ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A1V6GRT0 | MKGYFGEFGGQYVPETLLPALDELDAAMEEAFADTAFRDEFTSYLVDYVGRPTPLTYAKRLSEHFGCEVWLKREDLNHTGSHKINNAIGQILLARRMGKQRIIAETGAGQHGVATATVCALFGMECHVYMGSVDMARQRMNVERMRLLGTRVVPVEGGTATLKDATSEAIRDWIANADTTYYLIGSAIGPHPYPTMVREFQAVIGREAREQIVAHAATLPDAVIACVGGGSNAIGIFNAFMDDTAVELIGVEAYGEGNGRHGASISFGSPGVLHGTRSFLLQDKDGQVKDTHSVAAGLDYPGVGPQHSFLAATKRARYGL... | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phospha... |
R4YKA7 | MDNNTTAWLTVPAPAKLNLMLHITGRREDGYHELQTIFQFLDYGDQLSFQIRTDDTLTLTPEISGLNFEDNLIIKAARSLQSHANARGKNCGANIRLEKTLPMGGGLGGGSSDAATTMLALNVLWQLELSLEELAKIGVKLGADVPVFIKGQACWAEGIGEKIIPLPDLAENWFLVACPNVHSDTKEIFSHKELTRDSQILNMRHALEGQAANNSRNDCQLVASKLNPEIGKTLNLLNKFGSAKMTGTGACVFLSVASENKATQVANKLPAELTTFIAKGTNLSSAHKVLFGSV | 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... |
A0A1E4RBF0 | MNSLLVSLYSRLVTHTRDSPCSTPLDKLIHSALDHDLAIEELNHYSKIDNNLILNDKSALKTLNNDKIIGSDLSQGFQYYRPSSNEEIYQLNDLFQVLNQIPGSEVPRIVSIRRNLMILMLIPLTEQECEFNVIYKDNDIIIDYKWDETTTNDTLVAYGGFKFEELMTNNQSNDSTYYTVINQTINDLNILITAEIDSQSNGDYIELKTHNYKSSPSKLAKKLLVSWCQTRLINSNKVIVGFRSASSSGRFKLHSIKHYNDNDIPKLLCRKEYRIPFQDSYITCQGLLKWYKTVMKWIQMQIIDKKNQGDKNGAFNLKYS... | Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA.
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside-ribonucleotide in mRNA + ... |
C4GH18 | MMKNNPFLKPAVIGLVTLLHAGVIALSWNGFKSPEPEQADAIAFVDLGSVTGDDKPLGDGAPAPLEQPEPPQPQPPVEQPKPEPKVEPKPEPKPEPKPKVAEQPKVAAVVRNDKPADFRQPEKVVKPQKHEPKPEPVKQPEKPVEKPQPVRVEHPKPAVTPPANANPSGTSNSSATANKDAANRAPDSMGGGGSSANSKVPQNGAGDKNSDGGGKKGDAPKPSNANHASTIANGGYISLPNPPYPRSAAEHEEEGVVKLSVLVSAAGKVMNVKVTKSSGSAALDNAGKRAAQSASYQPKKIDGEPVSTEFNTQFTFKLDR | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
B9Y594 | MRNFLKTLSISSIFLCLSLFSGCQKNIPYENTEGKTFTNYFDVFTDSEGNLVLPLNTTIQLTMTDEKKLAEATTLVEAQLPFWHKLADSHHRYLDDQGNELHNVAYINQHPGETISIEPELAAMLSAAIELSQLSDGLFHPLLGSLSALWEPKFAPFPTENTDPDSALIAQITGCLPAAADLNEVLQLDPERRTVRFEPGACENSLQISLGAMAKGYILDQLAAELKPLNTPFLLDAGSSSIIAWSPDDAPYSWKIGVRDPSGQTSLLYAFTLTQGVVSTSADDQNYFLIQDGDQQIRRHHILNPRTGYSENWLRSVTLS... | Function: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein.
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
EC: 2.7.1.180
Subcellular Location: Cell inner membrane... |
A0A1F4VCU0 | MKERISLDYTFMREEGIGKNGIKDLEIEEVFEKLKRAKKELTLNKKSCLFEFSCLPYTLKNLQIIKDKVSSLKERYKTMAVFGIGGSDLGTRALYEFLDLNGSFKLKFFGDTTDPYDIERFMKEIRIKETCFNFVSRSGETIEILAPFGFLKGKLNKEQVVVTTGEAGYLRDEAQKEGYFLFEEPKGVPDRFSVLSVVGLLPMLFAGADIEKILDGAIYLSNLIDETSVREDPMLIYAGLLYLAYAKHKQCIGLFMPYSKRLSAFGRWVRQIFAESLGKSGLGITPLDLMGPTDQHSFLQLILDGPADKVTTFFKVEDRG... | 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: 423
Sequence Mass (Da): 47951
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D9J2F4 | MHLLPLATLLLVTLAEATNVTDSYKGYRLPETQVPHAYAVDLHLSESVFRGNETAFSGSVMITFQVTESTSEIKLHSAVSISDVNILSSTNENISVMNFTTNATTEILTIRLDNTTLNVSTDYALTIKYVGQLDTSNMMGLYRSQYEDGTGTQYLVTTQFQPTNARRAFPCFDEPRYKATFVLSITHPTELQAVSNTPFNSDLAFNDSYRTTVFTKTPTMSTYLLAFTVSGFTCTSGQKIDTNVTHQVCSRPDTESDRALAADFGTKIMNTYGELFDYKYQDMNIGKIHQVALPDFDAGAMENWGMVTYKESALLYNTNH... | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.11.-
Subcellular Location: Cell membrane
Sequence Length: 929
Sequence Mass (Da): 104663
Location Topology: Lipid-anchor
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A0A327LR72 | MIDPDDRTPGEPQGDHQGDHQAEHQPVSLLLLMPNMVTLIGMSFGLTAIRFAIEGRFSAAVFLILLAGLADGLDGLLARRMGAESAMGAQLDSLSDFLCFGVAPAILIYQVHLAATGGMGWTFALLFAAATCLRLARFNVLSGAADTTKEAKRHFIGVPAPAGAFLGLLPVFLTQAGLSAPGDAPTLVAIWLALVGVLMISKLKTLSPKTVKVPRRLVAVILFATVTVIGLSLTRPWYILVILALAYLATVLHAIIRARGQLFR | Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CMP + H(+)
EC: 2.7.8.8
Subcellular Location: Membrane
Sequence Length: 264
Sequence Mass (Da): 28004
Location Topology: Multi-pass membrane protein
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A0A651E8R3 | MIQPDILRNQIDLIREVFLYANRFRGATFVVKLDSSLHDSSALSGLVSDLSLLRQHGIRIVIVPGARKRIDEILERYGQQAEHVDGLRITPEQSIPLIKMAAFDVANRIMTQLSARGISAVIGNWVRARGVGVSGGIDFQHTGSVERVQREILERVMNDAMIPIVPCIGWSATGAPYNVSSDELAVQIAGSLAAEKLFFVTDGPSDSSLKLVLPSDVIREDDGRMSRLTVSQAESVIELNEHQKDLPAILRLRHTIRALRSGVKRVHIVDGTIDGFVLKEIFSNLGIGTMVHANEYESVRPMVSEDLTDVLRLMQPYIDR... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
EC: 2.3.1.1
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
Sequence Length: 444
Sequence Mass (Da): 49098
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A0A940ASB1 | MTIYTALIRQFFILLGLEGQRRKLHKLAKKGLIKERDELAFSIAQNWGRNLIKSVGGKETTVTVIGQENIPYNTSVVFIANHQSFLDIPLMFGYAGRQAGFISKAEFSKIPIFADWMRILQCIFLKRGNPKQSIQAMADGVENIKRGYSMMIFPEGHRSKSSEVHEFHAGSFKLAYRAEVPIVPVTISNTYKMYEETGHSQATNLTLIFHPAIITKGLSREEQKEIPGRVQALLTESVKSLQILKK | 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: 246
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):... |
A0A843BBJ9 | MMSGTLARLCENSRRALQEGIYDTGDAGERSDIRMSEALQTREIAIISEIKFASPSLGTIRDTQDPGEVATQMVQGGAVAISVLTQPYLFGGSPEYLAQVRKVVRVPILMKDIVVDAIQIEAARRLGADCILLIQAVFDAGHAHDMDGMIDTAHGYGMQVLAEVHDTHELESALATKCDIIGVNNRNLDTLEISLETTKRVLAGYADHRPAISESGIESSSDIAYLKGCGASAFLVGTGIMRHGNVKGGVRRLVES | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 256
Sequence Mass (Da): 27468
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A0A843BLS8 | MLDSEMSHLRQSLGREPTETETAIISAEWSEHCSYKSSREHLRILPRDAPYVISDKGLDSGVIDVGGGYVVTAHIESHNHPSAVEPYGGAATGVGGIIRDIMSAGTRPICILDGLRFGDIEADRHAAWLLRGAVRGISDYGNCLGIPTIGGETGFDPSYSKYTLVDVAAVGFGIRERLIHNTAGPGDHIVLLGGPTGYDGVGGAQFASERMDEEDRSAVQIPDPFMEKMVMEAILKLRPYIKALKDLGGGGLACAASETADALGVGIAIDTDAVHTRDNNMTPPQIMASESQERMLAIVDDTGLAHIREVCGRFRVPHSI... | 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 1/2.
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent ... |
A0A951YTS3 | MSRPAFAQGANVDDPLAGLEIVGAPVPRGINLQPSATNIGDDLHWLDNMLNWVIIPITLLVAFLIIYVIFRYNKRANPVPARFSHNSPLEVTWTLLPVLTLVVIGAFSLPILFNAQEIPDGDITIKVTGHQWYWEYEYEDVLDADGNPLNFESFMIGSDILGGDNTLNDDARADLADLGYSDQEFALATDTSVVVPLGAAVVMDITGADVIHSWAMPAFGVKQDAVPGRLAQLWFRADREGIFFGQCSELCGRSHAFMPITVKVVSPEAYAAWIDRVQNDPDYVMW | Cofactor: Binds a copper A center.
Function: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
EC: 7.1.1.9
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(... |
A0A151TX72 | GNTASFLVYFAPIVTFYDIYCGGSTLDYDAVPYSMALFCATLSLYYAYLKGNEETLLIATSSFGCGIEVVYLIIFYIFATNRVRRRIVRMVFLFNGMVYLSIICSSSFVSPLHKKLKVMGWICATSAVGVYASPLSVIRRVIRTKSVKSVPMPLSRCLTLSSIVWFFYGCFSHDYSIVMASVLGCLLSVAQIILYRKWNGSGDDERERVAIASKTRENNKDTLDDEVLQVIDIAVRKVKVRKSDNSNEEEENATRVELEATETVELQNIAVTGNDSVMDSEIHSVVEPEIVEVLDKPKYAMLDRAPSKLS | Function: Mediates both low-affinity uptake and efflux of sugar across the membrane.
Subcellular Location: Membrane
Sequence Length: 310
Sequence Mass (Da): 34708
Location Topology: Multi-pass membrane protein
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A0A1Y3B866 | MFCLTAFILSGVVGSSISVSRLNDNNYNEINSNNNNNDVFDETDPLYWYLQAYRNLKQRQYSVPIPNRPAKNTYNVDQQIPDSAATATAFLSGVKNNFNTIGVSAKVKRNDPDCDSVHRNSIDSIFTWAINSGKVAGVVTTTRVTHATPAAAYAHIQNRKWESNVDQSIINDTFSETDCKDIALQLIENDPGKRLSVILGGGRKGFLPESVKDPRGIKGDEKEKFGERKDGRNLIEEWQANQRYSGLNETEYAYVNSSRGLRTLDYLKTKSLFGLFNYSHMEFDQLRDRSLDGEPSLTEMTEAAIRILSKHDKGFVLLVE... | Cofactor: Binds 1 Mg(2+) ion.
EC: 3.1.3.1
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Length: 480
Sequence Mass (Da): 53845
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R4YS29 | MNKRHAVYLISAVLVTALAVFMNETETPSATFSTQFLENNSTIITEEITENPGASIPDSLRSDLASSLAGTHHGVQLKSRHQQLIITASLKDLFDYYLSAAGEESTEEINQRVKKELAGQLQTEALAQAIDIWNSYLTYKRELVEFDQQYPAYSSQPEKREQLIILQQRQLALIALQDQIMGASIAEIIFKFDRQLDGYTLEKAELLASDLNAEQIQQRLINLSAQLPIDTILSVQRNEQQKALVEINQQEGLSVQQKFQQREQQVGAVAASRLQELDEKRAIWKGRIIDFKQEQQQLQQAGLANEEYKVSLDKLYTQHF... | Function: May be involved in the folding of the extracellular lipase during its passage through the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 336
Sequence Mass (Da): 38147
Location Topology: Single-pass membrane protein
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A0A2E9QGP7 | MKVIALDGPAGSGKSTIAGMLAEKIGFLHADSGAIYRTLTLASMQKLGAGNSPQDFGELFQKAVLDPDQLGIQVVLADGKQSNRIGQADVGREIRTPEVTSRIRFIADNVPCRNTVNRLLREFAEQTGVVADGRDMGTVVFPDTPNKFFLEASVEVRARRRYEEMLGQGSSSQSLAEIERDIARRDQEDRSRAVGALRKADDAILIDTSDLSRDGVLSRILAHIQYRF | Catalytic Activity: ATP + CMP = ADP + CDP
EC: 2.7.4.25
Subcellular Location: Cytoplasm
Sequence Length: 228
Sequence Mass (Da): 24977
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A0A6C1RQR5 | MRHFVLPAEYTAFGRHTLSGQSFHYLCRVRRYAEGEAFDATDGRGGVYRCSVLERTDNSCTIEVAAASAGRTAAGDARALQQSVSITLFQALPKGRKLEQIIRQTSETGVARIVPFSSRFCVAEAVSGQRLHAKLQRWRSIARQAVQQCGSTLAPVIEAPIELEQIPVVDDSFDLGLLFHQQPLAQQTLHGYLERGPQRVAIVIGAEGGLADEEIDFLCRDRGFLPAHLGPTVLRCETAALYAVAAVQTILREIEIEGD | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A812R9W6 | MTFELVVIGGGNMGAALVGGLLDGGVVERDQVAVVEPAETRRELLTGLFPDVAIVADVPPCRAAVLAVKPQTIGAVAATAAQAGATRLLSVAAGVTTSVIAAAAGEGVAVVRAMPNTPALVGEGVSAIAPADGAGDDDLDWAEQILGSVGLVVRVAEDRLDAVTGLTGSGPAYVFLIAEALVDAGVLAGLPRTDVEPMVAQLLVGAAALLQRDGDAAGLRAKVTSPGGTTAAGLRVLEERATRAALIDAVQAAADRSRALGFSPTVILGERTGRKTGSAEGPVTEPRYDTVSFLTDYGTADEFVGVVKAVIRDLAPHSTV... | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
EC: 1.5.1.2
Catalytic Activity: L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADPH
Sequence Length: 576
Sequence Mass (Da): 58193
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A0A963NCE6 | MKVFSQGNVRVILPAGDWNLSAVAAIDRELRNLVDPLVKGGNGATGQVRMAMESLGRLDTAGAWLIARTIKELEAANIPVELIDADDEQKALIDLVRNGVACEPSRDHEVHAIKRGIEHLGQATVRAIQEGYTLIAFFGAVVWTLFVNFFKPSTWRITAIFHHLEHTGVNAIPIVTLMSFLIGIVLAYQGSSQLTQFGAEIFTVNLLAVSVLRELGILMTAIVVAGRSGSAFAAQIGMMKVNQEIDAMRVIGLDPLDVLVMPRLIALMIALPLLFFLAIVSALVGGALVVVFGLDIPMVQFIRQLQSAVGAEALFVGLVK... | Function: Could be part of an ABC transporter complex.
Subcellular Location: Cell inner membrane
Sequence Length: 377
Sequence Mass (Da): 40451
Location Topology: Multi-pass membrane protein
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A0A194SA06 | MLPLRPSPPHLSISPPVSKAQQRLPTLADFPPDKIRNFACIAHVDHGKSTLCDRMLEMTGTIPPAAVSRDQPEQEAKNEQVLDTLKVERERGITVRAQSATMFHRHSDGAEYMLNLIDTPGHVDFASEVLRSLLASQGVILLVDAAQGVQAQTLTVLDEALKRNLTVVGAVNKWDLVKDDGRGEAVLSELSDLLGCAPSDILRISAKTGWGVDSVLDAVVERIPPPPPRASEDVKEPFRGLVFDSWYDSFRGVVSLVSVFEGEVKKGDSITSTITGNDYTVLDLGILSPREISIAEHPDAHSRSLRKGMAGWVVRRSGPD... | Function: Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate... |
A0A137NYQ0 | MQAPDYTLNPPPIANYPTNTSEKPTGERFSYKPHFRDWWALLLYILTISAFFIVLGLNLYKLNFSSFSNSDFLSVSNDTYIISLVGGIILSLVLSAVYLIAPGLLIRLSYWFNVVLYLCLGLFLLSTYSNPLNLIIGILMLVTAVIYVFLWFSWRNLIPFSTLMLRNITKFILKHPSAIMLSFSFLIIGFLFYSVWLFTLMSVLFNYSNEGCEGYTCNQVGLWFLIVFLVFVVYWTSQLLKDILHLAVSGTFASDYFFPGREKYPIFKSLSRALSTSLGSACFGSLLIAIVQSLRSLASFARGTDNGIIIFVGCCLECLL... | Function: Probably involved in transport through the plasma membrane.
Subcellular Location: Cell membrane
Sequence Length: 468
Sequence Mass (Da): 52783
Location Topology: Multi-pass membrane protein
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A0A651ENS8 | MGGMEYFVEQGRTHTEAMEKVRAKYGPHAKVMHHRSVRMGGFLGLFTHEGVEVTGYISQAAQKRADNSFEEQKKRFLGSVAEKRGGEEVTESPAPADMMQSDNNRRDAGDSRAMQGSGGAPRATLDTLLQEVKTLRSTIETRSHDRNEVAVGGDHPTVARIRDLLELNEFTTPYIRMIVDRLKREFALEELAETEAIERRVVDWIGESIQIDRYRPEGNGHVFILVGPTGVGKTTTIAKLAAMWGIEQADRPAKDVRMITIDNYRIGARQQIETYGEIMGIPVHAAENYADLEKQIAVYRDVDVVFVDTIGKSPRDYVKI... | Function: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum.
Subcellular Location: Cell membrane
Sequence Length: 448
Sequence Mass (Da): 49667
Location Topology: Peripheral membrane protein
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A0A7S0HUP8 | CNIDDVDSKTLGLCFVIHYGHTCIIKIKRCLIPIIYIFVEINFDDRFFYEKFLKNLCNLYKFYVVETVQYRTKAFFIYRAIKKLKSDAILPKIQPLSHGEILGCTTHSDKFLKNFIYIGDGRFHPEGLILSNPGSKIMQYNPLTKQIINFDLKISEVLFYREHQLSNTLLGSKIIGFIKGSMGRQGSFLLYRKIEYLIKKLYNNQINIVLSEIDFFLISLFEEFDIDFWTQNSCPRLSVDWGVFFIKPMITMFELLNLTKIFYKNKKKYPMNFYSDTIVPWSNNYDNKYIRKLT | Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
EC: 2.5.1.108
Catalytic Activity: L-histidyl-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + H(+) + S-methyl-5'-thioadenosine
Sequence Length: 294
Sequence Mass (... |
A0A6N2E7S9 | MRNERNSIDLIWNVAELAGLFEKKSTLEGFLSDVVRLIAEHMQSDVCSIYLYDSFRDSLVLRASHGLQLPDDTQVELRVGEGITGHSFAELRPIREADAPSSPHFKTVPGLNEEEFRSFLAVPIRRGPNRIGIMVLQHRQGDHFTQTDTRAMQAIASQLATTLENAEMLMQLRRVAPVPQRQYETSTLSVVRGQSVSEGFAEGRSVLLEDRAVQISTGDEQEADEQEGLNKLAAALEATHKQLESLQREIEDDLSDVASMIFTAHLLMLKDHEFVAGMERLVRNGSGPQTAVRSVVHRYVELLAGSSNARSQEKAQDLMD... | Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
EC: 2.7.3.9
Subcellular Location: Cytoplasm
Sequence Length: 756
Sequence Mass (Da): 83987
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A0A8B5WWX7 | MNKKAHAKSLENNTIWLFHPETGRVLPYGDAGFQSLKTVGARYEAIVNAANLPAETRAPDDPAAEHSESAPETSEASTSGPADPTRVGSIITELAGIVEDRLKTMPEGSYTTHLFTQGPDKIRKKMGEEAVELILARDEAEIVYEAADLVYHMLVLFAALGIPITRIFDELASRAK | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
EC: 3.6.1.31
Subcellular Location: Cytoplasm
Sequence Length: 176
Sequence ... |
A0A6N2E688 | MIGRFGPMELVIILAIALLIFGPKKLPEIGRALGKTIREFKAHTNKIASEDEDSKEDAKKLSSDESGQSSVDQSVKTESADEESRSS | 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: 87
Sequenc... |
A0A2N3G678 | MKLLFFASHRFAIESLELLLASRHEVIAVVGRPDMPSGRGLDPAPTPAVEEALARGLKLMQPENLSRECFSAFVEALEWDAGIVVAYGGLIPQWLLETPRFGFINLHPSLLPRYRGAAPIQRAIMNGASITGVTTIRMNEVLDAGDILMHSEARIGEDDRTGTLRDRLARIGSRVLLATIDNVEDGNVTPVAQEEDKATYAAPVLPSEVRIDWNSSAEAIDRLVRAMDPAPGAFSYFRGRRVKIWDAHVTDVPPEDEPGTIINLGKEGFMVNTGTTGLQPVKLQPEGKNRMSAAEFSRGQRLLPSERFTSDPRA | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
L1MMF4 | MNENAFPAVETLTYEAALAELIEIVKILELGQMGLDESLKYWERAEALSKRCEEHLAGARQRVETALGTDNGNDATT | 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... |
L8H4V3 | MKRTLLLAGRIATVHGSPQQQQGAATGGSTVDEEEVQRLSESARLRWWDPEGEMKPLHRMNPKRVAYLRTCLTKRLGLPPLAPQPFTGLRFLDVGCGPGLLTESLARLGGEVLGVDASAANIQTAIKHSSGDSSLSTLAYRHGTAEGLAAEGQQFDVVSSLEVIEHVNNPELFINSLSGLVKPGGSLFLSTINRTMKSYALAIVGAEYILGWVPPGTHQWNKFVQPTELGVLLQRAGMNLEELTGLAYQPWNGSWSFTTDTSVNYLLWATKPLAQ | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalytic Activity: 3,4-dihydroxy-5-all-trans-polyprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy,4-hydroxy-5-all-trans-polyprenylbenzoate + H(+) +... |
B9Y739 | MSFLMQNGEVLYRGKVRKMDVLVDDLGRVTAADQIDLTAEDVDEVIDASSLLIAPGLIDPHVHLREPGFEYKETIASGTAAAAKGGYTTIMAMPNLNPVPDSLEHLKVQQDRIRYNAKIQVIPYAAITQGQKGVGELVDFDALASEVIAFSDDGKGVQEEAMMRQAMLAAKRNNCLIVAHCEDESLIAKGACIHAGRKAEELGFTGISSASEYQQIERDLRLAEETGCQYHICHISCKESVALVRQAKQRGVQVSCEVTPHHLLLCEDDISADDGRFKMNPPLRTKADQEALIAGIQDGTIDMIATDHAPHSAEEKAKAL... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
EC: 3.5.2.3
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-car... |
A0A2N3G4S3 | MGQTIAQKILAAHSSRKECDVGEILNPQVDVAMSHENAALVSKVFKTIGVERVWDADKIVIPLDHRVPANDIKTAEGHKWIRGIVKEYGIKNFYDIRAGICHQVLPEKGHVKPGMLIVGTDSHTTTYGGLGAFSTGIGATEMAAVWATGSLWLRVPETLRINVEGNLGNGVYSKDVILKVIGKLGADGADYKSCEFYGDTVENFSVGSRMTICNQAMEMGAKAAICPPDEKTFAYLRERTDGRFDPVYADADAAYEAAYDFAAGDIAPQVSCPHNVDNVKDVDDPKIAGLEIQQAVLGSCTNGRLEDLEAAARIM | Pathway: Organic acid metabolism; propanoate degradation.
EC: 4.2.1.99
Catalytic Activity: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-aconitate + H2O
Sequence Length: 315
Sequence Mass (Da): 34018
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A0A1G1N1L0 | MDISSLACDSRSVTKDSLFIAIDGTKVKGSDFIAEAIRNGASCVVAAHRRTALFERRVPVIYFPDTRYALAVMADEFFGHPSRKLKVIGVTGTNGKTSITYLIRSILQEANFSCGIIGTINYSFKEKIIPAQNTTPGPLELQMFLKQMVRAGCAYCIMEVSSHSLDQQRTAGIDFKAALFTNLTHDHLDYHLNLENYFSAKAKLFRGLNKDAFSIINADSPYAGRLATIGLGKLITYGIDSECDIRAENLALDLAGSEFILHTKKRKPSSGGKTKIKTRLIGRHNISNLLAAIAFALSQKIELAQIVRAVENFNGVKGRL... | 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... |
A0A137P0Q2 | MATIQFKYNLIKESSFKFRLGELLSKNEKINTPNCILYTKNGGLVPHLIKKLEDNLLTRAKEPNLGVLIHLEDYFDKKYYKETLKSGLGEAINSKSPLLLVDLNDNKLIKNADEDLNTNNTGVSLSAHQGKLRVGADEYNEIINNWKPDIVIPLHDLLCSTTKIPSEKRANKSVRRNINWLNELLESDLKGSNLLGVLGGSIYYAERKRASEMLKEHQKHIKGYLISSLHGTPSQKGEQISQSLESLTPEYRDKPNFCFEMNTPEELLEGIVRGVDVFDSSYATQVANYGNALNLEFQPHGTFLQPIVSLNPEETDFSED... | Cofactor: Binds 1 zinc ion per subunit.
Function: Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hype... |
A0A963QUY5 | MDGPAVHAPPVHVESTVRDEADDFERAVSVIPDRSLAVPFGSDLWLDGILGLLIGLCVGSLIANYARSWPDLRRFLAGRSRCGGCGRRLGVPDLVPVASWLVLRGRCRRCGVAVPAYYTRVELTAGGVGLLAAILLPSAAGWCAALVGWTLLAMVLVDLDHLVLPDALTLPLLAAGLAVAVLGTLDAAWPGPGPAPAAAGVVLGGGGLWAVRTLYRRWRGREGLGLGDVKLFAAAGGWCGAEALPWVLLAAASGGLLFAFAHGLDWRSTRPLPFGPALAAAFWVVMLIGWHGARPG | Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to rel... |
A0A194S4Z5 | MLRAPSRLAAPRLAPPLALSNSHRPPPFYPIPTWAERFPKALRWTHPYLSLARMDKPIGTWLLYWPCGASPWGITMAAYSSALPPSAWAWNLALFGTGAVVMRGAGCTINDLWDRDIDQKVDRTKLRPLASGEVKPLQALTFLGGQLSLGLAVLTQLNWYSIALGASSLSLVVLYPLMKRITHWPQLVLGLAFNWGALLGSSAVLGQCDWTVALPLYAGSVAWTIAYDTIYAHQDKTDDVHAGVKSTALLFGDQTRPILSAFSASFVSLLALSGYLNGQGPAFYALSVAGAAAHLAWQLRTVDLDSRESCWRTFASNRDL... | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, ge... |
A0A3B5MFL8 | MSASLSFSLKPISGLLLTLALQFFVIVAPDTGLPGMVPERPDSVDIVKKESHPVLVRQKRDWLWNTISVTEEREEPIPYKIGQLRSDRKVAVRTFAIEGEGVNQTFIVDNKGNLYVKERLDREKKALYHLTARMYDGNGLLIEDAGEFAIEVNDINDNCPVFQEEYKGSVMERTSMLDHKQRKAFDAHANYLYTHSSCADNTAALLVKEGPFNLEDSSDYSVEVRISDGGQPLMSSITKLQIKVLICFALNEMSSEAIDILLAMISIIDINIYLLCTVIVILIVMRKHYQKDSLASMKNSGEIHEQLVTYDEEGGGEMDT... | Function: Cadherins are calcium-dependent cell adhesion proteins.
Subcellular Location: Cell membrane
Sequence Length: 446
Sequence Mass (Da): 49946
Location Topology: Single-pass type I membrane protein
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A0A1Y3BRZ4 | MKYILVTGGVISGIGKGVVSSSIGTLLKSMGFIVTAIKIDPYINIDASLFSPYEHGEVFVLDDGGEVDLDLGNYERFLDIKLHRDNNITTGKIYQKVIEKERRGDYLGKTVQIIPHVTNEIQEWIERVAQLPVTEPLAVDDHHNDLANESSGEVPDVCVIELGGTIGDIEGMPFVEAFRQFARKKGPENFCCVHVSLVPKPKSTGEHKTKPTQVSVRELRALGLSPDLIVARSEDPFNESVKEKISNYCHVDSDQVICLSDQTSIYHVPLVLSQHGLVEYFSKKFHLTLNPDPSKKFLHKWRRLAERHDRLLKTVSIALV... | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.
EC: 6.3.4.2
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + pho... |
A0A3C0WWC3 | MGMRIFELFPELAVVHHKDDDCRFGHISYVSRNNNLGPMLQDAIAKNYGKYAFRYTEDMRCGMVDVRGLFENRDNPLCVEIGFGKGDSTFRDAKENPNVNFICFDVYLQGFAILMSKAADAGLNNILLCHYDALDFLNRSMPESCVDEFKILFPDPWPKTKHKKRRIVNPSTSGVFASRMRSGGIIHAATDVEDYAKCMLDALSSEKNLENLYPSFAPKGIRKNTTSYERKAVAEGREIFDIIFRKI | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
EC: 2.1.1.33
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 247
S... |
A0A343A5R7 | MTMLMIMTSMAMAITTLMVLLLNLTAKKAISDREKASPFECGFDPKNNARMPFSVHFFLIAIIFIIFDIELTLLLPLVLISKMSSPLTILLCSTTFIMTILYGLLHEMKQGSLDWTI | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NA... |
A7C3S7 | MGGFLAVSWTDVLQGLLMLLALIIVPIVTFYEVGSWETITTRMSQIDPALLDIFHDMSLLSIISLAAWGLGYFGMPHVLVRFMAINSEQAIPRARRIAMFWMITSTLGAVLTGFFGMAYFADNPLDNPEKVFLVLTQVLFNPWVAGFLLAAILSAIMSTIDSQLLVSSSAVTEDFYHYIRPNAGQTELVWVGRFAVLIIALVALMLAYNPKNTIMELVEYAWAGFGSSFGPLILFSLYWSRITRNGALAGMIVGAITVVVWERLTAFGIIPFSLYEMVPAFTLSCIVIVMVSLFDKRGFQNLDSHPK | Function: Catalyzes the sodium-dependent uptake of extracellular L-proline.
Catalytic Activity: L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out)
Subcellular Location: Cell inner membrane
Sequence Length: 307
Sequence Mass (Da): 34031
Location Topology: Multi-pass membrane protein
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A0A4R1BTJ7 | MQWVSSTTSRRGGGISAVRGDSGLPGGRERARMVREMFDRISGRYELLNAVMTAGLYRLWNRRAVDLTWLGPGGRVIDLACGTGSLTRELARRVGPGGYVLGVDFSENMLAAARERPVGQIEYRLGDATRLEGVPSGGFDAATIAYGARNIPDLEALFAEMARVVRNGGRVVCLEIAEPEDPLFARFYGIWFDKIVPRLGAVISGDARAYSYLPESVKEFVSPEGLAAIMRRNGLQSVRWERLAGGIITLHHATKRA | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
EC: 2.1.1.163
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquino... |
A0A0U3AL50 | MIQISLLPAGVKADSLAYQLAYAAQAVAAVRTGQALPQVLAQIFARSDAPPPARGAIQDLSYRAMRHLGLTDSLLSLLANKPPQPEVLHGLLVTALALLVDEQDAGYDSFTVVDQAVQAAAISQEMNFAKGVVNAILRRYLRERVSLMPQASKTPPGTWNYPTWWIDRLKAAYPEQWQAILLAGNQPPPLTLRVNRRRASVEQYLATLQGAGIGARAVGPYAVRLDKPVPVQQIPGFAEGVVSVQDAAAQLSAPLLDVADGMRVLDACAAPGGKTGHLLELADLELQALDHDARRLQRIAENLERLQLKARLTAGDARED... | Function: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
Catalytic Activity: cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.176
Subcellular Location: Cytoplasm
Sequence Length: 439
Sequence Mass (Da): 47843... |
A0A1F3CC56 | MNYSKISIRYSKALFELAKEKNLLEEIRNDVNLIHESFSVPEFSILLNSPIVKNSVKFEILKKVFSNNLNALTFSFLKMIVDNKRENHLNDISRNFLDFYKRDKGIKSAVFTTASDIDKTLLESIKKVIKDVFKSDIDLAHEINNDIIGGFVLRVEDQQIDSSVSTQLRTLKRNLINTSFEVKLPNLK | 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... |
A0A6C1QUU3 | MGLFPLINTIQHYPWGSTTGIPSLLGIENSAGAPMAELWMGTHPGGPSRVVLGATTISLRDFLQSDPTTHLGPGIAERFGAELPFLFKVLAAERALSIQVHPSREQAQAGFAREETLGIAVDDPERNYKDRNHKPEVLCALTRFEGLAGFRDPAAIRADFDEPEFSVDAAEPLRDALVRDEQPAAVCRTFLHAMLSQKPRQTGELVSCALALASRRLDGRPVENESINAPDSMARFRWIQRLTVQFPGDIGVLSPLYLNHFALSPGQAVYLAAGTLHAYLHGVGVELMAASDNVLRGGLTGKHIDRDELLRVVDCGITTP... | Cofactor: Binds 1 zinc ion per subunit.
EC: 5.3.1.8
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Length: 432
Sequence Mass (Da): 46660
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A0A554KQB2 | MKETKAIYGGTFDPPTYGHFWMIEQGAKLFDQLVVAVAVNPHKKCLFTPEERVEMLQKGMVLPENVQVVTMNAGLLVSNAFALGANFILRGIRSTTDFVYEYGMRNVNRDINSSIETVFLTPPREIAEVSSSMVKELVRADGGVKFILKYAPTFVCSRLLQEVQNAKQK | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
... |
A0A7S4DEC0 | SGDDAEPALFLEVTSGPLRGERRRVGREGAALGRATDNAISVADKELSRRHSLVEYDRGRGAYFLCDVGSTNGTYMQLVGPYANSYKLTFSDHILVGRTGFSINRFDYGVSEEIGRRPNMEDKSIIIQDLGIEHLYQLGMGPQSFVAVYDGHGGAHASNYLWRHLHLNVSEALEKVGQEIQAAHPGAGPGAVPARLLDELVAAGVARCFRRTDEHYLNTSDNPQCGSTATTVLIIGNRFYNFNVGDSRTLLCRNGKVRLVSQDHKPSREDETERIKKAGGFVIHKRVMGELAVSRAFGDKEFKMGLQAILNEEGRPGPG | Function: Enzyme with a broad specificity.
Subcellular Location: Membrane
Sequence Length: 319
Sequence Mass (Da): 34959
Location Topology: Peripheral membrane protein
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D5E510 | MKNKILEYSLKLKKHVIQNKKKIIINYIIFITIMIALILIDQLTKTFIFKHGDVFKFEFDKYGNELIQSPDSIGNRYETTWISPQSIYPNDPQKWGGNAFMGTRFIWHRGVTFLPSGVNISVIQFISMLILIIGITVPLFTKRKILIVALAIVLAGDFGNMLDRFMFRGYVKDLFYWPWLEKWLNKSIGTFNFADTCVMVGAILSIISIIWDVIETSIAEKKKARIEKDKIIQDEISPLQEEQVVQNTDHAKPEELDCISKTNNEDQILDELVNIQIQNETNSIEIETTIVSDESIVKKEKAPIKKSSRSKKSIVVSTDS... | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, ... |
A0A554KQ98 | MVAGSIRQLDPKIAASRKLNFYAYAISGEGEQYLKDYPTHDSEYETLREFGIAPNPDGRVVNSLEGIFKFHTEVGKKRDKLAYEIDGVVVSVNDKKLYNRLGVVGKAPRGAVAYKFSPKEATTIVEDIKVQVGRTGALTPVAELKPVEVGGVTVSHATLHNADEIDRLGLKIGDTVIISRAGDVIPKVNGVLKELRTGKEKAFKMPAKCPVDDSPVVRDGVAYKCSNKNCGARQREFLYHFVSGNGFNIEGLGPKILDRFMDEGLISDAADIFTLKKGDIEVLERFGEKSAENIVKEIEERKKIPIEKFIYALGIIHVGE... | 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... |
A0A2N1TAI5 | MRLNTLYNNKFAVSFEIFPPKTAEGEKNLWKELDILSSHKPDFVSVTYGAGGTTRVKTLEIALKVRDKYGIPPLVHFTCVGAGKNEIEAYLQEVKSHGIENILALRGDPPVGESRFTPHPDGFSHASELIDFIKSINGFTIAAAGYPEGHLEAPDLDTDIDNLKKKVDAGAQFIITQLFYNNDAFYDFMDSVEKKGIGVPIIPGIMPVTSLAQIQKITGLCGASVPDRLLGILKSCGSKDSICEAGLDYSIEQCHELKTWGVPGFHIYTINKSMAVTRIMDALGL | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 1.5.1.54
Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH
Sequence Length: 285
Sequence Mass (Da): 31178
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A0A2E9Q8Q0 | MADQETSFDVIVIGSGPGGYSAAIRASQLGLRSAIIEKESLGGICLNWGCIPTKALLESAHLLEKMKKAREFGLSVQDPGAEFGSVIDRSRRVANRMSMGVDYLMKKNNITVINGTATIAGPGKVAVTQRAEDGSDSRLELQAGDIVIATGARARALPGLEFDGEKVLDYRAAMSLKNCPANLAVIGAGAIGVEFADFYRSMGSEVTIFEMLPQLLPIEDEEVSKALKKTFDKRGIKCELSISESKVSRTESGIHIDYKNKKGEEQSADFDAVLVAIGIQANTENLGLELKMEKDRIQVDEMYRTSVPGVYAIGDCISGP... | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.4
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH
Sequence Length: 475
Sequence Mass (Da): 51001
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A0A1Y4VHF4 | MIYTVTLNPALDKTVEIPSLTVNAVNRITTMRTDPGGKGINVSKVIAKLGGKSIATGILGGGTGRAILSALKDLELTTSFHFVEGETRTNMKIIDPVQHTNTDINEPGVTVSEEILHELLEELLENLTAKDIVVISGSMPKGSPQDTYYTWTKACREKGAKVILDADGDLLKAGLMASPYLIKPNNHELSSLVGRTLTTPEELAKTARELMEQYGISKIIVSMGGDGALYVTGSETLYAEGLKVPVGSTVGAGDSVVAALAVAEEAGMSLSDTVCLSTATGAANVMCSGTQAAEYSVIQELLPKVVFHQIEI | Pathway: Carbohydrate metabolism; D-tagatose 6-phosphate degradation; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate: step 1/2.
Function: Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
EC: 2.7.1.144
Catalytic Activity: ATP + D-tagatofu... |
A0A533VWE9 | MLHLRLPCRRQVFYLRDEGKGGRGPGKGSRRTRAEEVLLQADADLLRRRHRPGPSVLRQEGHKLLTGSALRIQALSARVAFNGRGDPGIEAELSAGGEVGRALSPSGASRGIHEAAPFSPGGPDETARLVSTYKRRVIGEDAADLRGLASTIKKIDGTPNYSRIGGSAAYSISLAAAVAASSARGVLPCRLIDPRCNSLPYPLGNVIGGGKHAGEKSPSIQEVLVAPLGARSVREAIQLNFDVHSRVGRELSSRLPYPVGRGDEGGWCPGLTDEEAIQLASEAAREVADKSGRKIRVGVDFAAGSLYNPKDGRYWYRASG... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phos... |
F2IBJ0 | MLRTRKEIAFMVMAGIFITSAIVAELISAKLVYMGSYLAPMIAGIVPWPVVFLLTDVMNEYFGKQAVRRLSWITTGLIAFCFFIVYVAVQLPTAEGSWLSDKEFAKAFGGSLWIMIGSICAFIVSQLLDVQLFHFFSKLTKGKMIWLRSTGSTVVSQLVDSFIVALIGLYLSGAYPLKMVLVLAITGYLTKLVIAVCLTPLVYLMHYLAKSILGEKANQ | Function: Involved in the import of queuosine (Q) precursors, required for Q precursor salvage.
Subcellular Location: Cell inner membrane
Sequence Length: 219
Sequence Mass (Da): 24230
Location Topology: Multi-pass membrane protein
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R4YM65 | MTLTILFQDTDIIIVDKDSDLLSVPGRGPEKLDSVYHRLTLQFEEVHIVHRLDMATSGIIVFARNKEALRHLQQQFQHRQTEKSYQAIIAGRLTPTKGAINLPMRCDWPNRPKQMVCYEFGKKSLTRWRVMGYEDNSTRVELIPVTGRSHQLRIHCDALGHPILGDNLYGTSESQAATKHLCLHAQSLTITHPNSLERLTFTSPVPF | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 207
Sequence Mass (Da): 23624
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A0A1V6GSD9 | MPQQQVHILHGVPASAGIAIGQAVVIDTKKIERYPKLRVSEDRVEDELGRFEHAVQLSQKQITEAIHTLEAHQVIREHILILETHLLMLKDPALVDRVKQLITEDYINAEWALKIALREIEEAIEAIDDEYIRSRVTDTSFVGERLLRNLVGKTTSGFHLAENSIVVAHDLSPADTAMLNKGMVLGFATDVGGITSHTAIIAHSLEIPAVVGLENASSLVNPGDNLILDGISGVVIVNPSESQVLEYQTRARSYLSLELKLKEKAKEPAITKDGKYIKVKGNLEFKEEVRTVLDHGAEGVGLYRTEFLYLVRKEIPSEQD... | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfer... |
A0A2K6WHR8 | MQLLITVWNQEPWHRRSSGRSKNVIIEVDGDGIIGDVANKLSARLGIPHSNFLFILCGNKLTNDTPISTLFLGPQTSLTAMVTQLCSSEEDEKQRSGPSSSSENNKTAEITSFKVFCKNCNLLKDGKLRVYCAECSSSSLILTREPSSWNDVLLKNSIQADCKDCEKRTATFFCFKCVDCGQVAVPLTHVRNFRGSGSCSICCDSHMKVIVQLNCHHHTCVECFSTYIKTAFAEHQFAFIPPNGYTVSCPVYGCRGCVVDTHCFYLLGKSNYDEYQRQAAERFVTLEQEGMFCPRPNCGACFLWEFDPLYPKITCPECCF... | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
EC: 2.3.2.31
Subcellular Location: Cytoplasm
Sequence Length:... |
A0A533X8P2 | MANTKNSATDSLNRVIGHLDLDYFYAQVEEVQDPSLRGRPVLVCVFSGRTEESGVVSTANYIARNLGVRSGMPISLAKKRLAGKDASFIRMQHEKYEAISDRIMQIARESVDVLEQSGIDEAFFEITRRSGGDYRNASSIARGLKEKILSSERLTCSIGIAPSKVVAKIASDFQKPNGLTIVTPEETKQFLKPLPVEKLYGVGPKTAQALKGIGVETIGHLVGQNPEPLEKLFGRKLAVYLHDAANGVDEQPVTEGREATQLSRIITLKKNTRDPEEIFSQLSPAIDDLHSRLLAENRSFRNVSAIAILSDLSTRTRSVT... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
A0A6P4YWB9 | MNLNLTVPVVLFLLLCLNAFRPAKSACTRQILGRRGQIWSIKDVTSDHCEWDIWTSPYDIILINFDSSGYRRGSENCTADVLKFHDGNSPTSRTIDTFCGDQTPATGFEDVRSLLDLSTASTGPQMYVVYHRNPLSQHRSEFKLTFTTRHNNDVPEFNEETFVPQTAPVFNYTTAGDFVQVELEHLLDADPFYYPYGYTTYKRTGDSLQLYVTIQDYVLTASILASNFDYTCWYTSDNSPASVLLTVPAEYDRSGSHQLDWPWVPVRSHDALNFEKTEGVIIYNISGEKLQTGEEITVQCEIFIGTLTTKVRVTACPIGR... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
EC: 2.7.10.1
Subcellular Location: Membrane
Sequence Length: 861
Sequence Mass (Da): 96707
Location Topology: Single-pass type I membrane protein
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A0A4U2ZCU5 | MKATVENVKEVIAEAEVLGDASEMKNDIPLRDQGIDSLDVVNVYLLLEEKFDIKIPDEDLSQVRTISDIVEYINKKVD | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Carrier of the growing fatty... |
L8GGE7 | MFWWTYYLTFTVGPGYVPKDWSADLEDAHAGRQVLWCSKCSAFRPERAHHCKFCQRCVLMMDHHCPWIQTCVGYHNTKYFLLFLFYGLISCSSFLYLFYQHYHQLPSPDESMPEDFAAAAETANWRGNAFLLNDHVRLIARNKTFIDYLAVHSNPFLAKMAMSWGTSARRPKKSEEDYNRYDLGTMANIRYFLGDSMWMWFWPTPPRGTGFSYPSNRRERSDDSYDVPGESYDLRRR | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 237
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 28057
Location Topology: Multi-pass membrane protein
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A0A2N1JE32 | MRCVLSALRVPARRLMPVNGIARVVPICRAIHTDVPKVVAPAAELPRKLRRAPRKLFSALSIFIALTGGLFFGVYCLDSRAGVYRWLFMPVIHTLMSPETASKFAITMLRLGIAPRDKCVDDEVLHTELFGKPLTNPLGLAAGFDKQAEAIDGCFDLGFALVEVGSVTPQPQPGNPAPRMFRLPLDQALINRMGFNSDGHAAVQGRLHDRVRDYIVRVIAAGKALVSDVGVESLEKDATQLRRAQFFAAYADADVALLDRLGIPRSLKQDRLLGINLGKNKTSREDSSADFVQGVWNLGPYADMLIVNVSSPNTPGLRRL... | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
EC: 1.3.5.2
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Sequence Length: 655
Sequence Mass (Da): 70832
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A0A3N5TZH3 | MKTLFTGIQPTGELHMGNYFGAVKNWVALQSEYNSYFSIADYHAITIPYDIETMQKCIMDLACGLVACGIDMKKAPLFVQSEVPGHAELTWLFNTVTPLGELERMTQFKDKSKQHRANVNMGLLDYPVLQAADILLYKASVVPVGEDQVQHVELTREIARYFNKRFGDTFPEAQALLTKTPRILGLDGDAKMSKSKGNAIGIFEKPEEIWEKLRPARTDPARIKKTDPGTPEKCTIWSYHQLFSPEEVKKEIHAGCTSAGIGCIDCKKRLHEHMMREFDPMREMYYTLRAAPEKVREQLDTSAQVCRGVAGRTILEAKEK... | Function: Catalyzes the attachment of tryptophan to tRNA(Trp).
Catalytic Activity: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-tryptophanyl-tRNA(Trp)
EC: 6.1.1.2
Subcellular Location: Cytoplasm
Sequence Length: 329
Sequence Mass (Da): 37276
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A0A6I7PAE2 | MFDLGWAEMGIIMLVALLVLGPKELPRLARDIGRWTGKARAMAREFQRSLEDIAREAELDEVKKQIEQASRFDAGKQIEKTIDPDGTLKRAFEPPRVNPAPKPPAQSAGQSAPQSPVQPAAAAELPAPPPPPASEPAAAEPVAANAEKR | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding... |
A0A963KYF7 | MFDLGWSEMAVIMLVAIIVIGPKDLPRVARSVGKWTGKARALARDFQRSLDDMAREAELDEIKKTVEKASPGKLRNTVTSAIEDSFDLDDRKSAGKERRPTAAPSADKAGTSPLTEGAGGQTPGTDRRSSSGDAATTDG | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding... |
A0A940GAJ3 | WERLAESEMAWRVTVAQSLPKGDKLETVIQKGTEAGAAAFLPFLSQRTVVQYDDRKEAKRVDRWRRIAKEAAEQSHRGVVPEVMAVSSWKSLIGRFAEYDLVLLCYEEEGRAGNGLRRVLTEFAANRVEGGEPRILIVVGPEGGFDEREAEAAAAAGALPIGLGKRILRTETAALYALACIGYASGELGGDS | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A651E634 | MRPTRAIIHLENLKHNIRSVQAWTAEHSPGPSTVRPKLCIAVKADAYGHGIVETARAAVECGTEYLAVATVDEAVQVREAGIALPLLLYSLPGTSEIPTVIAMRITPLVTDRAYVDALARESRAQGLRTSCHIKVDTGMGRIGCRPEDTITLVEAVRSHPELRLEGISTHYPMADHADERYTRDQTRRFASLIEDLRSRGVNPGLVHASNSGGVLRFPEGYFDMVRPGIMVYGYYPGPELDRPIDLKPVMEFRSKLVFVKKVATGTAISYGHTWKSDRDTWIGTVPCGYADGYPRLLSNRAQVWIDGRRCPVVGAVCMDQ... | 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: 385
Sequence Mass (Da): 42508
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A0A6C1QV07 | DEERLAWDEAWEITVKTLAYTNHTLMPEALEKWSVPMMESLLPRHLQIIYEINQRFLQRAAIFFPGDPQKLSAVSIIEEGTEKQVRMANLAIVGSHSTNGVAELHTTLLKGRVVPEFAAIFPDRFNNKTNGITQRRWLLKANPPLAALITEAIGDGWITDFTQIAKLKPFAEDASFRARFRDVKRQAKVALSDHLQRHHGWTLNPDSLFDVQIKRIHQYKRQLMDALGIVVLYNRLRAGTMPDFVPRTFLFGGKAAPGYDLAKLTIKFINNLAAVINSDPAVRGKLSVHFLPNYRVSLAERIFPASDLSEQISTAGTEAS... | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
EC: 2.4.1.1
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + phosphate ... |
A0A084J7S5 | MGVAGLVILKKRIKSIENTKKLTKAMALVATSKLKKVRVSLYTNDTYFKSYREVMNEVIPSLPKENRYMQSNGSKKKLIIVITSDMGMCGAYNNNVIDKLKEITKGHEEDYLIAVIGEKGKSLAKRHRIKTLDKYNQTISDVPTATEAKSIFEYSFNMFSEEKVGEVSILYTWFKNPIVKEPKECRLLPLTFEESEEDHIGEDEFDIEGNKEELIESIVPSYCNAMILNAMINSKASEQGNRMETMNSATQNADELIASLRLKYNRVRQGAITQEISEIIGGAQAQS | 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: 287
Sequence Mass (Da): 32427
Location Topology: Per... |
L8GH71 | MNAKFLFAAFCLLGFVASMQASNVADLTDDSFAEFIANNEFVLAEFYAPWCGHCKQLAPEYEKAADQLLEAGSPVKLAKVDCTVQQQIAQQFEIQGYPTLKWFRNGKATEYQGPRDASGIVAWVNKKSGPPTHTLTDKAQLDAHIAAGTVVVGFFEKDSDAHKAFVAAAQSPQADSFTFVDVVSEDLIKEAGEKVGTVKLYRSFDEPLALEGEVTEQAVVSLVTGHGFPYFEPAPVAWARLIGRGLEYILLIVADVTEEDVWNPINTFATKLAKQYADKVGFVYLTKEFFPRVTQFGLSGKHFPAALVMAPHREKTFLLD... | Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
EC: 5.3.4.1
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 482
Sequence Mass (Da): 52926
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A0A1Y2ENG8 | MTDQNDTPSVAGPGGAAPTSARSPSHRPSPSQRATTQRRPPPNIAGPTNNSYTPPPNPTRRNTAGEVVSEDQIEKKGDSGKAAAVWGVGGVFPQREEKRGMPKKEKEKHDDEREEGKRVSAPTETDWPASEREDPFSSSPSSPPPHHNEVDSPTSVESNPHSESSTVCEEQPRQKEGESSGGDEDQDQGQVGGELPQDGEWEDEMEKQDGDPPVHTWWGSVRFALREPLAEFLGMLLVIALGTGANCQVKISQDSAGTYSNMNFVWGMAVMVGIYVAGGISGGHLNPSVTISLAVFRGFPWRMVPRYLIAQVLGAFCGAL... | Catalytic Activity: H2O(in) = H2O(out)
Subcellular Location: Membrane
Sequence Length: 590
Sequence Mass (Da): 63772
Location Topology: Multi-pass membrane protein
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G9X334 | MLGLKFDDFIDEKLMNPYVVMTTLFVWGIVIIFIEARHKKAKIKSISDMSYKTALLIGLAQCIALVPGTSRSAATIIGAMLLGCSRTVSAEFSFFLAIPTMFGATSLKIVKAILRGTPMSMWQVFLILLGTVLSFIFALIVIRKFIKYVKEHNFIAFGLYRVVLSVVMAIYFLIIAK | 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: 177
Sequence Mass (Da): 19758
Location Topology: Multi-pass membrane protein
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A0A813BRT5 | MAASSALPQLQFNWTHHLERWGTPGTEQSAAGWRDGSWYSFHNRPYKQLPEMIPALAPFYTDAELNFDPGNFVVFAALNYPLVFGIVTAYAVLVFGGQYLMKGWPAFDLQRPLALWNLALSVFSTMGMLRVVPHLLYNLYTHGLAYTQAYGSGATGLWVMLFIFSKIPELFDTAFIVLRKKKLLFLHWYHHITVLLYCWDSYASYAAPGLWFIAMNYTVHAIMYFYFFLTACGYRPSWAPLVTTLQISQMAVGVMVCTMVYLLKFRGADSTCDVSDINFLAGLAMYASYFVLFGLFALKRYCSGSAPRSSAAKAKAGSAY... | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 350
Sequence Mass (Da): 38932
Location Topology: Multi-pass membrane protein
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A0A6B2BYM9 | MISYFTELNKLTASVNDALSKLGITTTSVYVGEPTEPAFGEITTNAAFVLAKTFKKPPYEIAKDFLNKIEYDKENLSAEIHPSGFINFRFTERFYLSFLNEILKNDGFGEIQVKEKKKIIIEHTSVNPNKALHVGHARNVVLGDTFYRLFKRLGHDVKVLNYIDDTGVQVADLIVGFKYLGYSLESDDKFDHYCGDVVYVNANKAIEENEELKKKRSEILKDLEEGGEIYNFAKPIIEKIVREQLKSAWNIGARYDILNWESHFIHGGYWKKMFEILKEKGLVKFIKEGKYKNCWVLLDKKILIRSDGTTVYTAKDLTYA... | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
EC: 6.1.1.19
Subcellular Location: Cytoplasm
Sequence Length: 614
Sequence Mass (Da): 70549
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A0A6N2E686 | MKKLESTFVNMFVVLSLIALLSAALLSFTYSKTSVVRAEVEREQQQRALAAVLPEFDNSPGEEAFEREGFELQELYPATRDGEKVGIAVRSVTRRAYSGTMVFLVGFNAQGVITGIQVLNHAETPGLGSRVTEDEFLGQFIGQDLNEFNPALRADGGEVDVITAATVTSNAAIHAIQTAFEAAFDGEKE | 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: 189
Sequence Mass (Da): 20493
Location Topology: Single-pass membrane protein
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D0X3B8 | MVYGAVKKKAKQSLATSHLVSWMLTKKTKIDLVEKERDFAPAPEDDFEIIRKDRKEPDFGMASSFDNKFESDPLFGGPSEVKQTQQEPDDIPSFVAEKDKEEDVEPVVQATVAEEPFQPAVEEDVIPAAFDITEKEQQVETVSEPVVAEPKEEPKPEPEMQVIVLNVHCAGEEPFVGTALFESMQQNGLIYGEMDIFHRHVDLSGNGKVLFSVANMMHPGTFEHADPAEFTTKGISFFMTLPCYGEAEQNFNLMLRTAQQIADDLGGNVLDDQRNLMTPDRLASYRRQIVEFNAANA | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 2... |
A0A137NQH5 | MSEFKKGLPKLSQSLDGSELRVLIIHARWNKDIIDKLVEGCEIKLRELGVKEENIEYKSVPGSFELPFAAKRLIQKSKQDTSKRAYDAVICIGVLIKGSTMHFEYICESVSQGIMDTGLETEVPVIFGVLTCLTDDQAKIRAGIEVGGDPGHNHGLDWGAAAVEMALLVNILDKQLSLQLAVFPLSRFPQATATHLGNRKLLTIAKTDKNAFGGNAPVIDTEYGIFVENLGEFFKFNLKDGVERERVEKIMEEQKKLEEEDKMDIESDIGEGSYEDASSKHIAATVSTPTSKTTMNKR | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This ... |
A0A939X600 | VSSVLSKTPLSLYKAGEKPLATVDEVRDSLSGLEGISVKATGTGNDVAFQIRAGDDGKDKEVRNTRRNQIYNALSAKFGKDNIAVVKTDFIGSNFSKGLVLGSIVLVLATLALICVYATIRFKWDLALAAVLAIIHDALIMVAFVTFTQMEFSSITVAAILTIIGYSINDTVVVLDRIRENIKICNLKSFKDIWDLSQSEMISRTIITTVTTLLAVLSLYIFTTGSMKDFALVLAVGMISGVYSTIYIAGSFACLCRRNWKPSDEVKQTV | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 270
Sequence Mass (Da): 29368
Location... |
A0A6I7QPG1 | MKSGNTVEIRAEPGDSPSWLAALATYIHAVLALLGVENRELSVLITDDPTMQDLNKRFRAIDEPTDVLSFGDDPPEETGPMGDLVIDLAQVGRQAPLFHVTAEEELRRVTVHGILHLLGHRHQTDDLMAEPMLQLQEELLQTVEERLF | 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: 148
Sequence Mass (Da): 16529
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A0A843BKG6 | MRGAAFCPAHVTGFFGVEESGSAADTGSVGAGFSIQRGVTTTVEDAGHDAVRPGMAQYVLEEFRRATGVSTPVHMSHEMGVPAGYGLGSSGALALSALYALDTALGTRMPKESLAMMAHISEVRLRTGLGDVLAAYHGGFEIRVRPGGPGRGIIRRLEAGDPAVVVACLSPLSTSDFLRDRMGILNGMGGRMVAELDRHPDMGTFQRLSMEFARKAGTITPQMESGASALERAGYPCGVAMLGGTIFSMVPQDDAGGVMEALRPYDPVLTGIDHEGARAI | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Function: Phosphorylates (R)-pantoate to form (R)-4-phosphopantoate in the CoA biosynthesis pathway.
EC: 2.7.1.169
Catalytic Activity: (R)-pantoate + ATP = (R)-4-phosphopantoate + ADP + H(+)
Sequence Length: 280
Sequence Mass (Da): 29199
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D2Z369 | MSYSLSQLSEILEGRCIGNGDVLIGRVSTPEGASGDSIVVVLDGKVLKDIPGGVSIVGKEEVFSDGRRGISVREPRLAMAVLLGLFQEKATVQAGIDPSAVIHRSAHVDENASIGPLCVLSEGTSVSAGAVLRANVFVGRGVSIGEDSVIEPGVVIYQGCSIGKRALIHGNVVIGADGFGHIPASEGRRVVKVPQIGGVRICDDVEIGANTSIDRGTIGDTVIGEGTKIDNHIQIGHNAFIGKDCLLAAQVGIAGSAVLEDRVVMAARSGVQDHTRVGSDSIVAALGGVTKDLPSGSLVSGFPARNHRSKLRQDAYVARI... | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.... |
A0A2N1JGK6 | MVRDVFELPNLASLRGSMGVGHVRYPTAGSFAHSEAQPFYVNSPYGIVFAHNGNTVNQAELRKMLDGECHRHVNTDSDSELLLNLFASYLQETGKFRVNEEDIFTAIKKLMGKVVGAYACVAMIAGFGIIAFRDPHGIRPLGMCSRRSQHASRGGDDKDICFASESVVGDALDYTDFEDVRPGEAIIVTRSNITRKKLVATSSADAFTPDIFEYVYFARPDSVIDGVSVYRSRMAMGERLARTVSSELLEKGVKIDVVIPVPDTSRVAALQVAQNLGIHYREGFVKNRYVGRTFIMPGQSVRRKNVRRKLNAMALEFNDK... | Cofactor: Binds 1 Mg(2+) ion per subunit.
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 1/2.
EC: 2.4.2.14
Catalytic Activity: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1... |
A0A1I7BZ69 | MAYHSRSRDPLLDSNMQAAIEKRGKELIGIVLICLGLAAAAMIASYTPDDPNWMVSTDAPVQNWMGRIGASVAAPLFMIVGWGSWGIALVCLVWGVRFAFHRGEERAVGRLIFAPIAIAVASIYAATLVPDATWRATHSFGLGGLFGDTVMGALLTLLPIGSHLALKLLSLLTAVGMVVLAAFVLGFTRADIGRGIRATLIGLVMAYGALATLLGRGASTVMERARDKHAQLQERRDEARQVRAEAAMAYQATNDALAVSAPADFAQSEIGEQIEDTGERSGFLSRMPSLIRRPEAMPQAELVDPEEIEGYDDMPGDDRI... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
A0A2N3G7A6 | MCRKCSRSRRWPMPSPGSGGPMKSKGSCVVTISGVRVFARHGVLPKEKKRRQEFLIDIEIELDGPPLSDELSSTVDYADVASKAASLATNRSYDLIETLAFDIASSVLESRFARKATVTVKKPGASMPVHVECVGVTVSKDRPAESGGCGDARKSVSS | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydr... |
A0A533V720 | MMYVPKAMFFTKGKGVHKDHLTSFELALRDAKISDLNIVSVSSIKPPKCKIISLQEGRNYLVPGQVVFVIIARQSTNEPNRLIAASVGLANPADEGQYGYLSEHHSTGETAQKAGDYAEDMAMEMLASTMGLLVSAAVLLI | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
EC: 4.1.1.19
Catalytic Activity: H(+) + L-arginine = agmatine + CO2
Sequence Length: 141
Sequence Mass (Da): 15270
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A0A1G1N9H9 | MKFNSPTGMKDILPEEALLWHLIEEKAISIFNLYGYKPLRTPILEESALFNRSLGEEAEIVRKQMFEVKRGSSESYALRPEATAAVVRAYLENNLDRTNTFIKLFYIGPMFRAERPQKGRLRQFHHIGVEALGSDSPYLDSEIIALARRILEELKVHGFTIRLNSLGCSSDQQKLKSILRIKLKGHLNKLCADCNERYKKNVFRVLDCKNEGCPQVVATLKLRYEDYLCSGCSEHFLIVRKNLDRLKINYSLSPTLVRGLDYYSRTVFEITHQGLGAQDAIAAGGRYDRLIPELGGPELGAAGFAFGVERLLLASGLECA... | Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 418
Sequence Mass (Da): 47210
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A0A1E4RFF2 | MIISSILRKRANLPFKCDSFFQFVHDSYPDYKFELLQDTDQFYDKGVVKKANFFKDRTRDLLKERKKNEEIQIITKNDNITINNDFLARCQQTKIAGQKMADTITLMRIYGQCFIKNHPNNLNNDILKFGNNQKWFDQYTKTLFYYLSDKLPTFENQKYNLDLYGDQLPLFNENNLFEGETVSYRENQHNLLQFLKENSSGKGIAISASTRFTKDIIKLIRVLRALNNKLPIQIIYRGDLNQRSKEYMKAAAQADIEQLLGLEMSPDVNLVLPELNLIKTAEKLGSTFPKQDIWFINLSPTISRSHKFYFSGYTNKVLAL... | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 792
Sequence Mass (Da): 91677
Location Topology: Single-pass type II membrane protein
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A0A1Y3BH93 | LIAQIPKDYYEFLLKLQKNLASKIKSVGKIDYDYWRTYTNDKKTEPALNFIDGDLIESFLDLSSAEMAECTEGIMYNMNGQNRKATVDDIIKIVEELSRIH | Pathway: Protein modification; protein ubiquitination.
Function: Plays a role in DNA repair. May be a component of an E3 ubiquitin-protein ligase which promotes histone ubiquitination in response to UV irradiation. Histone ubiquitination may be important for subsequent DNA repair.
Subcellular Location: Cytoplasm
Sequen... |
A0A812LLC6 | MPLRRVCNRNGGVLCISTLRLHHPLPLAVVHTHMAERSFVLWALALSLLGFWWWLCYRRKCLLAPSAHALVAALAESHSSEISEKVGRGDRICLRAMSSEGVTVTGAEEYPVFESFDDYELDENLLRGIYSYGFEKPSAIQQRGIKPILDGRDTIGQAQSGTGKTATFVIGALQRINYGERHTQALILAPTRELANQIYKVALALGDYLKVRAHACIGGTSIQEDKDKLRDGQHLVVGTPGRVYDMVNKRHLNVDYLKVFVLDEADELMSRGFKDQIYDIFKCLPPDVQVCLFSATMAPEILDMTTKFMRNAVRILVKKD... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 420
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 47363
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A0A2T7UU72 | MKPPRYIRRRRSPPGTAPGTLTADPGAHPSTIHAFRYSAEGVEESDQILTCKPGTVLWLNVDGLADTALLQRIGEIFGLHPLALEDVVNGHQRPKAEEYEAHQFIALRMPDRRAGLVATEQVTMFLGDGFVITFQERSGDVFDPVRVRLRNPQGQMRKRGADYLCYALLDAVIDAFFPVLETLGEQLEALEDEVVFKASATEMGDIHAIKRDLMAVRSAVWPLRDLVSALTREETPRFTETTRLYLRDCQDHAVQLIETLQTYREIATGLVDILLSSQSNKINEVMQVLTLIATIFIPLTFVVGVYGMNFDDMPELHWRW... | Function: Mediates influx of magnesium ions.
Catalytic Activity: Mg(2+)(in) = Mg(2+)(out)
Subcellular Location: Membrane
Sequence Length: 350
Sequence Mass (Da): 39525
Location Topology: Multi-pass membrane protein
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A0A0G1ZBK0 | MATTSDIRLGFYLVHSGEPYVVFATDFMKKAQSKGMLRTSIRNLLNGNVLKVTYRSGEQIEEADITHSKATYLYEDGTQFHFMDAKSYEQFFLPAASIGDQKDFLMENQEVDVVQFNGSPITIELPKKIVLEVIETEPAVRGDTAQGTVTKPAKMSTGAEVAVPLFVKTGDKIRINTETREYVERA | Pathway: Protein biosynthesis; polypeptide chain elongation.
Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increa... |
A0A963KRD6 | MSEEGGPDPRTDGERTVRGRPAAPGTGIGTLVSLDAPTVGIAASAETMPPERIREVLVGAIRDTGEALAALSLSLDPQAAEILEFQTAFLADPGLIEEINTVLGTADDRPLAVWSRVMEAQIRPVEEEEDEYFRARAADLRDMERSVADRLAAVRTERRTIPHGSILCGDDLSPSTFLSLDRDRLEGIALARGSATSHVAMLARSRGIPMVVALAEPPAPGARAIVDGSGGNLVIHPSISTLATFERRVEAAGVSDEILFAPAILPSGERVGIHINVDDPSAVSEREWRACDGVGLMRSEFLFSSDGSPPDEESQYSAYR... | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfer... |
A0A963NCF7 | MTSRTARSESGRPGHSHHRKTVFVNIGLIVSGGIAAFKIPELIRRGRERGMAFTCIMTRAASRFVAPLSLAALSGNRVYDDLFSLTDEAEMGHIRLSRENDILVVAPATADIIARMATGQADDLATAVLLATDKPVLVAPAMNPAMWNHPATQRNLRQLGADGIRQVGPDPGDMACGETGSGRMAEPPDILDAIERLLRPSGQPLAGYHAIVTSGPTHEAIDPVRYIANHSSGRQGHAIAAALAEAGARVTLVSGPVHIPDPRNVTVRHVISASDMLAAVEEALPADIAVCAAAVADWRPAHAGDQKMKKDGSGPPSLTM... | Cofactor: Binds 1 FMN per subunit.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5.
Function: Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the se... |
F2F590 | MPMFLIGIGGAIGAVLRYSISLFLITNDTAAFPFATVAVNLVGCFLLGLLSSGFEQKITANSNYLSALKTGLIGSFTTFSTFSVEVIQLLQHHSYLFAILYIFISAIFGFLFVALGMKAGRSLWERKEPV | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 130
Sequence Mass (Da): 14126
Location Topology: Multi-pass membrane protein
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W0U5N8 | MKLVIASNNKGKIREYKQILEPLGYEVFSQSEAGLILDVEETGTTFAENSALKARAAFKLCGCAVLADDSGLEIDALDGEPGVYSARYGGLETDDERTALVLKKMKEIPDDKRGAHFTCTIHFIKADGEEIAVEGKVFGKIAHEPVGENGFGYDPIFMYGNKSFAQVDSETKNTVSHRANALKALLEQLTKQ | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
A0A963QZH7 | MRQPSGKTHLYAILGHPIAHVRAPEFLNPLIERAGRDAFVVPFHVLPEDLEEVVPRLVAIRNLRGFIVTIPHKPAMARMCAELGPAAEATGTANTVRLEETGRLVGDMFDGVGLVEGAKAEGMDPTGRSVLMVGTGGAGRAIALSLAQCGVKRLVLANRTASKAEELARLVRARVPDCAVSVGPADATGHDLVVNATSLGLHAEDALPVDPATFAEGTALFDIIAARDTELMRAVRARGCPVAGGRPMVEHQAAAQIAFLDAPMLPGAKP | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Length: 270
Sequence Mass (Da): 28284
|
A0A8R1XMM4 | MKSTALLWFPVVRNSKGVAVWQESNRIKFPKGKSERRFAFHKSPAVYALIFTLYIFYARIRTDRDKNYKPIWARLSANQEEAATLPDRSQLTKYFFFNILVHKSVQIKTLVKEPPPETNDFYFQQTMLRIKDPRKTLPFYCNVLGMRLLKQMDYPDGKFSLYFVGYKPASEIPNDPIEQKRYALSTLATIELTHNWGTENDPNFNYHNGNKEPRGFGHIGIAVKDVYAACKRFEELGVQFVKKPDDGRMKGLAFIQDPDGYWIEIFNPHTV | Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
Function: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
EC: 4.4.1.5
Catalytic Activity: (R)-S-lactoylglutathione = glutathione + methylglyoxal
S... |
A0A533W8M3 | MCGIIGCVNDEAVAPILLQGLKRVEYRGYDSAGVATVSESVIRVTKAAGRIDDIERKYGLSTLTGTTGIAHTRWATHGGVTDRNAHPHTSCRERVAIVHNGIIENYLELKKQLRAKGHIFKSETDSEVIAHLIEAEYRQVKDPVKATILAAKRLKGQYAFAALFQDAPELITGARKDAPLLIGVGDTKNFIASDVLAFIEHTDRTIFLDNQEVVKVTNRSVEIFDMNGRPVRRKPTQVAWELADLSKMDYAHYTLKEIHEQPKTVVSAMMQNEEKLAEFVEKIRGARSVFVTAAGTSYHAGLLLKYRLERDAAIRCEVTL... | Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic Activity: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
EC: 2.6.1.16
Subcellular Location: Cytoplasm
Sequence Length: 587
Sequence Mass... |
A0A6B2C0B9 | MKKESSPKRVQSPELGENEGKYVELHGWVHDIRILGKLTFLIIGDPYGYYQAVLKGELAKKGSSIPRQSYVILRGNVVKSVSKINPYEVQVNYIEIVNEADTVLPLDPASKVQSELMTRINNRPLDLRDSEERKIFLMRADVLHIIRDFLTQNGFVEVDTPKIIATASEGGAELFKVDYFGKPAYLAQSPQLYKEELVLALGKVFEIAHYFRAEKSNTVKHLNEFTSVDIESAMMGKFDVMKILEELIKHIYSSLKAKGYQVNELKGNFPIYTYEQVCDSTGVNFGEDLSSEVLNEFGKDKEFYFIIDWPLSLKPFYTMP... | Cofactor: Binds 3 Mg(2+) cations per subunit. The strongest magnesium site (Mg1) is bound to the beta- and gamma-phosphates of ATP and four water molecules complete its coordination sphere.
Function: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to fo... |
D5XFK2 | MGEISKKNHNIALRCGITTGASAAAAAGAATALLSRGERLEFYKVVNPNGQELVVKIKSVRLDGDKATGIVVKDGGDDPDTTHGLDIVAEVSFIPGTGVEITAGTGVGTVTKPGLQVPVGQPAINPVPRQMITEAVKRELPEGFGARVCISIPMGEEVARRTLNPKLGIVNGLSVLGTTGIVEPMSEDSFKRSLAPQISMAKANGFRTVCLTPGRLGEKWAVEKLGLPVDCVAQMSNFVGYMLEVCVKEGIEGVILVGHHSKLTKIAAGCFHTHNRVADARLETLAAHAALMGASRQVVDRLMRSNTAEEGYQVLKENNL... | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 6/10.
Function: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
EC: 2.1.1.195
Catalytic Activity: Co-precorrin-5B + S-adenosyl-L-methionine = Co-p... |
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