVSDFHGDKDAIQTVLDAKPEVFCHNIETVERLYPKIRDRRFTYRAALDVLRIARNTNKHTIVKSALMVGNGETPDEVRATLQDLKDAGCEAVCIGQYLQPTKQQADVEEFVHPDQFAEYETWAYDMGFPFAVSAPFVRSSYKSELVLETDYAKQKLGLKEASTATS
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Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
EC: 2.8.1.8
Subcellular Location: Cytoplasm
Catalytic Activity: [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Length: 301
Sequence Mass (Da): 33320
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A0A956C4U3
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AFGANALTAFLAVLANMLYVLAYTPLKQRSHFALHVGAVPGAIPPLLGWAAATGKVDAAGLILFAIMFIWQIPHFIAIALFRRADYARAGLVVMPNVTGELASRHAIVRWLFAGVAMSLLVVPLGVAHKGYLAVAALLGGGYFLYGCLGLRDGSGKSWARRLFGFSMLYLVVLFAALVIDP
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Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
EC: 2.5.1.141
Subcellular Location: Membrane
Sequence Length: 181
Sequence Mass (Da): 19270
Location Topology: Multi-pass membrane protein
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A0A973CY21
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LIRPREVYVGYDFHYGRDREGSMRLLTETGPRLGFSVTIVPGTDSNSRRRRQIMPSGVSSYASTSRFEVFAAIAAPSLASRALANSSKIPNKNTPGLSDRGHWEKMERETGLEPATLSLGS
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Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
EC: 2.7.7.2
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 121
Sequence Mass (Da): 13301
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A0A973HRB0
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MSIVRASLTPFRLPMQWPLETARGVTRVREGLLVELRGRGELRGYGEAMPLPGFGLESLAESRAALAAALPALLGLDAKDLETNLALAERATGRAPSARAALDSAFHDLAARSRNISVCELLAPCSREPVAVSALLAAKTPREVASAARQAADAGYRTLKLKIAATSVDRDVARVERMRDALGDDCALRLDANGGWEEATAREALRRLAPSLPEFVEQPVAARAIESLARLRSDSPVPVAADEALCHAGGAPAVLAHHAADLLILKPAALGGLRAAQRLADEARRAGVHVVVTGFLDSAIGDAAALQLAAALRSSEHAAGLGGQQLFADDLATIAEPQEGLRALPEAPGLGVEPDPLRLERLASGPAQIFAA
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Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 4/7.
Function: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB).
EC: 4.2.1.113
Catalytic Activity: (1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H2O
Sequence Length: 372
Sequence Mass (Da): 38792
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A0A3A4KGE1
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MINRIKGMYDILPPDTAVWRRVEDAFLAVSRRYGFAEARTPILERTELFSRSIGETTDIVEKEMYTFADKSERSLTLRPEGTASMVRAYIENNVPASDAAAKWVYIGPMYRYERPQKGRNRQFSQLGAEVFGVDAASQDAELIVMAWRFLESLDLAGHVSLEINSLGDAEERRRYREVLVGYLEGHRAVLCEDCVRRLGANPMRVLDCKMEACSAVAAGAPMLLDHIDGASRTHFDALRRGLEAAGVPYAVNPRIVRGLDYYNRTAFEFKTGELGAQDAIGGGGRYDGLVAELGGPPTPAVGFALGLDRVVLLLGGSAVEAAKLDFYVAPLSEAAQTTAVALSDRLRKDGLIGEVDFSGRRLKHLFARAERRGARTVLILGDDELAKGVVQARDMAAKTQREIRIDDLSRRTLG
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Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 414
Sequence Mass (Da): 45618
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A0A956DP29
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MTPPLVLGVLLAVTAFLSGSVPYGAIFARRRGVDIQAEGSGNIGATNVARTLGKGWGAAVLLLDAAKGAAPVAVAWWQASRLPAWAFAAAGLLAVVGHCYTPWLRFRGGKGVATALGVFLVLDPLATLVSVALFALVYAATKKSSAGSLTGALAMPVTLWIRGRGALELGLAVAVVLVIFLRHRDNLRRLAEGKEHGV
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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 phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Subcellular Location: Cell membrane
Sequence Length: 198
Sequence Mass (Da): 20460
Location Topology: Multi-pass membrane protein
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A0A077ZJ52
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MPGYIRLNSQQRCQNVGEASSQNLLSNEATFAPNQMLEAATDALSNWQHVQNLDEFFTNIYEYHQRHGFYCLLLADLLELFQFVFVVAFAIILTTCVDYRILFDGRIADMTRASLWDVIDCSGDGAACSLSNPWMIVTIIFASVFWLHRLVRFFYRCTVFLDIRNFYYTVLKVEDSMLRNMTWYDVQDRLCDKNAPYKLCIQKSHLTSMDIYQRILRRKNYMVAMFNKGLLPVRLKLPLIGDVCFMTLGFKFNLELLFFWGPWAPWENYWQLKADYKRRDGRQKLRDHLSRVILWFGLVNLLLAPLVFIWQILYCLFTYVEMLKREPSILGTRKWSMYGRYFFRHFNELDHELDNRLCYAYKPASLYMQMFYSSTAEIIAKNVAFVASALFSVFFILSIYDEDVLRVHNVLQLLTISGCIVAACNMFIQVSINSHSILMQ
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Function: Phospholipid scramblase involved in autophagy. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion.
Subcellular Location: Membrane
Sequence Length: 440
Sequence Mass (Da): 51859
Location Topology: Multi-pass membrane protein
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A0A833UMZ2
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MLDVGFSELLVFGIIALLVLGPDKLPEAARFAAKWYSKFKRAITSVQNDIDRELRLSEFREQMQQEMQKIQELEQKMQAQMQELQQQKIAIEQETHAEQLGQKNLLATYHYHKLDTQVPSIYMLNHGLNQQSCMMPAPQIVPIEMVTAPQLKVAV
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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. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Subcellular Location: Cell membrane
Sequence Length: 155
Sequence Mass (Da): 17867
Location Topology: Single-pass membrane protein
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A0A4V2AJF6
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MHPPRAPLHPLLSGEHPLPKELGNYLVKVLRLRAGDRFVLFDPETRSEADAELLRDVPAVARVAAVRTAKRSSLRDVTLLQGLAKGDKPDQVLRAAVALGATHVTFVRTERSMPGAELRDERLRAVMLDTARQCGRGDLPELAPLSSLEAALQASDGLGVLLDPNAEQSLVELLRVVAPTQSIALAVGPEGGFSEKETQRLLAAGFQPVRLAPFVLRTELAAVAALAVVAAHAGLETQSAAGEPRATDP
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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
Subcellular Location: Cytoplasm
Sequence Length: 249
Sequence Mass (Da): 26461
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A0A074KV40
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MQQSNAYIITFSVILTVILGFLLSGTSELLGPIQQKAIELDTKKQILGAVMPAEELDRMEADAVIDFYERRISSKVVNIEGEEVEQDTDGNALIAENVSIARNFKRSPEDRLYPVFIFHAEGNESEVESYILPVYGNGLWDEIWGYVALQTDLNTIEGVTFSHAGETPGLGARITSGDVQARYQGKEIFDEGGNLQAVRMQKGEGKDYSGEPHKVDGLSGATITAEGVNRMVESYLSHYQNYFSRQREGGDAAPEEQEPVALN
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Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+)
EC: 7.2.1.1
Subcellular Location: Cell membrane
Sequence Length: 263
Sequence Mass (Da): 29030
Location Topology: Single-pass membrane protein
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A0A077ZE41
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MNEGKLQSYALESILADDLEAVSIRRQWFAGVSSKHQNIGDIPFSPYDYSSVTDSCCENVLGFVPIPLGFAGPLKVDDEVVYIPMCTTEGCLVASVNRGCREGGGVLTALLSDCMTRGPVVSFENVRQAALFKSWLEDSANFSYLAKAFEDTSRFAKLKTVQVALVGRFAFIRFGASTGDAMGMNMASKGVEAVLEMLQRNHFPMLTVISLSGNYCVDKKSSAINWILGRGRSVTGEAILPDNVVRTVLKTDVDKLIQLNTVKNLVGSAKAGVVGGFNAHCANVVAAVFAATGQDLAQAVGSSQCLTFMEKTDEGDLRISCTMPCLEVGTVGGGTGLLAQKACLEILGCAGSCDSSPGKNARRLSQIICGAVLAGELSLLAALACGSLVRSHMRYNRKNAKSEKPTESFEWLVSWCHPLSGLKCGEDRISKFPKASVLLFLITVKPPEFTT
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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: 451
Sequence Mass (Da): 48190
Location Topology: Multi-pass membrane protein
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A0A0S8IHW4
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MKGIFITFEGSEGCGKSTQSHLLYQYLKRKGYKAIYLREPGSTAVGEKIRKILLDAKNLTLTPVSEMLLYMAARSQIVEEIIKPALDSGKLVICDRFLDSTLAYQGYGLGLDIRLIEEIGKRVTRKISPDLTILLDLAIQKGFKYRNRQKDRIEQRSLSYHARVRSGYLRLARRYAKRIKIVKVKGNKNQIQKQIRKLIDSFLERR
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Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 206
Sequence Mass (Da): 23795
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A0A0S8IMS5
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MKNKILVLGKGFIGTKLQEAFQCPLSAKFIQSFKDVQGEINKYRPKILINCIGHTGGRNVDDCERDKDKTLFANTYVPLLLGEVALRNRIKLVHISSGCIYHFNYAKTSPIIEEEIPDFLDLYYSRTKIYAENGLKALFKDCDILILRIRIPLDNRPHPRNILTKLTNFKKVIDLPNSLTYIPDFIKALKHLLRIDARGIYHVVNKGGLRYPDLLDVYKKYVPDFHYEIIDHKKLNLVRTNLLMSVNKLEKSGFPVRNIKEVLEECVKGYVGF
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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
Sequence Length: 273
Sequence Mass (Da): 31539
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A0A956G5G3
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MGKLRDRKNRHDDFYRRAKRESYAARSVYKLEEIDRRFKLMKAGQRVLDLGCRPGSWMQYAAARVGPRGMVVGLDREPVDIALPPHVTTLVGDVLEIDVAELRQGCSCFQLVMSDMAPDTTGVAFTDQVRSAELTGRALDIALAVGCPNGAFVAKLLMGEGFEPLLARLRETYASAKTVRPQATRKSSTEVYLVGTGKKAGAGKAEPEAEPAPASSEPEQNA
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Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.166
Subcellular Location: Cytoplasm
Sequence Length: 222
Sequence Mass (Da): 24198
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A0A7C7YH69
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MRLSTRSWVSWWAAEGFGEKSRPTGNFQGLFASGDGLGVAHFGEQSMLKLLLIAVGGGLGTLARYGVTGFAQRLSESHFPLGTLMVNLTGCLLIGGLSAFFAGGVGVREEYRWAITVGFLGGFTTFAAFGFETFALFENRHGGLAVANLVISNLGGLIAVWAGYRLVGLLRVAGAA
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Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 176
Sequence Mass (Da): 18482
Location Topology: Multi-pass membrane protein
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A0A7X7Z2F4
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MREFEWIGKAAELFGREHDGAPVGIGDDCALLTGPGPVLASIDTVVAGVHFEPCLMTAPDIGWRALAVALSDLAACGADPARPIHVLLSLQLPDDFPDTELLGLAAGLRDCAREHGGRIVGGDTVGTPGPLAITVTVLGSADRPVWRRGARPGDLLVVTGELGAAGLGLAALRAGWDDDDARRCALAYRRPRARLAAGFALARVATALIDISDGLLQDLGHVGAASGVGANVDLDRLPVAAAAREVARRLGADPLEYAAGFGDEYQLLAAVPPSRLAELAGELPDLTPIGEFVAGSAVVARQNGRPVEPRRRGYEHGRKK
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Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
EC: 2.7.4.16
Catalytic Activity: ATP + thiamine phosphate = ADP + thiamine diphosphate
Sequence Length: 320
Sequence Mass (Da): 33217
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A0A816WKJ7
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MELLSFQLDTFDIAIFIVLLIISLIAIYWFQRKPTLSKPDDIQQTIRNFRIDNGGVKGAGASHEGSFVDRMIHSNKKMVVFYGSQTGTAEDFAQRIAKQAKRYGISAAVCDPEECDMEELQRLIAIDKHLALFCLATYGEGDPTDNAQEFYEWLRENGRDLTGLHYAVFGLGNKTYEHYNAVGKLVDKRITELGGVRVCDLGLGDDDGNIEDDFMAWATIFWQNVCHKYELVINTDGTSMRQYKLVPGPFPVDSVFTGEIGRLKSYERQKPPYDARNPYLAPVTNTRELFQNDCLRSCLHLELDISATNIKYEAGYHVGVFPSNDAALVNRVGELLDVNLDEIISLLNVDEDAQKKYPFPCPCSYRTALTYYLDLTKDAQKKYPFPCPCSYRTALTYYLDLTSMPNTQILKEIAQYATDENDKTLLTLMGSYSEEGKIQYKEWILDSCRSIVAILEDLPSLKPPLDHLCELLPRLHPRYYSISSSPKVHPTSIHITAVIVHFETPTKRVAKGVATNCFKELYMKHQAIGCAQHKEGDTCHLPGRLPIFIRKSTFRLPFRFQTPIIMIGPGTGLAPFRGFIQERHFFKNQVKPQGKPVGETILYYGCRNRAEDYLYEEELNYFVKENVLELHIAFSRDQEEKIYVTHLLKDHGAKLWKLIKEDNASVYVCGDAKNMARDVHSILIDIAQTYGNMTSERAAAFIKDLIQKERYSQDVWS
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Cofactor: Binds 1 FAD per monomer.
Function: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5.
EC: 1.6.2.4
Catalytic Activity: NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450]
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 717
Sequence Mass (Da): 81810
Location Topology: Single-pass membrane protein
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A0A7C1GVW8
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MRTFIAIELPEETRGALYAFSERLQKSGLRASWVKRDVMHLTLRFLGDITQEQCDALPSFLDDAYKNKAAPVLLARGVGAFPSPRRPAVVWAGVETVAGDLAAVQHIAESAARHIGLPVEMKPFHAHVTLARLRKHDDSRRFSVALTPFLSQGMTPEFGYEFRAANVVLFSSTLTKYGPIHRKIEEFSLQ
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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: 190
Sequence Mass (Da): 21218
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A0A8J7XCY6
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MYMLMIDAGYVLDRVRGYPGIKNITVQAPEGLRKKALELSTFLETAGYTVVISASPCYGACDLEEYGDLLVHVGHTRIYSTKRPVVFVEVTDDFNFVPTLEKNVERIPARVGLLTTAQHRLQLESVGSFLRDNQVQVHTATGSRTEFEGQILGCDLTAATKISHEVDAFLYLGTGTFHPLGAAIATRKPVFRVYDTFEPVNSEKMLRKRHALIFEASRASTFGVVISTKKGQYRMSDALAARAYLKEKGKNTFLFVCNEIRPEYLYGCDAYVICACPRIALDDAALFEPPVLTCNEVPLMFEEGEYTMDMIV
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Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Function: Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2).
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: 312
Sequence Mass (Da): 34826
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A0A2A5DU95
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MISCTSVTGVALELPNGCELSMKQDTTIGFLGYGNMGQAIANGLMQAGTVKPKQLAAYDVDAAKLNELQTLGGSTVTSIADLANQAQVLVLATKPQDMDAALETLQAAATSATLYISIAAGLSIAYFQERLGTDARIIRVMPNMPAMVSAGASGIALSDTCTDEDGCIADAIFGAIGISERVSEHELDAVTALSGSGPAYYFYLVECFVRAGTMLGLSEEKATRLAAQTLYGTGLLLKESDESPAELRERVTSKGGTTYAALESFRAHGLEDTVYTAMKAAADRSKELGK
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Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm
Sequence Length: 290
Sequence Mass (Da): 30276
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A0A1H7LES1
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MVEWPSYSAAVLAGGKAQRMGGVDKGLLDWHGQPLVEWVRQALGEPQAWLVSANRNQAHYAALGWQVVEDPALAGVEPFAGPLLGLLALLRACPTPWLLVSPCDTPDLPADFAQRLIGAGAQVVCATDGERIHPLHLWLPTQLADSLEAYLRSGERRVMGWVMAQQPALVSFADQPQSLRNLNSLPG
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Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytoplasm
Sequence Length: 187
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence Mass (Da): 20201
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A0A964NET0
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MEVGVGVGSPPLVLTVIIENAGELFGIDGVIPGSCVGIIGDTVVALGDLGGFDTRSAVRLDARGGLVTGGLVDAHTHLVFAGDRADEHALRARGATYLEIAEGGGGIASTMRQTRACPVEVLVLEATRRLDRLLLGGVTTTEIKSGYGLDAQSELKLLHAIKRLSETHPMEIVPTFLGAHTIPPEHRSNRTRYVDLVVEEMLPEVAEGRLARFCDVFVERGAFEPQEAVRILGRARSLGLGVKLHVDQLTAGGGAELAAHLGATSADHLEHVSPAGITALARAGTVAVLLPGAGLFLGEDVRPPARALLDAGVPVAIATDCNPGTCPSTNLGLMMTLAVSRLHMQPDEALRAVTSSAARALDLPPRLAGLTIGAQADVAIFGVPTHRHLPYAFGADVTRAVVKRGKILFEREPCPSFSSLTTR
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Cofactor: Binds 1 zinc or iron ion per subunit.
Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
Function: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
EC: 3.5.2.7
Subcellular Location: Cytoplasm
Catalytic Activity: 4-imidazolone-5-propanoate + H2O = N-formimidoyl-L-glutamate
Sequence Length: 423
Sequence Mass (Da): 44239
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A0A956L3H2
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MLPDALEHWGALQAALPPGPLAVFLDYDGTLTPTRARPQDAVLADSTRQAVARLAAHCRVAVVTGRGLADVRAQVGLPQLCYAANHGLEIAGPGLALEAEPELRPTLEALAPRVHALVRGIEGIEVEAKGLSISIHHRRASPSCVPALEAALDELLAELPRVRRATGKALIELRPVTDWHKGSAVRWLCTQWAAGGAAPVPLVLGDDRTDEDALAAVREDGVGIFVGRPRWPSAARFGLRDPAAVEELLRRLVDDGTATRR
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Pathway: Glycan biosynthesis; trehalose biosynthesis.
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
EC: 3.1.3.12
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Length: 261
Sequence Mass (Da): 27823
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A0A0T6ASJ9
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MTVIMANGVNEVESNLKSILERVSKEAIQANDVFKIGISGGSALTYFTNSVLSMQEDLSKWKIFFCDERVVPEDSKDSTYGTVKRGKLMRDKLDEKQFIKIKSGINAPEAAAEYIQQMEQYFQRGSLPDFDLLLLGMGPDGHVCSLFPGHKLLDEKDVWVAPIEDSPKPPPCRITLTFPVINNARNCVFVATGEEKA
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Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequence Length: 197
Sequence Mass (Da): 21949
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A0A956CBK9
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MTSRPYGRPSACPAPSRRRWPVLERIGEYFAQRSPTQLARDALDILLVYYVVYRALLVLRGTRAMQVGVGLGVVFVFYLVAQWLQLVTVLSILGALISSIILVIVVVFQNDIRRGLMRVGSRAWLGSLTRSHESKVIDEVVEAATELARHRIGAIITFEQDANLDEFVGAHKGHVIDAAVSRELLVSMFIPEGINKLHDGAVVIRNLRIAKAGVFFPMPEARVVDESFGSRHRAALGITEETDAVVVVVSEERGTISFCFNGNIASNLDGPKLRAMLEAIFSPKVRSKKRKGGKRPTLGSVIAEAEAPPSAKPESERATTAPETPSRTPEPPAPEEQEEEAPVSVRDRDSEPPAPLRPRVSSTDDAPASVGRISTVPLRPSGPSRAIEIIHTPLPRVSDSPRISSTGDDDAEDDGSSRGSDPS
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Function: Catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria.
EC: 2.7.7.85
Catalytic Activity: 2 ATP = 3',3'-c-di-AMP + 2 diphosphate
Sequence Length: 423
Sequence Mass (Da): 45921
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A0A955ZTM2
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MSKKRPVFLVGMMGAGKSTVGPALAARLGRRFFDSDEEIERRAGRSIPAIFEDEGESGFRAREVAAIGSLAEHEDGAVVIALGGGAIVQPGALERLRARGEIVLLEADAAVLARRVGAGSGRPLLAGLSARARAERIEALLAERRPWYEAADHRVDADAGVDEVIDRIVAALRRDSGSGNGARRSMSESGARAPKRAARTGSKGAPASARPSKRSAKGEGRVHARVPVALADRSYAIELGQDWLTTIGRRIGDLLACERIALVTVPTVARRYAPRLSKGLTASGARVGRIVVPDGDATKNPRELARLWDRFLDLGLDRHSAVVTLGGGVVGDLGGFAAATFLRGIPFVQVPTTVLAMVDASIGGKTGINLARGKNLVGAFHQPRGVFIDIDTLRSLPRRERAAGAAELIKAAAIWDAELFAWLESEIEAFLDLEPSVVLHALERGCAIKAEVVARDEREGGLRRLLNFGHTLAHAIETHARYRGILHGEAVSIGMVFAAERSEALGLSPAGTRDRLAALLERAGLPTRAPDRPRRAYLSAIAVDKKKQGGNIHFVVLKGIGNAGTVSLSPREILPPGWKP
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Cofactor: Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Function: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalytic Activity: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 580
Sequence Mass (Da): 61628
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A0A956BEC1
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MTRAEKAERIGQQLDDLYPQPPIPLHHVDPFTLLVAVLLSAQTTDKKVNEVTPALFEVASTPQQMAALEVDTIRELIRQIGLAPTKAKNLKALSEKLVAEHGGEVPADEAALEALPGVGHKTASVVLTQAFGVPAFPVDTHIHRLAARWGLSSGKNVVTTERDLKKLFPRDTWNRRHLQIIYFGREDCPALYHDLSGCPICSWAASKKRIAEEAAQDQARRKRR
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Cofactor: Binds 1 [4Fe-4S] cluster.
Function: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
EC: 4.2.99.18
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Length: 224
Sequence Mass (Da): 24803
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A0A7C4UNT2
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MGTELKLSVLGFGNMGQAIVKGLINKGILPVHSLLIYDPDEEKQKVARELGINVCSAPELLIKENKVILIAVKPQMLKEALSPFKNDFMKDIVIVSIVAGVPIQFFKQFFNKPLLKVIRTMPNTPALVGCGITGISLSSECSEEEVKIAEVIFSSVGEVVFVPEEQIDIVTAVSGSGPAYFFYLCEALISAGEALGLSRDIAYKLAVHTLYGAGALVKSTGESPEVLRMRVTSKGGTTEKAIKYFQSKDFETIVKEAVRSAYLRAKELGKQNLSD
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Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm
Sequence Length: 275
Sequence Mass (Da): 29847
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A0A964NG89
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MWQTTWSAMPMRRGLDLSLCTLSAVLIFMGFPTALAPENSFWPTLWVSHVPLLFLLRDKAPAQAFRWGLLCGVLTNAGGYYWLAEMLERFGHLPSPVAYLGLALHSLHVGLMWGFWAFLINRVTNTTRVPLEWIAPAAMVAIELAWPRIFPAYMGNSQYLFAPVMQVVDLVGIYGVTFLLYHVNAVLFLWLRARIEGRKTPVRALGVAAFLVTLALGYGLVRIDQVDALVAAATKLRVGLVEGDVGIFESEPLEKRRDHLRIQQRLTADLESRGAELVLWSESAYRMSYDGEPGLPQSITRLPPAQTPLVSTHREDQFQRTPQADLYAPIRGFKVPTLIGATSARPREVPRYEGDTPDAYFNSAFLLDGDGQVHGRYDKNYLLIGGEYIPLSEYFPWIFKLIPSAGDLTPGKSLKTIDADLWGKGLVRLGVLICYEGILPAFARGLSSERPHFLVNMTNDDWFGDTAERHLHFALAVPRAIEHRLAFARVTLTGVSAFVDPVGRIVSQTPVTGEDTLMWDVPLLQSQTVYQRFGDAFALLCLGLTLAAYFWGRVRRA
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Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
EC: 2.3.1.269
Subcellular Location: Cell membrane
Sequence Length: 557
Sequence Mass (Da): 62251
Location Topology: Multi-pass membrane protein
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A0A7X7UCU7
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MNSWRLFIAIPLPEPVKQELARAQDALTHANSHVRGVGLAGMHLTVKFFGDTPAERVADIGHAMKLTAATVEKKIRLTCEGIGVFPNVEKPRVVWAGLRGETAVLEQMVQRLELAMETIGFAREERPFHPHVTLGRMKLPKQLGSLHKAMHQLEGRSFGEFDAEALILYRSDLLPSGARYTVVERAPLP
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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: 189
Sequence Mass (Da): 21006
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A0A1X9SZX2
|
MRLELQYLKDKKSLLAFSYGVDSTALFYLLKSAGVEFDCAMVNYQTRPSSLDEELSAKKLCDKFDKKLFIYRANLNLTNSNFEKTARDIRYDFFARTMCEFDYDTLILAHQLNDALEWLLMQLSKGSGTVGLAGMMPHSKKRVEFQNISKDIDIVRPLLGVSRNEILEFLHSKNIKYFIDSSNQNLKFARNKIRAEFSDEFMRQFSSGIKKSFELLRNDARLLLGEFEYDNGNIFVVAKSPNSINLIDQACKRLGVLMSQKTRQLCTQSDCVVSHKVAITSNQNYYFIAPYIKTIMDKKIKEKFRILKVPILLRPYLAANLNQLNALDKFL
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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) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 331
Sequence Mass (Da): 38274
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A0A1K1LY17
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MSERLKVNICGVEFKNPVIPASGTYGYGREYESLYPLSKLGGISVKGTTLNPRQGNQGPRVAETPAGMLNSVGLQNGGVKKFLEYEMPNLLTKDIRIIANIAGASVEECAELASLIDPSEVDMVELNISCPNVKQGGAAFGTDCAVAAAVTAAVRKELPHKPLMVKLSPNVTSITDIAKSVEAAGADALSLINTLLGMRIDIRTRRPILKNNVGGLSGPAVFPVAVRMVWQVANAVKVPIVGMGGIATWEDAVEMMMAGASAVQVGAAIFADPYAPVKIVDGLEQYCIDNSIANISEIVGTVQPW
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Cofactor: Binds 1 FMN per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway.
Function: Catalyzes the conversion of dihydroorotate to orotate.
EC: 1.3.-.-
Subcellular Location: Cytoplasm
Catalytic Activity: (S)-dihydroorotate + A = AH2 + orotate
Sequence Length: 305
Sequence Mass (Da): 32092
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A0A2D5QNE5
|
MNSKSLPLVFNQAQDLKRWRESLIYTGSLPLLGFVPTMGFLHEGHLSLIREAKRRAEYVVVSIFVNPSQFNNSSDFEQYPRNEERDINLASLAGADAIFIPTVEEIYPHGAETLVNVGSLAQNLCGATRPGHFQGVCTVVTALFNLVGCQIAVFGEKDYQQLAIIRRMTRDLHLPVEIVGLPTYREGNGLAMSSRNARLSKTARQKAGDIYSALKEAQVLWQQGQTLLSVLEQSIKASLPANLRIDYLSFCDPQTLQLLDVSERKESQDSPILIAIACFMEDVRLIDNIILAPL
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Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
EC: 6.3.2.1
Subcellular Location: Cytoplasm
Sequence Length: 294
Sequence Mass (Da): 32719
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A0A9E5AKS6
|
MNFEADWAPMRKLASRCTLPAPAPLAGIWPPMSEPKDKPTAPAHARTRRHSVTTEVPAESIEIVPVDENPRKNEHLRVALDARVERPGRGNGLSAYQFDPQSLPELDLDQVDTSCIVLGKRLSAPLLVGAMTGGTAQAGAVNRVLATAAELCGVGFCLGSQRAMLDLAGDHVRSFAMREVAPTTLLLGNIGAIQLRDHLSGKDLERLALAVGADGMMVHLNPLQEAIQPEGDRDWRGVYDALGDVAASCGLPVLVKEVGAGLSATSLNRLKLLGIAGVETAGVGGTSWSYIEALRHRGRTPQAIAGEVLADFGTCTADSLQLARVAFANRVVIASGGLRNGLEVAKCMALGASACAMAAPFLQAATVGVEAVVTEILGVIETLRITMFLVGAPDVHQLGQTPLVRTASCTPR
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Function: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
EC: 5.3.3.2
Subcellular Location: Cytoplasm
Sequence Length: 412
Sequence Mass (Da): 43229
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A0A2D5QQV2
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MSTASFDLSLIDLTIPLEQGLTKLFIRRGEEVGINAKVATVFPSNKGADFQCNGALASAKALKSSPRAIAQKWIEQFSEEELGLFSKLDIAGPGFINISISDEVLAIRSSLALNDKRLLCPKSNEPKKVYIDFGGYNVAKQLHIGHLRSTVIGETLRRIYSFLGEDVIGDAHLGDWGTQMGMLIEAVKEEQPHLPYFDDDFSGDYPKESPISLADMNRLYPQASAKSKEDPAIRAKASEATARLQAGHAGYRALWRHFVDLSIQEVKRDIAPFDVHFDLWLGESDAQAEIGPMVERLINDGVAEKSDGALIIPLQNDKGDDMVPLMLQKSDGGATYHTSDLATIQMRMYEDAEEMLYVVDARQEMHFKQVFNAAHKVGIVKPETHLEHVKFGTINGEDGRPFKTRSGGTVKLREVVNMALEAASTRLNEGEMQSQTLKEADEATRDAIAEMVAVAAIKFGDLSNHRTSDYILRLEDFCSFEGKTGPYLLYAAVRIKSILAKATERGIEPGEIRLRGGADRALALELSKFPSVLMQVRTKNTPHLLCEYLFNLSQSFSSFYQACNIVREEDSAQQSAWLSLVSLCLSTLELGLDLLGIKVPERM
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Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
EC: 6.1.1.19
Subcellular Location: Cytoplasm
Sequence Length: 603
Sequence Mass (Da): 66738
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A0A8C4UD32
|
MCAGDWIWVVWGALGAGGGCRWLGVPCSLWGRAVTVPPWQLNPNVSAFQRRFVGEVRRCEEMEKTFTFLQQELRGAGRVLGPCPESPRAPLAREALRVQEQSEQLAQELREVSHNRASLRGRLRELRQYLHPHLCAPHHHR
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Function: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Subcellular Location: Membrane
Sequence Length: 141
Sequence Mass (Da): 16096
Location Topology: Multi-pass membrane protein
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A0A7Z9HY35
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MKRKMPESKLKEHIVVTTGPPSSKPIPLQKIRKAYSLPEFHIPLNVGGRFSVFTPVGLLPAAILGIDVDGLVQGCRIMDKRTSKPSLKENPAYLRAAIHYLLCKEKQKSISVMMPYSDKLSAVSDWYAQLWAESIGKIVPGTKTTPAHAVGQTPVSALGATDQHSQLQLYLDGPNDKLITILEETAFDSRLNIPAVFAKIKAAEYLEGKTMNQLMAAERKATIDALRSKNRPVIRVTFPRVNASTIAQFMYMLEVETAMAGQLFGIDAFDQPAVELIKVFTRKNMGDSSG
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Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
EC: 5.3.1.9
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Length: 290
Sequence Mass (Da): 31928
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A0A1Z8KMS6
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MNEKITELKNSLSSNLDEMKTSQIVELINSEDSKISLVIKEIIPRISDLINKIIQNIKNGGRLIYVGSGTSGRLGVLDASECPPTFNVKSNLVVGIISGGANALHTSIEGAEDDTELAINDIKKYKINKTDTIIGISTSGTTPYVHKFLEESKKIGSFTSILTANKIKKKSYIDDYIEFIVGSEILTGSTRMKAGTATKMILNIISTTTMIKLNKVYKNYMIDLKISNDKLHKRALNMVSEITDLNIMESKNLIKKSHGHIKNAILMHFKKITYDESCKILNKNKDSLKESLNNN
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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 6-phosphate
Sequence Length: 295
Sequence Mass (Da): 32757
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A0A418Q882
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MGGFRARSESARSGSDRHDSGRSSSGNKQRTGRPRTAPDRSKGYQQRRPEERQMKAKQHGSGDKVRDVVLHVLREVTTEDAYGNLVLPREIKAARLNKRDAAFATELTYGTLRASGLLDAVIAKAAGRPVDKIDSVVLDILRLGAYQILRTRVEDHAAVDTSVKLAKANGAGQASGFVNGVLRTITRSTPKQWMERIAPDDSLASLAVRTAHPEWIAAVFADALEQQEAGLAASELEQALQADDQRPTIHLAARPGQISAEELALVTGGEEGRWSPYAVYLDEGSPGELEPIRDGMASVQDEGSQLIALAMVRAPLERTDRGRWLDLCAGPGGKTAFIASWAVGEEAKVDAVEVAEHRAKLVSSAVRDLPVAVHVGDGRKVAQIAGIDMPTGGFDRVLVDAPCSGLGALRRRPEARWRKDPKDVPPLVALQKELLRSALSVAAEGGVVVYSTCSPHPAETSEVVRAVAAETGATVLDVQEILPELDNVGTGPFVQLWPHRHGTDAMFIAALRPAPEAGAGSGAKA
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Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.176
Subcellular Location: Cytoplasm
Sequence Length: 525
Sequence Mass (Da): 56036
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A0A517ME74
|
MSKSALITGITGQDGSYLAELLLDKGYKVHGLVRRSSTFSTERIEHIYCDPHEKSELRLHYGDLTDGQALTNLVLEIEPDEIYNLGAQSHVRVSFDQPVYTLQTVGVGALNVLEAARLLHARKPVRVYQASSSEMYGDVMETPQRETTPFNPQSPYACAKVYAFHQTINYRESYDMYACNGILFNHESERRGETFVTRKITRAATRIKMGLQKKLYLGNLDAKRDWGYAKDYVKAMWAILQQDKPDDYVIATGETQTVRAFLELVFGQLDLDWQQYVEIDPRYFRPAEVELLLGDPTKAKEKLGWTAETDLRELARIMVDHDLDLAKREAHAASFAGSDSSQKD
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Function: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose.
EC: 4.2.1.47
Catalytic Activity: GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O
Sequence Length: 344
Sequence Mass (Da): 39116
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A0A3A4K3P1
|
MRDDLLYLITDRHACGADRLVVRVRQALEGGVRLVQLRERDLSDAELLRLAQPMRKICGEFEARLIVNRRLSVALAAGADGLHVGADQIPLLGDLRAIAQRPILIGVSTHSVAEAEAAERAGADFVTLGPVYETPSKAGMGEPLGPTEVGRGVKACRIPVFGLGGVSVDRLDEMKRAGIGRISVIRAVLAAADPAQAAADLLARLRS
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Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
EC: 2.5.1.3
Catalytic Activity: 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Length: 207
Sequence Mass (Da): 21998
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A0A7C4YT21
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MANELDRVPQFYLDPGYIYFSKAPLNLYAVLGSCVAVCIWDENLKIGGMSHYLYPKSPSKDKTTSKYGDVAVLSLIKMMEKAGAKRESMYAQIVGGAHPPFLRNNRDSLGDKNVEIAREILSKKGIRIASEDTGGTMGRKIVFNTYTGHLMVLKVYKIRRDDWILEIKD
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Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
EC: 3.5.1.44
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Length: 169
Sequence Mass (Da): 19041
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A0A8J7M1E9
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MLNILSSAMTRFFSLTIRAQLVFIVLITAVPAGGMILYSGMKLRSEAIKIAVLDSQRLADSMALQQKNLVAAAQQLVSALAQLPAVKRGDPANVEPLLAEILRLNSHYSNIAIINPDGLVLASAVKALRNRSVADRRYFKNPIAAGRFSSGEYIISRAIFKPVFNFGYPLRDERGEIIGVLSLGFDLGPYEKAFADAKLPAGSNFLIIDHSGVILSGAADAIRFVGKRLDPRLFDEMKNGPEEGHGLSRFLGDGTYYVAYRKMRLAGEEAPYMYIRVGIPTAAVLANANKILWSNLALLMPGLIVALYIALLIANRSIADRILVLKKASQHLADGGLDAPISGLVAGGELGSLGESFDNLAKELALGEEARRASEMKYQMIFDASKDAIILHDRESGRILDANDTVQQMYGYSKAEILSLTVQDLGVASAPIPWLTAGEGETSRNLADAASFEWECRRKGGEPVWTEVLISPTSIGGEACFLAVVRDITERLEAETEKKQLKDQLHQIQRMESIGRLAGGMAHDLNNLLTPIMVYTELLKMDFIAERGGVDMADQILLAANRARILVQQLLSFGRKQMLDIKVVDLNQVISSFYDILRRTIRENIEIQWKPSDQIHNIRADVNQIEQIMMNLAVNAQDAISGKGTITIETALMVLDQAYARHHTSVKPGRYMMFAVTDDGCGMDTQTMEQVFEPFFTTKPVGQGSGLGLATVYGLVKQHGGSIWVYSEPGKGTSFKVFFPVVDDEVSAERAEPCGEVVFAAVSHSILLVEDNEMLRVMTANLLSTRGLNVTQADGPQQALELARGRTFDMLITDVVMPDLSGPELHQQLLEDHPDLIVLFMSGYTRTVVDNQGFLGDRRNFIQKPFAVNDFLAKVKELLYANPGG
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Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 885
Sequence Mass (Da): 97067
Location Topology: Multi-pass membrane protein
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A0A2E6VRX2
|
MSKKNKTDDLQNESFENLMGRIETVVQSLEKGELPLEDSLKAYESGIQLINVAQQKLGQMETRIEKLKSDGTTTALNNEEMAAVHSED
|
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 Location: Cytoplasm
Sequence Length: 88
Sequence Mass (Da): 9841
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A0A3A4JQ59
|
VDLEALRALVRFQLDNGVHGLVPLGSTGEAATLTLAEREAVVNAVRDEARGRAPIVVGASTNDTRTTIELVRQAKDLGADAAMIVMPYYNKPTPDGIVAHFAAISEAVDMPLVAYNVPSRTGVNLAPATAARLAAMPKVVGLKEAAGDMAQAMEIARRTQGQWSLLSGEDALLFPFLAIGGQGLISVTSNLLPSKMARIYDLWQAGDLAGSRQQQLELLPAIQAMFSSTNPLPVKAALSLRGLIRNEARLPLLALSGPTLDALRAELTRLEAI
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Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
EC: 4.3.3.7
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
Sequence Length: 273
Sequence Mass (Da): 28891
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A0A956AX90
|
MGFRDRVEKVGPAHYVLAPVGDMRCPVDAWLDEGLFAQTDESLWRQAALAAAYPGAQGLHLMPDTHLGYGIPVGGVLVTDQTIVQAGSGYDISCGVVYMKARGLAAADVVDWERRRQWVDAVEARVATGIGNHRPRLAPQISHRLVEDVLFNGAKALGVSADLCERHAIEVDPQLFDRKRVPKAAAKAQPQLGSVGGGNHFIEMQVDRDDGSVWVMVHCGSRGYGWQTANHFFYEGAALRGLPKNQREASWLRADEPLGRRYWAHHNSAANYAVANRHTIVDGVGAATEEV
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Cofactor: Binds 2 manganese ions per subunit.
EC: 6.5.1.8
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP + H(+)
Sequence Length: 291
Sequence Mass (Da): 31768
|
A0A956F1W7
|
ITRMGAQRVSEALPALVKAIQGDGRRVLWISDPMHGNTHATSSGIKTRNFDDILHEVQHSFDVHESLGSRLGGVHFELTGEDVTECTGGGLSEADLDQNYVSRCDPRLNYRQALEMAFRIGERMAQSPDALGMGRAHA
|
Cofactor: Binds 1 divalent cation per subunit. The enzyme is active with manganese, cobalt or cadmium ions.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
EC: 2.5.1.54
Catalytic Activity: D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
Sequence Length: 138
Sequence Mass (Da): 15116
|
A0A2E6VU98
|
MLALRKVLFGITFALSGLSASSALAAGGGHGEPHVTNWFSLPIFNIELSESIHAPALGWVMVSFAVYVGIIVFIMSKKLPDFLAQRSELIRQAIDEASEAKKEAEANARKYEERMAKLDEELKQMREDFSTQGQTEFERIEQSAESAAQKMQKDTEATIDAELQKALAQLQTETAKLSYDLAKEQLEKSLNASDQARLEETFLEDLNRQAQA
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Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 212
Sequence Mass (Da): 23586
Location Topology: Single-pass membrane protein
|
V4XTM4
|
MRVVVSIGGSVLAPGLDSDRIAAYASAVGSLVDEDCEVGVVVGGGSVAREYIDAARDLGANEVLLDRLGIGVTRLNARLLIAGLSERATPTPPEEYEAAGQALRRGDIPVMGGIMPGQTTDAVAVALAESIGAELLIFATSTTGVFDIDPETDSEASQFAELSPQELVDVVVPMARDAGASAPVDLLAAKLIDRADMRSIVLDGSDPERIVSATLQGHHDGTDIVPAGADSPDRWGNRMTPRDDDSGSESGVETASGGANDSPHLLADSTPDTERAYWAETVADAIDARNPDQPIVIKGGVSPSGVSHLGNFNEIMRGYLVAQVLRDRGHDVRQVFTSDDRDPLRKVPRTLADSDGSLVDLGDVDAESLGRSLGMAYTDIPDPFGDAPSYAAHFASLLKSDAERLDVPVEMISTTDLYENGTFDPILDRVLGDVEQARDVIAPYQDTVDESYVPFNAICSECGQMTDTVTAVDPDARTVEYRCTGMDAGDRTIDGCGHEGTAGFREGKLPWRFEWPAEWAVLGVDFEPFGKDHAEGSWPSGVDIAHNVVNVEPPVPTVYEWFTLNGEPLSSSAGNIITVQQLLELLEPEVVRYFFARNPKKARDLDISRLDQLVDEFDRFERAFFDETGDEHLAPFARAAYPHVVDEVREGRVRLPYTFAAVLGMVDDRELQVRLARSEGHIAADTPQWAIDDALDRIERARSWARQMDNAYNYELQAELPEVTFTEATTAALDDLAEFVAAGHDGEAIQSEIYDTARKHDLDVGDFFEAGYRLFFDDTAGPRLGEFLGDLEREFVVTRLRREG
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Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys)
Subcellular Location: Cytoplasm
Sequence Length: 804
Sequence Mass (Da): 87225
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A0A2E8RZZ1
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MAEHTQITTPRELPRVDRMLEDSAIGNLIEDHGRAPVTTAIRRALEWARQQLREGPIASSDLHQQVALEVEILLGSGLRPVINGTGVLLHTNLGRAPISNHALRRATTLGQGFCNLEFDLEDGNRGVRGGAVQPLLETLTGAEAALCVNNNAAAVLLSLAAIGGKGEVIVSRGELVEIGGSYRMPDVMRLSGVRLCEIGTTNRTRVEDFATAIGPDTQAVLRVHRGNFHIEGFVQSPDLADVCTAAHKEDIPVLVDLGHGCVQNLSLPEGDGLPSTVQGCLKAGADVVLFSGDKLLGGPQCGIAVGRADLIESMRKHAYYRTVRVGKLTIAALEAVLRDHIAGRIENIPALAALSLASEVLQIRAQALVETYAQQYPDSGVKLAPTPCESEVGGGSDARYQIDSYGITVQHDTHSAHVISTILRRATPSVVGRVENDKVVLDLRTIQEAELEDLRQVLAQIDNGP
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Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route): step 1/1.
Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate
EC: 2.9.1.1
Subcellular Location: Cytoplasm
Sequence Length: 465
Sequence Mass (Da): 49673
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A0A2E7BRF1
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MSSMVRALYGGSFDPPHFGHQMAILYLLEGGYADEVRVIPCFDHPFGKELSPFPLRLSYCEALVRPFGGRAVVDPIEETLARPSYSYRTAESLAARFPEDQLRWIIGSDAAQAADQWAESDRLQRVAPFLVLARKGAPPDKNQAPLVLPEVASRDLRQRLAQGENLKGWIPESVLTRLNN
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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 = deamido-NAD(+) + diphosphate
Sequence Length: 180
Sequence Mass (Da): 20092
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A0A968MM82
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MDRARLCPRDRLFVVGRRGGPPSRHREARRVDAAGVSVSTSPDSRKRHSRGRNGDHRLFYAFYLAAQFSGAGIVLQQTFGIEPRLGVAIGAVIIILYTMLGGFLAVAWTDLVQAILMVATLIVLPIVAGVQLVSRDPSALEAVSASSLSWTGGATGVAAVAAIVSGLSWGFGYTGQPHTITRFMAIDRPEAIRVGRFVAMVWAIPAFAGAMAIGLIGARLYSVEAIPSAESPDVQQLMPFMAMELLPDWLAGIFISGAVAAMMSTADSQLLVGTSAVVEDTLHKGFGLSLSDRQWMWLSRGTTLALGTFGYILASTSSDLIFQLVSYAWSGLGASFGPAVLFTLHWKRTTGAGVLAGMVVGALVTVGWEMLPINELLHARLVSFVLACVTIVVVSTRSAKDSRQA
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Function: Catalyzes the sodium-dependent uptake of extracellular L-proline.
Catalytic Activity: L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out)
Subcellular Location: Cell membrane
Sequence Length: 405
Sequence Mass (Da): 43023
Location Topology: Multi-pass membrane protein
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A0A956CH24
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MQYQTFKGADVNQALSRVKAACGPDAIIYSTRKVSNGRGGALGSHYVEIEAAPPNERFNWGFQDPRSKHPTERASAAPARPWSGGRRGHGTPTLGLDVHQLQREIGTLRAMLEDLNASRPPKQRALSMLASWGVELGLARTLVTGSTRAARRGELALRHWLADQLRDRIQVAQEFLTCQEPTVVFAVGQTGVGKTTSLAKIAARARLDYGHPVTVITLDTFRVGALEQWQRYANLMGVTLRVARSVEEFENTLAEVRTPLVLVDTAGRSTASDSDWIVPGCVQAVENRNTHVMLVLPAWTRGSDAERVVKGYLDAGLTGICVTKLDETVQYGGIVHAALPQELPIYYLCDGPRVPEDIQPATIDAVVAALTEGSN
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Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 375
Sequence Mass (Da): 40767
Location Topology: Peripheral membrane protein
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A0A970M9B0
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MEVSTLFNALKVELGLELVAGRAGLDRGITGDRVQKPALALTGFTSMLSPGVVQIFGKTELDYLWSLPPVERRLACDFVTSCSPPAIIVTRGLDMPEQLLESADHYRVPLLLTGLRSSLFIEALHKFLATRMAQIRAIHGVLVDVFGVGVLIIGKSGIGKSECALELIMRGHRLVADDVVDVSLVPPSTIIGAGNELIRHHMEIRGLGIINIKDLFGVAAIRETKKIELVINMEEWDASKSFDRLGIVMQTHDILGVMIPRVDIPVRPGRTLTAIVEVAARNQILKSMGHHSARDFQSRMDAASRQGAESRNSRIWSTAPHALSSRVIDDKQD
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Function: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr).
EC: 2.7.11.-
Catalytic Activity: [HPr protein]-L-serine + ATP = [HPr protein]-O-phospho-L-serine + ADP + H(+)
Sequence Length: 333
Domain: The Walker A ATP-binding motif also binds Pi and PPi.
Sequence Mass (Da): 36443
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A0A0T6AU70
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MKNIIPQLVKYSPNTILLIVSNPCDILTYVAWKLSGLPKERVIGSGTNLDSSRFRFLLSQKLGVASTSCHGWIIGEHGDSSVAVWSGVNIAGVRLKELNSKIGTDDDPENWKDLHKQVIESAYNVIKLKGYTSWAIGMTVASIASSILHNIGNIHALSVLVKGYHGIEEEVFLSLPSVVGAGGITDVVIQPLTDSEQEALRKSAKLMGEVQAGIKF
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Pathway: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1.
EC: 1.1.1.27
Catalytic Activity: (S)-lactate + NAD(+) = H(+) + NADH + pyruvate
Sequence Length: 216
Sequence Mass (Da): 23352
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A0A1C5RSV4
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MKPIQTAGVIGLGSLGVLYATLFTRALGKEQVPVLADGARIARYRKQGFWYNDAPCDFNYTDAAARTEPVDLLLFAVKFGGLQNAIETCRHLVGPDTLVISVLNGISSEEILGDAFGPEHVVWCVAERMAAKKEGNRVVCDPIGELAVGVPAGEDTSRLQRLTAFFDSIGFPYVVPADIRTHMWSKLLCNTGCNQAALVFQCDYGPLQVPGKPRDTMIGAMREVAAVANAEGVPLSEKDVAAWVDIIDHLPSNGETSMRQDGKNHRKSEVELFAGTIRRLAAKHGISVPVNDWLYQQIQEMERNY
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Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 305
Sequence Mass (Da): 33346
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A0A518BW89
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MLGWLVFAGVALSVFAADMVSKYWAFATVAGIPVRPDPSYPGSGIPEHASIAVIPHVLDLHLILNRGAVFGMGQGQQGLFVVVSVLASLFIVWMMSVSSRRAWLMHVALGLILAGALGNLYDRVMFGAVRDLFWMLPTLGLWPWIFNLADAVLMTGVGLILLMSFRGGQRAEPASA
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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-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
EC: 3.4.23.36
Subcellular Location: Cell membrane
Sequence Length: 176
Sequence Mass (Da): 18954
Location Topology: Multi-pass membrane protein
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A0A2M8DQS4
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MIDREIEDINIEDNNNDDQGAESVKSFIFEIVKVLIISLIIIIPIRAYVVQPFYVDGDSMEPNFSDGQYLVVDEIGYRFKEPQRGDIVIFHPPNNPKVYYIKRMIGLPGEVVDIKDGVIRVFAKDSTEALIIDEQKYLSADFQLRPSEKDHVVLADDEYYLLGDNRQSSLDSRRLGPINVSMIKGRVVLRAFPFDEFTVIKTPIYN
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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: 206
Sequence Mass (Da): 23649
Location Topology: Single-pass type II membrane protein
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A0A9D7CX71
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MIPSNRRVAKPQLPPDVLGDEFEESEPLTVSEPPSVAPPPAAAPPSRFLVGFMAVIRVVLSVLLVVSVAGGLAWSTRRYVRESPRFALTNVAVSGNHHRSEAEILERAGLALGQNVFALDLADVKEKLSSDPWLREVTLSRRLPGTVLVHVIEREPAALVGIGDTVYLAARDGEIWKRLEASDPVDMPIVTGLRADAVLEDRDGVVLEIKRALDLVAEYGETSLSAKAPLQQAHVGDDGAMTLVVGKSGLSLSLGKPPYRRRLEQAVRVVAELERRMGPRALTEKADSIMLDSDARPDRVVVRMR
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Function: Essential cell division protein.
Subcellular Location: Cell membrane
Sequence Length: 305
Sequence Mass (Da): 33144
Location Topology: Single-pass type II membrane protein
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A0A2M8DRC0
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MHKIVILGPPGSGKGTQAEFISVALNIPIISTGHIFRNEMKNQTDLGKRITAIMDSGGLVPDEITNETVKNRLQQDDVKNGYILDGYPRTIAQVEYLDQLDELSRVVNIDCSDSVVTDRMAARRTCSKCGTDFNILFKPTKVDGVCDQCQGQLITRTDGEPDAIKERIYIYHQQDDPVLDFYKNKGILININGEPSIEEVWQQIREKLNLDS
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Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence Length: 212
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Sequence Mass (Da): 23799
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A0A970M6Y0
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MTFGDEAVLRIGTRRSQLAMWQANTVAAQLRQHFPALRVVLVPVATTGDRDKTTALSNFARPGIFTREIEQGLIDRHFDIAVHSYKDVATQYPEALDIGAVLERETPNDAFLSRHKTPLHALKPGSVVGTSSLRRRAMLLHARPDLRIVPLRGNVPTRLRAVGISPAESTAESLGAITESTESPGATAAPLLDATILALAGLRRLGYAEHAAETLKAPAFVPAPAQGAIAVQIRRDDETTRQKIQPLNHPATRAATDAERLFMRLMEGGCQLPLGAHAHITPSGDMRMTAAVLTLDGAQRIDGTCEAATPDELAHALFAQMQRAGADAVLREVRRHLESTP
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Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Length: 341
Sequence Mass (Da): 36810
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A0A7V4TI22
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MKSAPIGIMDSGIGGFSVVLEVRKLFPFCPIVYFADPLHFPYGEKRKEELAPIVQPVVDFLVHGIKVGLLVVACGTVSSLLLPELRERYTLPILGIVEPACREALAVVQEGAIGVLATRATIRVGGFRQALTRFRPGVEVVEEAWPEFIEAVEGGVFDTPSWRLWARERLEALHARGVRGVIMGCTHFALISTFFEELARGLFPIVNPAVSCAQEVGKFLPLGQPQKPGPLTVFVRGDREGFLRVIERFCFPLEMDVVSFENACRWVAHAWG
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Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
EC: 5.1.1.3
Catalytic Activity: L-glutamate = D-glutamate
Sequence Length: 272
Sequence Mass (Da): 30056
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A0A0A0F2K0
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MTQNTSLRSLEHHDAFIERHIGPNDAEIAQMLRVVGHDSLESFTDAIVPGSIRSAEALALPEAISEVEALAKIRGIAKRNQVFRSFIGQGYAGTHTPNVILRNILENPAWYTAYTPYQAEISQGRMEALINFQTMCADLTGMEIANASLLDEGTAAAEAMTLAKRSARSKSNVFFVSNAVHPQTVEVLRTRAEPIGIELVFGDESEAATTESFGVLLQYPDTYGRFGADYQAISDAVHARQGLVCVAVDLLALTLIAAPGEWGADIVVGNTQRFGVPYGFGGPHAAFMACRDAYKRSMPGRLIGVSVDVEGNNAYRLTLQTREQHIRREKATSNICTAQVLLAVMASMYAVYHGPEGLVRIARRTHRLAAILAGVLRKAGVTVGDQFFDTLHVTGIDAGALHHRAQQAHINLRVIDNGSLGIALDETTTREDIAALAGLFGAEITDIDALDTATADALPQGLLRTSRFLTHPVFNTHHSEHELLRYMRSLADKDLAMDRTMIPLGSCTMKLNATAEMLPITWPEFANIHPLAPAAQTQGYKELIDGLEAMLVEVTGYDNVSLQPNSGAQGEYAGLLAIRAYHRARGEAQRDICLIPESAHGTNPASAQLCGMKVVVTKCDKDGNVDVEDIRAQAEKYSDRLAAIMMTYPSTHGVFEEDVVEICEIVHKHGGQVYTDGANMNALVGLAKPGKWGSDVSHLNLHKTFCIPHGGGGPGVGPCAVKSHLAPYLPRALGGDGVRTQGVGEGAAVSAATFGSASILPISWMYITLMGREGLRKASQVAMLNANYVARRLAPHYPTLYTGRNNLVAHECILDLRPLEKATGVSAEDVAKRLIDFGFHAPTLSFPVAGTLMVEPTESESMHELDRFCDAMIQIREEIRAIEDGKLDRGDNPLKHAPHTAAQVSATEWTHAYPRELAAFPLPVLRQQKYWPPVARVDNVYGDKNVFCSCVPINEFAGEIEAFSEPMVS
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Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
EC: 1.4.4.2
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Length: 969
Sequence Mass (Da): 105060
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A0A9D7GYG6
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MSDIKRELEELRQSLGKIDGDLLSLIDKRARLARRAGELRGGDPAQLSSIEGLLDALVARAGGDMPEASLRAVFRELLAACQTLEMPLTISVLGPEGGPAFVAARSRFGAAVAVTAQETPAAVLAEVAGRRADYGLVPLEGKTDGPIQATIESLMASDLRIASVVESSATCHLMNKTGDASTVVRVAATAADAAREERFLASGPTRLLSVDAKSPVAACALANAEEGVAALVTEPIGVAAGLKMARRNPGHEEVRFAVVGGRPSGRTGRDIMALAFSVKDTPGALLDVLRQFSERGINMLTLQSHPEAGDGWNYVFFAEVDGHSTDRSLVTAFEEVKKLTRFFKVLGSYPADA
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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: 4.2.1.51
Subcellular Location: Cytoplasm
Sequence Length: 353
Sequence Mass (Da): 37164
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A0A3D1R253
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MVLRRESCLPIALAIVGALSSMAAAPVADRPQASTERASASRAPPEGFVDLTAAVPCLRLEIRYHTSGNFTGAPLPGYGTAGAWMLEAPAKALAQVQADLAPKGLGLLVYDAYRPHRATRAMVAWAERTGQIALVNGGYIARRSGHNHGHTVDLTLADLQTGRPLDMGTDFDTLSPESHTMRVKGKALEHRLLLKKAMEARGFRGYSKEWWHFRFPIKGSKARDVPYACFEADEGRWSPPEGWTEKGFEMPKTWEPTACEVR
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Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
EC: 3.4.13.22
Catalytic Activity: D-alanyl-D-alanine + H2O = 2 D-alanine
Sequence Length: 262
Sequence Mass (Da): 28711
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A0A956CKQ2
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MAHLDFEQPLVELEQRIRDLKAMAEVDASLVEEIEELQVRAERARAQIYADLGVWQKVQLSRHPDRPYFRDYLERIFDDFIELHGDRRFSDD
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Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
EC: 2.1.3.15
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Length: 92
Sequence Mass (Da): 11060
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A0A7C8CHZ8
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MRWLITGSGGQLGQCLTSAVQARPGEVLAGALSHSEFDIARPGALAQLLKDGRIGRPDILVNAAAFTGVDRCESEEALALRINAEGPGWLAEDCREAGINCIHVSTDYVFSGTARDPYLETAAVAPRTAYGRTKAEGERLVLKALPGAVVVRTSWVFGPGRNFVGAILRQARRRAQGLESGPLRVVSDQYGSPTYAADLAEGLLDLGSLAFAPPDADRGNVPSVRSPGTHGGEESGMSGIFHLSNRGKTNWLEFARSILELTGYGDLALEPLATADLELPAVRPAWSVLGCERAGRLGIGLRPWREALAGYLNSAAGVALREESV
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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
Sequence Length: 325
Sequence Mass (Da): 34356
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A0A8J8BSQ6
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MTSDYDEIGLKCGIEIHQRLDTHKLFCGCSSDLAEEEPVLEVNRKLRAVAGELGEVDRAALHEYLRDRNFLYEAYDGETCLVELDEEPPLPLNEEALDIGLEASLLFASTIPDEIHVMRKTVVDGSNTGGFQRTCVIGLDGEMDGPRGKLGIPTICLEEEAAGIGGQRDDSVVYKLDRLGIPLVEVATDLMEGYLPEEVQDVAHRIGMMLRMTGKVQRGIGTIRQDVNVSIRGGSRVEIKGFQEINRLAELIRNEVLRQSSLLRIKKDLEDRETGISEAMDATEYFEGVEKGPLAKILKRGGRVLALNLRGFSGFLGRELCPGRTFGRELADHAKAHGIGGIIHSDEDLEAMGLTGIFAALGKSMASEPEDAIAIVAGPPGRASRAMEAVRKRLKLAGGELPEETREPNPDGTTNYKRPLPGSDRMYPETDIPPIPISQEHLERIKEALPEKPEEKRARFVASGISGDLADQLVRDPNLALFEKIAGEVEVDRTLLANTLVNTFRSLRRDGIGVDSIPEVELLEFFAASASGRMVRQDFEPILGEMAGGKPLKDILGEREMIGEDDLREIVRAVLEEKSDFIQERGERSFGPLMGEVMKQARGKIDGAIVGKVLREMLDKKLSN
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Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate.
EC: 6.3.5.-
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Length: 624
Sequence Mass (Da): 68653
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A0A4Q5X780
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MAASLGKEPPFGLILTLFVLSGATGLIDQLCFSRYLSYVVGATAHAVSAVLSAFMTGLALGALLGGRYSRRVKRPLVAYGVLELVVAVTVAASPLAFQALAPLYAAIARAFPESLAALSAARWLGALLIVVVPTTAMGATLPLLSRLLPASADALVAAVREKRLGALYASNTAGGALGALLAAYLILPALGLSSTVLLSAAGSAVIGALAIAFGRRAPAQEPLADASVSGVHDGRGVVKDAWVAYVVAALSGALVFAAEVIFTHLLALIIGSSAYAFGLILAAFLSCLFLGASRAEAVRRRFGEAALPFGLVLSGLALAITLPLWDKLPMVFNGSGGFFSSFAAREAMRGSIAFVVLAIPTVFMGLTFPLLLQRVAASDDLGWWVGRLTTVNTLGAVLGSLLTGYVVLPALGSEGSLFAVALVFALTGLLTTRFVTGKKRLWALGLAWATAAVWLFTPRWDLARLTAGTNVYFEKWNEPDEILFVRDDVHGGVTTVTRVGDVRTLYTNGKFQGNTGWEMSAQRFFAHYPSIFVSEFERSLVIGLGTGTTLGTIAAYPWKKLDLVEISPAIVEAAGAYFESVNGGALRDPRLSIHLGDGRNFLLVEQHRYDLISMELSSVWFAGASSLYSQEFYRLVEQHMKPRGIFQQWVQMHHIRRKDFATLVHTLRTVFPHVALFYGGQQGILVASMQPLVASESRVHALQLTPEVIAKTPGNRPLMSLLDDVLLADADLDHFLEASAREEGEPLSELVSTDQNLYLEYATPRGNTLPWSAREELVSKILEFKSEVSSAGLRGP
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Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Subcellular Location: Cell membrane
Sequence Length: 796
Sequence Mass (Da): 84924
Location Topology: Multi-pass membrane protein
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A0A2E7BVA2
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MYLRELASPKLRQWLKPSLEMLAGIPTIVYGYFALLFVTPLLQEFLPNLSGFNALSPGIVMGFMITPMIASLSEDALSAVSNDLREGAYALGAGRASTIFRVILPAARSGIAAASLLALARAVGETMIVAIAAGQQPRFTFDPQVPVETMTAYIVQVSMGDTPQGTLEYQTIFAVGLTLFAMTFIVNIFGQRLARGKRS
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Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 199
Sequence Mass (Da): 21410
Location Topology: Multi-pass membrane protein
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A0A8B9H003
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MESWRPVLLLFLICHARGTGARDARQHVYGKVVHLLSPGEDELSDSAVRSFFSLLEKRVQWAGVSCGKSLLEDNLNQLVSNYSSSSGLQEDGFFRLAAGCCLFLSSASNTCTAIREGRWAQETDQFIQSMLTHDDHSDHYEEGLEKLLHDMEEYYVPELHDEHCLSVTDILQESNVTNEHDHQHADPHTDLDAVLGTVIYHVLLGDCMSAHSLPEMQFFMNYIFNHFGPDNITVGDLQSLMNALNLGRTGGNSDNDHGHDHAHEVHDDGEGPRHAHEEPHVLSSSWNTCFSAQELLMIYRLNSSGLNRDQFTQLSPALIQQLLSKACTETSPITDPTGDKLSTTERKSQIDYFYQIQPVLKKKNLETFIFLIDKKIQCHIFLGLHVHGEGQSDGHGHSEENSTYIFKLLVVVGGIYYFYLMETIFSIITRKNSDHHHHHHHHGVIVFLLKPAPRTREQKLLPYMITISDGIHNFADGLAIGAAFSLSWRSGLATSLAVLCHELPHELGKYKHLHDHMTINFLSTCFSGMYISI
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Catalytic Activity: Zn(2+)(in) = Zn(2+)(out)
Subcellular Location: Membrane
Sequence Length: 533
Sequence Mass (Da): 60145
Location Topology: Multi-pass membrane protein
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A0A7Y5GVW7
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MKVSVDAVTPTSRRVCVSFPATEITREFNEAYRSLNKVPLKGFRPGKTPRSVLTRYYGAKIADDIADKLVEKTVGKALVECDYPPASSVTFDRPKPQEGHDFTYTLTFHIVPVPRPLITEGLATLDGVDFSASPDEISEEMKRLRVASSELVPIEDRGAELGDIVTLNRTGLLDGIPSESLAAEDVSLKLGEERRYPEFSDALLGAKVGDTRQVTIMIPDVSFDDTNMAHDAGDQDGTQPQPPAKEATLTLVVTGVSREDLPELDDEFAKDHGFESLKELTEHVALRIKERKIKQHTSAIREQNLNTLLEMNPFPVPDEVIEDRAHASFHASNPDSGDSHDHTSEQLESHRTLVRLQLRRDSLIQELASQKQITVDHDDLESALSEIAQQFRVAPEIAMKLMGGPERSYDYLHARLLRDKTLDFLASGAHPAGTDPDLTRDPKDGDIIAENEQAAEVGA
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Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 459
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Sequence Mass (Da): 50718
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A0A2F0AN87
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MKRRRPSDARSVALMVLRSLEDETTFLQFKLDQVVKQAGLDGRDRRLAWNLVLGTARWLGHLDAQIEPYLRKRRLDQLEPDVLMILRLATFQLRFMDRIPEHAIVNSSVVLAKAFVGPRATGFVNGLLRNMIRHPKDVSFSNGADGIARRYGHPAWLVEQYLELMPLDAVVKRCQLNNEPAPLTIRICHQDIDAVVQALMDEGATVNRCTVAPDGFYLVDHPDPFGSLSFKNKQWAVQDEASQLVVDLLDVQPEHTVWDACAAPGGKARYIRDRLAGTGRLLATDINEDKVTALGQTIAGPGVTVKRHDAADPLHQTFDRVLLDAPCTALGLIRRHPEIRWRRQPSDVTDRTQYQSRLLDNASDHVSKGGIMVYSVCSDIPDEGQLLIDAFIARRPEFELVPPAPDSATGPLTTGGMIRFDPNQLNCDGFFGARLRRKTD
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Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.176
Subcellular Location: Cytoplasm
Sequence Length: 440
Sequence Mass (Da): 49244
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A0A4Q5P474
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LYDETIWQDARDGTPLVRLIEQAGAIPGIKVDEGTQPLPNCPGELVTVGLDKLAERLARYYERGARFAKWRAVIDIGKSSSGDRMPSMTAIAVNAHALARYAALCQQAQIVPIVEPEVLMDGDHDIDRCVEVTQRVLNKTFQELRIQRVALEGMILKPNMAVSGKKSAKQAGVDEVAEKTVRMLKNCVPASVPGIAFLSGGQSDEDATAHLDAMNRIGGMPWPLTFSYGRALQAAPQKAWSGKSENVAAAQKAFAHRARMNSLAASGNWTAEQEKAA
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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: 277
Sequence Mass (Da): 29993
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A0A2M7MBL3
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MVDKIWQTVYLGLGSNLNQPKKQLEKAMDTLNALSGCRWLSASSFIESLPQGPQDQPNFINAVVAIETCLSPMDLLRACQAIELRLGKQKKRDWGERVIDIDLLLYGQQIIDEADLIVPHPNMLTRDFVLLPLLEISPELILPNGQPVAHYASQLSETFVIRT
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Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
EC: 2.7.6.3
Sequence Length: 163
Sequence Mass (Da): 18308
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A0A838SVK4
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MSALWNGLLDVIEEVLRFFHTTTSPLFGEQAAWGWAIILLTVAVRIFLLPLAIKQTRSQRAMQRLQPEMKKIQQKYKVDRGLMKTNPEKYRDARQKQQEATMALYKEQGVNPAASCLPLVAQMPIFFALFNVLRDTNRVPELTAASFYFVQNLASTPAQAGIGAWLLIVLMGATTYYSSRQMMATTVVTGPQQQQQQKIMLYAMPLLLTVFAVNLYIGVLLYWVTTNVWTIAQQHVMFRNVEAVGTSL
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Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
Subcellular Location: Membrane
Sequence Length: 248
Sequence Mass (Da): 28111
Location Topology: Multi-pass membrane protein
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A0A956P8P5
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MSELVGFITEGVRNVIGSFSLAAVADVLLVALVIYRVILLIKGTRAVQMLWGIAVILLLFGVSAVFDFHTLHWMLSSFLSSMILVIVVLFQEDIRRALALGGQQILLIGSPRMENVLAIEEVVKACQSLATDRIGALIVMERETNVAEFVEIGVEVDGRVSRQLLQSIFITSSPIHDGAVVVRRGRLFAAGCFLPLTRRTNLDKSYGTRHRAGLGIAESTDAAVVIVSEETGKISLAFEGEIRTGLEASILREDLREIFEPRKKKGTERRASDAADVAPTQAMES
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Function: Catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP), a second messenger used to regulate differing processes in different bacteria.
EC: 2.7.7.85
Catalytic Activity: 2 ATP = 3',3'-c-di-AMP + 2 diphosphate
Sequence Length: 285
Sequence Mass (Da): 31105
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A0A2K3D6T6
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MACRAAGPALLTLHYLLMAGAIFGCGVRGLPAYYQAVVGVLLAASCGLLWATHLVDPGILPRSSSRDPVVVALDSGEGNVPNRSRYTRAVTGVWVRTMKMSEWRVERHHLLHPTQVGCFGADPTDDTYTAVATAAATAATAAAAATTAGDHYTEAASCGGSPSGGGAVALVGAGSLGTAATKGGLPPASTSASAGAAVAMGATAGAGHTTGGDQAFHAGLAVGIGRGTVGAGGGVGGPSPSPAPMSPSLPGYVPLAPSPTALAAAAAAAAGMHPSPSSGSSGAGLAAYKAIPGDGSDAAAAAAAASATAVAPTAAAATALEMEPLVVHKYCITCHIWRPERAHHCGVCGACMAHFDHHCGVVGNCVAHLNHRFFATFMLLAQIVALLTVGGCAWRLKNDGFPGARSWSDVETYLLLLLAAVAAYHVFMLGFGAMHCVFLMCDMTTKEMINGFAIFRRNLPCLPGGSRSPARLARAWRQMLLGPVRLRPRAFAAILDGICGHDHDQDPGGTSGFGRDADAWAAQHPAAFPAFAAQTQAQSAQAQSLALEGAGAGVGFPGMSVPGVHRAQSQSSASASAAMPMPMQPSALEPGSVAAPVAGAAGVTDLQSVGVGAYGYAYTATGGETSSGDSGTRLIGGAVV
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Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 640
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 63717
Location Topology: Multi-pass membrane protein
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A0A956LBZ2
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MKRALVCLSAVLLLGAAVAPAQTFVRLGTDEGDILLVLKPEVAPRHVANFLALGEAGMYQGTYFHRVIPGFMIQGGDPTGTGLGNPGYVIEDEFSPEVIHDRPGILSMANRSQPNTGGSQFFITLNPTPHLDGVHTVFGVCSDDAVALADDISLVPRGDGDKPEEPETIKRVDFEWRAPAS
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Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 181
Sequence Mass (Da): 19323
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A0A3C1L056
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MQVRFVGQDGEGLYGSVAGRHLCDYQHAIEAMNTLTARSPDAADLLLCVEHPPTITLGRRGGRASIHDTTLQVNEQSHPVAVYEVARGGAVTYHAPGQLVIYPIVQLPLLEPPIGVGPLGDLGGYVRALERCIVQCCAHFDLPTITREGFSGVWINERIKLASIGVGVRRGWTFHGLSLNINPHLEGFDLITPCALDGVRMTTMWQQLEELGRARPSYADVESDLLTRLSEALVRA
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Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
EC: 2.3.1.181
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Length: 236
Sequence Mass (Da): 25742
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A0A2D5ENH0
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MMALRMQDVGKELRWDELVTAVEEDRVKSVVLESDLVRGMLKGGGDSASGDSASGDSGSGERFRAVRVDDESFVPLLREHGVEIRAIPESDGSWTMWIWLALPLILLFWLSSRMASGGAASGALSFGRSKGKIFTERDIRVTFEDVAGVDEAKAELREVIDFLQQPEKYRRIGARIPKGVLLVGPPGTGKTLLARAVAGEAGVPFISISGSEFVEMFVGVGAARVRDLFEQAAKTAPAIVFIDELDALGRARGPGNMPGSNEEREQTLNQLLVELDGFEPLGEGRGPVVLLAATNRPEVLDPALLRAGRFDRQIIVDTPDRKGRRFILEVHVRKVPLDDDVDLDVVATRTPGFAGADLANLVNEAALRAAREGRDTVQMEDFSAAVDRVLAGLEQRSRLVDEEERERVAYHETGHAICATFGGSGTRVHKVSIVPRSVGALGFTMQLPERERKLYTVSQLKSQIVGLLGGRAAEELIYGEPSTGAADDLRKATDIARAMVLEHGFSEAVGPVAIEQRSHPYLGTVAGSRDVGEAVSDRADAEVRALVEGALEEAKRLLEAHREELEGMTRALLEREQLEGEELLPWLPAKNVQEEPARATEPPEMDEAGQGAGAEDGAGGAERAAPGAERAAKGRGPDGGDADTGDADADDEDADTDEAAE
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Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
EC: 3.4.24.-
Subcellular Location: Cell membrane
Sequence Length: 661
Sequence Mass (Da): 70983
Location Topology: Multi-pass membrane protein
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A0A8J2Y3H5
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MRVLNTAATALAALMIVAMAGVTAAEVIARFFFDVSFELADELGGYLLVASVFLGLGPALASGSLLRVEMVEQRLPAAVRRALDLLFHLGALAVSAIALYWIWRQVESSFRRETVSASWLEVPLWLPQAVMPLGLALLILTLLIGLARLLRRGAAA
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Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 156
Sequence Mass (Da): 16786
Location Topology: Multi-pass membrane protein
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A0A956KQG2
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MLGSGLAGLYFALEVADRRTVTVLTKHRRESSNTRYAQGGISAVFAPEDTLDAHVADTLRVGAGLCREGMVQRAVELGPRLVAGLARDFGVQFDRVGVGEDAPFQLGREGGHSQRRVVHYRDMTGAEIERALIQAVERHPNITVLEHHDVIDLLSWSKLDGGDGSPSCFGCYALDIEHDQVRAFVSPLTVLATGGAGKVYRYTSNPHVATGDGIAMAYRIGAQVGNLEFMQFHPTILFHPDAKSFLISEALRGEGGILRTAAGKDLMADRHPMGSLA
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Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1.
EC: 1.4.3.16
Catalytic Activity: L-aspartate + O2 = H2O2 + iminosuccinate
Sequence Length: 277
Sequence Mass (Da): 29891
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A0A2S7USV0
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MQKNHSRYFIGLDLSSTDKLAIAHWRDKQIFAATDKPVPVENFHITLSFLGQVTQNKLEQLETLLDAISTQRVNTITNELGVFSKPKILYLGVELTPSLQQLAKQCLGVNGKLALPSPHEIYRPHITLNRKHAEAVPIMFEPPKLELNFTEFHLFESVSSSKQGKPPHYPKRMSFRLE
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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: 178
Sequence Mass (Da): 20301
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A0A926Z0H4
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MKKLLKSPYLWPLLGVLVASRLLVLLSMLWLAPNVSIAYLNLQQPHSLGVSDLMGRPVVVEARSPDHQPHSLSYTFAGCPSATIEVTGLRQYELRSCPQAEQPRQLTLEVAPKLQVFYAGLAAMGAGQGNLLWLQFAKLDLQSQAAVHTLSLHELKPLERLLHSVYNWDARWYLSIARFGYFYNERLLGAQQYTNAAFYPLLPFLGRGLAFLTGLPPELTLLGMVQVLAVVAGVLLFRLALLMRLQPSAAFASVVLYALFPTSFFLSLPYTESLYITLSLLVFLNLENRWAPLAAALSVLARSTGIVHMPVLLLQTRGDWRQRLQRGLVAGLGLVAFATWLGATVKDPLAFVHAQQAWKEPMRPGNHWQHLLDALLLGPVVRLGNWIQHSPWSWASLNLVVAVLVLVTLFTGYQLIPKPLRLYTLLSLALPYFTFASSRVEMLSFGRFALAAYPLFLVWGQWLSPHPRLLATLVGLAILLLARLSADFGAGAFLG
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Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 495
Sequence Mass (Da): 54946
Location Topology: Multi-pass membrane protein
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U2J1K0
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MLNKVKRFIASEHLLRVDALYLVALSGGADSVALLLCLKELGYRVEAVHCNFHLRGEESLRDEQFCEELCQREDIPLHKAHFDTQAYADLHKVSIEMAARELRYCYFFQLKEALSADGVCVGHHKEDSVETILINLVRGTGLSGLMGIRPRNNDVIRPLLCVTRQEIEDYLQKYAVSFVIDSTNLVDDVVRNKIRLNVLPQLSEINPSVTDTILTTANHLSEVDAIVQESLKSALGKAISFVGSASQVSLSNLMNEPFQIDLSFVRVFPSPSYFLFHVLKPLGFSSSQIAEMVSHLDGQIGQLWYSSTHELTHDRGFFMVLPREEAEPRELVIPETGRYVYDEHLSLRLTQRALTPSSNVSYSKNPMIVDLNASSIRFPLTLRRVAEGDRFTPLGMCGTQLVSDFLTNLKRNRFEKRNQLVLLDATGTILWVLGLRINDCFKLIPQSSSCLQIEIL
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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) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 456
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Sequence Mass (Da): 51456
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A0A955Z6D3
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MSLRAMRVAAIVLAIVPGLGTGHLVLGRTRRALVWFAAPAALMTLIWAFFPLLARTIGLRSAVALAIALGGVLLVAGPLDAARVRPGSTRAPKTVVLAIYAALALASTFALRAMAASAFEVRMVPSMAMAPTLAPGDRVAVDRRKRSAPARGDVLLFAHPKTEAPFLGRVVGLPGERVEVARGRVRVDGKPLRVCPVAKDVALVDPPTPLDRGELFVEGDGNASYLAFVSEADSDAPARSFEVPAGSVFVLGDHRSRSEDSREFGPIAIERALGTAAYYAGRTSASDAAGLTFGAKLDHAQPTQMTALHAPAIRGCAVGAPIPPALAADVRAPR
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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: 334
Sequence Mass (Da): 34767
Location Topology: Single-pass type II membrane protein
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A0A2K3E872
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MPPGVKMIDGSMLEGGGQILRYSAALCAITGQAVGVERVRAKRTRPGLQPQHLTSLRLVEELCEGSLEGEGEGAETGSLEGGAVGSSHVVLRPGAPRCGRYVADTKTAGSCTLMVQAAMPVCVFAQPPPPEASSSASASSPVSTHLELRGGTDADLAPPAGYLREVLVPLLGRLYGGLMGGLAVETVRRGFYPRGGGVVTAVIPALPPGVPLPAFDLTRRGNITQVTVKSFSAGRVPVTVASRLAAAAEAALRRTLRKLPNGAVGVPPILVEATVETAEAAFGDGCGVLVYADTDTGCRLGASAKGERGVPAEEVGERAAAELAEALEAGACVDQWMQDQLIIWMALGSGVSRLVCAEPTLHTRTAMVVAEQLLPGVKFTLTRPAGAAGTSGEEGRRGTSGAEEEEKGRGKKQEGGGGGAGQGLWLIECQGAGWTVGRTLETPEGKAGGSAER
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Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
EC: 6.5.1.4
Catalytic Activity: a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate
Sequence Length: 453
Sequence Mass (Da): 46258
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A0A2F0ATE6
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MLLLTAPRGTPPPLRRLIIPFLFVTALFVTLYMRRVEPDFLTTEIRGQAMGTSYLVKVVSAANIPASYQALSAGVQTAIERVNQSMSTYQDESEISQLNRQSADVPFEASKDLRAVLTQALIISRETGGAFDPTVGPVVNAWGFGPNKTTKPPTETELLAAQARVGFKKIRIDDLTQTIRKAQSDVYLDLSAIAKGYAVDQVTAFLVESGQRDFLVEIGGELRTSGLNHRRKPWRLAVERPGPGQGDVHKNAIIDLGTGAMATSGDYRNFYEVDGRRVSHTIDPRTGRPITHSLTSVTVVAPTCMEADGWATALNVLGPDEAMGLAEKKKLNVFMLIRGKEGFEERATAGFTALRSNLKRPE
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Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 362
Sequence Mass (Da): 39560
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A0A956G8U5
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MHHDTTTPLRTRAAVYGASGITGCELVRRLDADPRCEVVAATSRQHAGAPLRSIDPAAPELLLVHPDEVPIAEIDVAFVCLPHGQAAPLVEVLVEQSRCRVIDLSADLRLRDSALHARVYGSTRGARVAEAAVYGITELYRGALCDARVVSNPGCYPTCAGLALWPLAEHGLLRERVTINALSGISGAGRATTPSTHFCAVADDVRPYKLGRSHRHSAEIEQILADAAPAGEQAPPVVFCPHVVPLERGMLATITVRVGELTAGEVHELFERRYADETFVELLPLGEPARIRAVVRTNRAQIGVHDVEGSDDVVLTCAIDNLVKGASGQALQTMNLMLGRAEHSGFAPTEHARLPRSSAPAAARRSACR
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Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
EC: 1.2.1.38
Subcellular Location: Cytoplasm
Sequence Length: 369
Sequence Mass (Da): 39448
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A0A7X7GZ68
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MSNRRTRTRARAKGKPEVAAPDERAFTPPEDPTESSPPSGWAQRLWSVTRVLFGAALVLGVAGIVGWGAHRYALTTPRFAIQSVEVEGARRLGADQVKELAGVEVGANVFALDVAGAQERLLESPWVAEARITRRLPGHVRIAVEEREAGALVLVGERLFLATRSGEVFKPFEEGDPYDLPTVTGVDLDALVRDEARELERVQEALELLRQYEKVPLAHVFPAQEVHMGPGGGATLTVGRQGLTLHLGAGPWKQKLLRATRVVERAQARGQLPGIVFLDNEAHPERVVVRMR
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Function: Essential cell division protein.
Subcellular Location: Cell membrane
Sequence Length: 292
Sequence Mass (Da): 31953
Location Topology: Single-pass type II membrane protein
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A0A973HSS0
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METLGGVELCVHERGSGPPLLLLHGFTGSARSLNELAGGLARTHRVIVPDLVGHGGSDAPLDLAPYRMERCIEQLCSLLDALETGPVGVLGYSMGGRVALSLLVRAPERIRSAMLVSASAGIAQPEARAERVRSDEALAQRIEEQGVTAFVDAWLSQPLFASQMRRLDPDARAQTREERLANSAHGLANSLRGMGSGAQPPLHDTLAAIACPVALVVGEEDEKFRRIAHELAQSLPQGRVHCVPRAGHAVHLENPAALLTVSLDHFASAGTAPRDAMHRSAPPAPRGRDQSTRGRESWHR
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Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 3/7.
Function: Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC).
EC: 4.2.99.20
Catalytic Activity: 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate = (1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate + pyruvate
Sequence Length: 300
Sequence Mass (Da): 32055
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A0A956LM41
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DAATAVAAAPAMGRSARIDRVLTHPLWGPLVFLAVMALLFNSIFSWATPLMDAIEAVMGWLSGLVKGGLGPGVLTDLLTEGVIAGVGNVLVFVPQIALLFLFIGLLEDTGYMARAAFLIDRLMARVGLHGRAFVPLLSGYACAIPAIMGTRTISSWKDRLVTILMIPYMSCSARLPIYVLIIGALFPGDARYGPFTLGGLVLLAMYALSTASALVVGAILKRTLLRSPTPPLVLELPPYRVPRLRNTAIYVYDRTADFVRGAGTVILAMTVILWALLSFPEPPAPPSPGDAPAVVQVVDGKPTKAPVDRDLSPIEYSIGGRVGKALEPALEPMGQDFRVGIAILGSFAAREVMVSTLGLVYGIEGADDDDTGLREAMRAAVDEDTGERRHTPLKGLALMVFFVYACQCMSTIAVVRRETGGWRWPAFMFVSMTTIAYVLAVLVYQVGLALGFS
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Function: Probable transporter of a GTP-driven Fe(2+) uptake system.
Subcellular Location: Cell inner membrane
Sequence Length: 453
Sequence Mass (Da): 48413
Location Topology: Multi-pass membrane protein
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A0A7Y5GUZ0
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MANPQEYIRNLTPYVPGKPIEELQREFGIQNVTKLASNENAVGPSPLALAAIVRELAELHRYPEGSAPTLVSELAAFLQVDPSNVVLGNGSDELIKLILQAFCPRNGVVVSSEHGFLMYKVFAGGFGIRCAEPPLAQNYRYDLRAVGSVAKESGAHAVFLANPSNPTGTTFTQTELLRFCEDVGPDLLLIIDEAYYEYVEMDDAVDSLALLRNRPNTVILRTFSKAYGLAGLRVGYGITSSEIANYINRIRTPFNINRLAQVGATAALGDKEHLAQVLEVNRAGKIQMTRGLRELGLNFADSQTNFYLVDLNRPAGPVYEALLRMGLIVRPMTAYGFPCHIRITVGQPAENARVLSALRAVLAE
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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: 364
Sequence Mass (Da): 39779
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A0A0S8IMB9
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MKIGILGGTFNPIHIGHLILAEEVREKLGLDKVIFVPTYLPPHKEVLGIAQAQARLTMVKLAIEGNHYFSVSDKEIKRDGRSYTIDTIREFKKEYPQDELYFIIGSDLLKYLEDWKDLHEVAKLAKFIAGTRPGYPLEEIPSYIDTVAIRAVDVSGFQIRECIKQSRSFRYLVPEAVYKYITENRLYED
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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 = deamido-NAD(+) + diphosphate
Sequence Length: 189
Sequence Mass (Da): 21811
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A0A956ACU0
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MARKWRPQTFDEVVGQEHVRQTLTNAISLDRVHHAFLFTGARGVGKTSIARILAKSLNCESGPTIAPCGHCTACKEIAAGTAMDVFEIDGASNRGINEIRELRESVRYRPSRDRYKVYIIDEVHMLTTEAFNALLKTLEEPPEHVVFIFATTEPERVPVTIQSRCQRFDFKRVPLDQVCGHLRTILASESITIDDDALFMIARESEGSVRDALSLLDQVIAFAGTSISAEQVTGILGISDRRALFEILEALVQGDVSRTLELCKGLFDYGIGTKELANQLLDATRDLLVVKSCENSRTLVDLTKSEWARFHGLAQTVEGGRLERMFGLLLDGCSEIARSPFAKMLLELALIRACQVPPVQSVHEILEQLSTLEARLAGGDAGGGSGGDGPGGGGRARGTATTDGPASRNQTQLLSPATTATQPSNTAGSA
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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: 430
Sequence Mass (Da): 46563
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A0A524P385
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MSSTRPPLILASASPRRREILSSLGVTTQVHPSGVDEKALHVVDDVEFVRAAARMKLEDVLAACAHPDAFVLAADTAVCVDGQRLGKPSDDADAVRMLELLAGRDHVVRTGIALGRVGEGVLECRVVETRVSFREASRAELERYVAAGESRDKAGAYGVQGLASGFVTRLDGSYTNVVGLPAAETVSMLLEHGALDRWP
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Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Sequence Length: 199
Sequence Mass (Da): 21189
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A0A956SUN2
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MAPTTAEDPKARRRRLLQLTHDQAFREGEFKLASGKVSDCYFDGKQVTFDPEGATLFAEAILDKIAAVDLDAIAGPESGALSIVAAVIVEGRRRGKSIRGGYTRKEPKGHGLRAMVEGRVRAGDRVVVVEDTITTGGSTLKSIRALEAFGARIVKVVCLVDREEGAAETLAGYEVDPVFTKAEVRAYAQGTP
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Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
EC: 2.4.2.10
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Length: 192
Sequence Mass (Da): 20590
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A0A2N2DQC2
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MTKQLLGKPVADVLRQSLREEIREIKAQGGKTPTLAILRVGDKKDDIAYEERLKKNCLEMELDCRSVSLPEAAPQETFLATLDALNKDDDVHGILVLRPLPETIDSRLVSRAIDPSKDVDGMSFENTARICSGDTSALAPCTAVAVIEILRHYEPSLQGKEIVLVNRSMVLGKPLAMLLLNENATVTVCHSKTADLSAVTRRAEIVVTGVGRPGFFDESYFAPDAVVIDVGINFDDQGMCGDVVRGLGTVAAVTPVPGGVGTVTSVVLLHNVLRAMKLQNGGRY
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Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Length: 284
Sequence Mass (Da): 30605
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