ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A9D6WCN1 | MDHSTTAVHLEPHDVTTAGETHAHLQRIEQEICWLREAAILAYFARLIYVGTASHLAWTIGIGALVYDVVVNWRVRHGHRIRATSAAATVCDSLTGFFLTYASGGIESPFFTLMYFTALTAAFRFGLRVTLAVTALNVSLAGALFVLVPGAGFETLLLTLFYLGFAAVLGATFAGWARRNLELAVAQADALALARDETRLLLHRLIRAQEDERQRLAGDLHDQMGGRLFTLQQGIDRCAEAAEPGLAATLEGLAHEARECTQDVRRLMNELRPTVLDDLGLFEALQEYLANLRATLPFALVAQIDPALRARRSGQDAVLF... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
A0A6N8VQJ0 | QELADFFSEYALIRYRLTAEIEWFKFLYAHHGIDEIPPLSDQAETFLDKILDEFDTQQAIHIKTIEKTTQHDVKALEYYIVSQVQTLPELSGLSNFFHFACTSEDINSAAYGMMFKAARGQCMLPRLHRIRDSLRSMATRYADVAMLAKTHGQPASPTTLGKEMANFCYRLHQQTEKFAAVKITAKTSGASGNYNAHHIAYPKIDWHQVGKDYLESLGLEQHPYSTQIEPHDQLAELMDAIARIAHILLDLCRDIWLYISLGLFKQKIIAKEIGSSTMPHKVNPIHFENAEGNLGLAIALARHLSDKLPVSRWQRDLSDS... | Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2.
Function: Catalyzes two reactions in de novo purine nucleotide biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]... |
A0A348ULR8 | MRCAGQRRDSTPLIGILGGTFDPVHLGHLHAARSVCDRLGLASVHLMLSARPGHRDAPLAPMAARWEMLRLACAEDLRLVPDDRELRRAERIGRPSWTVETLEEMRAETPHESVAWVIGSDALAGLDTWHRWTELLDLAHLVVLRRPGAELPASGPVAALLAAARADADDPTFRQTPQGTIVVLDVPMLRVSATSVRSALGAGRSVDDLLPRSVSTYIWQHQLYGVRSDPGSTA | 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... |
A0A938Q4Z0 | MPESQNLNSSCTIAVGLSGGVDSSVTAALLKEQGYDVHAFFMKNWNEESEQCTIRQDWKDAQKVAELLDIPISLVDFSERYWNDVFERFLKTLETGGTPSPDILCNQYIKFDAFWHYCQNLGFSKMATGHYAAINECNMLCQPCDRHKDQTYFLWSVNPQIWSHVLFPLASYTKQEVRRMAAERGLITAEKHDSTGICFIGPDRFRSFIKQYLVSQPGQILSLDGKPLGMHQGLFQYTLGQRSGLGIGGQKNAQGLPWYVVLKDLQSNTLYIDQDANHPLLLRSTIRITDTVWQNTQPQEGDRILVRIRHGQTLQSAVFE... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
EC: 2.8.1.13
Subcellular Lo... |
A8MAQ2 | MLGYLVNPPIEDAARFVSRYKGSGVVLIYGQVEATYSGRAAAQIRLMPRLVVTKPDGVLMIHEGRREKPIIWNPPGSQLFVSVDDGELILRSIRRSPREYVTVNIPEVYLVASMELGLSEDFKVIGSERDIVDAIVANPGLIEDGFRVISREYETMVGSIDLLGEDKAGNLVVIEVKRSGASPEAVHQLKRYVDYITSKNPGRVVRGILVAAWISASAYRYLKDYGLEFRRYTHANLTGFSLRSNG | Function: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 246
Sequence Mass (Da): 27360
|
A0A2E1Q099 | MKATLDKLDGLSRKLNVEVPTEKVNDAFGKVYKVLQKNANIKGFRKGKAPISAIKSMYQDRVHGDVAQELVQEGYSAALQEHDLNPIGYPQVNIEKLEEDHPFVFTAEFEIRPDVEVKKYEGLNIEREKLVISDEQIDQVLKNIQQNQAETAPVLEDRALQKDDIADIDFKGFIDGEPLQNGEAHGHQLQIGSGQFIPGFEEAIEGMKVSETRTINLKFPEEYHEKSLAGKPVNFEVKLNGIKKRVLPEIDDAFAKKVGDHESLQALKDAIREDIAESENKRIKEEERNSLLKALVEANPLDVPKSLVADQKQALENDFK... | 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
... |
A0A8T7J745 | MAVLKTLDHSLNGGLWLDGHKAISLIQGIQNWPTPSQVMLPLLDKNGARRALVSVGERVKAGQCVAICDGIAGSALHAPYAGTVRQITTLPNAQMVIDMHLSPSSEPCTLLEASTLLQRIDAAGIVGMGGAGFATARKLGQPVETLIINAAECEPYITCDEALLREYAAEVVEGAKLAQTAVGAKRLIIGIENNKTEAIEALKQHDGFELIAVPPKYPSGGERQLIELLLGVRLSPGQRPVEQGLAVINVHTAYAINNANDGRPLTQRVVTITGSAVATPANYWLPIGLPVKVVLNTLGIAANARVRLGGAMMGRPTDPN... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell inner membrane
Sequence Length: 459
Sequence Mass (Da): 48925
Location Topology: Peripheral membrane protein
|
A0A920HKL7 | MQTSAIISKHFNIRVFQTFLVTLSTLFGILMISRLTGYFEKASRGELELSNIFFVVLLRLPDFLSFLIPFSIFVSLIIVISRKFQNNEIYAVYNLGVSPIRHALFLWKQIILVILIVGLLSIFIGPYAKSISETYFNDQTAKDYFGAFEPNKINKIPNSNSFIFFDEGADNIFKDVIFINDDASALTIIESRLLEYKYLDNKIV | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Subcellular Location: Membrane
Sequence Length: 204
Sequence Mass (Da): 23422
Location Topology: Multi-pass membrane protein
|
A0A2E7LGX4 | MLLVPLLCIVGIGLAVLYSAVHQDLSILENQSVKLLVGFVAMTLAAWLHPRVYLRFAPVLYAIGLILLVAVFLFGTTVKGSQRWLDLPGLPRFQPSELMKVTVPLTVAWFLHDRPLPPRTIEVGIALLVAVVPGILVMLQPDLGTAILVVSGGLLVVLLSGVRWRLVLAGALTVVSLIPAYWYFFMNEYQKKRVFTLFDPESDPLGAGWSIIQSTTALGSGGLLGKGLFEGTQSRLEFLPESHTDFIMAVIGEELGFMGVMTLIILYVLVLARGMHIAVQAGDTFGRLAAGGLTLTFFVHVVLNIAVVSGLLPVTGAPLP... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Peptidoglycan polymerase that is essential for cell wall elongation.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-... |
A0A3M0YC59 | MKFQGSPAPTLGVEVELQLLNARTLDLEDGILPLLERFRDEPRVKPEFNQCTVELNSRLCRNAAEAEADLVPLLEALKEACGDLGMVLAGAGTHPFCQRLSAITPNPRYLFMAEKMGYLGHLLMTFAEHIHVGMPSGDEAVSVMARMKAYIPLLTALSANSPFWQGFDTGYACYRRRVLASMKSYGIPPSFPRWEAFADFFERTRRAHVFKTLRDIHWDLRPRPDFGTLEVRVMDVQPDLRRTFAIAAFVHALVVHVQRSLREGDELLPRQHWWFEKENDFRATLRGLEAHYILDNGERCLPIRTLIEETLARIAPIAEE... | Function: ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 374
Sequence Mass (Da): 42425
|
A0A3M0Z8E4 | MGPTASGKSALALALAERFPVEIVSVDSAQVYRGLDIGTAKPPPALRARVPHHLIDVCDPAEAYSAARFREDALRLIGEIRARGRIPLLAGGTMLYFRALERGLSPLPAADPGVRAELEAEAARRGWPALHAELARVDPAAAARIHPNDPQ | 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)-dimethylall... |
A0A1G3UXI2 | MFSQKLLVNKTLWLKIAVAFLPTAVFGFLFYKTIKALFGIETVAIMLIIGGVMFLIIEYFRRNHDESKDKTVDELSIKESLMIGFFQTLSMIPGTSRSGATMIGGLFAGLSRKSAAEFSFLLAIPTMFAATAYDLFKNRNELIVDDYSLLAVGFTMAFLVAFVTVKAMMKFLTTHTFVTFGIYRIAVGAVFLYYM | Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Membrane
Sequence Length: 195
Sequence Mass (Da): 21844
Location Topology: Multi-pass membrane protein
|
A0A969JL33 | NPNVRAAQLTELLVSIMGDGITAEARNFIHLIVANRRLTAVPEIHELYEALRREREGVVEAEISSAFPLEDSQLAALVTDLERRFKRKVQPRVSVDRELIGGVRIAVGDEVIDGSVRGKIAAMSTALLKV | 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 c... |
A0A3C0YGS0 | MRRSPAVIIVNGSDTFRDATGQVDLPANGEIYQNMVLVGLGSNQGESTEIVIAAMHALARLAQPGSVRSSSLWRTSPVNCPPESGDFINAAVVFDALPDLTPEMLLSRLKTLEREFGRAERYQRNAPRELDLDLLLFGSERRQSEHFTLPHPRAT | 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 ... |
A0A661ECL0 | MKIQRKKTNIVKIGDIKIGGLNPIVIQSMTSTDTADIQATTSQIIKLYNAGSQMIRITVNNDDSAKAVVKIKEKLLQKNINVPLIGDFHFNGDRLLKRHLGCAESLNKYRINPGNIKDNQFLNLIELAIKHNKAIRIGVNWGSLDQSLLAKMLDKNNQKKQSLPLDVINKQAVIESAISSAKLAEKIGLSKNKIILSCKMSAVQDLIDVYRDLNRSCNYALHLGLTEAGLGNKGIVSSVAALSILLQQGIGDTIRISITPIGQQKRDEEVKIARQLLQSMQINFFKPEIIACPGCGRTSSDSFIKLAQASENFINKNYHK... | Cofactor: Binds 1 [4Fe-4S] cluster.
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 5/6.
Function: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphat... |
A0A3C0YJ11 | MITSGKRFPPRYRLLSQPQFSQVFANAQIRKRSGNLRLHALKNKEDTARLGLAVPKRGTPKAHRRNRLKRLIRETFRVEREKLPSIDIVVQVSGPIDDSQLRKDLRDQLESLAKNSEYSIQH | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
A0A127Q972 | MTTLEQLNSADAQAFVTTLHGIYEHSPWIPLRAAAQRPFANVTALKQAMQAVVSSASREEQLGLIRAHPELAGKAAIAGELTAESTGEQAKAGLNLCTAEEFATLQKLNADYNQKFGFPFILAVKGADGQGLSRQAIIATFSRRLKNQFDDELGEALRQIGRIAEMRSNDLLGYTPALGKTIMQWAEQIGAWSDDDNGLTCAYMTDTHRRTAAQIAGWMREAGMQAEIDAVGNVVGRYLSDNASAKTLMTGSHYDTVRNGGKYDGREGILLPIAIVKHLHERGEKLPFHFEIVAFSEEEGVRFKSTFLGSNAIIGQFNLE... | Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 3/3.
EC: 4.1.1.97
Catalytic Activity: 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+) = (S)-allantoin + CO2
Sequence Length: 586
Sequence Mass (Da): 63024
|
A0A6L8EN52 | MGDKTVLLTGGAGYIGSHVALDLLQEGYEVIILDDLSKGFATAVTDCELVEGDTGNKNLLALLLGKRKVAAVMHFAGSTIVPESVEKPLRYYENNTVKSRNLVEVCVETGVKHFVFSSTAAVYGIPEAGQVTLQTPTEPVNPYGMSKLMTEIMLRDVSRVMPLKHAVLRYFNVAGADPEGRIGQSTPDSTLLIKVACEAALGKRAELYIYGTDYPTPDGTGVRDYIHVSDLAAAHVLAMQRLEAGCESTNLNCGYGNG | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Length: 258
Sequence Mass (Da): 27659
|
A0A6N8VKR8 | MNSLAKTAAIPVIAIDGPAGVGKSTVARLLAKTLGYNILISGVLYRALAMQLHEHGIAFDARAEIAALVADTDIKFVLDGEQVKTYINGTIAGRDIYSEHCAQLASAAGESAVLREALLPIQRQFRQPPGLVADGRDMATVVFTDAVLKLFLQADIAERARRRQRQLRQRKVYAKLGDLNNELLERDQRDSERSIAQLKIADDAVVLDTTTLSVTEVVDKLMKVVDAKLNERGKTN | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 236
Sequence Mass (Da): 25777
|
A0A962MTJ0 | MSEVSILPISPNGVYAERRLPVESAFERWWRRWLGGGMARSVSRDYAEMLALAHSHADELGRSSDSTLRARIETAFESLRAGSWQRPDFAEGFAVLREVAGRTLGKRHFDVQLIGAAVMLEGKLAEMETGEGKTLTAGLAAAAAALSGVPVHVVSVNDYLVERDAEQLRPFYEWLGLEVGIIVEGRSIPERQAAYACPICYCSNKELVFDYLKDQITLRGSGGPIALSLDRVYGAENRQSRLILRGLHFAIVDEADSVMIDEARVPVIISRTNDADALAGRVVEAIAIARELRTDDYVVNRERRSVKLTDEGRLRLLEIS... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular mo... |
A0A962R9A3 | MTTDFRRPFTPIARLLGSVLLMLLLGGCDEKPSQLERIQERGELIVATRYGETTWQRGADGPEGIEYDLVTAFAEHLGVTPRFVFPDRFTDTLGLVESGTVDMAAAGITVTERRKRRVRFGPAYQHVVSQVVYRRGERRPRRIADLAEGDLEIIAGSSHETLLRDRRRREFPKLEYTANDEVSIDQLLQWVAIGFIDYTIADSNQLELTRRRFPELRAAFDLSGKRELAWALPRGQDASLLDAVRAFFQIIEADGELNALIDRYYGHTEKFTYVEIRDFRRAIDDRLPLYIDAFKQASRDTGFDWRLLAAVGYQESHWRA... | Function: Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates... |
A0A1C3N830 | MRVLLVGSGGREHALALGLASDPAVTTLIAAPGNPGIAAVAELRTVEATDPAAVAALAVETGSDLVVIGPEAPLVAGVADAVRAKGIPVFGPSAEAARLEGSKAFAKDVMTAAGVPTARAYTCADPESVARALDEFGPPYVVKNDGLAAGKGVVVTDDRARAEEHARECGRVVIEEYLDGPEVSLFVVTDGEAAVPLLPAQDFKRIGDGDTGPNTGGMGAYAPLPWAPPGLVDEVMRDVVHPTLAELRRRGAPFAGLLYVGLAMTAAGPRVIEFNARFGDPETQVVLALLETPLGGLLHAAATGTLAEHPPLRWRDGAAV... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Len... |
A0A2D6JEN8 | MDLSKALEAREVLNITLVEPEIPNNTGNIGRTCVGLRSSLHLVGPLSFDLSEKKVRRAGLDYWPHLNLHQYESTEEWLSSLKDRSRVFLFTTKAEKSFYDVDYQVGDTLVFGKETAGLSAELRGMFAENCVKLPMPGEVRSFNLANTVAVAAFEAYRQIEKANS | Function: Could methylate the ribose at the nucleotide 34 wobble position in tRNA.
Catalytic Activity: 5-carboxymethylaminomethyluridine(34) in tRNA(Leu) + S-adenosyl-L-methionine = 5-carboxymethylaminomethyl-2'-O-methyluridine(34) in tRNA(Leu) + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.207
Subcellular Location: Cyto... |
A0A2E0GPY7 | MNKLKCPAKLNLFLKITGERNDGYXDLQTYFQAVDLCDYLNLYHREDDLVLYSDNYKHDLSNNNSCVKAAELVKNYTGIENGIEIQLEKNIPVGAGLGGGSSNAASTILGLNNLWDLKLSEAEMLNIGRQIGADVPFFVKQASCFAEGXGDELXDVDQPQRYFVIIDTEEIVQTKEIYQLISSADSFDSKINDTKNIDCIGYNFFEKIVCKKYPKIQEILEILRKYQNGVLTGTGGSVYSYFESIDDAKLIFQKLPDTLKKFLAKGLKSYTIYX | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
A0A920ANM1 | MFLSQAEVGRISAENILFALVLFSPGLINLVFPVSVFLAMGFVLTPLFRNHETVLTAGSMTTSRLLVSQKYLILGIFSISVLLSTFLAPYFTSKGEDLLDKDNSFASKILAPNGLVSLQADTFNVFGDKDNDIYRDLIFINSQSIDTFIYGTTGVIEDTASGASLVLYDGFLFDNQRNFISKFKKADIPFADYSSEEYVSTLIV | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Subcellular Location: Membrane
Sequence Length: 204
Sequence Mass (Da): 22512
Location Topology: Multi-pass membrane protein
|
A0A947BY74 | MSDKNHKNQDHFEKQLDELEQIIYRMEDGDLSLESSIKEFEQGIKLANDCQKTLSQAELKVKILLSENDTELSNFDVSAGDQAASDSQNN | 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... |
A0A3C0T637 | MRTGIAVLGGTFDPVHLGHLESARSIRDALSVNEVRMVPAFKPPHRNPPESSAEHRLAMLQVAVEGLPNIVVDDREIRREGRSYTVETLTSLRDEVGSEVAVYFVMGVDAFCTLDQWHEWRSIADLAHIVVLQRPGHEMKLSEKMAKWIEDRETEKLEELVNHPGGGVCFLELEQVAVSSTEIREALHRGEVPEGKLPGLVRAYIKCHDLYQRENSNAEC | 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... |
A0A6L9SAX1 | MSISPRITGATSRTVSATQGRGGSDGYRGFVRAVWKRRAQVLGAIAAGGVVGAEARYALTLLGGDDPRFPWATLAENITGCFLIGVLMAVILQLTAPHRLVRPFLGVGMLGGYTTFSAYAVEVRELIADDRAAAALSYLVITPLAALTAVWLGVRGTGAALGRLRHRGT | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 169
Sequence Mass (Da): 17697
Location Topology: Multi-pass membrane protein
|
A0A8T6HUW9 | MKLSNYIRIVLVEPSHPGNVGSIARSMANMGIGNLALVASRDFPSPVASNRACGADWILDGASVYRSLDEAVEDCALVFGTTARRRSISWPTVSPEEAMSMAVEAGSRFAVVFGRERNGLENRELDCCNYMIRIDVDEDFPSMNLASAATILSYEFRKAAQGKRESELPEVDYATSEQLGGLIAHLEETLLLTEFLDGRSSLLIRKLRRLFNRSRLSREEVNILRGILTSVERKAGRKPPVRQSPDLGRE | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
Catalytic Activity: S-adenosyl-L-methionine + uridine(32) in tRNA = 2'-O-methyluridine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.200
Subcellular Location: Cytoplasm
Sequence Length... |
A0A2E8BZ27 | MEAETSILALTKALIRRVSVTPEDAGCQELIGGMLQELGFATEQLNAHGVHNLWAWRGQDPAGEASTQRHVMFAGHTDVVPSGPSEQWRSPPFEPTIRDGLLYGRGAADMKSSLAAMIAAVRAFVEEYPDHPGTISFLITSDEEGEAIHGTRHAIAELAERGIKPDYCVIGXPSSSDQLGDVVRCGRRGSLNGRVIVKGVQGHVAYPEMVSNPIHMAAPALDALTREIWDSGNAYYPPSSLQISNIQAGTGATNVVPGELTAWFNIRFNTEQSEAGLRARVEELFXQHELNSVFHWQLSGPPFLTEQGDLTKAVQEAIMA... | Cofactor: Binds 2 Zn(2+) or Co(2+) ions per subunit.
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3.
Function: Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,... |
A0A946M964 | MQEQVILVNKKDKPIGLMDKLEAHEKGALHRAVSVFIFNSNNELLIQRRALEKYHTPGIWSNTACSHPRNNESTLSCANRRLFEEMGIKTKIFPIFSFIYKAEFQNNLIEHELDHVFIGFSDKKPKPNFKEVCSWNYVDETSLIKLLNDCPESFSPWFRICYERVFQKAYAQKNKKLISLS | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isope... |
A0A937II50 | MNLSKLSFLILGKGVTYNNCKIFFDKNSITYQAINTDDILNIDNDSILTKNGKINIRSINYIVISPGIKKENKYVKKLLDAGYELITDVELLQSQLKAKYICVTGTNGKTSTVNLLADILNNNNQKALACGNNGVSLFKALEEDFSYIIIELSSYQLEYIKNLDSFISIILNISEDHLDRHDSLKEYLDIKLQIFNNADNCIINSDIAVSKKYQTYNINKNKFLINGKILKKISFMDYKSVKLNKRIFKVNGKHEVMNLCACLAILKIIGLSINDTLIGFSQRLALPHRLEKFCTYKATNFINDSKSTNASSTLNALESI... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
A0A9C9SAE0 | MGRIRRIHFVGIGGVGMSGIAEVLLNLGYQISGSDLRENATVARLARQGIRIRLGHAAANVQGADVVVISSAVEADNPEVVAAREGRIPVVRRAEMLAELMRFRFGIAVAGTHGKTTTTSLIASLLAEGGLDPTYVIGGQLNSSGVNARLGASRYLVAEADESDASFLHLQPMLAVVTNIDADHMETYGGDFERLRQTFIEFLHHLPFYGLAVLCLDDPVVRGILPEVAKPVLTYGFHEAADVHAFDLQQEGSRGRFRVILPGRRQPLEITLNMPGRHNVLNALAAIAVAGELGVGDVAMGRALASFQGIGRRFVIRDAV... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
EC: 6.3.2.8
Subcellular Location: Cytoplasm
Sequence Length: 358
Sequence Mass (Da): 38552
|
A0A2E1Q304 | MDKIGIFGGSFDPIHFGHINSMTTVREKMGLDRVLVVPTAESPLKVKTQGESPEARWAMIEAGLSHQSEEFQISDLEIKRGGTSYTVDTLRELQNSGSEDQFFLIIGLDQLQQFDQWKNFDEILNRVDLIVTSRPGLHFPKIARQFPREIAEWIEDFDGQVAMLKNGRSIYFVQLEDVEASSSEIRRKIRLGQPIHGMVPSEVASYIEEHQLYAALNKKIGDFEKFTHFSADILKDHGGILVRAFDLREINSPSEFGLVTSGTSVRHASSLAEKLIEETRKKYGVWPQGIEGLKEGRWVVVDYGSLLVHVFYDFVRQEYR... | 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).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NA... |
A0A3D1EIS2 | MHAPQDADDGEAWYFAFEKQQLICKSVAGMPEPPTADDFRWMDYEVVSKHFLGRYQNRPCYALDVRGKASEGFSAVGLRSLLGRTSPALFYLAGRALQVVDWHSTHQYCGRCGTRMELHAADRAMKCPSCGLTNYPRISPSIIVLVTRGDEMLLARNAAWPSGMYSTLAGFVEPGESIEQTVHREVMEEVGLAVDNLQYFGSQSWPFPNSLMLGFHATYAGGDIVCQPEEIADAQWFTAATLPQTPPRTAISGWLIQEFIDQLENNSR | Cofactor: Divalent metal cations. Mg(2+) or Mn(2+).
Function: mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at th... |
A0A2D5I4G3 | MTEEIAHINKEFWDNXSSIYSXPIQTDNYLHRICXSIESKIKRXFKLAGLHDNYSLXAIGGFGKKEMFPSSDVDISIIKKNKDESKVPQLEXFIASMWDSGYKIGCSVRSMNELKKIVKEDPKELTAYLTIRPLISENKEYEKIQKIIAQAWTKRRYFKAKCDEKLHRHLSFDSSALSLEPDLKESPGTMRDFHNSEWILNYCFGLSNFKEIRSSDDFKEDFNSVVISYKFIKTLRYATNICTKNKNRLNFESQIDIAKQAITKNLNYKDKVELVMKSFYFHVQNILSFNEMVSQIFNEQSSIGIKRKKGSFFVKNNQIG... | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher ... |
A0A2E9EDA2 | MNLILLGMPGAGKGTQAEIIQREQGIANISTGAMMREISRAETDLGKKVQEYLSTGRLVPDEIIIQMLVERIHQSDCENGFLLDGFPRNLDQAKALDQAKVEINLILFLKISEKEIIERMSGRRVHLPSGRSYHIAHNPPKIEGKDDVTGETLIQREDNHPDVIKKRLNVYYDETEPLLSFYRQKDISFYEIDASRTLEEVSEDIRNVISN | 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... |
A0A2G6DZA9 | MWLLPVSSRRVVVEYGRTRHLVSALVGLADIHCGGSRVFLPCSQTLMSLSNAELLGWILGYMGLLSAVAYSAERGILPKSLSRHPLIYVLSLGVAADAMASFGAMELAERFGYGFLLYYIGIALVFFLSSTVVLPLLRLRQVYQLGSLADLLAFRFRSTKVGMAVTLAMFLLLLPLFALQIDTVSQSVSLLSGSGGEENSGQHLLGLLFCLAICVFTILFGTREQHSQHQHDGLVVAIAFGSLLKLVAMLTLMFAAIFAVFGDFTGLQHYLAQNPTQAQLLENEAAVTRAALLMFIAGAIAMPQLYQMAFKESPEHNHLN... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 1013
Sequence Mass (Da): 110273
Location Topology: Multi-pass membrane protein
|
A0A7W8N8X6 | MSESEETPVQARSREPAESTSINTPLPWAYGVPPLKAQLRSTPDDFRVEEVLGYDADGQGEHALLWVEKRGANTDWVARELAKFAGVAQVAVGYAGMKDRHAVTRQTFSVQLAGKPDPDWSTFPHADVKVLAATRHSRKLKRGALRGNRFVLVLRQVQGDRDAAEHVLQQIARRGVPNYYGEQRFGREGGNVAQARAMFAGRRVERDKRSFLLSAARSQIFNSVLAARVERDAWDSPLDGDIWALAGSRSWFGPEPFSEVLAERLARLDIHPSGPLWGQGELPSKGAAGALEQSIAESYSDLAAGLVAARMDQERRPLRL... | Function: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
EC: 5.4.99.27
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Length: 357
Sequence Mass (Da): 39476
|
A0A6L7VMC7 | MQDTLQDLIKDITAGVSFNRAANMLVTRVTNILNCNICSLFILDAKTEHLQLIANEGYLDLDPKQISVPPHTGVVGLVVERKEPLNLTDVNTHPAVYHINGHDEHAYPNFLGVPILHQQRILGVLLAQDEHKVFSEDDEGFLTSLATSFSAQVSHAIATNEIELDASIAMLHEEQHFRGFAGSPGIATGIAVLRHPPTHLDVSFRLIEKSDIEDELREFNGALRVVVEELTKGRERMMSVLGPEEIALFDAYLHMLDDEAIPQEVRTTIVDDCVWSQSAVSLVFNRHIRELERSENSYLAERGQDLRDLGQRLLAAMQHR... | Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
EC: 2.7.3.9
Subcellular Location: Cytoplasm
Sequence Length: 763
Sequence Mass (Da): 85054
|
A0A2D7RKF1 | MNFKELIPDYSGNINDLQLNSISINSQDITNGDLYISLAKNITNQKKYNLDAFKRGASLILTNKKSLEXREKKIIFVENLXXNLGSLSNKFYKNPSKKIKIFGITGTNGKSSVSYYLFQLLNQIEKRNGLISNLNLKKSGIHFSNLTTPDIFTLNKILSSFISDKKKAAIFEVSSHGIKQKRISGIDFDYGCLTSFSRDHLDYHSSMREYGKVKESFFLDNKFKGGVINIDSKIGQRIFSFKKDFISISKKNKKSDIYIEEKKGQFFIHSPWGNLKFPERIFADHIMMNMASAFGLYCISSKKIDLKMLNLNNIFDLPGR... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in... |
A0A1H3DEQ7 | MSFTLGKEEKLKSKKLIEQLFIQGKRVKLYPFQVIYSEIDHDGDFPIKFAVSVPKRNVKMAVKRIRIKRVIREIYRLNKHKISENIHKKYMCMFIFMGKEELDYATMEISYLKLIDKFLTKIKNDEE | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
A0A7X2N2D3 | MVVSFKPYSLALYELAKDKDQVPYYMEQLKKLSDIWKENEDFLKALRHPKITRREKKEWISQLFESELDPLLYRYLLVMVEHDQIGYIPEIYEAFIEVYKEDQNIESVLIESACPLSEDQIRQIKTVIEKKLKKNIEVRTNVVPELIAGVRVRTKDFVLDNSMLSRISNLKEKLENAY | 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 c... |
A0A661CPB8 | LILGMDAFLGLPQWHKWERLITLANLLVVHRLGADLPEKHTMQDFLKAYQADSHEALSKQTAGALWIEEIPILNISATQIRGLIAAGKNTRYLLPVAVLDIINTHQLYR | 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... |
A0A2E5I8H7 | MGVFLKRKDKFALISVSNKKNLQDFANFLKENNFHIVSTGGTKEYLENKGFKITSVSELIDFPEILGGRVKTLHPNIHAGILARENDSDLLEELNIKRIDLVVVNFYPFEEIIKDETNKLDDVIENIDIGGPTMVRAAAKNYINCSVITDFKDYEEFAKNYKDNDGELTLEFRKRLSIKAFQSVAHYDSCISNYLSMKAEKTKFPSRIFYSFIKEKDLRYGENSHQSASIYSNAFSDYGTLISSRILQGKEISFNNVVDSETAIKCAISFKEPSCVIVKHANPCGVSVANNSKTAYSNAYLCDPTSAFGGVIAFNSKINA... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-c... |
A0A2E3DCA5 | MRNSNPRVITIDGPSGSGKGTISVRLAEILGYNYLDSGLLYRLFGHEVRRRNIPLSFLEGSRKEARDISKSIKTKFPEFFFGENAKKMMGNTDDLFDVLRSDQAAVDASNVARLPVVRQELLDLQRTYRLHPGLIADGRDMGTVVFPDADLKIFLTASVLTRARRRYKQLKDKGMSVSLDALAVSIEERDRMDSMRKESPLRPSEDADVIDSSELGIDQVLEIIESRFKEKLTDS | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 235
Sequence Mass (Da): 26513
|
A0A355ATN5 | MTQTLTRTLRKIEQAGAANSLLSMRRGLEKESLRVNQGGIISQRPHPSHLGSALTHPYITTDYSEALLELITPPHLNTESLLQEMTDFHQFAYRNLGDELLWVNSMPCILHGDDSISIANYGTSNVGRMKTIYRIGLSHRYGKLMQTIAGIHFNFSIGDDFWRSWRTMCGSTVPLREFKSEGYFGLVRNVYRYGWLISYLFGASPAVCQTFLDGRDHHLELLGESSYYLPYATSLRLSDLGYRSDAQAAIRINLDSTDAYIESLIRATTESYPPYEEIGLRVDGEYRQLNTNLLQIENEYYASVRPKRTIQTGEKPTYAI... | Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 518
Sequence Mass (Da): 59133
|
A0A7K8KHX4 | VLVGNPFDCSCGLRWLQLWQDGGRAELGNQSLGCWDGSALVPLATHHLGACEPPAVRIEHPEAALRQGDGVNLTCRIAAQPPADAEWVLPAAATDLSERELVLEISNVSSKLNLKDLTCRAENAAGPAEDSVTLNVTFPPSILLLQEAIPQHFWCIPFSVDGNPTPSVRWLFNGSALAEGPYIHTRVVEYEHNSSVLHGCLQLNRPTHVNNGNYTLLARNALGSAACSVQGRFMENPFSFSPEEPIPGTRNSSLEGPVETADEHAFGVLVAVVLAMFACLFLSLTLIVLNKCGRRSKFGINRSAVLAQEDELAMSLRFMN... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
EC: 2.7.10.1
Subcellular Location: Membrane
Sequence Length: 534
Sequence Mass (Da): 57993
Location Topology: Single-pass type I membrane protein
|
A0A9D0VZY1 | MPATPWPATGSSGSSGSVSGTARRDWIPSTWSSSGAPASPRAATGSWSSRCNTTGRRSRTMRRLMLLMISGYRVLLSPLLGNNCRYYPTCSCYAHTAIERFGVLKGGWLALRRIGRCHPWHEGGVDPVPEKHIPHG | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 136
Sequence Mass (Da): 14781
Location Topology: Peripheral membrane protein
|
A0A523KDP7 | MHGETKMHLEGFRVSLYVGVVAVLAVSAVAQAQTSSSSAAAVEVSEAPAVEVSEFSLDTLMSRPEQILLQNAADRYTFYIPLSPRVRLRRATLALAFTNSISMFEPRSQLRVRVNGRVVGQTLLDARNPVRELSVDIPPDLMEPGYNEMEIQVAQHYASQCENPMAPELWTNIDTSTSRLKFEYELPAIQTSLAEIPILINPLGWNPYRLTIMTVTSKLQEFDLALGAVLSEGVATSLKYRPLKVSHAVALPVPEEIGETASGRVALIGNPADADATLFGTSAKASHAVMLPASEEVRESALGRVALIGNPADADTILFG... | Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Function: Binds the cellulose synthase activator, bis-(3'-5') cyclic diguanylic acid (c-di-GMP).
Subcellular Location: Cell inner membrane
Sequence Length: 811
Sequence Mass (Da): 87697
|
A0A2G6KRZ4 | MKIAIFGAGSIGCYLGGCLVANGANVAFIGRPRIQQELTQYGLSVSDWQGRKETCACDRFTFSDRPEACRDADFILVTVKSPDTTDAAIQLGPHIKQGAVVASFQNGIRNADLLRKHIKDNPVLTGMVSFNVSHTGNGRFHCGTEGYLALESRQDIEKPLVRLLDSSGLPCQACPEMKSVQWGKLIMNLNNPVNALAGIPLIEELEQRKYRKVLAASIREALEVLKQAGIKPARIGKVPPSLMPAILELPSWLFKLVARAMLKIDPQATSSMQEDLVSGRKTEVDYLNGEIITLGEKSGLQCPVNRKIVALVKESESGRS... | 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: 345
Sequen... |
A0A2E0MYW2 | MLNLDKLSLEEMLGYQRIGIAFSGGVDSHVLLHFLTKKLHKHTNLFALHINHGINDQSNLWERHCKEICNSLGVNFVSFKLSFKDSSSVNEHDLRKARYSKLLSWANDEDVICTAHNKDDNTETILFRIIRGTGIKGLKGIPFKRKIGNVHLIRPFLQISKSEIIDYAKKNNLFWIEDPSNQDITFSRNFLRADILPLIKKRWPKYTDSFSHLSIHAKYSQEIAEEVADLDLKKYLLGSSNQLSLSCIGHLSEARFLNLLHRWLSNYSTQPISFKIIQEIKKTFLTENKQTDPIITLGGVDNEGSFQLRKYGEVLFILPH... | 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)... |
A0A964PI18 | MCGNLKPGPGGAGSPAAGPPQGEASALAIGLIQGYQRLLSPWLGMNCRYVPTCSSYAVDAIRRFGAVRGGWLALRRIGRCQPFVWLGGSSGVDPVPQDYVWWGRH | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 105
Sequence Mass (Da): 11170
Location Topology: Peripheral membrane protein
|
A0A2E8NJL7 | MLTIDAWLRQNGARFQHELEILARAYFGISKAEFICESDQSITPNLKNYLSDALVKLKRGTPLAYLLGYKEFWSLEFQVNRNVLIPRPETELIIEKSIELANDGDSVLELGTGSGAIAIALAKERPDLSITATDISIQALEVARENARKHKCKITLEHSDWFESVSGTWNLILSNPPYIAENDPHLDFLAMEPRVALVSGPTGFEALDVLIENAHNHLKPCGHLIIEHGIGQAQEIKKKLASHHFTEISSHKDLANINRIVTAQQVSPEYG | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A2E0GMU0 | MSKKIFVANWKMNGNTEMIDKFSGSKILNSSPKKDIIICPPYTHINYLSSKIRDKNISLGAQNCSHKENGALTGEISAEILKDIGCEYVILGHSERRANYSEDXSLIXQKXILAXKNNIIPILCCGENLEDRKNNLSTKIIENQLSILKEISDNFTCDKFLIAYEPIWAIGTGKSASSSQIYEILNFIHEYTYDIFSQLDLSILYGGSVSTSNIKELLTIDKCNGFLIGGASLSLDSFELICESI | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Lo... |
A0A534AHF9 | MPIPATQFIWFNGKLVPWEKATVHVLAHALHYGSSVFEGVRAYETPRGVAIFRLRDHTRRLFDSAKIYRINIPFSAEAINEACRQVISANALERGAYIRPVVFRGYGEIGVTPKVEPPTEVAIAAWEWGKYLTHEGEEAGVDACVSSWQRVAPNTLPALAKAAGNYLSSQLIGAEARRLGFAEGIGLAPDGTLSEGSGENLFLVKDGVLLTPALAHSVLGGLTRDTVMRLARERGLEVRECAIPRELLYLADEAFFTGTAVEITAIPRARRPTSGAGSTTSTCRRRGSPPPAERARVSRMARSPQTLFDKVWQRHVVSAE... | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.
Function: Acts on leucine, isoleucine and valine.
EC: 2.6.1.42
Catalytic Activity: 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate
Sequence Length: 599
Sequence Mass (Da): 64847
|
A0A6N8VIZ7 | MMIELDTQNPCFPAVSAADSDGLLAIGGNLEITTLCAAYRRGIFPWYEDGQPLLWWSPDPRMVLLSNGMRVSRSLNKVIKSKFADIRLNHNFKAVIEQCAIPKNRRTTTWITETMRDAYLKLHQAGYAHSMEVYEQETLVGGLYGIGIGQMFFGESMFSNESDASKVALFYLCRHLYGHQLMLIDCQVQSPHLQTLGAFNIARTQFIEYVAKFCKLETPAGLWRPQRFPSLCVPQR | 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... |
A0A920ITN7 | MNEISSEYSALAARVEELEFNKMFSQKADPNSAFLDIQAGSGGTEAQDWAEMLQRMYFRWAEAKDFSVEIIELSPGEVAGIKSVSMHIKGSYAYGWLRTETGVHRLVRKSPFDSGNRRHTSFASVFISPEIDDSIEVDLNPADIRIDTYRASGAGGQHVNKTDSAVRLTHEPTGTVVQCQNDRSQHKNKENAFKQLKSKLYELELQKQKEEQKVLEDSKSDIGWGSQIRSYVLDQSRIKDLRTNVETGNTQNVLDGDIDIFIRESLKKECSE | PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF2.
Function: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
Subcellular Location: Cytoplasm
Sequence Length: 272
Sequence Mass (Da): 30732
|
A0A6N9C0L3 | MAWRVGSISTTAVRVLVGLGSNRGASVDIVSRVLEDLREMSVGEFRASSLWRTSPVDCPPGSADFVNAVAAFHADARSPEWLLSRLKAFEGRYGRSMAPIRNAPRELDLALLLFGDVVRRTQRLTLPHPRALARGFVMTPAAEAAPEWTWPGTGRTIADLARGLMTDETLTRLTEPPGVAVERAG | 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 ... |
A0A1X6P804 | MASGGVGTRGTSGRCYSLWMDYSQCVDDAAVPTACLDVRDDYIECLHHYKEFMRMKVVAAEMVAKGLKTVGEKPPPSAATPAGHGGGGH | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
A0A2D7G392 | MSLLVYGINHRTAPLPLREKIAFSEIEQPHSIQNLLSNNSSVKECFIVSTCNXTEXYCSIESANSVDIKYWLINEKPVSNEELINCSYEYWDSDAVSHLAKVACGLDSMAVGEPQIMGQVKQSIETANQGNLIGENLDLAIRAAISAAKEVRTRSKIGENAVSIAYAASSLATKIFSDLSKKKALLIGAGETVEIVASYLNRRKIGSLTIANRTISNAEALASRYTAKTTSLSSVNSCLHEFDIVISSTASSFHIIGKGTAEAAIKKRRRKPIFMVDLAVPRDIEPEISELPDIYLYSIDDLQEITAQNVQLREEEKVFA... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tR... |
A0A521Y673 | MYSFIKKALFQLDPEQSHSVALHALQLAYRLKLLQLYPTVPNNPRQVMGLTFPNPIGLAAGLDKNADYVDALAALGFGFIEIGTVTPKPQSGNPRPRLFRLAEQEAIINRMGFNNKGVEYVARRLEQTRYRGILGVNIGKNKDTPLEKAIDDYLIGFRKLWKFASYIAINISSPNTPGLRDLQQDNLLQQLLTELQHAQQRVMQS | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
EC: 1.3.5.2
Subcellu... |
A0A2E6YEF6 | MAFVIITTIIVIGTVLFNLVTPWWFTPLASNWGSLDQTIIITLWVTGVAFVLISAFILYCVVKYRHREGHKSKYEPDNPKLEFWLTVVTTVGVVIMLAPGLIAWKDYIELPEDALEVEGVGQQWTWSYRFPGEDGIYGNTNGRLISSKNTFGIDPSDAYGQDDVLVLDNKVHLPINKPVVFQLRSKDVLHDFYIPQFRAKMDLVPGQQSNLWFIPTELGTYEVACAEFCGTGHWAMRGEITVDEMADFEAWLSQHPTFVETMNKSSEGRGKQIVQSLGCVACHSDTGASGIGPTWQNSFGSQRNFVSGESINIDGAYIKE... | EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 360
Sequence Mass (Da): 40110
Location Topology: Multi-pass membrane protein
|
A0A938WHW2 | FASRVIRGIDPAAATPLWLRERLRRAGLRPRGPAVDVTNYVMLELGQPLHAYDLRRITAPVRVRMAEAGERLRLLDGSEIAIAADTLVIADAVGPVGLAGIMGGEKSGIADDTTDVFIEVAYFAPEAIAGRPRRYGLTSDASQRFERGVDPRLQERALDRATRLLLEIAGGRPGPALMTQVDAALPRRPGVTLRPERVQALLGIQIPRAEIEDILRRLGMQVAGAGDVLGVIPPSHRFDITLEADLIEEIARIHGYERIPALDAAMPQQPQPASEQAVPRERLLLLLADRGYQEAVNYGFVDAGLQRLLFPQSVALPLEN... | Cofactor: Binds 2 magnesium ions per tetramer.
Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 577
Sequence Mass (Da): 63088
|
A0A6P1M514 | MKNLIRKSVQALDGYVPGEQPQGSDVVKLNTNENPWLCSVEVHDILREIDMAALAKYPDPVCTEVRKVIAENLSVGIGNIFAGNGSDEVLALCIRAFVERDGGSVGFFDPSYSLYPVLANIEDVETRPVALDENFGWQMPDGYESSVFFLTNPNAPTSLLFPKEKVEEFVCSFPGVVVIDEAYVDFASETCMDLATQYKNVLVCRTLSKSYALAGIRFGYCVGDKELIDALYKIKDSYNVNTLTQEVARVALLDHGTMEAITTAVKNSRKLMTEELQALGFDVLPSETNFLWVKPPKPGAKKIFEELKKRNVYIRWFEGD... | 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: 354
Sequence Mass (Da): 39272
|
A0A944USC5 | SRPLTMFCYSLGWSEGDWVPESQMQVLESLQGWGFRVNPLVEVVTDSKGCMDYIHNILEQRSRLGYEIDGVVVKVNSLEQQSILGAVTRKPRWAIAYKYPAEEATTQLLNVEFQVGRTGAITPVARLAPVFVGGVTVTNATLHNMDEIARLGLHVGDRVMIRRAGDVIPQVASVILSQRPGDARAIELPTQCPSCNSAIVRLDDEVVARCSANRNYCPAQRKECLRHFASRLAFDVDGLGDKIIEQLVAEELVKSAADLFRLDAVQISGLERMGEKSAKNLLQALEKSKQTTFPRFIYSLGIREVGEATALSLAQHFRTL... | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
EC: 6.5.1.2
Catalytic Activity: NAD(+) + (deo... |
A0A8T3SEG0 | MNQPKKKIEQQFIIPSEFATLRLDQALAKLLTDYSRVQIKTWIDAGNILLNNQLAKAKTKLRGGEAVSLKAEFEAQADWEAEAIPLPILYEDEAIIIIDKPAGMVVHPGTGNQSHTMLNALLHHAPQLALLPRVGILHRLDKNTSGLLLVAKNHASHKFLSGQLKKRLIGREYQTIVNGLFISGGTVSAPIGRHPTKRQQMAVVPLSLGKEAITHYRVMEKYRSHTRLKITLETGRTHQIRVHMHHLRHSVVGDPTYAGRLQFAKGLTEELKNEIKLFKRQALHAYRLTFIHPDTELEVSFESKIPSDFQQLITALKKDN... | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 327
Sequence Mass (Da): 36947
|
A0A352KLH6 | MMQIVIGQHNLDVGNAPCVATIGNYDGVHLGHQSVIKHLSERALSLNLPTTLVLFEPHPQEFFHKQHAPSRIYTFREKVELIRQAGIQRLVCLRFNQAFSQMLPEEFVQQLLIDKLAVKHLVVGDDFRFGRDREGDFAFLNQYANRGDFSLEAMPTFEVDKSRVSSTRIRQALEQADFTLAEKLLGRAYSLSGRISHGQKLGRKLGFPTLNLPTRRLRSPLQGVYVVEVA | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
Function: Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD.
EC: 2.7.1.26
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 230
Sequence Mass (Da): 26110
|
A0A520TQU4 | MNILAPAKLNLHLQVVDKRPDGYHNLKTAFQLIDLYDELEFKLQDEEIEIEETNLEIENNLVLLAADALKKASNINKGAKIKLIKNIPLQKGLGGGSSDAAATLLALNSLWSTNLSINELMSIGLDLGSDIPFFLYGKNAWAEGRGEKMDSLFLPKSWFLLIFPEKNISTKEAFREIKPDDRNYINKKDFLQGKAFNTFEDWARQKYSEINDLFNLLETIGKPRLSGTGSTIFISFSNKEDALSAKEKFSSSVLVNSLDDSPLRQLIE | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
A0A8X7NC89 | MLSASRILRSAASPALRAASAAGNVSAGPSISTPSIAPRTKQTTEIFGIDVHPSPLTDLRETYKRTLSTLNALPEGTVYRQATEALTSHRLSIIENALSQSKIVDEDVIKSVEDKLDLGQIEEVIMQANDEFGLVAKMIDWKASEPLEHPPSASQWKYFDMTEEAGEGEQK | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
A0A661EGP5 | MKIKTRFAPSPTGDLHIGGVRTALFNYAFAKKNNGLFVIRIEDTDISRSTKESTTIITSAMDRLSMQSDEPIVLQSQNTKKYQEIIDTLLKSGNAYKCYCNKQRLEDLKITKKKEKKTYKYDGKCRYNKEDKNLPFVVRFKNPQDGRVEFDDLIKGKIIIENSQLDDFIIARSDGTPTYNLCVVVDDITMKISHVIRGDDHLSNTPKQINIYKSLGANIPKFAHLPMILGEDGKRLSKRHGASSVLQYLDDGFLPSALINYLARLGWSHNDLEFFMPDDFFKIFNLKNVNKSAAIFDPAKLLWLNQQHIQKTDKQEIADK... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
EC: 6.1.1.17
Subcellular Location: ... |
A0A6L7XUI4 | PPPPPPPPPPPPPPPGRASARETAMRVAAGAIARKYLAERAGVTVRGHLSQIGRLRLEPVDMDAVDSNPFFCPDPDAIDAIAGMIEALRRDGDSVGAQVTVRASNVPVGLGEPVFGKLDAELAGALMGINAAKGVEIGAGFAAIEQRGSEHRDERDLTGFRSNHAGGVLGGISSGQDIVARVAFKPTSSITKPGRSLDIHGNEVEVVTTGRHDPCVGIRATPIVEAMTALVLMDHLLRDRGQNLDVARDG | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Length: 250
Sequence Mass (Da): 26064
|
A0A8T3RX90 | MRIIAGTWRGRRIPVLNAEGLRPTKDMVRETLFNWLTPRMAGARCLDMFAGSGALGFEAASRGASHVLMLEQQAILVKHLRTQKDLLNATQIEIQQVDSLQYLASLQQIFDIVFIDPPFTALNMQQVLAVLHSSQCLTAHTLLYIEQSAAQGLPALPSGWHYERQKQSGDVVYGLVAIN | Function: Specifically methylates the guanine in position 966 of 16S rRNA in the assembled 30S particle.
EC: 2.1.1.171
Catalytic Activity: guanosine(966) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(966) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Length: 179
Sequence Mass (Da): 19899
|
A0A938PWN5 | MDTDAIMQWAAMGQHGFYVWLAYGVSLVVLLLVIVKTRIEASGLKKELELDLQLKARESGRTVSSAREG | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 69
Sequence Mass (Da): 7651
Location Topology: Single-pass membrane protein
|
A0A3C0L184 | MSYQVLARKYRPGHFKAMEGQGHVLQALINALDQNRLHHAYLFTGTRGVGKTTIARIFAKCLNCEQGVTSEPCGTCSSCVEISEGRSVDLIEVDAASRTGVDDMRDLLDNVQYLPTASRFKVYLIDEVHMLSKSSFNAMLKTLEEPPEHVKFLFATTDPKKLPVTVLSRCLQFNLKNMTPERVVNHLKVVLAEEGIEAEDSALWQLGRAADGSMRDALSLTDQAIAFGSGKLLGTEVASMLGTVDRQEVYRLIDAVAAGDGAKVYEVIDQVAEFSPDFSALLDEVLTVLHKVAVFQVVPEGVDNSFGDRDKIGQLATHIS... | 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: 454
Seq... |
A0A661CSA9 | QYLKELEAFVPDIAGVCRLAIDNALEDKDFLRLDAASFKASPSDSIDYAVMENTKAAAVIPLEAGWNDVGAWSSLWEVSEQDSDGNVILGDVLTEKVHNSYLRAEYRLLTAIGVENLTIVETADAVLVAHKDHVQDVKQIVARLKSSERSEANLHRKVYRPWGNYESIDAESRFQVKHITVNPGGSLSLQMHYHRSEHWVVVKGTARITRGDETFILTENQSTYIPLGVKHRLENPGRLPLEIIEVQSGGYLGEDDIVRYEDVYGREGLE | Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1.
EC: 2.7.7.13
Catalytic Activity: alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose
Sequence Length: 270
Sequence Mass (Da): 30276
|
A0A6L7N2T5 | MKPGCRFRWLGLSEYTSVADRMLQFTDSRDRETLDEIWFLEHFPVFTQGTSSRLEPHRNPDGIPLIRSKRGGQITYHGPGQLIAYLMLDLRRLGIGPRRLVELIEDCLLRLLADYGLEGKRRAGAPGVYVEDHKIAALGLRIRNGCSFHGFSLNVNMDTTPFTWIDPCGYPGLVVTSLALNGVDRKMETVCRDLKRCLSDVFEWESDGTGAGVEGIR | 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-A... |
A0A6L7VQ70 | MPLLVYGLNHESTSLDMRGRLSVAEDELAQALLELRAETPDLAEAAILSTCNRIEIHAYANEDGIESIKQWLAHSRQVPIEEFSFASYVHKGRAAAAHAMRVAAGLDSQILGEPQIQGQFKLAYRHARESGTLGKELSLLEDFTLQTAKRIRTETKIGAEPVSVAFAAVTMAKQIFAEFATQSVLLIGAGTNIQLIAKYLRELGITSFTIANRTRTNAEILASDLAGRVINLDEIADELHNFDMVVSSTGSAKPIVTEKMLSNASRLRRHRAMFVADLGVPRDVEAKAANLPDVYLHTVDDLSTIISQSLTKRQEFTTIA... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tR... |
A0A6L7XSA7 | MLDVDVAAAKLGELIEPLRGTERVRVDAALGRVPLQNIVAPLSLPPFDASAMDGYAVRATELASEGRKRLKVTGQSLAGHPAREAAGAGTAIRIFTGAPMPEGADSVVLQEDVTAKAAAIEFDESVRVGQHVRPSGNDIAKGDTICRAGHRLTPYDLAWLAACGISTVRVRRRVRVVLLSTGDELAEPGMPLGEAQIYDSNRFAMTRLLEGRGSDIIDLGCVPDDPDQIRAALEEAADIGDIIVTSGGVSVGDADHVRDLVAELGSIDFWRIALKPGKPLAVGDIGGTPFFGLPGNPVSTIVTCLLFVAPAIDLLAGATP... | 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: 407
Sequence Mass (Da):... |
A0A6B0YH71 | MPRRYARSLAALAAGALLPLALAPFAVWPLLLVSAGALFWVLRGTETGKRAFWRGWLYGVGKYGAGASWVYVSIHVYGETAPWLALLLVTVFVGGMALFNGLFGWVFHRLARRQASETGAAFTFGVLWTSLEWLLTWFLTGFPWLFAGYAFVDTPLAGLAPVGGVLLVSFAAVLTASLAVAAVGDGLVPSRGLGPSGASESAPPHAGDRASWRTRWGRPERVFSRLRWGVVAVLVSIWIAAWALGSVTWTERGETRTVALAQGNIPQTTKWTPEGVAQSRRTYRELTASAGDVDIVVWPEAAIPDYLRRTKRYIEAQRRG... | 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-[lipopr... |
A0A850AQD9 | MLRTPLFFIVVFLATLVSAFSVMLIGLFRRHSDAAYRYVFRPWARSIAWAAGVKVEVSGQEHVEPNRAYVIISNHQSHMDVPVLGGYLPLKLTIIAKKELFRIPIFSHGMRAFGILEIDRSNRTRAIHTLEQAAMILREKNTSVLTFPEGTRSADGRLQPFKKGPFALASAHRFPILPVSVCGTFPILPKGKFWVKPGRVSLKIHPPLHPGEDGAGNREELIERVHQTIAAGLYEHENA | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 239
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da):... |
A0A8T3RYP9 | MIKDLDAHYQQVFVDLEQVGLAAWAELGRQQIQSWFSPEHRSDMSQWLTQLDALKILIAHKSVSIETLTPIFKSFTPWRKGPFCLDDIELDAEWRCDLKWQRVQSAISNLSNQLVLDVGCGNGYYGWRMLEAGARQVIGLDPTLLSVMQFHLVRQFYGQGGCTVLPWRLDDVAFVAVFDTVFSMGVLYHHRAPLEHLRQLRSVLKTGGQLLLETLIIDGDAQQCLVPEDRYARMRNVWFIPSIDMLQIWLKRCGFTKIEVVDVSVTTSHEQRVTMWSGTESLSNFLDAQDQTKTIEGYPAPQRVLLRCV | Function: Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
EC: 2.5.1.-
Catalytic Activity: 5-hydroxyuridine(34) in tRNA + carboxy-S-adenosyl-L-methionine = 5-carboxymethoxyuridine(34) in tRNA + H(+)... |
A0A2A4RGB6 | MELDFWIERWDNGRIGFHQDKLNPYLAYFYGEKGPTLSLREKLKIFVPLCGKSKDMLWLSQNGYSVFAVECSKTAVVDFFEENALNYKHVEKDQIALFQTTDQNSLIEIVQGDFFAIEKKDLAGVTDIFDRASLIALPENIRSRYVDKMTELQDSGIRTLLVTLTYDPTEMNGPPFSLLEKDVHDLYSEHFSIEKLCTKDVLSEETGLKNRGLTALTETVYKLIRQ | Catalytic Activity: S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.
EC: 2.1.1.67
Subcellular Location: Cytoplasm
Sequence Length: 226
Sequence Mass (Da): 26040
|
A0A496WI06 | MTWNRRLVMFKFLFWILFLTALVLGAILFVQEDPGFILVKYADYKIETTLAFGIIAVAVATVLIHILFKLLMGVWHIPRAVKNQSKGRRFNKSRKLLNQGLIDLAEGHYDKAEANLVKMVDYSESPLLHYLAAARAAQLQGRYQERDKYLKAAHEARPEAEFAIGVTQAELQLAHQQTEESLATLTHLRGIAPRHDHVLRLLARVYLELEDWSSLIEILPDVQKKKLLSDHLLKTMETKTYQGFLAGAEGSQQALEKAWNKIPKTAHTDADLVVYYINLSNQAASSSSNTEQLIIRSLGQKWDNRLIEAYGLFRASDPNA... | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in a late step of protoheme IX synthesis.
Subcellular Location: Cell inner membrane
Sequence Length: 414
Sequence Mass (Da): 46717
Location Topology: Multi-pass membrane protein
|
A0A3M0Z6K8 | MHAALLILHVLVAGAIIALVLIQRGRGAEVGAAFGSGASSTVFGAQG | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 47
Sequence Mass (Da): 4572
Location Topology: Multi-pass membrane protein
|
A0A947USU0 | MPGWLSSLRDLIADASPVRRFMLALLVILPLAALAAAYLWFNPPVYRVLYTQLSDRAGGDVIAALEQLDIPYRLSAADGTIEVPATQLHAARYRLAARGLPKSDDDAQDEVDRAPRFGASSLQEQQRFQRALEIDLARSIQKLEAVELARVHLALPKVSPFLRDAPPATAAVLVRLRPGSQLDAGQVATIQTLVAAGVPRLKRAEVQVLDPRGVLLGGAAPEAVQSQRLALEQDLVRRALAALTPWLGEDRVSVQVTATLEDSETRQTVERVRNVVVAGQARPLEKTVRTTRVPEGRIQRINAIVILGFDASANEQWRAR... | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 451
Sequence Mass (Da): 48693
Location Topology: Multi-pass membrane protein
|
A0A496VD10 | MFHEILVIFHVFLSVGLIGLILIQHGKGADAGAAFGSGASSTVFGSQGSGNFLTRTTGVLATLFFITSLTLAYFSVQHIERPKSVVETVQPAPTSESETPSAPSQDNSELPPVQTSPSADKDSEVPNPSPGTNN | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 134
Sequence Mass (Da): 13958
Location Topology: Multi-pass membrane protein
|
A0A3M1DLJ6 | MNPSVILPELILLTVTFVVLMVSACTRDSGARISMWLSQLGLIAALLAVAAQIGAGGGVWFDGLFVNDPLSIVLKLTILLLSLMVLVYSRAYLSARGILRGEYLALLLFAVQGTMIMASAHHLLSIYLGLELLSLSLYAMVAMQRDSKAASEAAAKYFVLGAIASGMLLYGMSIIYGVTGTLAVDRIAGVLAGGEVPLVLSLFGTVFMVAGVAFKLGAAPFHMWLPDVYHGAPTAVTLFLGTVPKLAAYAMAVRILADALGGLAQDWNAVIVVLALLSVAVGNVIAIAQSNIKRMLAYSAISHIGYLLLGVAAGNSAGFA... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
A0A2E1Q196 | MEKVLTNKEVQEILPHRYPFLLVDCVLELKDSEQPDSKVGRSAVVIKNVTANEPFFQGHFPGFPIMPGVLLVEAMAQAAALAYYRDGEPKLNFMIAGVEKAKFRRPVTPGDQLEMHARILKDRKNMIQAECFVRVAGKVTTEATILAAISAREGEGSF | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
EC: 4.2.1.59
Subcellular Location: Cytoplasm
Sequence Length:... |
A0A6L7TF60 | MTGEFMSKQEENTAVDFEKDIAELEALVAKMESGKLTLEESLKAFEKGVGLARRCQQSLADAEARVSKLMQEMNFDTDD | 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... |
A0A946VNS0 | WLEQYQDMDGIIAGAEEIKGKIGERLRENIDQLRLSYELATIKRDVELEVDINALVAGEEDGQELHRLFSELEFKSWIKELESQGIEAAEGQKEGQKEGQETGSASVGSLDVEALKVPDKLEYQTVLSEQALDELIDRLQASERIAITVEHDSGHFLDSELIGLAFSIETGKASYIPLAHEIAEDDQLLDRRKVLERLKPLLEDRRKIKVGFDLKTNCHLLQNYGIDLAPFKSDILLASYVLNSVAIKHNLPDMVRYYLDLQPVNLEEWLGKGRGKLTFAQLDLEKATQFAAEKADMILRLSTLLEHELKSTGHLAGLYR... | Function: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 721
Sequence Mass (Da): 81187
|
A0A946WZS4 | MSKNSSSVQNIIESKIKPLLPNNICVAFSGGMDSIVLLHAVNNLLDGQSKIRAIHIDHNIVNNSNELAQSCKKICKNYGIDLEIIALKIKHKGFGIEAAARDDRYKMLKEKLQENEYLLTAHHEDDQMETIFLRMARGTGLNGLQGINEKYPFGKGIIFRPMLTANKKSVMEYAKEHQLKWIEDPSNQDTYYDRNYLRKKIIPEFRERWPSIATSVSRLSQLSAQNIEILNQVAEEDIGVIENMNELPLSKLHEKSFERANNIIRYMILANGMNIPSMMTFQNGLRRILENNNDKSVIEWKGCSIRKYNNNLYFLDNKDI... | 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)... |
A0A8T6CPS6 | MGTSSQGSVRKKHARTGKKAAVRIIGGEMRRRLLHFPEVDDLRPTPNRIRETLFNWLRDKVEGRTCLDLFAGSGALGFEALSRGAARVILVERNAAACRALAENAKILKTENAEVHHTSAWDWLRQTRQPPASIELVFLDPPFAGGLLPQACETLERSGLLAQAALIYLEAETEVRPQQLPGNWTVEKSGSASDVHYFLARRE | Function: Specifically methylates the guanine in position 966 of 16S rRNA in the assembled 30S particle.
EC: 2.1.1.171
Catalytic Activity: guanosine(966) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(966) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Length: 203
Sequence Mass (Da): 22537
|
A0A3D5W703 | MQRFWTILLVLFLGVTLAGCAASKKKGGTVEVEDATIGGSETEVTTEATASGVDSDDTTAGEIITIDQDDADMDDPLGQRVVYFDFDSSNLTPEAQRVVEAHAQYLSSNPGMAVVLEGHADERGTREYNLALGERRANAVSEIFQALGVAPDAIRTISYGEERPISMGQDESAWSLNRRVEILY | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Subcellular Location: Cell outer membrane
Sequence Length: 184
Sequence Mass (Da): 19906
Location Topology: Lipid-anchor
|
A0A523L5K1 | MVDYTDLFNHLLNAGLSQWVEQLEQQRKNWLVHHGDYLRWSAALNSLPPIDKIQAYFDRPEVTIEGVCEDKDALFRSLKSLMPWRKGPFQFADVLVDSEWRSDLKWERLLPHLSPLKNRRVLDIGCGNGYHCWRMLSGSPQIVIGIEPSVLFNLQFQAMQRYLHIPEICLLPIGIEQMPSEMAWFDTVFSMGILYHRRSPIDHLLQLNDLLVSGGELCLETLVIDGGRGDILLPKNRYARMKNVWFIPSALELESWLERCGFINIRISDISTTTKNEQRTTEWMEFESLSDSLDKQNTSLTVEGLPAPKRALLFASKA | Function: Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
EC: 2.5.1.-
Catalytic Activity: 5-hydroxyuridine(34) in tRNA + carboxy-S-adenosyl-L-methionine = 5-carboxymethoxyuridine(34) in tRNA + H(+)... |
A0A2E9EBD4 | MQADKINWFRSAAGYIDAHKGKTFIVSLCDGAISSENLEKIVSDCILLNTLGVRLVIVFNGDQRIQNKLRLDWAEYKGKKITRFSQIALLSEVIGSIRNELEAIFMSHSFHLPGGKKEILLTSGNFVKAKPLGVVDGVDFESSGEVRKINAFAINRQLDTNAILLIPPIGFAPGGELFYLNSDEVACKIACAVSADKLIYLSKVSGLLDQEGQVISEIDLSREKEHITEQNLYKFCKEAC | Pathway: Amino-acid biosynthesis.
EC: 2.7.2.8
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Length: 240
Sequence Mass (Da): 26527
|
A0A9D6PRH6 | MIKRFSHNLVVLEKMLVAASLFLLLAFTLIQVIARNFFDTGFPALDIISRHLVLYIAFLGAALITEDQKH | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 70
Sequence Mass (Da): 7930
Location Topology: Multi-pass membrane protein
|
A0A9D6VRJ8 | MPTLLTVQLACTQTPHPSFAEMQRWVSATLSPSQDKISLNIRLVDETEIQMLNKQYRHKDKVTDILSFPFMPPEGISGHFMGDIVLCTAKVNQDAAEQNKPYLDHWAHLCVHGTLHLLGFDHETDKEAEIMIKKEVEILHSLHIPDPWQHKESKHESS | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 158
Sequence Mass (Da): 18099
|
A0A9D6VSE8 | MKIFFLKLAEKTINTYLNADLEISSRLNKHNEKTIFIKLLDLNESFVLSIESGKIILRADLGDFIPVVTVKGRSLSLLQLLMNRSSFNYAELEINGDILFLQALREILMSIEVDWEELFSPYLGNSLTHHMGRAIKKMKKIVQKNSGLLKENIKLYTQEEVKLFPPKEEINDWYDEISRLKDDVARAEARVERLMIELLPICRD | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Required for ubiquinone (coenzyme Q) biosynthesis. Binds hydrophobic ubiquinone biosynthetic intermediates via its SCP2 domain and is essential for the stability of the Ubi complex. May constitute a docking platform where Ubi enzymes assemble and access... |
A0A2E6YZD3 | MFSVILQFILPKKGLTLLAGILSRCRQSFLKALLIKAYCRVFEIDLREAKYQNIDEYESFNEFFTRELKEGARHSPEKANAIASPADGTVSSSGLIKQGSLIQAKGKQYSVNSLLGFEENIPTNYEGGSYITIYLSPKDYHRVHAPIAGSLDYTIEQPGRLFSVNESTQTRVPNLFCRNERLICTFSCGQEKQYSLVMVGALIVRSIETTWDGPISPYRSRQKRDAKNINFDQGDQIGHFSIGSTVILLFPKSTGRLKRIADGSRVKVGEEIGEKFTDVETQ | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.