ids
stringlengths 6
10
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stringlengths 16
1.02k
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stringlengths 117
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A0A3M2F1H2 | MGRGDIVKQEGRCGVTFPRGFRVASARAGLYPDADRDDLVILAAEKPVVTAAVFTTNRFVAAPISYCRDLYRDRRRFRAVVANAGNANCGTGRAGEEIVHATARVAAEGLGTVEEEILVASTGVIGRVPPREQLLAGVSRCLERLAAEPDPTAAEKAARALMTTDTVPKLTERESESVRWGGMAKGAGMIHPCMATMLAFITTDAVADPDTADRTLRAVVDRTFNTISVDNDMSTNDMVLLMASGASGKKPATFEEDLEMICRDLAEQIVRDGEGATRVARIVVSGAVSEKEARRIADAIGTSFLFKTALHGGDPNWGRILAAVGRSGVAVDPENVSISIGENLLFRNGEPCAENQEKCLRAMREKVVVVTVNVGRGHGEWTHLTCDLSKEYVTINADYTT | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate
Subcellular Location: Cytoplasm
Sequence Length: 401
Sequence Mass (Da): 43026
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A0A3B8T8N6 | MTQSKTPLALLILDGWGYREAAENNAILAANTPNLDALRAQYPNTLISGSGLDVGLPDGQMGNSEVGHVNLGAGRVVYQDFTKITKAIADGDFQTNPVLVAAIDKAVAAGKAVHLLGLLSPGGVHSHEEHIFAAIELAAARGAKAIYLHAFLDGRDTPPRSALASLAKADAIFAKAGVGKTATMVGRYYAMDRDNRWDRVEQAYQLMTQGKGLHTADNAEAGLAAAYARDENDEFVGATVIGEPVTMDAGDTVIFMNFRADRARQLAHT | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.12
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 269
Sequence Mass (Da): 28486
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A0A7C4YR92 | MLITIEGIEGSGKTTQAIKLESYLKSSGYPVLRTFEPGATQLGSKLREILLNESSIKLHPVTELLLFSADRAQHLFEIVIPALEKGTIVICDRFIDSTSAYQGGGRSLNLEEIQQIHNIASLGITPNRTYLLDLPPEIGLSRIMKERNKLDRLESEALEFHTNIRKTFLKLAEYSPERFLVIDATQPEDVVFEIIRKDITRIIDEQSVRKK | 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: 211
Sequence Mass (Da): 23878
|
A0A947MNU1 | MTLAATPARAEWVSRTEVWLHTDVTVTIPASKAASLAFDAVFAVMAEVERLANEWKPESPIGALNRSAGGDAVVLPPSVFALLDASRDLAVKTGGAFDPTWAALWGLYDFDAGRFPDHATLAARVALVGHEDLELDRAHSSARLRRRGMAVGLGGIAKGWALDRARDQLYALGLNDFLLVAGGQVTASGSKAGAPWKAGLRAPRGSPDDLFAVLPLPVGQRSSSLSTSGDYERFFIKDGVRYHHILDPTTGRPARGLQSASVVAPSGTDADALSTAVMVLGKDAGLRLIESLPGVGAVLVDAAGTVHVSKRLATHVQVLDTVR | 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: 323
Sequence Mass (Da): 33926
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A0A2N2LSR6 | MPFRAGLLFPYPRPERSGGRAKTGQCRLRRPIEYMTTPREILHRYNIRPSRRLSQSFLVDVNTIHKIATAGRILPGDVVVEIGAGIGVLTKDIAHAAGHVIAVELDPRLVEILHDQFAGCGNVEIYSGDILKFDFAYKSDQYKSKIKVIGNVPYNISSPVIFHLLSYRAVITNFTLMLQKEVVERLVSAPGHKSYGVPSVLLQMYADVERLFDVSANCFYPVPKVASSIITGEFREKPLMELTDETFFNRLVKASFAQRRKMLINNPVLKY | 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(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
EC: 2.1.1.182
Subcellular Location: Cytoplasm
Sequence Length: 271
Sequence Mass (Da): 30584
|
A0A0T6B058 | MEDSLEDLSNSFSEQDEEELIGKLKMVDGIEPPHQRHLDVLFKIFGHKEFRPMQWKIINSIINDRRDNCAIMATGYGKSLCYQYPSVYCGGITIVISPLISLMEDQVLSLTVANIPACFLGSAQSQQKKALKDIFDNKYSIIYATPEFCCGEYGQQLLVDMDKKLSITLIAIDEAHCISSWGHDFRHQYRQLAKIRNLVPHVPILAVTATATPKVRNDIISSLQMRNPQIIYSGFDRPNLYFSVYLKENRGIIGDLRNAMTRNDGEWAFSGSTIIYCNTRKQTEQITDLLKNQGIQCLTYHAGLTIKQRREIHEQFVRDKVSVIVATIAFGMGIDKPDVRNVVHYGAAKDMESYYQEVGRAGRDGQPANCTIFYSSADLEVLRSLRELSYATEMTIKQKEAMVQNFWRYLETTSCRRQFILRYFGDTSSIIDQAKLNCCDNCTRKLKQKNPVEYEEVNSNGLIDITDYAHTFLSSIAIMGSGLGLNTYILFIRGSKGSKMPEKHQSHPLHGSGKHKTDDWWKCIARLLEHESYFKKQTVKRPTYSYCCLSLTNKGKQFLQDVLKDREKVQILVEPPPDLRVLLKKKNSTPYDPCWSSQNSAWIKPDSSNLVNTSNDKSDIQHNKKIVDIEDESQKEERMKIYRELLNKRSQLASDLNCMPYMIASNEILMNLARLRPRTMDMIRELKLDGFTEAKINKFGEEFIGVIRPFCPVKNKKSIQDILAEHPFDNTMFSPTTELTYNMFKNVKSIEDIANARKLAPSTILSHLTNCMKLGYPIKLKDLNVSNTVKEMIIGVLRRMSPSEDKKFIWIKDRCPEEVTFDKIKA | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 826
Sequence Mass (Da): 94761
|
A0A3B8T422 | AQFNIKAYPKKDAPGVYVNEQKICSIGLRIRKGCSFHGLALNVNMDLTPFNHINPCGYAGLEMTDSARLGGAADLARVGQDIVAHFCTLIGVQQVQFREGFDE | 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: 103
Sequence Mass (Da): 11242
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A0A0T6BBN4 | RMEFGDSSNHLRQQANLNIHLEKNKLCLSGIVCTIGPASTNANILLDMMKSGMSVARLNFSHGSQSEHTDRIKVIRKALELYKTASNETYPLAIGLDTKGPEIRTGNIMQGSQSKVEIQAGTYVRLTTDPRYKTMSTNRIIYVDYQRLPQVIKVGDTVYIDDGKIILNCTQIQTDIIECKVINGGMLGSKKGVNLPGFKLGLPAVSEQDKEDLSWGIRNNIDMVFASFIHTAGDVRDIRNALGPLGKDIWVIAKIETQEAVDNIEQIIEASDGIMIARGDLALQIPIEKVFLAQKSIIAKCNLRGKPVICATQMLESMLDNQRPSRPDVSDISNAILDGADCVMLSGETAVGKYPVECVKTMTKICKEAEAAVWNGRLLQEMLANSSSLDERNAISAASVVTATLCKASAIILSSGSSVELSELISKYKPRCPILAVTKDINFAEKIGLFRGVHPIISETGTFSTGLEAQQLLQNVLGYVKSKGFVNNGDRVLFLRKGIKVSKSYKDRFLLEVLTVTDLNEK | 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: 522
Sequence Mass (Da): 57186
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A0A955VKT8 | EGCHAEVDLRRTTAPAVFSWLRRHGVSLDEMARTFNCGLGLILVVAPEQTDEALELLGEGALVGAIDEGERGVSVRGLEVFDG | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
EC: 6.3.3.1
Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Length: 83
Sequence Mass (Da): 8879
|
A0A3A4K2A6 | MPRVADSGKRASGVAGPACAFFSPVAFRGKSLTSHDDSQTASPYRSGFVTIIGRPNVGKSTLLNGLVGERVAIVTPKPQTTRHRLLGVRHFAGGQIVFLDTPGVHKARGGLNEYMLDTAMAAIADADLVYLMVEVGPGFMNKDVPGDSNRRILEAIAAAGKPAFLLINKIDLVDKRELLPFIERWRAVHSFDEVFPVSAESRDGLETLVAATVARLPQGPSFYDGETITDRTMRFLAAEIVREKTMLLFRDEVPYSIAVVIDEFRELDSGERFHIAATVIVERESQKPIVVGKGGQTIKKLGEQARKDMEVFFERPVGLKLFVKVKKDWTNDPRALAELGYK | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Subcellular Location: Cytoplasm
Sequence Length: 342
Sequence Mass (Da): 37610
Location Topology: Peripheral membrane protein
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A0A3A4K165 | MLKMIDVDQALSLVLEHAAPRAAQTVPIAQSLGCVLAEEIRADRDYPPFDRAMMDGFAARVADAGKRVKIVGELAAGAETDRKLTDGLAFEIMTGAPCPAGTQAVAPVEDVRREGDQVELPPALRVGNHVAPRGSECRAGATVLPAGALVTPLALANLAMFGRETVRVIARPALAIITTGGELCPPGETPSGSRIRNSNGPMLAAMAGLAGIARVGLAHAADVEAELLDRLGAQADADIVVLSGGVSAGKYDIVPHVLEAHGVELIFHKAKQKPGKPILFGKKGTRLFFGLPGTPQGAYLGFNRYVRAAIARMSGLPWARPVFQGRLVAPLASKGDRFQFILARVRFTEQGWEVEPTPGQGSSDIYAPASANAYIRLPGGSLSLDRGEIVSFEPIGDVA | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 399
Sequence Mass (Da): 41839
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A0A956IA29 | MSVVAFQPSRDAQAVDAVAEVLGVELGEARAGWLRFAELVGQWGQRTDLVAAESAQALAEILFLDAAALVNLVPPGATVLDVGAGVGAPTIPLALLRPDLRIELLEPRRRRVTWAATAIGSLGLASRAKVVEGKLGDEGHAPVDVALSRATFAPDEWLRRASGFAGRVVVLLGRGEEPASNGWKVEGDRAYEVPSSGAHRRAVVYAPDA | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 209
Sequence Mass (Da): 21958
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A0A2E5HPJ1 | MSRLRIVFMGTPDFSVPSLKALIDGPDEVVAVVTNPDRPAGRGRRKPVPSPVKQVAVEANIPVLQPRSVKKPPFREELAALNADLAVVIAYGKILPQAVLDTPRLGCINVHASILPQLRGAAPINWAIVRGHAETGVTTMQMDAGMDTGDILLIDRIAIQEGETAGELHDRLAPLGAETLMKTLERLVAGTLTPQPQDDAAATYAPMLSKRDGALDWSATTAELVGRVHGFNSWPGTFTTVLEGEDERTRGIRFKVHRAKAVEGYTDSPEAPGVVLEADVEQGLIVRSGDGAVSLLECQLPGRRALTIDPWLHGFNLSRGDRLGAPES | 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 Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Length: 328
Sequence Mass (Da): 35166
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A0A7Y5GST7 | MNADWLWEPVRVVIDVTIVSYLVYRTLLLIKGTRAIRMLAGIVILILLFFVSKDEYFDLPTLNWVLDKFIASFIILIIVVFQDDIRRALSQVGKKPIVGGGQNVDTDTLQEEVVRAVTALSAQRLGAIIAIERSADLSSYTEEGVPIDGRVSRELLFSIFLTSHQNPLHDGAVMIQKGRIAYAGCFLPLTVNPKVDRELGTRHRAAIGLSEETDAVVLVVSEESGAISLALHGELMRDFDAQSLRRVLNDSFGGMSRSTLWRRFGRAKGGSRTK | 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: 274
Sequence Mass (Da): 30413
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A0A2D5EPU6 | MSARDERKKKRKRKGASASKPRRVSERGAAKKGTAKKDTAKKGTAKKGAAEKGAAEKSAADGNQPREDGTHEAPALAPRQRFGHLLLAALGGALQCLGFAGFSLWPFALVCFLPMFYVVEVERPTRFRRLFALGLAHGFVGYTGGYYWLVDMLENFSGFEGWPNWAFASIFFLYQAGQHVLIYWVYARARRRGWPILGAAVASLLSFELIYPVLFPSFLSTGFHDVTPFIQIADLGGPMLVSAVVMSVNAALFELLWAWRRGPLPRRSPAIAAAAVALTLAYGYWRIAEVDARAEAAPKLTVGVVQVNMGIFDKRADPLEGHRRHLVQSRRLERNHDDLDLLVWPESAYTFFLREGVQNLKRRVLGPLSTPTLFGGLARREGEERMLAFNTAYLIDGAGDVLGTYDKTYLLMFGEYLPFGETFPILYDWSPNSGRFTPGDHVRPLELGDVRISTLICYEDVLPGFTREAVREGDPHLLVNITNDAWFGDTHEPWIHLALAKFRAVEHHRALVRSTNSGVSAFVDPAGRVLHTIGVFEQGEAAEELALLEGDTLYLVLGDWPGWAALFAMVWMSFVGRRRREDPAPEGDADDAAAAA | 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: 596
Sequence Mass (Da): 66084
Location Topology: Multi-pass membrane protein
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A0A2D5QM67 | MTADQFDQERKWSTQDFDFDLPDSLIAQRPSEKRGGSRLMCLNANSKAEFKSFVDIVDAFQGDEVLILNDTKVVPARLYGKKETGGKVEIFFLEPLGDSQFLAMTRGKLKPGHRVKLALDAQATLMSRDEHGRAIFDLHLSSRFTDDHEGEVALWAWLSEAGKLPLPPYIEREADDLDHDRYQTIFAKEPGAVAAPTAGLHFTQDLLTALQNKGVSIAYITLHVGPGTFLPVKTNQIDDHMMHSERYSVPLSTQDLLRSQRPVVAVGTTCVRAIESFMALCEQDPETWGSEGLHATDIFITPGYQWRAVDGLLTNFHLPQSTLLMLVSAFAGYEQTLDAYRRAIEEKLRFYSYGDASLFWRPNGRWVHN | Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Catalytic Activity: 7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-methionine = adenine + epoxyqueuosine(34) in tRNA + 2 H(+) + L-methionine
EC: 2.4.99.17
Subcellular Location: Cytoplasm
Sequence Length: 369
Sequence Mass (Da): 41554
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A0A2A5EAX9 | MSRRSLTERIRRGDPIPLPLSVLLQSATPITRVGMALRKRKPVVKIDAHVISIGNITAGGTGKTPAVIERAQAELDKGKKVGILTRGYHAQSGNRTVVSXQVSSEDRFAEXGDEAALLLKRVPGVTVFKGADRIHTARLAVEQHGCDVLILDDGFQYVPLHRDENILIIDATNPFGNGHLLPRGILREPVDATERASEVILTRCDQAKEIASIIETLHTHAPDIPVRTTSHEASGLWQVNSGXXWSLDRLHEQSVKAACALGNPEAFLATLNGLGVSVTEFHAYPDHARIPDELVNTDEMLVVTEKDAMRMKSPGPGVVALAIALQNYSLD | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
EC: 2.7.1.130
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Length: 331
Sequence Mass (Da): 35930
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A0A2E8S3S0 | MTSSTSDGRLTLALPKGRILDELLPLFQQASIGMPDFAASPRAMVFDAPELPIRVLLLRGHDVPVYVAQGVADVGVAGQDVISEYDADLYSPLDLGIGLCWMSLIGLPGHDPREMQLGRPMRVATKFPRIAMRYFEKRGQSAQMLHLHGNVELAPLCGLSDCVVDLVSTGETLKRNGLVDYHRFQRITSRLVCNRAAYRLRFDAVNDMIGALRTQLIGS | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
EC: 2.4.2.17
Subcellular Location: Cytoplasm
Sequence Length: 219
Domain: Lacks the C-terminal regulatory region which is replaced by HisZ.
Sequence Mass (Da): 24106
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A0A956LMZ2 | MNVIDVAIVTALASGSAPVVDIDGTMWIQLGTFLLLMFILQPLLFKPWLETRQRRIEAIDGALESATALRERADAVQHQYDTQKAEAERAALELRSHERREAETTRQQALTEARAEAAHHLETAREQIAKQGAVARESLQRRVDELAQHVANKILRRAS | 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: 159
Sequence Mass (Da): 17856
Location Topology: Single-pass membrane protein
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A0A956R416 | DLGFITDANFGTARPLPGWEARCREAVAALPQSELPIVTGFVGKTEAGEITTVGRNGSDLTASLLGAALGAEEVQIWTDTDGVMSADPSVVKGARNIPHMRFDEAAELAYFGSRVLHPSTLLPAMAGDIPVRVLNTNRPEHHGTVIRSDEVDNPSPVTSVAYREQQSVLYLQTTRMFAQPGFLAKLFAILGRHRIDVDVVTTSEVSVSVTSGDRRRLEAALPELAALADAGGENGGGTCELRHGKTVLVVVGQHLPQRPGIGARILAAIADAGVNVEMVSYAMDSINFTLVIDDGDIDRAVPLLHSLLFAG | 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: 311
Sequence Mass (Da): 32966
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A0A1A0XQ80 | MDKYSAEADKAPLNIAILGLGYVGITAAACLLSQGHTVVGVDVNAGKVQQAARGISPIAEPGVPEMLQSGFDDDRLSATTEVPELSGFDCVIICVGTPSAPDGSHNLSFILEAARQVADSISSGEQSQRTEPISVIFRSTFRPGTMENVVVPLFQSKLGDSYSDYVDLVYNPEFLREGTAVSDYFNPPKIVVGSAKQSLPEAVKKLYSGVNTPHYFTTGFREAELTKFVDNTWHAVKVSFANEIGRICSAYDVDSSVVHRIFVSDSKLNISQYYLKPGGAFGGSCLPKDVRATQYIASAAGIKCELIDSVLTSNESHKQHQLMRVRRLASPPARVLIVGLAFKSGTDDLRESPNVTLAADLVSDGYEVSIYDPIVKSANIVGQNFGYLIDRIPNVSEKLLSGENIDAGDYDLVVVNNSLVADLDLALAKKIVDLRVVTGGLSGIESHG | Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.
EC: 1.1.1.22
Catalytic Activity: H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate
Sequence Length: 448
Sequence Mass (Da): 48013
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E2CIF3 | MTFSNERPFLLVGAGKMGGAMLSGWMAEGVDPSAIIVSDPGPPDEVREVLTKHGIKLVDRPPEDVQPGLVMIAVKPQLMDVVLPGLKSVVASDTLVLSVAAGTPVSVFENAFGRVPLVRAMPNTPAMVKRGITAAFPTAAVSEAQKETVTQLLSSIGQVVWLESEEQVDFVTGVSGSGPAYVFWMAECLAKAGEDVGLPAGMARQLAIATVTGAGELMHQSDIDPSTLRQNVTSPNGTTAAALNVLMADDGLEPLVTAAVQAAVKRAGELAGK | 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: 273
Sequence Mass (Da): 28254
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A0A819A895 | MTQTSAAGSAKDAADQNFDYMFKLLIIGNSSVGKTSFLFRYADDSFTSAFVSTVGIDFKVKTVFRHDKRVKLQIWDTAGQERYRTITTAYYRGAMGFILMYDITNEESFNAVQDWCTQIKMYSWDNAQVVLVGNKCDLEQDRAVTEERGKRLADQLGLEFFETSAKENINVKSVFERLVDIILEKMSDASDESTATGQANNVYGNQPGAYNKGTARLTTMNTSEFEKNPLSNIILRSTYVPSENDVDKTFFLGIDEAGRGPVLGPMVYSAFFCDEKQLSILNDLGCADSKQLTEERRSSIFAEYEKHNNHLGFILKVLSPHMISTSMLRRDKYNLNDISHDAALELIQLALDQGINVKQVFVDTVGDPDKYANKIRARYPKIKVTVSKKADSLYPTVSASSICAKVVRDQIVQNWKIDEFDEEKQSIKYGSGYPGDPQTKRFLIESIDQIFGFPKFVRFSWSTASTIIENKCIKVTWDDDEDENATSKNTTKKRKSEVIETTTTTTTTTKTLFNYFSQKPSTRNDAANRRVPGSHFFRAAHVKPAVFST | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 549
Sequence Mass (Da): 62017
|
Q11BZ3 | MLARILAATARFGEIAAGAVLVAMTAYMLVEIVLRWTLGVSSNQVVEFVGYGLATMTFLGAAQTVRDGGMLRINLLLYFLPEGVRKAFDLLCIAIGIFAISFVGYYYCVDMYSSYVRGYETEGVIALPLWVPPLGLVLGSVLFLVEMVRQFIMIMIGGERFAESMAEAT | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 169
Sequence Mass (Da): 18490
Location Topology: Multi-pass membrane protein
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A0A4Q5X6T3 | MAKHLLAIDQGTTGTTALVMSTAGTTLGRVTRELPQHFPQPGWVEHDAREIWASVEGAVADALALANVSGADIAAIGITNQRETTLLWERDTGQPVHKAIVWQDRRTAPLCARLKAEGHEARVRELTGLVLDPYFSGTKLAWLFEHVPGARQRAERGELAFGTIDSYLVYRLAGGGASAPHVSDATNASRTLFMDLASLSWSEEMCSLLGVPRQVLPRIVPSAGVVATTRGVPGLPDGIPIAGLAGDQHAALFGQGCLAAGDAKCTYGTGAFLLVNVGSRPVPSRFGLLSTLGIQAGGEVMYALEGSVFIAGAAVQWLRDGLGIIGSAKEVEALARSVPDSGGAQFVPALSGLGAPHWDADARGLICGITRGTTRAHLARATLDAIAYSVNDVVAAMREDLGKPIDRLRVDGGAVENDLLLELQAGISGLTVERPLDLESTARGAAMLAGLGAGIYADGRDAAKIVKLDRAFPATMRAEERAARLSAWHEAVGRARSTRA | Pathway: Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
EC: 2.7.1.30
Catalytic Activity: ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate
Sequence Length: 500
Sequence Mass (Da): 52387
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A0A524NPA5 | MKFLFVMDPIERIDITKDTTYTFLREAQKRGHENFYCGVQDLTVAGSHVHARSKPLEIGPVQGKHYRFGETLLAEAESFDAVFMRKDPPYDLDFFFATHILSLIDESKTLVVNRASGLREASEKMFILRFPDLITDTIVSADPDRILAFRADIGGDIVVKPLDGCGGMGIFRITHGDLNTHSILETVTMDGKRQIMAQRYLPASREGDQRLIYLDGEPLGTMLRVPADGELRGNIHVGGNCVAHPVGDREREICKRLAPALDQLGIWFAGLDVIGDRLTEVNVTSPTGIQEIDVLNHTNLEAKVIDFVETKCGARGG | 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: 317
Sequence Mass (Da): 35196
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A0A2F0AQI1 | MTIYLLNEAIAFPDPRKTDDPSGILAVGGDLSPARLLLAYSLGIFPWYDDAYSPILWHCPHDRFVIRPDHYRLGRSLRKAVNNFEGQFSYNRSFSEVLELCASVPRHDQLGTWLNAEMKTAYLKLHQLGYAQSAEVWRNGRLIGGLYGVTLGAVFFGESMFSVEPAASKALFAALAPRLWAAGYQLIDCQIYTEHLARFGGLEIERDTFLSELKTALAAKPEAIWPASVS | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-arginyl-[protein] = H(+) + N-terminal L-leucyl-L-arginyl-[protein] + tRNA(Leu)
EC: 2.3.2.6
Subcellular Location: Cytoplasm
Sequence Length: 230
Sequence Mass (Da): 25688
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A0A956KTX4 | MSDPAAAAPRCCFEVFTLFPAAIEGFSSAGLLGKAIEQGRVQVRCTDFRDFTTDRHRTVDDAPFGGGAGMVLAPGPVVRMLDQVDDRAARAEGTAAPRRVLLSPAGRPFDQAAAQRFASGSGLVLLCGRYEGIDDRVREHWVDECLSLGDFVLGGGEVAALAIIEAVSRLVEGVVGNPDSVRDDSFGGAGDAGLLEHPHYTRPADFRGHAVPAVLLGGDHEAIARWRHRQALLRTWALRPDLRPRQRLRPRHPIHLAVSPQARPDAAALTAVVRRHGVAGLAVVGAGPDELPAWPEATGGRAPVAIFADPKALRRRLRRGGTGEPRLVVLAHAPPPASSLAPVCERPEVLLDLLAEAPGEPLGPVVLWTGPGPVPPGLPVHAIYAPTDAAADDLTPGEDPADSSGLALGDVIAQSPGPRPRTAALAHAALTQLLDRG | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.228
Subcellular Location: Cytoplasm
Sequence Length: 437
Sequence Mass (Da): 45853
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D9Q2J8 | MEALQISLGITVRLVQYTPDAPRIVAAASKMSTSRKGSPELLKIDESEVETWIRETLKRGHLSPWEHSSYTFIVEGCSRVCSHQLVRHRIASFTQQSMRYTEASLREMALTAASKLGLECPQRPKGERAREVYACYSESLRRAAEGLSLEEMVRLASTAYVIPPSLSDEKRLEAYARGLLLATSTYYRLLSTGAPKEDSRFIIPMAVRTKLTFTMNGRELVASFLPLRMCTHAQWEIRHVAWLTWSELMKVHPQLFKYAGPSCVLLNNGQLEDPAGLEDYLSGKTRFVIAKCPELVPNKNIPSCLLFASRSLSGNPLEPESSAGEDETGGASE | Cofactor: Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as the reductant.
EC: 2.1.1.148
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H(+) + NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + NADP(+)
Sequence Length: 333
Sequence Mass (Da): 37146
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A0A3A4K612 | MFGLGMWEILIILALALIFIGPKKLPEIAQMLGKGLREFKRAAWDIKDAIDITPPPPQPPAPPQPPAAPPALPPAGAAPIQAAAASETPPPPAKTADSPTPESSSPDDSASSKPDATPK | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 119
Sequence Mass (Da): 12239
Location Topology: Single-pass membrane protein
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A0A9E3VKC6 | MLRKAIRTTAILILCSVTPIVSSSCAHVQREKESMVQLCTIDALMEGVYDGSFSIPEVKRLGNLGIGTFDHLDGEMILLDGICYKAQASGLVSRVNDSETTPFATVVRFRPDRVVTIGDTSSFKSFCAELDKQLPSANLFYALRIPCVLDSLKIRTVPSQTKPYPRLAQVVEKQSIFERKNVSGTLLGFRCPEYARGLNVPGYHLHFLSDDKSLGGHVQDFSGKEFRVQVDDIAEIRVVLPDDKAFLGADLSTHKAEELQKVEK | Pathway: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-butane-2,3-diol from pyruvate: step 2/3.
EC: 4.1.1.5
Catalytic Activity: (2S)-2-acetolactate + H(+) = (R)-acetoin + CO2
Sequence Length: 264
Sequence Mass (Da): 29239
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A0A955ZM05 | MSGIVVVGAGAIGGVAAGRAIERGHDVVACVRQGFRELQWDSPEGSRRLALGVVTDPRNVEPAAWVLLATKAHQVEGAGAWLSALVAQHTRVAVLQNGVEHAERVARWVPPERVVAVVVSCPAERVAPGHVVQRGPARFTVADDAKGRSFAELVGAEVTADFGRAAWEKLCLNVVSGALAALAGKPLPQIAHPQKLDLARGLARECARVARAEGVALSDDAATEIAERTVNVTRGGEPSIYRDRMRGEPLEWDARNGVIARLGARHGIPTPLSDKASALLASAHLERSRDLLPSLSESLLD | 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: 301
Sequence Mass (Da): 31796
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A0A956GI25 | MSEAPNTQEPKEPSGARLALTLAFAGLISGVALVFTYELTKPVIARNREAALRAAVGRVVPGAKSMRKLVWRDGALQPASAADKDAAVLIAFDARGAAVGFAIVTEGPGFQDTIRLIYGFDASTNTITGMEVLESRETPGLGDKIYKDPDFVKQFKKLSVQPSVKLVKKGKGSGTANEVDAITGATISSKAVIKIINTADKTWRSRLGTVDRNKVRAP | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 218
Sequence Mass (Da): 23142
Location Topology: Single-pass membrane protein
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A0A955X2J2 | MSEQSFTGLGVCAGIAFGKVHLVDRRRVTAPHFHVVPERRAQEILRFEAAVKVSEQQLDDLDSRAAGTGLGQVQALLQAHKMILRDAALLDATRQRISDEGMNAEWALQDTVRELKQLFDRLDHDYFKERRSDIDVVGDRLMRNLIGAETELLGNISEDAVVVAYDLSPADTVSLAKFKAKAFVTESGGPTSHTAILARALDVPCVLNVHGIMDVAGFGDDVIVDGMAGEVVLRPDKVASSRFKGVARRREKARDALLVDRDLPAETTDGVQISLLGNIEVTQEIEGILTAGGEGVGLYRTEFLYIEQPSLRGADAHYAAYARVAERMKGHVVTIRTVDIGGDKFLRRATDEEDTRAALSPPPAENPALGLRAIRLSLRDEGPFREQLEGILRAAVHGKVQVLLPLVTELEELRRTRQIITELEADLEARGRPHVKNIPVGIMVETPASAVVADLLAREADFLAIGTNDLVQYTLATDRSNEDVAYLYRPCHPAVLRLIDSVCRGADSQGIPARICGEMAADPFHTPLLIGLGLRSFSMTARSIPVVKRMIRRLSAAECREFAQEALKMSCARDVETALAERLKAWSPELFAGG | 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 transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
EC: 2.7.3.9
Subcellular Location: Cytoplasm
Sequence Length: 594
Sequence Mass (Da): 65022
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A0A956FH18 | MDPRTQTVEMTVSDEHAWARVDAFLALQMPWRSRRSLVELLASGAVAINGRPVLKKAHRLAPGDVIALRVPLRPEAEIDLGAIELRIVWEDDDLVVVDKAGDLAVHPASTCQYRNLQARLLHHYRHERPDPRVEPCVLHRLDRTTSGVVAFAKRRELVDGYTRQFAARTTSKQYVAIVHGTVAGPRTIERPIHVPPDRLSWVGEGGKPSRTDLRVLATAGGCSRLGITLHTGRRHQIRVHLAAEGHPLVWDELYGDAPRDEGWPPDARPLLHAASLELDHRDGRRLRFEAPVAEDMERAWAALGGASLERIEA | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 313
Sequence Mass (Da): 34945
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A0A956HK04 | MASKRRSRRAAKGRREQRDELQDFRQIQPGAAPGTLIIEPDAPAPQLSAYAYGADAIVARDPMTLAELPALLGSAPVVWVNVVGLGDVAVIQELGRIFDLHQLTLEDLVHVQRPKLEIMGDRALVIARAPKLDGGVKTEQISLLVGDGYILTAQTGEQRGLFEPVRVRLVTGAGRIRTMGADYMLYALLDTVIDSTFPLLEELGDELELLEDDILQRPEPDCLHRVHKVRHDLLTLRRAVWPLRDVASQLSRTPVPTITDETRVYLRDCYDNVIRAIDLIETYRELSSSLSDLYLSSVGQRTNEVMGLLTIVATIFIPLTFLAGVYGMNFDRASPWNMPELGWRYGYPAFLVANVVLAALMIYVFRRRGWLGGRAP | Function: Mediates influx of magnesium ions.
Subcellular Location: Membrane
Sequence Length: 376
Sequence Mass (Da): 41954
Location Topology: Multi-pass membrane protein
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V5V549 | MTAVTPVVSPYEPTSRGAIIAELYQVTKSFGGALPCLHRVSWQLRRGDFYFLTGASGSGKSTLLKLLCGQLRPDHGIVRLFGEEVNPQQDRRMAQLRRRLGVIFQDFKLLGDRSVAENVAFALLVRGIPKAEIQQRVQTALKLVGLSHKANANPQSLSGGEQQRVSIARAIVGGPELLLADEPTGNLDPQTSQQILALLHRLHQHGLTVLFTTHDLALTRLVPHRILHLHHGKLEFLTHP | Function: Part of the ABC transporter FtsEX involved in cellular division.
Subcellular Location: Cell membrane
Sequence Length: 240
Sequence Mass (Da): 26491
Location Topology: Peripheral membrane protein
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A0A2M6X8N6 | MTLYRKYRPQKFSDVEGQSAIIQTLKNELASGKIAHAYLFSGPRGIGKTTVARLLAKAINCRNKKSAAERRMGKVEPCNRCVSCQEITSNGSLDLIEIDAASNRGINEIRALRENVRFAGTANASKIFIIDEVHMLTREAANALLKTLEEPPANTVFILATTEAHEVPDTVLSRCQRFDFKKLTIAEIEHHLEKILKQEKTSLDPAILNLLAVKADGGGRDAVGLLGQILAWPKKDLTLAKVADFLGAVDWSRVADFARRLAIRDQAHLIREINKMVSDGQDLFNFTEKLIDYLRMMMLAKIEEDLADKEGSLTAAQKQEMLALAKEFFLKDLASLLRIFSSAKNNLENAPISQLPLELAVIEYAGAQDVVLEAQAAEAKPAAPILPPKMEIEKIAPIDSPLKPAASMEKVGEKWADVLKAVEPLNYSLCAFLKLCQPVAFRDGSLILGFPRDFHRNIVSQARNKKTVETVLDQILGGKWRIQCEKVEGRGENHFAREALEVLGGEIVR | 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: 509
Sequence Mass (Da): 56398
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I4ECS3 | MVFSKLFRRRAKPEPKIEAGLKKTRRGIFQDIAALFERSEITEDLYDDLEALLIQADLGVETTVELLDNLRARIDRERIRQPSDAREALRTEMIALLENATRNRKIKIYQRGVPFVTLVVGVNGTGKTTTIAKLAKYHQNQGRSVLLVAGDTFRAAAIDQLKVWGDRLDIPVIAHAPGADPGAVVFDGMQAAYNRNADILLVDTAGRLHTKFNLMEELKKIRKVMQRHVAEAPQEVLLVIDATTGQNGLVQAKKFAEAVDITDIAIAKLDGTARGGIAFAISRELGIPISYIGTGEQVTALAEFNPETYVDALFFGDEEEL | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
Subcellular Location: Cell membrane
Sequence Length: 321
Sequence Mass (Da): 35495
Location Topology: Peripheral membrane protein
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A0A9D7D5M4 | MSDSKKDDKKDEKKEAPVAAKPSKVGAILGVVLPAVFAGGAAFGGAKVAGAGHQKTVVVEVPAAPKPPGPTLPLEAFLVTLSDTSGKPHAMKVVLAIEFSNTTKEEVLKPLVPRVRDAALGYLRTVSFDLASDRTKGEVIRKELLEHIKKSGAATAEQVLITDFVLQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 167
Sequence Mass (Da): 17533
Location Topology: Single-pass membrane protein
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A0A2S7UUD7 | MRTDISYNLSSEKTPIVLLHGWGMNKTIWSAVVKLLPQDIQSRIRCLDLPGYGDNRLELADYNLPALTHWLASEITSPSIVIGWSLGGLLAQNLAFHSPEKVTKVGLIASSPKFMQSDTWAGIKPDVLTLFLNQLSKDHVKTVERFLAIQAMGSESARKDITALKNVVLNVELPSQIALQEGLRILQDVDLREQLSQLTCPVFALFGKLDSLVPIVVEQELKNLNANIQTSCFNKSSHAPFISDTAKFNTWLIKNIE | Pathway: Cofactor biosynthesis; biotin biosynthesis.
Function: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.
Catalytic Activity: 6-carboxyhexanoyl-[ACP] methyl ester + H2O = 6-carboxyhexanoyl-[ACP] + H(+) + methanol
EC: 3.1.1.85
Subcellular Location: Cytoplasm
Sequence Length: 257
Sequence Mass (Da): 28577
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A0A2D5EMY4 | MHLLNALLSEGSIIDLDGTFFIQFAIFWVAFFVLRSLVFKPLVAVFEEREEAIDGARRDAKQFAREASEKEAHFDKELHKVRTAAGEERDALRTEAKHLEGSILEKVRAETEKSLKEADEQLSHEAKRARQEIQATTPALAKQIATKLLQREVR | 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: 154
Sequence Mass (Da): 17572
Location Topology: Single-pass membrane protein
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A0A5J6NVA8 | LIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAVNFITTIVNMKPPATTQYQTPLFVWSVLITAILLLLSLPVL | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 167
Sequence Mass (Da): 17856
Location Topology: Multi-pass membrane protein
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A0A7C7U7A1 | MSRGDAAGCTHRLGNGHSQPCQSAHHLGDRRGPCDCRRRRRHSQRRRLRTGTRSHGATDEYRHRSREGAGQDGPGYAIRGGCGPPRLRIRAHAPASLRFGVEPSRRNRELLTRIRSGRTRLAKDSPAATPWNAPRPILCLVVDRAASRRPLVETVAEACAGGVDWLQLRDRELEGADWLQWGEELAAAARRSAPKIRILVNRRVDVALAMGADGVHLGFDAMTVADARPLLGEGALIGASTHGVAEVRALSNSRIDYVHLAPIYPPYSKPASRPPLGTEALAEACRQGIPVIAQGGIDPQRCSAILQAGAAGVAITGTLLGAENPQKTAEALRAALDQPL | 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: 340
Sequence Mass (Da): 36514
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A0A0S8HW47 | MAVLEILHYPHPVLKQKTRPVQKVDEEIRQLVRDMAETMYSAPGVGLSANQVGYPLRLAVIDVTPVDQPKNLLVLINPEIVSLEGECTWDEGCLSVPDCNEEVKRSKKVVVRYRNLEGETAEIRGEDLLAVALQHEIDHLDGFLFIDRLSPLKRRLVKKKLQKKEKGEKKV | 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 Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
Sequence Length: 171
Sequence Mass (Da): 19444
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A0A951TB66 | MAAGRENIPRRSAAPPSKGDGGGASPGLSALADAVRAEALALGFDACGVAPAEAERDDGFDAWLDAGYHADMYWMPRTRALRQSVETLLPGCRSVVVVARNYNHPRPPAPEGAGKISRYAWGRDYHRVLIRPLRRLGGFIAAHQPDAAWRAWMDSGPVRERAWAARAGIGWVGKNSLILRRGMGSWFFLGVLLTTAELAPDGPASDRCGSCRACLDACPTGAIVSPRVVDANRCLAYHTIENRGEIPPEIQRQSSGWVFGCDICQEVCPWNLEVPVTTEKEFAPRPGTANPMPGELAEMDETAFSERFNGTPVRRAKLEGMRRNARMALDNPAK | Cofactor: Binds 2 [4Fe-4S] clusters per monomer.
Pathway: tRNA modification; tRNA-queuosine biosynthesis.
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
EC: 1.17.99.6
Subcellular Location: Cytoplasm
Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA
Sequence Length: 334
Sequence Mass (Da): 36273
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A0A955UR68 | SGQTVDAFWTSIQHCDPWSVGVNCALGADAMRPHVEDLSRLAPCWVTCYPNAGLPNAFGGYDELPADTARVLREMADGGLLNVVGGCCGTTPDHIAAIARIMDGVAPRVPVVPDTTRSTYSGLEPYVIGPDSTFTMIGERTNVTGSRRFADLILNGDETAALEVAAQQVRNGANIIDVNMDEG | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.
Function: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
EC: 2.1.1.13
Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine
Sequence Length: 183
Sequence Mass (Da): 19366
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A0A418Q915 | MARRLIEGYQDNLSGLKMGPTCRFDPTCSSYALEAYSRHGFVKGTLLTIGRLARCGPWHPGGWDPVPPRWPRRRSRGESRTV | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 82
Sequence Mass (Da): 9288
Location Topology: Peripheral membrane protein
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A0A2E6VRT2 | MNSLRDDSKKTSFEIFDRIAKSYDLANRVLSFGLDAGWRKKVGTFLPHRTRLKLLDLATGTGDQIIMLCDSSHDIESAVGMDLSEEMLALGRKKTSRFNGKVKMKTGDAVQLPIKDAQYDVITISFGIRNVSDVPASMKEMYRVLNKEGKALILEFSMPENSIFRLGHVFYLRWVVPVIGGLLSGDYAAYKYLNTSIEAFPHGDAFCKLLKEAGFEKVQAHPVTFGIATIYEAYKKQTEELSS | 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 menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 243
Sequence Mass (Da): 27235
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A0A956J1N8 | VLLCLAEIARGRDVLVSRGELIEIGGGFRIPEMLEVSGARLVEVGTTNRTRLADYERALNDNTACILRVHPSNFRAEGFVARPLLSELSALAQRAGVPLIKDLGGGRVSELGELSRHEPSVQQCLDAGADAVCFSLDKLFGGPQGGAIVGREALIGRFRAHPLARVLRVGKLTLGALGPVIRAHVTGASSEVEVSRMILLSSAALKQRAERWLEALDDCPLALSIEPTSGAVGGGTLPGVELDSWALVVRGVKPHQLAEVLRSGDPAVLARVQHEALWIDARTTGIEQDASLLEAFRLVATRLSRATSQS | 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: 310
Sequence Mass (Da): 32959
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A0A4Q5XFZ4 | MSFPKDAGVLLVAHGTVENLDDLGAFVARIRHGRPAPPGLVEELRGRYEAIGGSSPLLQTTREQAVALAKRLEAPVLVGMRLWEPGVEQALAGAAALGLSRLVVIALAPFSQHVYWQAALKIAQAAQTPIQLVPSPPYAEEPEFVAAHAELITRHAPEAAPLVLSAHSLPRVAIERGDPYARLVEGAANAVSARLGRPVRLCYQSQGADGGAWLGPDVRETLSALAAEGHREVAWAPFGFLADHVETLYDLDVEAKAIAAELSLSLVRVPALNLHPGLTAALATVAIRSISTEASG | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
EC: 4.98.1.1
Subcellular Location: Cytoplasm
Sequence Length: 296
Sequence Mass (Da): 31175
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A0A2E5HMF8 | MLSVDEARAIILSAVSRGERELVAVTAAAGRVLAEPIRSTIDHPPFHNSAMDGYAVRWDEVHRATPDSPIALPVTLDVPAGEAPATLPPGGAARIMTGAPLPEGADTVIVREDTDESRPGQVLIQGLPDKGRGAHIRWRGENVAAGDLILDAGAPLRGGEVGLLAMNGRVMVPVSRRPRVAIVSTGDELVDLGEQPGPGQIVNSSGPMLAALVAEAGGDPWLLPIARDTLEATRARFQEALGGADLVVSMGGVSVGDHDVVKVVLGELCDGLEFWKIRMKPGKPLAFGRSRQGGTPLVGLPGNPVSSWVSFLQFVRPAIRKALGLARLELPTVQARLTCAIRSPGSRLEFQRGRLEPAEPGSGAPFSFTPIAGQGSGNLMSLVQVDGLARIPTGCSSLGAGEVVTVEVVGALHGAPVRV | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 419
Sequence Mass (Da): 43531
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Q67RY3 | MAETRNLILEIGTEEIPARFCAPALEQLKENAAKALAEARLDYELVDVFGTPRRLVLYVRNLALRQRDVEVEVKGPPRKIAFDAEGNFTVPARKFAEGQGVALEELEVRPDEKGGEYLWARKRIQGESVETVLPPLLAGLVTSIHWPKAMRWADRELRYARPIKWILALLGDWRVPFDVDGIETVSTTRGHRVLGPAEPIAVSDADDYFAKVAGGYVMVDQAVRKQVIWQQVTAEAARVGGFVRRDEDLLEELTWLVEQPTAFAGSFDPAFLEVPAEVLVTTMKDNQRYFPVYKAEGSEELLPYFIGVRNGGHEHLDIVRAGNEKVLAARLSDARFFWDEDRRQPLESFNARLKEAVFQEKLGTQFERVERLVSLSRPIAQALGLSPEQEEQAARAAWLCKADLMTRMVFEFPEVQGYMGKQYLLHQGGDPAVAEAIYEHYLPRGAGDDLPRTGPGIVVALADKLDTLAGYFSIGLIPTGSQDPFALRRAAQGVVQTLVENGLRVDLAALVSRAIEQYRLPGEAAVKTHSDLMEFFRARVKVLMEQREIRYDVIDAVLAAGFRDVTDAVNRAEALAAVMAEPEFAAVTGAFKRVANLAGKANEAGAVSAEIDPELFTEPAERDLYGAFVDLRPEMKRAYEAGDYRTFYHLATRLKAPVDAFLDTVRVNVEDEKVRANRYALLQALGGLLSAPADLSKLAG | Catalytic Activity: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
EC: 6.1.1.14
Subcellular Location: Cytoplasm
Sequence Length: 700
Sequence Mass (Da): 77795
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A0A3M2F4A2 | MMLPHAEEAERSILGAILIDPSMVNLAIDLVSPNDFYREANRIIFESILELAAKDVAADTIAVADHLQSRGQLERVGGYAYLGQLAAETATAANIESHCRIVAEKSILRRLLLATERIRKAVREEGSSVQDVLETAEHEIFSVATDRSRKDPVPVREEIRGALTRIVELQKSPTRMTGVPSGYPDLDRLTNGFQPSDLIILAGRPSMGKTSLAVNIIEHIALEEKRPVFFFSLEMPVESVLRRLLASRARVAYEKILSGDLTEDEVSRIVRASTPFCSADIFIDDSSSLTPLELRSRARRLISRVGDPGLIVVDYLQLMHSGRRIDNRVQEVTEISRMLKCVARELRAPVLALSQLSRAPTHRSDRRPQLSDLRDSGAIEQDADLVAFIHREEYYEAGEAERTGEAELLIRKHRNGPTGTVTLVFIGELMRFESAAMDMEPDAETSVYA | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 449
Sequence Mass (Da): 49994
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A0A3M2F0X8 | MGGTGNLGTFEGAPGRRVRRRFPLEDSYRYRRVRPGKNPHPRTLGITLPRFLGIDAGRKRVGLALSDPTLTYALPLESVSAKESVNRIAQLLQEEAITHIVIGLPTSLDGSSGPQRKRTEKFLRLLERCFPEIPVIAFDERMTSRAADALSPYSRSTNRDAGAAAVILTDYLRSRKHSSSPAPSHHG | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 187
Sequence Mass (Da): 20614
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A0A7Z9G813 | MTDHLLINAALGKPVPRTPVWIMRQAGRYLPEYQAIRRQMSFLDLCHTPEKAAEVSIQPLDILGVDGVIVFSDIMVPLEGLGMDVQFIEGRGPVISDPIRSVSDISRLKPYDANVETKYLPDAIRMLVNEIGHRAPVLGFAGAPYTLACYAVEGTTSRHYHETKKFMMSDPVGFKKLLDVLADAVAELLIAQIDAGASLVQLFDTWAGALMPDQFREFALPFAQKIFERVRRPGVPMVYFVNGVAGKLKDIAQSGASVLGIDWRIGLDQVRAIVGNDIPLQGNLDPCTLFAPPEVIEERVKKVLAAAGDSPHVFNLGHGILPTVPVSHAQHLVKSVQRLGVK | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
EC: 4.1.1.37
Subcellular Location: Cytoplasm
Sequence Length: 342
Sequence Mass (Da): 37444
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A0A7C2WSZ6 | MVRLSPQRGFEAFLDQIHHSIRENGEGEAYVFESISDLLAEWCSDQMVGNFFMLTCPFLRAFKAVAYFALLRDFHSAYATDPIEQTTQILLDVHRHENKLYLHPHRVKGRRASGRLHRLFVLDGDSVRPLQESGAIARVMVGAPRSGLGLIQRHLGVWTRSFMQAETLLEEWRAGHVSEERVRETSRHLMRMAITRDERMLRLAARHLDLDDLVWLGTRMLGTGLIGGKSVEMLIARKVLLQADPRWQELLEPTDPFFVPSDIFYTYLVRNGCWAIRKRQLSAEDPLEGAEEAYQAILQGSFPAHIEKRFAEMLDYFGQTPLVVRSSSLLEDSFGNSFAGKYESVYCANQGSREERLEEFMTAVKTVYASTMSREALAYRVRHGLLQSDEQMALLVQRVSGAQHGRYHFPHVAGVGYSFNPYVWHDRIDPHAGVIRLVCGLGTRAVDRRDDDHTRLIALNAPELQPENDSEARAQPAQRRMDVVDLDKNRLCTVDFDHIVAEIPDAARSLLVSHDIRVARAARERGMRPANVQRLSFDGLLQKTDFALDMQTMLQTLEAAYEYPVDIEFAATFREDAFYQIALLQCRPLQAKGVSQPLEPLDDIPNDKLILRAKGPVVGRSRWCPIDRIVYVSLDEYG | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 638
Sequence Mass (Da): 72722
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A0A951TE91 | MTHIGNCELGKRPRVVVALRDGVPRREVESALAAGADIIELRVDLFSSLEPGFPEAECGRFTGIPRLGTLRCAAEGGGWRGSEEERLACFNAILPHVEAVDIELSATDILDRVVEAAHDAGKTVIGSFHDFAKTPDDAHLEETAARADRAGVDILKVAAHCATLEDLRRLAAFTLRREGRPAAVIGMGPAGMPSRIFFPLLGSMLAYTFLGTPSAPGQLNCADTVKYLSLFCQFTNSPE | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 239
Sequence Mass (Da): 25630
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A0A7C2WF24 | MAVFTGLLLVDKPAGITSHDVVDRIRRAAGMRRIGHTGTLDPAATGLLVLCMGKATRLSEHLTGLDKTYEGAMRLGLITDSHDLDGEVLEESPIPSLDMEAIQSVCNRFSGEIEQVPPMVSAVKVGGERLYRKARKGEEVDRPPRCITIHEFRVLAYAPPDVSLRVRCSSGTYVRTLCHDVGAILGCGAALASLRRTAVGRYSVEQALPLDAFTGPEIVKERLIAMDDALDLPAVYVRNSSQALIAEGSSLGISDLREPCPVQEGWVQLKNAKGKLLALGVAQATLVGPRIHPKRVFI | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 298
Sequence Mass (Da): 32138
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A0A1M2ZFF6 | MTDFILASASPRRKELILNLPYSFRIETKETDEILDPDAMPEENVMAIARQKAAAVAQDNRDSLVVGCDTVVVYDSLILGKPKDAKDAGRMLRLLSGNTHRVYTGVSLILRSKKLSHSFFVCTEVSFKQLTEDEINRYVATEEPLDKAGAYGIQQYGSLFVEKIHGDYFNVVGLPINRLYTELQRTVRDYGLF | 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: 193
Sequence Mass (Da): 21771
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A0A1N7INI8 | MNRTIRGMSILGAAGTLLIVLMGALVTKTGSADGCGNTWPFCHGEIFPSYHTLELWIEYSHRIVSGLVGLIVVVASVGAWLLHKQNFTVKFLAFNSVFFIVLQGLLGAAAVIWGQSDAVLALHFGFSLISFASVLLLAVVLIRINRQGPSRGGNASTVSRQLKYGIWGLAVYTYVVVYTGAYVRHTGSSLGCADWPLCGSKWVPDLFSQVGIQLTHRLLAGLLFLFAVWLWWAVRKKYPHRKDLNRGARWSLILTLLQVLTGGAIVLTKLELMVALAHATLVCLFFSAVCYLCMQVGPPWKDHRDSSSLQGKQGDPLTP | Pathway: Porphyrin-containing compound metabolism; heme A biosynthesis; heme A from heme O: step 1/1.
Function: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Catalytic Activity: 2 A + Fe(II)-heme o + H2O = 2 AH2 + Fe(II)-heme a
EC: 1.17.99.9
Subcellular Location: Cell membrane
Sequence Length: 319
Sequence Mass (Da): 34885
Location Topology: Multi-pass membrane protein
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A0A4D7QB00 | MQQTNLRAHRTLRGAAATVTWLGLAMIALIWTGVETDIRQEREFAHRSASQTASNYARLFEEHIARSLTEVDHTIKFIRQDFLRDPAAFDLQAWVKNQYSFTDLALQFTLIGRDGIMHSTTTPGASAGLDLSDREHFRVQVQGPADMLFISKPVLGRASGRWSIQLTRRITDAEGRFAGVVVASLDPYRLSRFYESIDLGRSGSIAVVGRDQVVRARAGLSADNLGSRLDDPQFFERVLYNSIGIFDRPSETGDGVTVTAYRAIEDHPLIVTVSVGDTDAAAARAATAWRMRLIALAMSVVVLVVIALGVRHRRRLDHVIDELSASRAEAAEKSRELDLTLNNMSQGILMVDANEQVAVINRRALELLDLPETLMAERLSFQKLLEYQWRADEFGVAGKDIPDALRDYVQSGGLSTALPVYERTRPNGTVLEVRSVQLAGGGVVRTYTDVTERKTSERDLREARDRAEAASEVRTSFLATMSHEIRTPLNGIIGMSSILEQTDLNDDQHSYLRTIHGCGEALLEIINDVLDYSKLDSGMIELDATDVVLKEIVSSTVDILGARIHAKHLSLDVQMAPELPAVVHTDGSRIRQVLINLVGNSAKFTEEGGITIRVEAREGVLDVLPRLRFSVVDTGIGIPEESRDRLFREFSQVDASITRRFGGTGLGLAICKRIIEALDGEIGCDSSPGVGSTFWFEIPVRKVDGHVAEGKTGAVRANPLPAIQRSLRILLAEDNKVNQEVATLLLKRIGHEVVVAENGQQAVARAAECRYDLILMDMQMPEMGGVEATRAIRSGRGASRDAPIVGLTANAFASDRQACLDAGMDAFFAKPITRAKLDDALAVAGSDTVAENTSTAASDATMLINTEYRDMLFGEIGPDAGRALVQSFWGDAETIVEALHLAVSRGDRDAAETHLHTLKGAAANMGYEAITRATGNRLVAGGDVAAMEALQAALRQTRQLDAPKERPGEENNLARKLAS | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 979
Sequence Mass (Da): 106843
Location Topology: Multi-pass membrane protein
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A0A970M716 | MITLLHCGPHSPQRLVNAFAAIDVPVQLATSADDIRTAEQLVLSSEAPFDATIRQLLCRNLLTALRDYLFDKRSFLGIGTGAHILFDTREHAPAWTGLGVFPGTVRPLYADRPTHPFMGWAGIRAQANSRLFHGLAGDEKFFFAHVDQAVPARDNLCLAQTDTASPVPAVVGDDTRLGVQFLPHKSGSAGLHILKNYADTALAAPQSNPGHTSQRPATPARSIVACLDMHADTHGNLVVTKGDQYDVNVGGTVRNLGDPVEMACHYYDEGADEIAFLHIAGYRDDPLRNTAVTDIISAASRRIFVPLTIGGGIRDYTDDRGLPVSALEIAARYFRAGADKISIGSNAVDIAKRYLRTGRKTGGSAIETISQCYGAHTVVVSVDPRRVYVTSPSDVPHHVVPSDPPGPAGEAFCWYECMVKGGREGTGIDAITLAQAVEALGAGTILLNSIDKDGTNSGFDLALINAVREAVTIPVVASSGAGKVEHFSEVFAQTRAESALAAGILHRREVSIRDIKQHLHGKVEVRK | 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 HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
EC: 4.3.2.10
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
Sequence Length: 527
Sequence Mass (Da): 56423
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A0A970QG61 | MDEERLAALRELTEALGLKLPSYEALDEALTHASCLCEPDSEELRCYESLEFLGDAVLDLAVSDFLFNRFPDGNPGRFTEMRATIVNRNSVAEVARRLGIGAYIRLSKGEEVLNGRNRLSLLADSLEAVIGAVYQTLGWAAAHAFICDAFASELNQVRMEAPVWDYKSKLQHYCQAQHIALPHFVTKDEGPDHKKVFFVDVFVQDQHLGSGRGSSKKEAEQRAAQQALHMIQDKK | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
EC: 3.1.26.3
Subcellular Location: Cytoplasm
Sequence Length: 235
Sequence Mass (Da): 26267
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A0A7X7C998 | MKKMFLSILIILATTLSQEAIAMSYQPDSNAPRSSVPDEYKWDTSVIFKSDAAWNAAFSKVMNSLGSLQKYKGKLDSPEKLSKCLDEFFDAKLQMSRLSLYAELKLAEDKNVEKYQIMFQKTSDMATSFNTKTSFIKETILRAGNEEMEKNLAFGEIKKYVPYIKELRRRTDRIRGEETEQILAMSGDNLFASSWPTSDIEMIFKSIMRDLQFPKIKDEGGKEVQLNLSNYSKFRASKDRVVRKAAVEAFLESLKKYENILAATLAGEVKRDVFFAKARKYDRAVDAYLDADDIDAKVMDNLIDTVNENLKPLHRYVELRGKMLGIKDIHLYDLYTPIVQKADASISYDEGANMVVESLAPLGKEYTDVVAKAVKPGSGWIDAYPNKGKESGAFSTSAWGIHPFIKLNYQEKIDDVSTLTHELGHTMHSYLNMNVQPFVTFGYSTFTAEIASTFNENLLTEYLLEKYADNDEMQLYILGNLLEQIRTTIYRQTLFAEFERKIHSFAEAGIPITADLFNKTYLDLIKKYYGPKFRIGKDDEVEWAFIPHFYYKFYVFSYATGLSSGIALSQKVLSEGENARIKYIEMLEAPSTSQPIEILKKAGADLTKPQAIEAALNLMDETITRIEKILAKKNKS | Cofactor: Binds 1 zinc ion.
Function: Has oligopeptidase activity and degrades a variety of small bioactive peptides.
EC: 3.4.24.-
Sequence Length: 636
Sequence Mass (Da): 72433
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A0A2J0M838 | MSYLDDKMKNLKIGIVGCGAIGTSLALLIDKRLSNAKVISLCDIDSVKSLALKKKLGAGKVCSLQQVIKTSDLVVEASSAKVSFEIARQVLLGRKDVLIMSIGGVLGREKELFDKAKKNKARIYFPSGAICGLDGLKALIPAGIDEITLRTMKPPRALEGADYIVKNKIDLSRIKKDKVIFSGDAYAAVKAFPQNINVVALLSIAACGQVVPKVEIIASPGLKRNIHTIDVRSKAARLLIRCENVPSPDNPKTSYLAVLSAFLVISGISDVVSIGS | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.
Function: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.
EC: 1.4.1.21
Catalytic Activity: H2O + L-aspartate + NAD(+) = H(+) + NADH + NH4(+) + oxaloacetate
Sequence Length: 276
Sequence Mass (Da): 29457
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A0A7C7YL31 | MSFFPFRTAREFLRGSLLLLVLAAVFGYWFYDHYLGDLPDLRRVEDYQPALTSVVLDRHGQLIAEFYEERRRLVPIAQIPRVTQLAFVAAEDKNFFQHGGLDYTGILRAALANVMGGGIKQGASTITQQTVKSLLLSPERTFRRKIREMVLARRIEDYFTKDEILYLYVNQIYFGHGAWGIGQAARDYFGKEVQDLTISESALLAGLPQRPSDYSPYRNPDSAERRRLYVLGRMLADGFIEPGQYEEAVAHRPIIRNHPDDENLGQADHFGEFIRRYLFDTIGGEAVLRDGLTIETTLDLGLQTAAVAALRKGLEAHDHRQGYRGPLRRVDPSEIDAEVLRLGDLNAEHLPVPEALAGDQEDGDDAVVFQTPRPVIPFDQALEGVVVGVDAETQRARVIFAPGVAGLVDLEDVRWARKPNPEARPRPVKQIAQIFASGDVTRFVRLADRPPEVDEAVLDEALGNEALLDGALLEDAPLEDAPLPDALLPRLGLHQTPVVEGALLSFENGTGDLLAMVGGYDYRSSEFNRATQAERQPGSAFKPFIYGAALEKGYTPVSEVVDRPVVYTDPVSGFTWAPRNYGRHFYGPMPLRNALKKSINNATVHLFRDVGVDYVIEYANRFGIHSPLVRDLSLALGSSSMTLLELTTAYSVFPNKGRLVAPRFLRRVTRRDGTVLLEDIPLVDPRTFAVPPVAAQGQQAGESASPDPPESLAEAGAESTPPSDPTSPGEPALADDQVISEASAYLMSDLLSAVVQEGTGRGLLRLGRPLAGKTGTTNEQGDAWFMGFSPDLTTGVWVGHDDNRVLGFGETGAGAALPIWRDFMRVALKDRPSRDFEVPADHIVFQRIDRDTGLIADASTQNAYFQPFIEGTEPRRSMSEQESASDARRALREDIF | 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: 896
Sequence Mass (Da): 98948
Location Topology: Single-pass type II membrane protein
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A0A947HSL4 | MSVLELIELDNLPYAEGLALQHHRRELVLSGGSGAIFLVTHPPTVTLGRHAKPASVIGRHELERRGVPIIETERGGDVTFHGPGQLVGYPILDLTRYGLGAKRYVELLGQVLADVLGAMGIAATWDDTAPGLWTARGKIAAVGVHLHRNVPIHGFALNVDVDLRWFDLIVPCGLTRPVTSIERELGHDAGGVGAIRSAVARALQSRLTSRREG | 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.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
EC: 2.3.1.181
Subcellular Location: Cytoplasm
Sequence Length: 213
Sequence Mass (Da): 22911
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A0A7C8EKE2 | MPTNLERSAELLALNGILLGSKAEARIAQHAKLVREWNAFASLVSENDLTVIEDTHVVDSLSLAPWVIGAGGRGAALLDIGSGGGFPALPLKIALPELRVTLVERSERKVGFLLSAAGAMGLDGVTVVHGNFPEGVSGLSPDAVTARAVEKPDKVGKAILAFLPGGSTFLCQSGAALKNLPPMFHVERIHDAWSRAGLRRGELFVVQRLDPDRPIEPRGT | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 220
Sequence Mass (Da): 23234
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L7N6J5 | MMSSLFSSFDPTTIFNSQLNWMVIMITLVLIPLNYWIILSPLHTLWNTLQLLIHQELKKLLAYKYMGSTLMMVTLFMIILLNNLMGLFPYVFTSTSHATLPMIMSFPLWLSFMLFGWLKTTNKKFTHLVPEGTPSYLMPFTVLVETLSNIIRPGAITLRLMTNMTAGHFLITLLGNNFPTLDKLFLPVMVLMQSMLIMFETMVSYIQAYVFTILIGLYFEE | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Subcellular Location: Membrane
Sequence Length: 221
Sequence Mass (Da): 25552
Location Topology: Multi-pass membrane protein
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A0A1Z8S9J5 | MKDIKQQFPILNSKLPSGNTLVYLDSANSSQKPQRVINRMTQFYSQEYSSIGRSIHELSNNATMLVEKSREAMQDFINASEPDEIVFTKSATESINMVATAYGRIMEEGDEIITTEIEHHSNYIPWHLQRKHNGFKIKFITVNEQHRLNLHELESLITPKTKIIAITHLSNTTGEIVDIKKICEIAHKHDIAVCVDGTQGAPHLKVDVRDMDCDFYVMSGHKMYGPSGIGILYAKRDWIEKLDPALGGGGMISKVEHDNVEFIDGSKKWEAGTLAVAEIVGLHEALKFYINTGVDNMIAHEKEIIDYAYSELSKLDKIKIIGTQDRSAVISFNIEGIHHQDLAMFLDSYGIAIRPGHHCTQMLHRQIGWSGSCRISTGVYNDKQDIDYLVSCLKEIQKKFS | Function: Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.
EC: 2.8.1.7
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Length: 401
Sequence Mass (Da): 45280
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A0A956HIR1 | MHDERDDAWTRYLTWRWADAELGVELDLGDAGLAAEQFTGAWEDRLTRALAAMAALEAGALANPDEGRQVGHYWLRAPSLAPDPAITAAIERSWEAIEAVAGPFRAGELTGSNGQVLDRVILVGIGGSALGPQLVADALAPAGARLTVLDNTDPIGMRRALAEHGPLAQSLALVVSKSGSTVETRNGMVELTAAFAGAGLSFEEHAVAITGPESQLDLRARGEGGGAPWRARLPLWDWVGGRTSVCSPVGLLPAALLGIDWRGLLAGAARMDAATRAGALRENPAITLARLWFSETGGRGERAMVVLPYRDRLVLLSRYLQQLVMESLGKRLDRHGNTVHQGLVVYGNKGSTDQHAYVQQLRDGRDD | 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: 367
Sequence Mass (Da): 39155
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A0A2A5D6X4 | MRMLGDNQDQDMMRRQMMAIFLIGFIMMGWMFFFAPTPPPVVAPEDPAEEITTTRESGGAAQRSRTETANPTEALQAWPNLPPVFEQDDPISDEIVIRDEWLELVFTRIGGRLKRALVLLGDNGDDTIQLVPEAGILPDTEVVYPLGLRFLHSDIRDELDYRRFDAVVSRDERSVTFTLTLPNAAVVRKTFTLTPDAHVLDIEIGYENLEGRGRSLGVDAEPAYILNWGPGLVAEGEGTFFKPSILWRADGELEKLYIKDMPELGETPEDKRISDAEWLGYRSKYFLSVLKSNDGESSGDAWVYGNEDDLRFGLQTPRFLVDAGDEHRTTYSLYLGPMELKSLDAAWPTLSSAMTYFDYPKLLDSFAKFLLRIMNWFHGFIPNYGMSIVLLTVLIRIAVLPLTLKSMRSMKGLQTLQPEIKEIQEKHKDDQQASSKAMMELYRERGINPLGGCLPMLIQMPVFIALYRMIMFAFEVRGEEFMWIDDLSLPDRLFHIPFMMGMPLVGDALAYVNLLPILMVXAMVISFKISPTSATQNPQQKMIMMLMPIFFGLISYGFSAGINLYVLTSTVLGIAQQQVINRSGTTEAPKKKEVKSVKDIRKKRKQHFYNRAQERKREQAKAAKKGKKKK | 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: Cell membrane
Sequence Length: 630
Sequence Mass (Da): 71593
Location Topology: Multi-pass membrane protein
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A0A2A5DLS4 | MSDISTSVLKVNTAAYRHNIGVVRKHIGDDCGIIAVVKSDAYGLGMIPMAQRAISENVDMLAVATVAEGMELREHYPDIPILVMVQPSEEDIPAAVQGDLRITVSNYATAEQLGLQASKMKKIMAIHCEIDTGMGRQGFSLEEAPKSLLKITRISNVDIEAIFTHFPSADEPEDPYTANQAKNFRTLQTQLSKDGIPFEYCHASNSAGIMLQQNCSFDMVRPGIMTYGVWPNNKVPEDSPLLPVIQWESKLVLIKNLPGGVSVNYGRIYKTQKPIRTGVIPVGYADGYPYALSNNADVLIRGTRCPVLGTVTMNQIVVDLSEVPEATVGDIAVLIGQDDEERIQVEELAHRANTIGYEILTGISARIPRVYLPA | Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
EC: 5.1.1.1
Catalytic Activity: L-alanine = D-alanine
Sequence Length: 374
Sequence Mass (Da): 40896
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A0A7V2Y3F9 | MISLNFTLICQFVLFLIFLWGANTMVFRPLLKVMDDRKAKVENDRAVAEAETREVQELDSVYTRRLAEAHQAAAQRLHQARHDVYQRNRDFLEAQKRKADAEVASVRAAMDARIEAERQKFPELLPGIVEAIDRQIDAEGSLL | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Location: Membrane
Sequence Length: 143
Sequence Mass (Da): 16439
Location Topology: Single-pass membrane protein
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A0A970M4X1 | MPRYALTLEYDGTRFSGWQSQEGLRTVQGELENALGVLLREPAKAMGASRTDKGVHALGQVAIFDTEHPVPTHRLIRSLSALLRPDIAVIDAREVPADFQPRFAATGKHYRYRVLNRSAPSPLLACTSWHVFSALDDGAMRDAADLLQGTHDFAAFRAADCHRDNTVRTLTAIHLTRARDDLLEMHVYGDSFLKYMVRIIAGTLVEIGTGRRSLDEVRRALQTTERHWAGRTAPPHGLTLMEIFF | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 245
Sequence Mass (Da): 27401
|
A0A964JQS6 | MRLPLRLVVVAVGRLRIPWAQAACSDYGERLKHRFKFELVEVKEADRRGGSKDVSRQKEDEAVSIWAAVPTGATVLALDERGLSFTSPQLAAFVDDAANRSKSALCLLVGGPDGHTDATRERADRLWSLGTLTLPHELARIVLLEQLYRAATINAGEPYHRA | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.177
Subcellular Location: Cytoplasm
Sequence Length: 162
Sequence Mass (Da): 17858
|
A0A2E8RVB4 | MGRRDDFVVGLDIGTRHVRAVVAEADEKGVHITGIGQADGLGLRGGTVVNIESTTRAIQKAIDDAGRMAGCEVGRVYVSVGGQHLEGSNSQGVVAIKDGEVSEDDRDRVLDAARAIKLSSDREFLQMLPQKFRVDDTEGIRDPIGITGVRLEARVHVITGAKASLQNLRRCVIQSELDIAGIGASPLAASSATLYDDEKELGVVLVDIGAGTTDVSIWHDDALVHTAVLPFGGNHVTSDVAFGLRTPRAEAERIKCRSGCATVHLVDEEDIIEVPSVGGRQPTEQSRQFLAEIIEPRVSEILEMVREEVRKSGYQELLASGIVLTGGTANLEGISDMAEEIFGTPVRIGVPENISGLKDMVADPSFSVAVGLVKHGFAAAESAQFEAYRRSQNSPMNWLGERMRRVASIFF | Function: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular Location: Cell membrane
Sequence Length: 411
Sequence Mass (Da): 44107
Location Topology: Peripheral membrane protein
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A0A7C7U4R4 | MRTLPAPTRLIVGLGNPGPEYAATRHNVGFQVVDGLADRAGGEWSKLPRLEALGCYVEIGSETCLLLKPQTFMNRSGEVVRAACQFWPGLSPGSDLLVIYDDMDLPTGRLRLRPSGGSGGHRGIGNILGELETKEIPRLRVGVGHPGSASEVVDWVLEHFSEDEEANHLPAILARAADSVEVVVREGVTSAMGQFNVSL | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
EC: 3.1.1.29
Subcellular Location: Cytoplasm
Sequence Length: 199
Sequence Mass (Da): 21322
|
A0A0S8IGU2 | MKKSITTKTGDKGMTSLLGGRRVRKDHIIVRTCGQLDELCSFLGLAKSLISERGGKKLLESIQKDLYVICSEVACEKRLSGKLKQRIGRSHIKRLEDRIYDLESRFKIRKCFTLPGENSVSALLDVARARCRSAEINIVTLKKKKLLHNGLIPVYLNRLSDLLYLLSRSRGSATSVKFDELS | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
EC: 2.5.1.17
Catalytic Activity: 2 ATP + 2 cob(II)alamin + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)alamin + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphate
Sequence Length: 182
Sequence Mass (Da): 20523
|
A0A7X9ITJ1 | MTPLMTRAQMRRYDAAATERYGIEGLVLMENAGRGAAEVIRRLVAGLPRGPRAAPHRVGLVCGPGNNGGDGFVVARHLANAGIPVRVHLAFPADRARGDAARNLAVARAMNLELLDASRPAALPRLRRALAADAVVVDALFGTGLDREVEGHPRRLIEAMNAAPGLKVALDIPSGLDADTGRPLGVCFRADHTVTFGALKIGLALHPGVELAGEVDLVDLGAPARLAEEIGWAAALLDEAGVAARLPARPPAGHKGTFGHLLVVAGSRGKSGAAVLAAQAGVRSGAGLVTLATRGDARDVVEARVREVMVEELLPPPGTVRTGAELDRRWEALARGKTAAAVGPGCGTDGPAA | Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
EC: 4.2.1.136
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Length: 353
Sequence Mass (Da): 36313
|
A0A3B8LNR4 | MSYLFQTPVISIVGPTASGKSGVAIEIAKRLNGEIVSVDSLQVYRHFDIGTGKVTLEEQSLAPHHLIDIVAPDKEYNAADFQADADRVIAEIHARGHVPILAGGTGLYLKALLHGLFDTPSDQTLRESLRARAEAEGLLTLYRELQDVDPKAAEKISSRDAVRIIRALEVFQLTGSPFSSLAAQHRHGERRYPVLTLGLMWPRPVLYERIVRRVEMMFQEGWSTEVEMLRGMGYGPELKPMQCIGYREINAVLAGELDADILYQRVCKQTKAYAKRQLTWFRKEAVSWFPSPQALLEDAVLPREIESFLAAPETYTPPEPLLQPKKE | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Length: 327
Sequence Mass (Da): 36677
|
A0A956BTA0 | MDQELEDLRAALDGVDSKLVDTLVERRDLVKQVARFKVARGRGIRDPQREQELLEKLVARGESAGLDSHFVTRLFREIIDHSVRLQQEYFSTSGDPNGAPRRTIVVAFQGGEGAYSHLAATRHFGARDAKVLYEGFPSFKLMLEAVKNGMADYAVLPIENSIAGSINENYDLLAKMDLHLVGEEMQRVEHCLIGVAEVPLTKIRRIFSHPVALAQCGAFLATLTNCHAEAFSDTALSVRRVKDEQDLSQAAIASEEAARVYGLPVLARGIADQKDNFTRMVMVAKEPVVYDAALQCKTSLILSTKHEGGALLKVLQTLANHGLNLTKLESRPQPDSPFEYVFYVDFEGNTVTPETQAALEELRACTSFLRVLGSYPARRPS | 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: 381
Sequence Mass (Da): 42156
|
A0A3M1IGI2 | MNFLPYTKTKAKLPLNTDFHSLPILLLYGGRSAEHEVSCISAIFIFEKLVEARFTVYPVYVAKNGLWYLQEVPSAAEENCIGNSCKVRFVQQDSEFFLEGERDKVPVKFVFPIIHGTNGEDGRLQGMLEFYQIPYAGCSALSSALCMDKWFMREIFKAAHLPQVEYAKLEKKQWEEKLSDIMEKFSYPVFVKPCNMGSSVGVSKVKEQSELKTAIEDAFRYDDHILIEQGVDPEEIEVSILGNFPDYKVSLPGKLLPNHEFYSYEAKYEDENGAHFEIPANLEESVRKEVQEMAKKAFAAVRGEGFARIDFFLEKQTNKLYLNEINTLPGFTPISMFPRLFEVSGISPSDLLSEIVALGYSRFEKQSTFVA | 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: 371
Sequence Mass (Da): 42278
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A0A955Z8S5 | MTPRLPDSAKLALERLKAGNARFISRDVNVDARVKHLDRGELAKGQAPVAAILACADSRAPMEILFDEGFGDLFVVRVAGNVVAPSIVGSLEFAVGKLGVSLVVVCGHSNCGAVGATLAAVQGEGGAPTDTSIGDIVERIRPSVAELVHAGLTGDVLLQRAVRANVRLAADHLRHGSTLLERRVLGGELGIIGAEYQIETGKVEFFEEPGV | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 211
Sequence Mass (Da): 22035
|
A0A838E864 | MLTVTNTRTRSRQELVRPRGRPLTLYACGPTVYRTAHVGNLRTFLLADLVRRALASEGVDVRAVQNITDVGHLAGDTHDEGADKVQLAAEVEGRSTEEIAAFYTERYMADADALNLRRYDAYPRATDHIDAMLDLIRRLEAGGYAYDTRAAVYFDVRRFPRYGALSGNRLEDLRPGHRSGRTAPDKRFHADFALWRKAGPRRGAAWDSPWGRGFPGWHIECSAMGLELLGERIDVHLGGVDLAFPHHESEIAQSEAAVGHRVVDVWMHGAHVLSDGRKMAKSTGNVLDVAALREGGLDPLAFRLLCLQARYRTQLNVTWDALAGADRSLARLRQRVGELSRATDDATDQQAADEVEARFLAAVCDDLDTPTALQLVHEVAAGEGCAAELSPGARAALLRRCDAILGLDLVRDLDRVHSDGPPLPPGAPEQMASRERARAAKEWTAADELRTELSALGVDVIDTPDGPRWTLR | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)
EC: 6.1.1.16
Subcellular Location: Cytoplasm
Sequence Length: 472
Sequence Mass (Da): 51893
|
A0A7Y5C598 | MTTLKYAASVMCANLARLEDDLRELEQAGCDELHFDIMDGQFVPNFTLGFDFIKAARRVCGLPCHAHLMIAKPEDYIDRFVEAGCNTVTVHVETCIHAHRTLAQIRGAGASPGIALNPATPLTKLDFLFDHIDRVLVMTVDPGYAGQKIIPNSFERVRILRENINYRERAVAIEVDGNINVRNAAQLANAGANVFVLGTSSIFKGNGRLGEALHSFKQKVAAERTTA | Cofactor: Binds 1 divalent metal cation per subunit.
EC: 5.1.3.1
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Length: 227
Sequence Mass (Da): 24923
|
A0A9E5DWT6 | MELPVTESNSPTTPATLTTPATLTTPATLTTPATLTTPATLTTPATLTTPGRSGPLQPTTGAPADSPQVTGVPTGALNAGPHVRRTEPLHVALCGNPNTGKTTVYNVLTGANAQVGNYPGITVERRTGAHRGPTLRWLVHDLPGCYSLTAHSPEEQLAFLALTGRLDGPKPDVAVVVLDATNLGRNLFLLLQIAELQIPVVAALNLMDAAEHDGWVIDIAKMTTVLGCPLVPMAARSGRGVDALRLAVEHVAHDPQQGRGPQPQWSLEVQTAIAAQRRTDHPVAATDGELVWQLGTDVQPSPRMAASTGASGGPAGQVQIAAGDRLRRQLVHDRYRLIDSWVGQCVQPPQVTTPSHTDRLDRVLLHPLWGSVLFLAAMTLLFQAVFAWATPMTDAVNAAMGGLAELARGHLPAGLGRDVLVDGVLAGIGGTLVFLPQILILFMGIALLEDSGYLARAAFLIDRTMARIGLPGKAFVPLLSSYACAVPGIMAARTLADPRDRLLTILIAPLMSCSARLPVYTMVTAAVFAEIPKVGGVLAVGGLVVAAMYVLSFLLALAVGAVFRRTLLPGHGAPLLLEMPPFRRPQLRNLLRVLWERGRLFVTETGTTIVALSVLLWVLMTFPRLDHDTVAHQAARQHILTTIADPIASQSALAAAEATAAQTRLQHSIAGQLGRALEPAIAPLGFDWRIGIGLIGSLAAREVLVPVMAQVYGRGSGADVDDRFAADIGHTMAKAGALTPLKGLSLMVFFAIAMQCLSTLATMRRETQSWRWPALALVYLNSLAWLASLAVYQAGRALGYS | Function: Probable transporter of a GTP-driven Fe(2+) uptake system.
Subcellular Location: Cell inner membrane
Sequence Length: 801
Sequence Mass (Da): 84720
Location Topology: Multi-pass membrane protein
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A0A7C4UQX9 | MYRDLARREEGGRGPIAGPIVAVAVILNGKVNGIDDSKRLTKRKREVLFDILMNGQHDVGISIVSPKEIDSLGIQEANYKAMLEAILKLKSRPDLVLVDGYHLRGAPCEVWRIIKGDRKSATIGAASIIAKVTRDRIMEEMDKIYPGYGFAKHKGYATKEHLMALERLGPSPIHRLSFAPLSNRVENDLFNSKELCREG | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subcellular Location: Cytoplasm
Sequence Length: 199
Sequence Mass (Da): 22178
|
A0A7X7UCD9 | MATLKSIKTRITSVKNTHKITKAMKMVAAAKLRGSEERLRAGRPYAERLDEVIGNLYRRTETEGFPLLEGKKEVKKIELLVITSDRGLCGSFNSNILRYAWQTRRKLVAEGKEVSISVIGRKAADFFRYRDVAARQKYLNILGDHNYGLAIRIGDEMVEAFQNDTVDEVRLVYNEFVSAIAQRIVDRPLVPVILQSLERPAGMEAIVDYRFEPQREAVLAELLPMQIHYQLFKAFLESYAAEMGARMSAMDAATTNAEEMIGKLTLQYNRARQAAITNELMEIINGANAIS | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Subcellular Location: Cell membrane
Sequence Length: 291
Sequence Mass (Da): 32894
Location Topology: Peripheral membrane protein
|
A0A8J6R3Q8 | MSQSLNTLREQRGSTDLKLTQLSASQTPSHDQRVIGLTGGIGMGKTTVSDYLSSAYQLPILDADLYAREAVGPDSDVFQEIVERYGVGILLANGDLDRRRLGKIIFSSSAERLWLEQRIHPYVRDRMESQMQALPAEAYPTVVLVVPLLFEARMTDLVTEVWVIQCASVQQVERLLERDAKTSPEGDRLSLEQVQARINSQMAIEKKIACAHVVLHNSSTLDDLLSQVDQAIAGTRQAPQADASPPASRQASQGKSGLLQP | 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 Length: 261
Sequence Mass (Da): 28695
|
A0A7C7ZL84 | MSDPIQEDEDLAIDAESPGGEFSFDVAEDERGRRLDALVSERVATARAQVRRWIDDGLVEVNERPARASRKVSPGDRVTARIPETPPSGVFPEPIDLDILFEDDSLIVINKPTGMVVHPAPGHATGTLVNALLHHCAELAQVDDPLRPGIVHRLDRGTSGVMVAAKTIAVHQHLSKQFHDHTIDRTYWAFVRSLPSAESGEVDAPIGRHARDRKRMSVRTENGRPARTRWRIAARFPSSGICKVEVHPETGRTHQIRVHLSSQGMPIAGDPVYGRQRKEKRGRGVKIEFARPALHAMRLGFTHPATGERLDYTTPLAPDLADFERALLERDPIEDASESDA | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 341
Sequence Mass (Da): 37769
|
A0A7X7GRW7 | MRKLARALCAAAALLVVLPGPVLAAPAQPHGDEAHEGHHVPRFEDVNWFHGLLGEREGVEPNLLWRAPGTPAPVGAMVLNTVILVWLLVRFGGPAIRAGLTSRKQRVEGGIRSAAAMKSEAEDQLAHYEGKLERIDQEIERVRTEMREQAEAERKRILAEAKVRREQMERDARILLAHELKAAREVLFHEVVEGAMRSAEEAVRARLSREDQERLAEEFVGGLEASLDAAGLEVRS | 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: 236
Sequence Mass (Da): 26155
Location Topology: Single-pass membrane protein
|
A0A3A4JYX6 | MGWTMSGGAADKDKMAERRERMVREQIAGRDVTDARVLAVMGKMPRHDFVPERYKDQAYDDNPLSIGEGQTISQPYIVGKMTELLRLKGAERVLEIGTGSGYQAAILGELAKEVYTIEIVETLCKRAAALLAAKGCANVHVRCGDGYKGWPEAAPFDAIMLTAAPHEIPKPLIEQLKPGGRLVAPVGDWHQELVVLTKQADGSIARQSVFPVRFVPMTGEAEKRERP | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.77
Subcellular Location: Cytoplasm
Sequence Length: 227
Sequence Mass (Da): 24911
|
A0A7C1CJ77 | MQQSTHNGRLVVVAAPSGAGKGTLLKRVREQLPNITVTVSATTRPPRPGETDGVEYFFYSPEEFDRLIAENALVEWAHVHGERYGTLKSELDRVLRGDNIVIFELDVQGMRHIKRLYPDAVSVFIAPPSMEELERRLAGRGTNNAEDMALRLKNARGEMSARLEFDYVVVNDDLARATAELIAVVRGEARSTKIP | Function: Essential for recycling GMP and indirectly, cGMP.
Catalytic Activity: ATP + GMP = ADP + GDP
EC: 2.7.4.8
Subcellular Location: Cytoplasm
Sequence Length: 195
Sequence Mass (Da): 21743
|
A0A3A4K585 | MAELIFEIGCEEIPAGYIAPALEAMAASLAKDLDALGVEHGRIQTFGTPRRIGVVIPSLAAEQPDRVEKVLGPKVELCFGPDGAPTKTALGFAKSRGVAVEDLEKVETPKGACVQATVHTQGQRTKGLLPELLKKQIPRLPFPKSMKWASHDETFVRPILWILAVFDGETVPFDFAGVQSGDTSRGHRFMRPEPFAVRGIEAFFAHLSQAYVIADPEERRKLVRQEATRLADSLHGKLRASDALTAEVANLVEYPFGEIGSFDAAFLAVPKEVLISSMTKHQRYFPVLDDKGRLLSHFVLFSNTQVADPKVTIAGNERVLRARLSDARFFYEEDRKKRLADFAPGLAGVTFEERLGTIAEKVQRIQEHVRFLVSHVNAEALEDALRAAALAKADLLTSVVYEFPDLQGAIGSIYAELDGEKKAVCEAIEQHYWPRFAEDALPESDVAALVALADKMDTVAGCFGVGLIPSGAADPYALRRQSLGVLRILVQRGYRVPLQAWIQFAVSALGSKLRRPAEATAADIAAFIEGRYRNWRVSDYPADVVDAVVGAGFNFLPEAEAKLAALVSFMKRPEFQSLAIAFKRVMNILKQRPQAVVTPNLFADDSEHQLWARYQQVRDKAGVELKQGHYGAALEAMAELKAPVDKLFDDVMVMAEDKAVRDNRLALLGHLADLFLQVADFRRLQTE | Catalytic Activity: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
EC: 6.1.1.14
Subcellular Location: Cytoplasm
Sequence Length: 687
Sequence Mass (Da): 75709
|
A0A7Y3FJI3 | MTTALETCLQGVTAEIRAILEQSLDGDELSIEHGVKLSGARGSDLQALCMVADELRRQQVGDRVTYVINRNINFTNVCIKNCKFCAFARSVRSEQGYFLPKEEVVRRVVQAWEMGATEVCLQAGLSPNLTGDSYIDLCRVVKDAAPEIHIHAFSPEEVKFGASLKRVSYAEYLTELLDAGLGTLPGTSAEILDDRLRKTISPTRITTREWLDVVTAAHRLGIRTTSTMMFGHVESVEDRIRHMDLLRRVQRETNGFTEFVPLSFVHEEAPLFAASQVPGVRPGPTGDEVLRLYATARLMLGRDIPNLQASWVKEGLRTSQLLLGCGVNDLGGTLMNESISTAAGARHGQLMSPATLRRVIRDSGRVPVQRDTSYGTIREFGDSPDEDPIEPLDSIRDPDAVFGSYDALTMDSRFHYEPRSV | Pathway: Cofactor biosynthesis; coenzyme F0 biosynthesis.
EC: 2.5.1.147
Catalytic Activity: 5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 2-iminoacetate + 5'-deoxyadenosine + 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + H(+) + L-methionine
Sequence Length: 421
Sequence Mass (Da): 46614
|
A0A955XWJ2 | MLEDLQNIFQIRTFGDFLAGFLDIAIVAYLIYRGLLLIRGTRAVPILFGLVAIIIGYFVSKDAYLGLSTFNWVLEKFIAAFILLVIVIFQEDIRRGLAKVGRYRFFRAETAAEETHSIEEVVRACVNLSGAKVGALIAIERESDLSMRAEEGIPIDAKITHELLFSLFNPAFANPTHDGAVILRHGRITAAGCFLPLTSNPRVSKQLGTRHRAAIGLSEETDAVICIVSEETASISVAYQSEMTRGLDANSLRDVLQRLLTTNDGEGDEESSEGGRSLANMLKGSPALSTTEETSK | 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: 296
Sequence Mass (Da): 32398
|
A0A2H1L515 | MRLAHATGTDAARARASALAGSAAPLPLADAFGRTLAEDLRALFDVPHYDSSAMDGYAVSGPPPWTLEDAGSLHELRPGHARPVVTGGVVPAGASGVVRIEYTHRDPDGGGVRIGMRPESPGSELDPGRHVRLAGREAAAGDVLASAGHPLTPPLLAMAGISGHDDVSVLPPVTAVLLLTGDEVRTSGTPAAGEVRDAFAVQLPHVLRAAGIEVVAVHRIGDDRAVTREALAELVDLADVVVSTGGTGRSAADHVRAVLQAETQEGPHSSSRIVIDELGMRPGHPTMLALLDRRVPAGTPRPVPVLALPGNPLAALAAMRIVGSAVLRGLRGADPEVPLSVPAAQDLPAEKVDRLVPARPARSAPPAGHAPAADPGTPAGPGTPAGPGAPPDPAPQDLESAWIPVEHVASNMVRGLTTGRGWLILPTRPVSAGERIAFLPLEW | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 443
Sequence Mass (Da): 45309
|
A0A2H9NZ44 | MMKKFVPNHVAIIPDGNRRWAKKKGMISFKGVEYGGSYEHLKELFEGLKDSGVKHVSVWGFSTENWKRPKKEIESVFKLIEKSIDKFRKDAFENKIRFRHFGRKDRIPRKIVELLDNLESDTKEFTDFNVQLCLDYGGRDEIVRAVNKIILEGLKNIDEESFSKYLDDSEIPDVDFIIRTSGEKRTSGLMPFQSDYAEFYFIDKYFPDLNSNDLREAIEEFERRKRNFGK | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids.
EC: 2.5.1.89
Catalytic Activity: geranylgeranyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + tri-trans,hepta-cis-undecaprenyl diphosphate
Sequence Length: 230
Sequence Mass (Da): 27173
|
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