ids
stringlengths 6
10
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stringlengths 16
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stringlengths 117
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A0A0D6GPL2 | MSKQFDVVVIGAGPGGYIAAIRAAQLGMSVACIDAWQNGQGGPAPGGTCTNVGCIPSKALLQSSEHFEQANHHFAEHGIEVKGVSLKLDTLIGRKNSVVKQNNDGILYLFKKNKVTFFHGKGAFAGQVEGGWAIKVTGTAEEDLVAKHVVVATGSSARELPGLPFDEKVVLSNDGALNIGAVPKTLGVIGAGVIGLEMGSVWRRLGAEVTILEAMPEFLAAADQQVAKEALKAFTKQGLNIQMGVKIGEIKATAKSVTVPYVDAKGAEQKLVVDKLIVSIGRVPYTGGLNADAVGLKLDERGFIAVDGDCKTNLPNVWAVGDVVRGPMLAHKAEEEGVAVAERIAGQHGHVNFDTVPWVIYTSPEIAWVGKTEQQLKAEGREYKAGSFPFLANGRARALGDTTGFAKVIADAKTDEVLGVHIVGPMASELISEAVTIMEFRGAAEDIARICHAHPTLSEAVKEAALAVDKRALNF | 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): 49996
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A0A946L1I1 | MLIDRVQYRYGLILGLLLSLCSLTVVAEDEEEPPVPISEYMVLSKEPFKVNLSGKGEHVMVLHAQVYLITQRAKDGVKLHLPKIQNDVLELLGEQSFKNMKKTKHKKKLRKKVLKLIRKVMADREILDKPAKQEEIAEVIFTQVLLQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell inner membrane
Sequence Length: 147
Sequence Mass (Da): 16915
Location Topology: Single-pass membrane protein
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A0A2E5RIQ2 | MNTTKKSKSIESKLKELEGLLEELESGKLDLDEALIKFEKGIKLSRECQQTLEEAELKIQVLMDDELKDSDDSLSQ | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular Location: Cytoplasm
Sequence Length: 76
Sequence Mass (Da): 8657
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A0A6A0H3R6 | MTSSILSPRETGKFVSSKASNVSIDNTAIELLASYLADTVEQTALQSVGNEKCYFPEFSGLTSSQIINCVFIVDALNFNFWTCANEPRYTVTWNKVTGSGYLGLIQAINRALANGHAMYNPNYYGQLQAEDLKAMFRSDSGIEIPLLSERQSVLHEVSQVLIDKFNSSFTEMLEKAAGDARKLMQLVVENFPCFKDEAVYCGTKVSLYKRAQILTADLDLVFAMKGMPRLQNMDTLTMFADYRVPQVLLYFGVLVYSASLLENVKDNLVFANGSNEEVEIRACSIEAVERLVQSCRQQLQDRGWSKARALSSVSSVQVDYLLWEYRLANAEKLVKIPYHKTRCIFY | Function: Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q). Is required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly.
EC: 3.2.2.-
Catalytic Activity: H2O + queuosine 5'-phosphate = D-ribose 5-phosphate + queuine
Sequence Length: 346
Sequence Mass (Da): 38945
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A0A6N9D297 | MEMIFVLVIIFAVVLLIFGTKKLKNFGKDLGSTIKDFRSSVRDDKGENDNSSKQDNAQPSSSEESVKTN | 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: 69
Sequence Mass (Da): 7669
Location Topology: Single-pass membrane protein
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A0A661EWS5 | MPGLTIQIASSAADLPDLETFRLWVDLAREGHLNRAGEVTIRIVDEPESAQLNQQYRHKQGPTNVLSFPVADLDMPLPPDSEPELGDLVICAPLVGLEAKEQQKSVSAHWAHLTLHGLLHLCGFDHQTDDEQLQMETLEISLLQQIDIENPYLMEDMESP | 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: 160
Sequence Mass (Da): 17882
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Q6TM15 | TLAETNRAPFDLTEGESELVSGFNVEYAAGPFALFFMAEYTNIILMNALTTIIFLGPLYYINLPELYSTNFMMEALLLSSTFLWIRASYPRFRYDQLMHLLWKNFLPLTLALCMWHISLPIFTAGVPPS | Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Membrane
Sequence Length: 129
Sequence Mass (Da): 14786
Location Topology: Multi-pass membrane protein
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A0A945VM33 | MRLLIALFVFLLAVLGAGYWLNDPGYVLVRLGDIAAETTLWGGFLILTAALVVLRLFYVTLRGFLRGSSWLLGWSGQRKAKGLHAHSEKAAIALVQGKWLLAQQHFIKAQKLGDIGFAGNLGLARAAYELGHKDVQINALTSAKTLSPDNSQSISNLAMAWQVAQDESEEVIEILEPLHAAGECTHQMHIVLARAYLSQQRWLDVKALWPSLEKQKLLKKELFDKDFEHLWAARLLAEANIADALKMLPKALKSDTAMLTQWVDLLLLEGKEDDAVAVIEVALAADWDEPLVRRYGTTHGSDIDAQLVQAKKWLKKNTNDVALLMTLGHLAIVKRQVSSARDYFENALAQTAESDPVRSEIYRELGRACHSLGDSQRALQYLLKA | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in a late step of protoheme IX synthesis.
Subcellular Location: Cell inner membrane
Sequence Length: 385
Sequence Mass (Da): 42764
Location Topology: Multi-pass membrane protein
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K5BFH0 | MSETIAVPEHLDDPAPPARKLRGNLGVAAIVFMVVAAAAPLGVIGGVVPLGLANGNGSGFPATFIISTVILLLFSAGFTAMTPYVEDAGAFFSYVRRALGFPTGMGIAFVAVLSYIALEAGVYGLIGPAGTAVVELFGGPSLPWWLFAAAAFAIITYLGYRNIELSSQVLAVLLTAEIAIVVVLDAVIVAQGGDHGLSTGIVNPGAIFSGSLGIGLLFAIISYVGFEATAIFRDEARDPDRTIPRATYVSLILIGVFYAVTSWALISGWGDQQAVARATESGDTFLGDTARRYIGIVGADIISVLYFTSLFACILAFHNVVSRYVFALSQRDILPASLSYPHPRHGSPHRASLWVSAVVAVSITAAVLFRLDPAGQFYTWFAGTTTVGIVVLLLATTVAVIVFFGRDRRGYSLWRVRVAPALGALGLALSLVLILTNLKDLVGGSSVLAWVILSLLVLAFASGTAVGIRLGDKVIESRTVAGDAAAGDPIDDEAVRS | Function: Probable amino-acid or metabolite transport protein.
Subcellular Location: Membrane
Sequence Length: 497
Sequence Mass (Da): 51906
Location Topology: Multi-pass membrane protein
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A0A960UMA4 | MTEQDDLSPYRKQIDDLDHQIVELLLRRAQAASHIGEVKRRKDEPVYRPDREQGVYENIVKYAAEVRKQWQGEPLPELPESTFRNIYREIMSGSIALEGGPSVGYLGPPGSFSHMATRYRFGNSVRGMPMDTIPEIFRSVANLHEASYGVVPADNTAAGSVGITMDCFLDSSLQIYAEQFVRVRHHLMAANHIELANIRKIYTIPIGLEQCKEWARKNLPMHDVQVVETSSTARAAQMVAETSDGVAIASELASEIYGLKILSRDIQDSSDNITRFWIVGHEQCPPGKKDRTSLVLSFHDEPGGLFRILKPFHDAGINLTRIESRATRKNYGEYNFFIDLEGHREAEPVKSILQELERYTSFLKVLGSYPMGQVD | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
Function: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
EC: 4.2.1.51
Subcellular Location: Cytoplasm
Sequence Length: 375
Sequence Mass (Da): 42355
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A0A945FVZ9 | MSPWRLRQIARKVNRGALIAYPTDTIWGFGCSPESAGAIKRLQRLKRRSANKGLILLSPKLDFLKPFIDSSKHHQLESQLKTETEKPVTWIIKASHYCPLWLTGYSDTIAIRLTQAPQVKLICQITQLPLISTSANITSRKPVRSSLQAHKHFQNNVDYIIEGFDTGCSQASQIRDLETGEILRA | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate.
Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate
EC: 2.7.7.87
Subcellular Location: Cytoplasm
Sequence Length: 185
Sequence Mass (Da): 20894
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A0A6N8UN50 | MIEELVRIAEIAAEEILDIYHSNFEVKSKSDESPVTRADLAAHRAIVQELRQLDPSIPILSEESTLPEFSIRKSWQRYWLIDPLDGTRNFVERNDEFTVNIALIQDGVPVLGVVGVPTLECVYIGDVASRKAMKRASGTMHSIGTRKRRRSRATLVESRHNTTPANEVIADYLVAKQQVSVDRTQMGSSLKICVIAEGQADLYLRMGLTSEWDIAAASAVLLAANGDLRMLGGYPKKYNEQESVLNSSFFACGDDPNYWTRVIADALPNPG | Function: Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
EC: 3.1.3.7
Subcellular Location: Cell inner membrane
Sequence Length: 271
Sequence Mass (Da): 30095
Location Topology: Peripheral membrane protein
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A0A2E6LVV7 | MNPKRKKKLILILSLFAGFACVFALAFYSLKGNLDHFYSPHEVLEGQVKPGQRLKVGGIVKDHSVEHSEDSLDVTFIVTDTLGDVIINYTGILPDLFREGQGVVIQGVLNEQGGVDADKVLAKHDENYTPPEAAAALMKAAEKQEQDAAKKYSNQ | Function: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
Subcellular Location: Cell membrane
Sequence Length: 155
Sequence Mass (Da): 16983
Location Topology: Single-pass type II membrane protein
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A0A1S8LPG3 | MKNQYFDRDKFFIILFSLLTTIYIIILCLPIASIVRYSGISSILITIQDSESLSAIKLSLETSLVSLFFTFFLGTPTAFFITLRKKLLLTRLIDLIIEIPITLPPAAAGIALLLAFGKNGILGGFFSRYNIQLTFTPTAVVLSQFFVSSIYYIQVLKTSLETVPIEIFEASYVLGCGKVETAIRVIIPMLKKSVISGLILTWIRSMGEFGATIVFAGNVMNKTTTMPLLIYTFMQTNIAKSAAFSLVLYIISFIILFLIKTWCARDD | Function: Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 267
Sequence Mass (Da): 29788
Location Topology: Multi-pass membrane protein
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A0A2E5RHY9 | MPFFMSCSVMLENFINWKIYGVSEQTFQSMKIKIISVTSKKNQFNSEIDRYIKMLPSFMKVEQLELPISKRSKQKAILQNIEEESERILRHIGPSDYLIIMDEHGKQIDTIEFSEWLKRWMDESAQPVLVIGGPDGLGQSIKERANASLSLSSLTYAHSMVPLILAEQLYRAWSILDNQPYHRQ | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.177
Subcellular Location: Cytoplasm
Sequence Length: 184
Sequence Mass (Da): 21387
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A0A0X3QBH8 | MGKSLIQFFSQRFIYFLLYTAFTDFIFVLFGAPLVSNQWSTFAFSMWFAFLSFAPFLAKFEPTLNNIRRILWDPTSSCEIFTMRCFWGTLLGTWASAFCLVLDWDRPWQTWPIPCVVGALLGDIFGFITFCCGQFPKSDWADSGRRHSNNPPAKVYLE | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 158
Sequence Mass (Da): 18327
Location Topology: Multi-pass membrane protein
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A0A945SMH8 | LQGYNTLVDFGAEESLGVLVALSLVRELGPVVAALLFAGRAGSALTAEIGLMKATEQLSGMEMMAVDPVHRIVSPRFLAGFLSLPLLTGIFTVLGVYGGYFVAVPLLGVDDGAFWSQMQARVDFYDDLMSGVIKSVVFGFVVSWIALFEGYDATPTSEGVSRATTRTVVHASLAVLGLDFVLTALMFGA | Function: Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 189
Sequence Mass (Da): 19974
Location Topology: Multi-pass membrane protein
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A0A6B0Z773 | MRTVVLLSGTGTNFQAILDRRASGSLAIEPVGALSDRPDAQGLERARRAGIPAIAMPRGDFPDAHSWWDEIAARLRALSPDVLVLAGFMRILPPELCREYKGRVLNIHPSLLPRFPGLNTYRRVLAAGDRWHGTTVHFVTEDLDAGPRVAQARIRVGSGDDPDTLRARVQACEHVLYPRVLEWMSQGRLTMGARHAILDGSDLSEPVVFEEGQLL | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Function: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
EC: 2.1.2.2
Catalytic Activity: (6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide
Sequence Length: 215
Sequence Mass (Da): 23701
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A0A142UNL6 | MAIYQNITQLVGKTPVIKLNNIVPEGAAEVYVKLEAFNPGSSVKDRIALAMIEDAEKAGTIKPGDTIVEPTSGNTGIGLAWVGAAKGYKVIIVMPETMSVERRKIIQAYGAELVLTPGSEGMKGAIAKAKEIAEEKNGWVPFQFANPSNPKVHEDTTGQEILEDFGTTGLDAFVSGVGTGGTVSGVSHVLKTANPDIAIYAVEADESAVLSGEAPGPHKIQGISAGFIPDTLDTSAYDGIIRVKSDDALATGRAIGGKEGFLVGISSGAAIHAAIEVAKELGTGKKVLAILPDNGERYLSTALYEFND | Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2.
EC: 2.5.1.47
Catalytic Activity: hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine
Sequence Length: 308
Sequence Mass (Da): 32052
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A0A6N9CP43 | MSCWCRALAASVRYPTVCGVDMLSKLGAVAALLGLAAVAGWIYVSLDRPVRSVEVVGALAPAEAAEVQRRLTEFKPGRLLSTDLGALREHLMALSWPRLVQVRRVWPDTISIRIERQLVVAKWGGEGYLTAGGELVSGVDRAASVPLLDCEITSPQKALEIYRHLQDIAAEDGLEIRSLAENALGEWRLELANGVRAHLGADALRSRMGRFMEVHRHLAQKSEQGVRYLDLRYANGAAVRFDGPELLAAR | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Subcellular Location: Cell inner membrane
Sequence Length: 250
Sequence Mass (Da): 27373
Location Topology: Single-pass type II membrane protein
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A0A6L7LUN9 | MNTDRGGTCTVGTFDGIHLGHQRVITTLVNRAIEFGTHPLVILFEPQPNEYFLKTEAPPRLTSFREKLVLLADLGVQHVLCIRFDESTRSMTADSFIRTVLVDSLKIKHLVVGRDFKFGRQAKGNIGMLRSAAHDYEFTVEQVDDLEIQDTKVSSTRLRKAFECSDFSLVRSCLGRSYFIQGRVVKGRQLGTTLGVPTVNIPLNRSRSPLEGVFAVTIDGIERTHFGAAYIGSANSGSSSGQVLEVHIFDFDRDVYGSELRITFLKKFRADRQFDDNRTLREYMLADIRQIKQWIQATVTVLAPQNS | 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.
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 307
Sequence Mass (Da): 34563
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A0A954AGD2 | MPSSDRSHRDNNHAGHQRPRLGVLLSGSGRTLKNLLERIADGRLRASVAGVASDRDDAFGLQRAIENGLETRVLPEPSAMWSWLLELDVDLVILAGYLRLLPIVPEFEGRVLNIHPSLLPKHGGKGMYGERVHRAVLEAGERESGCTVHLCDDEYDRGRVLIQARVPVLPDDTATSLAARVFAAECEAYPAAIHLRWAELGAHDAQA | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Function: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
EC: 2.1.2.2
Catalytic Activity: (6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide
Sequence Length: 207
Sequence Mass (Da): 22703
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A0A6N9B5J6 | MDIKSVTDELKHISMSDEYHTEVQEYLASDSSNQTLSRMPHSTEAERAVLACAMGDPSAWDRLTGLLESKEFFEPKNRKIFETIRTLANQGSPMDNLTVCDALKNAGLLEEVGGYPYLFEIEETVHDSRNVEAYAKMVRGAALRRELIGASTYIKNIAHTPEDRTSEQVISESEERILGISKGTTGEQYQHFLGDILSPAVSRIEELRSAEGKLPGLPSGFWDLDDLTGGFHNNDLIIIAGRPSMGKTAFALNICEQVILAQETKPVLFFSLEQDHSQLVLRLLAAQSSVPYRNLVTAELSTQQWKQLESATGCLSDKPLFLVDRPNLSVEEMRSYARRINREVKSAESSGEGLGSNRLALIVVDYIQLMRPSRRHDNRVQEMGDITRSLKALAKEFNVPVVALSQLNRRLEDRHDKRPKMSDLRDSGEIEQDADLILFIYRDEVYDRESAEKGKAEIILAKHRNGPRGSIKLRFVEPLMKFDATGEDFREASSATDSTKRSQPDVNFNKTDAAGYSNAEEEDPF | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 525
Sequence Mass (Da): 58951
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A0A814UXB0 | MLAWALLSVIFCMKSFELYGYTDSSLVTCILTVVYLAKFFWWESGYMKTMDIIVDRAGFYLCWGCLVWVPALYTLPSYFLVSHPQQLGLNLTLFVLLIGFLSVYVNYDADHQKLHVRNTNGNCFVWGNRPQIIRAKYYLLNGKKSESLLLVSGYWSISRHFHYIPELLLAFIWSCPNGFHYVLPYFYFIILFILLMHRAHRDDQKCKYKYGQYWYEYCQKVKYRVCPGIY | Pathway: Steroid biosynthesis; cholesterol biosynthesis.
Subcellular Location: Membrane
Sequence Length: 230
Sequence Mass (Da): 27360
Location Topology: Multi-pass membrane protein
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A0A967NJD5 | MNEQAWTATLAESVARVGERVLEYLPSILGCLVLLLLGWVIARLLRALTRHVVERATQRLTRMRPGQPTAEASRTYRAMPTVLGGVVFWIVFLFFAAAAVEALGLPAVSNVLGAVTVYLPRILLGLLIVGLGFWAGDVARAMLARAAARSGIAHSDTLARMAQLGIVFLAVIIAVDQVGVDSAVLITSLAIAFAATLGAAALAFGLGARTTVGNIIAARYVQRVYRVGDAVRIGGLQGSIVEISDTAVMLQTSEGRVMVPAERFNEEVSILVQEND | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions.
Subcellular Location: Cell inner membrane
Sequence Length: 276
Sequence Mass (Da): 29305
Location Topology: Multi-pass membrane protein
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A0A432EKG8 | MIIGRFAPTPSGALHMGSLVAAMASYLAVPADGVWLLRIDDIDAPRVVPGSADRIIRQLDTFGFQWHGEIVWQSRRLERYRSALDQLRQQGLVYACECSRKTLTGVAETGPQGIIYPGLCANKNLPEPGNALRLRVTDKALCFDDACVGRICENLNKTTGDFIVQRRDGVISYHLATVVDDADAGVNQVVRGADLLGSTARQIRLQHLLGLPVPDYAHIPLVVNAQGRKLSKQNLAPELDESRPLPLLLDAWRLLGQSPLTQGPDDVASFWVLARSAFDLSRAAAKQQQYD | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon.
EC: 6.1.1.-
Sequence Length: 291
Sequence Mass (Da): 31902
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A0A947Z3E7 | MGIRVLVLGAQGQLGHTIGQHAKPALMETMDACISYGRDKADLANPDTLINALKDVRPDVVINAAAYTNVEKAETESELAHAINAKAVGILAEQCKKQGVALVHYSTDYVFDGKATKPYLETDATNPLSAYGKSKLEGEKYLKEVGGNWVVFRTGWVYGQRGNNFCKTMIKLAQERDTLNVVDDQTGAPTPANWLAELGLSVAGVVAMHRYKSTGKLAPTFLPDFPSEIPSGEIFHASAAGVTTWFDYARLALELAHKQGIVQHMPNIERAKTADMNFAAQRPAYSVLNNKKLMDAFRVNPPEWTKGVRNFVLNY | Cofactor: Binds 1 Mg(2+) ion per monomer.
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 315
Sequence Mass (Da): 34498
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A0A100JGZ1 | MPLLVEEGAPLLIDCLSLWLTDAMDSVGAWDDAVWADGGEKALRARVGELLEALRGTRRTVVVVSNEVGSGIVPATASGRRYRDELGRLNAGVAGECEQVVLVVAGQAMVLRG | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = adenosylcob(III)inamide phosphate + ADP + H(+)
Sequence Length: 113
Sequence Mass (Da): 11917
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A0A813NN66 | MEFEEFVESLESLPIDLSRNLRLLRELDDKNLQLRQECFHISDKFKQEIDNIQKREHIKILNDIQIRRLQLADEKVVLAEQASELCEKHIRRLDDILDHITTQQSIMKMSNVHNKKRSLSPSTDDQNQNNNKKRKTKQILDSVLNKKQLPETKTFVRVPKKLLQSTTTNNITTDQERINIEEYGMEIDPNEPRYCTCNQVSFGRMIKCDNESCPLEWFHFQCVNVDVAPKSDQLWFCPQCRENIKHK | Function: Component of an histone acetyltransferase complex.
Subcellular Location: Nucleus
Sequence Length: 247
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 29295
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A0A0U0A1U2 | MAIIKKIVVLYGGLSEEREVSENSAKEISKSLLTLGYDVISIDLSQDCSYEIGEIEKSERGLNKQKVEIGSGIIDVCRKVDIVFLATHGGIGENGKLQAIFDVEKIDYTGNSFLSTAISMDKKLSKIVASSVGIKCASNLMVDRIQANDFPIVIKPIRSGSSKGIKIFQNKKQFDIYYKEHPELGSFFVEKYIKGREFSVGILGETVLPVIEIKVKNGFYDYNNKYTVGAAEEVVPAKISEKLTHTLQKSAYKIHKALGFNVYSRTDFIVDEKGDVYFIESNSLPGMTKTSLLPQEAKAAGIDFPNLCERIIELSREIRSQ | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 321
Sequence Mass (Da): 35675
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A0A2E2ZGZ5 | MMQELFDELGYKFQNDSLLYRALTHKSASSDNNERLEFLGDAVLNLYVSEKLFNSYPSINEGKLSLFKSNIVSRENLNLVAKKINLHQHVVIGKGEKLQGNSILGNSLEALIAAIFLDSDYECTLKVLDTLFKKDFLELEEDTELKDPKSSLQEYIQKKYKSLPHYRTKESAGPDGNVRFHALCTVDEASLSCEGSGRTRKRAELDAANNMLEILDNYDSTA | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
EC: 3.1.26.3
Subcellular Location: Cytoplasm
Sequence Length: 222
Sequence Mass (Da): 25081
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A0A2D9B0W0 | MDFTVLLVLITFISGICLLLSQSNNSANSLYSILQFMGSLFPILFIVLFIRSFIVEPYKIPSGSMIPTLLIGDFILVKKYQYGVRAPIINKVIFENEKPSYGDIIVFQYPQNKKINYIKRVVALPGDSVRYIEKELFVNGKKYTQKQEILYPSSSQYSSEEVYKETNIYNSYNILKSTNPSQDFEYRVPEGTYFVLGDNRDNSNDSRYWGPVPYENLIGEAFYIWMFWNPSGSDTIIDRIGTSLD | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 245
Sequence Mass (Da): 28254
Location Topology: Multi-pass membrane protein
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A0A2E6LZH4 | MKDNNLIIRDLGVIDYTTSFKMMKDAIQQRYPLEQHELWVVTHPSVYSQGQAGKAEHLLNLSGIKCVQSDRGGQVTYHGPGQVVCYFLFDLTRLGLTVKTLVDGTTDSVINTCNSYDINAFDDPKNPGVYTDQGKIASLGFRIRKHMSYHGVAINFDMDLRPFSGINPCGLKQSISQITHLTSAFSGMNKTQARQQFTQAFIESVTKTFKFDNVAHSKCWPTFSTAN | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
EC: 2.3.1.181
Subcellular Location: Cytoplasm
Sequence Length: 227
Sequence Mass (Da): 25399
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A0A814BC42 | MRPWSFSASLMPVLLGSALAYPHIYDISIILLILTGLSALCVHAAGNLFNTYYDFKYGVDEKIAKEIDISVDDDRTLTEGLLKPDDVIQLGLVLYGIGTFIFLILTYFSPAREPYLGIIFFGALPLSFLYTGGIGFKYIAMGDILILLTFGPITVLYSFISQSGYYNPYPVLYALPLTLNTEAILHSNNTRDMLHDHAVGILTLSILIGKKLSYYFYCLLIYLPYLMIIFIMFKISWLCFLPLLTLGHARQLCKEFRTNQLIKLPNRTAQLNFQLGSLYILSIVLTNTITTKQQFL | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Membrane
Sequence Length: 296
Sequence Mass (Da): 33454
Location Topology: Multi-pass membrane protein
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A0A350I2V7 | MHLSFLLKFTISLPRLHVTLVTAGLALLVSAQAEHSNSETEVRPENFVVIDQHIPGIKIQLRYSTASNFTGNVVTGYEKGNCWITKEAATALSKVQKEVQQMNLSLLVFDAFRPQRAVDSFVEWAKESGTSKQEKDQYFPNLKKSELFPKGYIADKSGHTRGSTIDLTLCEVNEKGELSPLDMGTPFDFFGEEAGTEFKGIPAQQRANRLLLKMLMEKHGFRNYPVEWWHFTLKNEPYPDAYFDFPISDNDTPNEINGF | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide.
EC: 3.4.13.22
Catalytic Activity: D-alanyl-D-alanine + H2O = 2 D-alanine
Sequence Length: 259
Sequence Mass (Da): 29358
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A0A2E7U8T5 | MRCRWRIVTLGELIEDPNWSAVAVSGISEDSRTVQPGDLFIAASKLPEQRVLHVQEALAAGAAAVLVPEPMNLQAPVPVVPLGDLAARRSEIASRYHQHPSSELCCIGITGTNGKTSIAWHITDLSQRLGVSAGYCGTLGWGALDQLQPSQLTTPSAVALQGYLAAMQTRGASRVAMEVSSHALDQGRVAAVQFDVAVFSNLSRDHLDYHQTVEAYKDAKAKLFQHWPLAAAVINSNDPVGREFVCTSRANEVISYGTHGDVSWHSQAVRQGMRVTFSTPWGRTETVMPVAAEFAVANVAAAMAVLLSLGHSLHRVTEAVEIMAPVPGRMQVVDGGSKWPRVVVDYAHTPDAVEKALAALRPQCRGDLICVVGCGGDRDRGKRAQMGHAAAKGSDRAWFTSDNPRSEDPERILDDMVRSLGGPKLERVRSEVNRAQAIAAALASACPDDVVLIAGKGHEQTQEINGQFLPFSDFAVVHEIQNENS | 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 the biosynthesis of bacterial cell-wall peptidoglycan.
EC: 6.3.2.13
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate
Sequence Length: 485
Sequence Mass (Da): 52133
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A0A8C4R8Y5 | MASANIGPLVVTLAHKFCREHVNERLAIHTLQGIAVLASLLLAFFWHLDVRVGKKNVSIPYLSLVFVLSVVCCTSNVTFLPFMYNFSAQYVKTFFLGQGLSALLPSAIALFQGAGVAVCVNATVNGSSYEIQTRYQEENFSATVFFFFLFAVLFISAVSFIVIGATLRPERAGLRDEYRQEVYHDSNEVQPSLGETHHRPAFSPNMLFLLSILGLSTALSYGALPSVQTYSCLPYGITAFHVTAILSNVAQPVACFLTMLLPCRSNVIFALLSALSLLIGAYILTLAALSPCPPLLDGVAGSILVVLSWLIFSGVCTYLQVMIGSLLHSMSHMALLWCGLVIQSGSLIGALTVFPLINVYHLFKDGDPCYNSC | Function: Plasma membrane transporter mediating the uptake by cells of the water soluble vitamin B2/riboflavin that plays a key role in biochemical oxidation-reduction reactions of the carbohydrate, lipid, and amino acid metabolism.
Catalytic Activity: riboflavin(in) = riboflavin(out)
Subcellular Location: Cell membrane
Sequence Length: 373
Sequence Mass (Da): 40515
Location Topology: Multi-pass membrane protein
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A0A450UCB7 | MSQHRDFILRPPVMEDAARMWRFVIDSKTLDPNSPYCYLVLCRHFTDTCVIAEAENALAGFIAGYRPPGAQNTVVVWQMGTGAPHRRRGLGLAMLGELLRREECREVSYLEATVTPSNPASRAMLTALARELKADYVASTGFEASLFPKERPHEPERLFRIGPFPRVL | Pathway: Amine and polyamine biosynthesis; ectoine biosynthesis; L-ectoine from L-aspartate 4-semialdehyde: step 2/3.
Function: Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl coenzyme A.
EC: 2.3.1.178
Catalytic Activity: acetyl-CoA + L-2,4-diaminobutanoate = (2S)-4-acetamido-2-aminobutanoate + CoA + H(+)
Sequence Length: 168
Sequence Mass (Da): 18934
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A0A6L8EFB2 | MPVGAPPALRNPAEKETDRLKAVSLAISDRLSIPIPVTDLVNSIDTLPGIEHAAVIPRGEHGISRKDISKAALRVVYDLQNAGFAAFLVGGCVRDLLLGLHPKDFDVATDAHPEDVRRIFRRSRIVGRRFKIVHVRFGREVIEVTTFRGHHEASNRFRNAPSREQSRELDSAHSHTGMTLIDNVYGDIDEDAGRRDFTVNALYYSTDGFALFDFHDGLRDLREGRLRIIGDAGERYREDPVRMLRAIRFAAKLEFGMDGATETPIRELANLLESASSPRLFDELLKLLCGGHAAESFRMLKDYGIDRALFSHGFVDEDEAADPADRLVGLALRNSDDRIARGLGVTPGFLLAALLWPPVQRRMARLEGDRHLMRLRECAEEVVLEQSQHTTIPRRISNVSKEIWELQIRLERKDRRSVNFCFDHPRFRAGYDFLLLRERSGEDTGGMGEWWTTFQDVDQNQRVHMLEQLSVRPKRRRRKRAGRRANRG | Function: Adds poly(A) tail to the 3' end of many RNAs, which usually targets these RNAs for decay. Plays a significant role in the global control of gene expression, through influencing the rate of transcript degradation, and in the general RNA quality control.
EC: 2.7.7.19
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Length: 488
Sequence Mass (Da): 55551
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A0A0X3Q384 | MLDEYELVLVLVGFIIAFLLAFGIGANDVANTFGTSVGAKVLTLRAACTLASICELAGSILLGGHVSSTIKDGIVDTGRFNNTLDGPRLLMQGQVSSLAGACIWMLIATFFRLPVSGTHSIVGATAGYGLVHFGLKGIKWMGLLKIVVSWFISPILSGAVSFFIFLFIKRFVLSKEKPLEPALRSLPFIFACTIIVNVFSVLLGGIPIFNLKIPLWVVFVASILSGLVVGLVVFFLVVPFVRKRTIRYVEMLKQRELEGWDGTLNFGESSRFRVFLKNAYSRFLDFVHCRSCRKDHTMDTESGLHGPTSAHVSADGDITPKPIHRNEVLSSKSELLHPVEFESTFDCRETPEQTLEDDDPVSMEKNNKLSQKNDIILLSETDVTASEDGDVISFAESAIKTDRPEEAKVFSYAQILTATFGSFVHGGNDVSNAIGPL | Function: Sodium-phosphate symporter.
Subcellular Location: Membrane
Sequence Length: 437
Sequence Mass (Da): 47749
Location Topology: Multi-pass membrane protein
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A0A2E6M1K8 | MNINTDALFFISDLHLDPRQPDITQAFHDLLEKIKEHPAATKALFILGDLFEAWIGDDAIDVSLWLQTTLKPLKELGIKTYFIHGNRDFLINKGFEDYCDIENLEEVTQVNYKGFNLLLCHGDHLCTQDVEYMKFRTMVRNKEWQAHLLSKTIEERTAIAQQIRDQSKEANSIKEMDILDVDPLTLKAFMQQHQADALIHGHTHRPAVHQDIYPRIVLSDWHPNASWLELHVQDEKLIGKLVTQDWSEDILIEK | Cofactor: Binds 2 Mn(2+) ions per subunit in a binuclear metal center.
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 4/6.
Function: Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 3.6.1.54
Subcellular Location: Cell inner membrane
Catalytic Activity: H2O + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine = 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + 2 H(+) + UMP
Sequence Length: 254
Sequence Mass (Da): 29562
Location Topology: Peripheral membrane protein
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A0A945R8K4 | MANELDKLQDNLNYQFSDLGLLELALTHRSAEKNHNERLEFLGDSLLGFIVSDSLYQQHPSATEGELSRMRSSIVNNASLAAIAREMRLGDHLRLGSGESKSGGNERDSILADSVEALIASVYLDAGISACIKFVNNWFAAALQTGNDLEQKLQQQKDSKTRLQELMQSKSLPLPHYEVTEVNGAAHEQIFKVSCQITSLNTLQQGSGSSKREAEQEAAMHTLKELGETP | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
EC: 3.1.26.3
Subcellular Location: Cytoplasm
Sequence Length: 230
Sequence Mass (Da): 25301
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A0A183B0I2 | MSCQAFSRNIGPALIAWFLLIALTSMYLFFICWEFSHQTSYSLIIAHSFLITYVVCTFGRATFMDPGYLPVGNASMVCYLRDLPTPQMLPLFYLQTLYRCKCSFLSRLILQTFDHHCPWLNNCIGKRNYRYFLAFLLSLTAHMLITFGISVTFVLMRTDRLSSYPVIIAYPLLV | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 174
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 20150
Location Topology: Multi-pass membrane protein
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E3MT65 | MFGSVHRNSDPDNPNTLNGPRIPQENEQQPTVTTGMSWELRVQSFVGLFILSIIASFCGSYLLLLTKITGFCIMTSISAILSLSSTCCLMGPCGQLKKMFDRSRWIASSLYILFIFLTLISGLWLKNAPLAIICTVGQYIAMAWYSLSYIPYAREAVAKIFF | Function: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex.
Subcellular Location: Membrane
Sequence Length: 162
Sequence Mass (Da): 18068
Location Topology: Multi-pass membrane protein
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A0A3B9V3R8 | MPDPFKFSKPRSRYAVVGHPVSHSKSPSIHRAFAKQCTVTMEYEAIQLDLGGFAQGVRNLQAADFGGANVTLPFKEQARRIADRLSPRATIAGAVNTLKFADDGGIEGDNTDGAGLVVDLIQNIGISLAGTRLLVIGAGGAVRGILEPLLGAGVAGVTLANRTHEKAERLVQEFSSHGLVEACVLAKVGQIPFDLIINGTAASLEGELPALPSTVFAETTLVYDLAYADQLTPFLSLAKSAGVDRIADGLGMLVEQAAESFAIWHGIRPDTARILTDLGDQARFH | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
EC: 1.1.1.25
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Length: 285
Sequence Mass (Da): 30067
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A0A961NHY0 | MNTNVTVNAPAVKTPGSGAVVSGTENDAPAFYIRNIPIHGRLFLAPMAGFSDGPYRLLCRRLGAAFAFTEFISTDGVRQGRREVWQRLRFRDQERPVILQLFGNNPDVMLYSARLIEEMQPDVIDINMGCSVRAIAHKGSGAGMLRDPLRTGRIMERLVRHLHVPVTAKIRLGWDAASRNYLEMAHVLESSGVAMISVHGRTRAQGYGGQADWEAIGEIKARSNVPVLGNGDVTSRSMALERRRQTGVDGILIGRGAMGNPWIFQSDRQDGQYRPDRRAVLDTMQAHLRDMQQWYGERGLMLFRKHAARYLDRIETPAATRRRLLTGTDPEEFVDICLDLRDAPGC | Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
EC: 1.3.1.-
Catalytic Activity: a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA + H(+) + NADH
Sequence Length: 346
Sequence Mass (Da): 38682
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A0A2E9ZGQ2 | MQRLSLLLIPAVIAIALFLGFESTNTRDESDLEITRLNYDAYSEGINSVLYDESGNISYTLQASRQVHFSNDVTEIESPSIRLFQEGKSPWKLIANSGRISASSAGPDGARQLIDLIGNVEVHNLDEFGNSLVISTEFLSIDLDSNSLETEEAVKVVTDNTEQTSIGMYADLNQKTILLIKDIRGNYEPPQQ | Function: Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA.
Subcellular Location: Cell inner membrane
Sequence Length: 192
Sequence Mass (Da): 21230
Location Topology: Single-pass membrane protein
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A0A967YT64 | MSEIIDFLAMGGYARFIWPAYVLTAIVLLLNVVLPIRKEKNLIARLRTYHSRNNL | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 55
Sequence Mass (Da): 6389
Location Topology: Single-pass membrane protein
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A0A936ADG1 | MTEQVAGLEHLKPLEQAAILLLSVGESNAARILRYLSPKEVQRVGSQMTRMNDIKVDDVNLVLEQFLVEVGAATGLSMGTENYIRNVLIEALGDERANTLIDQILMSDKTKGLEALRWMNPKLVANTIRSEHPQIQAVILSYLHADQAAEVLTYFSEAARAELVLRVATMETLNASALKELNKIVEGELSGSGLQQGQRMGGVKFVAEIMNNLDSAAEQALLDQIKESDEVLGSRIQDMMFVFDDLKDVDAGGIQALLREVSSEVLVLALKAADEELKAKIFGNMSKRAGELLKEDLEAKGPVRVSDVENAQREILAVARRMSDAGEISLGGSSEAMI | Function: FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 338
Sequence Mass (Da): 36861
Location Topology: Peripheral membrane protein
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A0A661U231 | MIGRIKKFFREVVVEMKKVTWPSYHEVLGSTIVVIITSLFFAVIVGVFDLFLEKVLFFIVGR | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 62
Sequence Mass (Da): 7194
Location Topology: Single-pass membrane protein
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A0A8S2E9V4 | TWRCYVEGVHCIIRTDHKSLKYIPTQKNLSRRVVRWVEQLQHFDYEIVNTIEATDWPIYVTSYLENGQSTTDDELSDEVKQKIQQESHMFIIDPSNDILRRKLDDGTTVPFVPFINRSDTVRKTHEAYGHIVAEGTYQLLRTRAWWPNMKQDIKKWISMCQKCQLSTATSGNHEELHPLTPVLAFNRWSLDFVDHATKWPVVKVVPTATTQTVAKFLHDEIMMNYGCPSELLTDRGPSTMSRELRAYLQTMGTKHLLTSGYHPQTNGTVERFNRTFMSMLRKYIQGKTTKWDEFVDQALFACRVIDTIAHAIAGVEGVALLDVDPGLSTNRTVYTFVGHPQAVIEAALAAARAAYNLIDMSKHSGEHPRIGAMDVVPFVPVQNATMEDCVEIAKEFGERLGSELNVPVYLYAEAQDKEYRRDLSQIRDGEYEGLYHKIRKSEWKPDYGPDEFIANWGATCCGARKFLIGYNVNILGTKEQAHRIALNPGKLMCVRGLGWWLEEANLAQVSLNLTDFEVTNIHQAYEQCLLDAQTLNIAVCGSQIVGLIPLRPLLMAADYFIKQQNLFILDEDQKIRLVIQQLGLNSITPFNPKERIIEYIIQAREGNDDDNLVSMELKDFIRHVGSRTIVPGGGSVTALIATLGTSLGSMCSLLTYGMRKWESLEKDMRIIIPPLHSATKTLMNYIDNDTEAFNAYLTVQKMAETNEEEKRFKQITQNRCLERCIEMPLAIARHINELWPVLKKLAPLFNISTKADFFVCIKCMETAVFGCYKNIEVNVVNFPQNDEYILKAAQLKQEGTQMWKTAQKEAQELIAVVEARIE | Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; L-glutamate from N-formimidoyl-L-glutamate (transferase route): step 1/1.
Function: Binds and promotes bundling of vimentin filaments originating from the Golgi.
EC: 2.1.2.5
Subcellular Location: Cytoplasm
Sequence Length: 822
Sequence Mass (Da): 93726
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A0A0N4XSW5 | MPLSLWTVFFHCGLAALFVLYLVFWIQLNMFETLKYLAIIGGFTYLAGNRVLKAIAEKRK | Pathway: Protein modification; protein glycosylation.
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 60
Sequence Mass (Da): 6941
Location Topology: Multi-pass membrane protein
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A0A814IYU8 | MPSIAHHQSTPMSAPSPTQITTAPHYHHYQEYFCCSQCTHDFDCELRKPITLVCGHTICQLCSRQFTNKCPIIVSKQQHQQPCNSSTGDIEHLYINYPILKLLMGNTKIPQNIDMRYQNCPMYIELDEKSKSSFMSTQQLLEDIILLLKPIGKEFVCPLNRAIVRKLFSLVNCSYLEVDGRIRALRQARNLGERIINDFLLHHQNPQQLTATLWSAVRARGCQFLGPAMQEEVLKLILLALMDGSALSRKVLVLFVVQKLAPQYPRASKTSVGHVVQLLYRASCFKVQKREDESSLMQLKTEYRTYEKLRGEHDSQIIAIAQEQGLRISPEQWSSLLYGDTQHKRQLELVIEKLVTPDSFDKCIKELLTVLARGGDPYHLQRLIPDFELLEKIPFELQSTSTSPTRHFDSISPTPDSNDTTDKKRELNTSWQFLCLVLKSSRTILQALIDFNDSTKQHHQQQQQQSSSSSLATSPLGGCGSDSLYGTGPSCSSGVSSSTTAVSKYKVSMCRDFTQKGSCPRNLHCTFAHSKQEMDKFRARNRRTCPQLQTQPTTTTIKQQLLPSPTPVQQYQSSLPLAPQVLTTTNPLNGLKPWPRTVQIQPQTDNFLAQQQQHYHHHHYHHLQQLPLAQTLQAPPMMVPTATSSTQIVAEAAQALINQAHVQAYYQSHHSTVQQQQNPHVLTVQMPPQSHQHQPMAS | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Cytoplasm
Sequence Length: 698
Sequence Mass (Da): 79120
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A0A5S6QYG6 | MEYSFSREVNGRNFRSSEAVKAGLPSKAQYYVNGDIFDASLLKCIDLRKAKCNIRQVENVCQPGDGLVMRPLHITDVNKGYLKLLSQLTEVGDVSHDDFVEKFRLIQNRTDSYYILVIEDTYMKIIVGTCSLVVEHKFIHSCGLRGRLEDLVVLREYRSRQLGKLLLESLRQLAKHLRCYKVSLECKDHLVPYYEQFGFQKEEGNSNFLVQRFPSIA | Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Length: 217
Sequence Mass (Da): 25078
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A0A0N4XKB0 | MLREMGGDAVGMSTCPEVIVAAQCGIKVFGFSVITNMANTDIDDAVVVSHEQILKVATEASPLVVRFVKDIVNELPRL | Pathway: Purine metabolism; purine nucleoside salvage.
EC: 2.4.2.1
Catalytic Activity: 2'-deoxyguanosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + guanine
Sequence Length: 78
Sequence Mass (Da): 8361
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A0A432G355 | MTPNWAVAAGTPELQGQARALARRADFPLLALDTEEVPFLLVLTPERLELRRTGVGAPGPLYADFVGGAMRRRLRTMGKRSPLGRALGFSRQPPEQVVDATAGLGQDGFVIAALGCRITLVERQLPFFLLVENALQRAALDPSLAPIVQRITLVHADARRWLTDLPQEELPDVIHLDPMYPARKKSALSGKAMQLAQQLAGKDEDTGELLQVALTSARRRVVVKRPTRAAPIAARQPDFAITGKKTRYDIYLAHEQQ | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.242
Subcellular Location: Cytoplasm
Sequence Length: 257
Sequence Mass (Da): 28249
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A0A2E6M2I7 | MARVITLKHNKSFHPRNKHIQGYDFQKLCFSTPELKKFLTKSPQGTDTINFARPEAVRALNKALLKSEYNIENWTIPDEQLCPPIPSRVDYIHHIADLIGHKQDVRLLDIGTGANGIYALIAAAEYGWHAVGVDINQGSLQNLQTIIDHNPQLQELVTLKHQTDKHAHFTNIIQPEDTFTITVCNPPFHSSADEALKANQRKNKNLGLKQQKEFNFGGIDPELWCKGGEALFLKKMVKDSVKFAQHCHWFTTLVSKQENLAPLEKQIKKAGASDIKVIDMKHGQKKTRILAWTFENY | Function: Specifically methylates the adenine in position 1618 of 23S rRNA.
Catalytic Activity: adenosine(1618) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(1618) in 23S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.181
Subcellular Location: Cytoplasm
Sequence Length: 297
Sequence Mass (Da): 33778
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A0A348RYP1 | MPEKKRDDRKADGDRKNDPTVSQTLAEWFYRILLNLGLVISAPYYFRRMQRRGGWKDRVGQRFGKYDADFIKHCSKGKRIWIHAVSVGEVHLSLELVKRLKARLGDCKIIVSATTTTGMAEWRKKLPPDIKTCFYPIDRRPWVRSAMDVIRPEAIILAEAEIWPNFFWEARQRNIPTFLINARISEKSFGRYQQLAFLFRPLFQSLAQVGTQNKSDADRLASLGCRQDRVQVTGNMKFDAALSGTRKPTLDVHQLFHESGITDNALILMGSSTHPGEEAILGKIYSELKPVHPRLKLVLVPRHFEKARAAGDTLKAASLKVCYRSEWKPGTDLSKNDDDACLIVDSTGELSSFYAHVDLVFIGKSLTAKGGQSPIEAAAAGTAMIMGPNMQNFRAITRTLLSNKAAFQVPDANGLKDAVSKLLKDSDARSSIGSQAKQVVQQNLGAVDRSLEMLVSHPSLSRLSEAP | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+)
EC: 2.4.99.12
Subcellular Location: Cell membrane
Sequence Length: 467
Sequence Mass (Da): 52180
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A0A496WUY1 | MELNSSTFILEIINFLILVWILKRFFYKPVLDVIARRKADIEETVAKAQTLQSDAENLEHQYESRLADWEQEKKVAQRKLADEIQQQREQQLAALESDLDVEREKEGVLIQRKLENERQQIVETALVQGAQFASHLVSNVAGPELEQGLVKLLLDELKKLPADQRDQLSAANGKKTGTSADKVTVTSAYPLDQTTRQTLERVCSESLSTHGPFHYQQDPALLAGLRINLGSWVLATNLQDELKGFTEIKQKSFAEFEQQGFTSFKHDR | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
Subcellular Location: Cell membrane
Sequence Length: 268
Sequence Mass (Da): 30506
Location Topology: Single-pass membrane protein
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A0A813SNP6 | MGVSSVGRLSILLIIFGNAIRYLAIKQLGNYFTVKLHIQNNQELIINGLFSYVRHPSYTGVIMSFIGLAFLLNNNYGTFAIILPVISVFLYRIYVEEKVLKAYFGSQYEKYQERVPMLIPRLW | Catalytic Activity: [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.100
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 123
Sequence Mass (Da): 14215
Location Topology: Multi-pass membrane protein
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A0A818DL29 | MGFILISMENVNQFIIHLLYLYHVKKGSSECDTYITEKYWIQGLTGHAVPIDLGATKEHYKRIAVPNSYIHVDDFQTVEDLAKELHRLNRNDSGYSKYISNQYSPLSFMNMHSTLCLLDHYRYLHFMKENNQEINYPLRTIRKIFRITNMHLPNSNRTAAKKNLIRI | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 167
Sequence Mass (Da): 19754
Location Topology: Single-pass type II membrane protein
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A0A818HKA5 | MTEKLTQRRRQNDNKHPSNLNNDQINEKVVAVTKKRKPTRNNASPKESFLLKIKSPIRLSIFLIMSIVVLFYLCKILIGFVSTEHTNVPINLPKLVNINEATPDRFWGTYRSNLYFGLKHQSSKSLSVGFMWFDYGTLQRSNDRFLRHGCDQNDQLKYGWTYHDGERFGIEDIKDNNLDLNIQWIKQLSGQHGGDWTTRINVTPKSVGSTIPISLFFYFHHEHPWIKEVKSISKQSPDTVTIRGQTNELDKFSIKIHLNTLSQQPVVRTLTDVFRLDTIHRDILTKLTSNPPKQPFFILADQTLKDSEPNTFFIQITLRQPVADEAFSFDIIYQSESSDREREQDLTGLYFNDELVRLQKQFDQRFETIFQLKTKQNMDETKINFARSTLSNLIGGISYFTGQSLVAKPGQKTPDQYFTTSLYTAVPSRSFFPRGFLWDEGFHNLLIARWNQNITIDILKHWFDMLNDNGWIPREIILGDEARARVPSEFVIQHTNNANPPTFFLTIDYLLKTNQANHLFTLPFIQRLEKWYQWYNRTQVGPTPFTFRWRGRNASSIYELNPKTLTSGLDDYPRASHPTDSERHLDLRCWMTLASSIIGKLYSILNNEKTNQYLAYAQLLSNNDLLDQLHWSDEYEMYADYGLHTDYVQLERVPIPKKSPSQQYQQTHIIRQVTKDSDVNFKYVKHFGYVSLFPLMTRVLNPHSNKLDKILNDLKNSTLLWTPYGLRSLARSSSLYGMRNTEHDPPYWRGAIWINMNYMVLSALQHYAKISGPYSDKAQDIYKQLRTNLLKNMLRVYEKTGHVWEQYDDKTGNGKGSHPFTGWSSLIVLIMSELESSAKKFFNQDVPLKRFTK | Function: Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor.
Catalytic Activity: H2O + N(4)-(alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein]
EC: 3.2.1.106
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 853
Sequence Mass (Da): 99676
Location Topology: Single-pass type II membrane protein
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A0A6C0W1E2 | MGRIPLSILTNKPNKLKIETTSEMKGTKQAQREDPSSSLFSKLNEKGGKNEKKEQKNGYIFSRLAVEDFSKSLVTLIFDHNRWNQRKRPFRYIKKKRSEGSVRNEMTQHFFDIPKSKTNVKKRISFTYPPSLFIFLERITKRFLLTLTKTSLFYTHSLYPKNPQSNNTNIEFRTRIETLEKKFPFIDIIDILETRIRLCTDGTYNNYFSKMYDPLLNSPYFFKLKKKPLPNNLKTYKENLRETVGINQIHDILFTFTYSDSEKIELKEDAAQYDNKLSISSKNLLLLTGEFDTEPTHNLNFNPCLLSDQKEVKIDFEKEREFFNFFFKTVPNHPNLNKIIKESSGLKEIRKRVPRQPYELITEFQQKSGEYPNRRSQIRSRKAKFVVILTPIKENTITNSNKDANKKKKDLKKRIVLVRYYQQSDFRRGIIKGSSRAQRRKISMWEPFQANVHSPLFLDIIKKSPWFSFDRSRLIKVIFPNWIHNRIDFKIFENTDEETKKEHKKETDKKEENRRQEQTRADIAEAWNSIPIARKTRSLMLIIQSNLRKYILLPSLIIAKNIGRMVLLQIPEWFEDLQEWNRELHIKCTYNGIQLSETEFPKNWLREGMQIKILFPFCLKPWHKSKLRPSRRNLMQNKKERNDFCFLTVWGLETDLPFGSPRQRSSFFKPIFKELETKIGKSKNTYFLVRKTLKGKTKLVSKQIKNWVIQNSFFIEKKIKIFSKLNPILFFSVSKVYKSNQMKNNKDSTSINEIIPESLISQIQSSNRTMTEKKNKNLTARAITIRNQIERMTKDKKKHTRIYISANKRIYKDKRLEFSNFIFERIYIESYISANNKNL | Function: Involved in protein precursor import into chloroplasts. May be part of an intermediate translocation complex acting as a protein-conducting channel at the inner envelope.
Subcellular Location: Membrane
Sequence Length: 839
Sequence Mass (Da): 99994
Location Topology: Multi-pass membrane protein
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A0A0F7YVQ6 | MKPVHPSNFENPLGVEMCKNRGVRGIVACDPRGVIGLEGKLPWHYPEDLQFFSETIQKFPIVMGRKTWETLPRKYFVDRAVVVFSHEKRQGVHGEIWVTSLEEFLLLDLSSPTFLIGGGELYSLFLENQIVRDFFISHIKKEYAGDTFFPLSLLETWTKTVLRDTQKITTCYYENHHSQNTKNISL | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Length: 186
Sequence Mass (Da): 21553
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A0A967TDA5 | MTERQSEFKVLVTRPRHQGESLCAEIERIGARAINFPLIEIVPLTENRETVRHLSENPDCDLLIFISQNAVAHAVEMLGGDISRIAELPIYAVGQATARMLHQAGIKQVHAPVTGSDSESLLELPGLQANQINAKKIMIIRGYGGREHLADTLRERGAEVNYVEVYHRKPAVYDQAMLEKIFGVDRPDLIVITSGESLQILFDMLISGGKHDMLATPLVLLGKRMSELADSLGFSGKRLIADEANDTGLTAAVKKLMELIRNE | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Length: 263
Sequence Mass (Da): 29028
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A0A2E6M2V4 | MTDSLYHPSRFCTAPMIDWTDRHCRYFFRLFSKEMQIYTEMVTCGAILHGDTDRFLGYSDEEQPLVLQLGGSNPADLGRCAKIAADRGYSEINLNLGCPSPRVQKGAFGACLMAEKQLVVDCVKAMQDASDVPVSIKCRLGIDNLDSDEFLLDFLSALDDIECHHWVIHARIALLQGLSPKENRTVPPLNYDRVYLAKETFPHARIILNGGLMGVDQSLNDLKNLDGVMLGRAAYQNTQVLLDVDQKVFDKETAIKTPFDVAEEYADYIKTLNPREQKVAIRHTLGLFNGLRGAKPWRRYLSEGLSNGEEPLALWDEGLRKIKHLNETTLIESDDPS | Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U20 and U20a in tRNAs.
EC: 1.3.1.91
Catalytic Activity: 5,6-dihydrouridine(20) in tRNA + NAD(+) = H(+) + NADH + uridine(20) in tRNA
Sequence Length: 337
Sequence Mass (Da): 37923
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A0A813R8Y8 | MPLYEVYSHPERCRYKARIFSSSILFLIVVAVLTFLSPILVAYFTGGFWWKELNYSEQPRITYTNKYILSIQNAMGNGARSFSSSYISLNAAFSSILLYANQKSVANDTDSDGIIDQYKIDFIVPLAGAYKIGNIDAWLFFDYELRGRQSVVMETLALISLVPPKSVYSNNVTVYGQLVFEQRKPIQSSGVDSSLNTSILTYDNGAVPVLNTILDNYFTRNYYTTFQQQYASWSCNISNSFTLSVVINVKQQSIRFIPGFWQEFKWGWIQYLAVLLPFIFLFSRLTEFVFKNQLVKTIIYSTHHRQRA | Function: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling.
Subcellular Location: Cell projection
Sequence Length: 308
Sequence Mass (Da): 35453
Location Topology: Multi-pass membrane protein
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A0A183B218 | MDLVFKLNNHSLMGKFLRLVFQPITYPILGAVVKLAVWRHNLKVIGKDRLMEAYKARPSRTPLITISNHHSCLDDFILFGTLLSLIDLMHVDRYRWSLTAVDVCFTNARDSFFFTWGHGIPVWRGVYQPSMTFCLDLLNRGKWIHVYPQVSTVCGFAIPIFYIDKVKPIKKYSYTRIAESKDKTNDDVLFELSSEAMCSGFSRNRARLGTTEERWALLRWYQIEEKGTLSDRRVVNAKCLKNVDYGRS | Catalytic Activity: 1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-phospho]-glycerol + a 1,2-diacyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-3-phosphocholine + a cardiolipin
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 248
Sequence Mass (Da): 28812
Location Topology: Peripheral membrane protein
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A0A815D255 | MNNNKLSEITSSNTKSHLFNDPYSNKINKEDFTLIWLDKTLDKDINDSRQISKLRQAVDDLKTYVDLNECENYIRSHEHENIVIVVSGTYGQHIVPNIHDLTQIKRIYVFCLNEASHIEWTKNYMKVNNNIFTQTEKLLESLKPYIRQYQQTLLIQKSIVDVENKTADFKWARLLIDTLIQLPPEPKAKLEMIETLRKHYHDNETQRKIIDEFDKNEKDESAVTWYTKETCIYKIVNRIFRQEQIDEIYNYRAFIKDLAEQLNQLYTDQLTLYRDEWGLSEITVYRGAGVGNHDIEVLKSNTGQLISFNGFLSTSPDEKLALSFLHGQFGSTDLTPVLFTYKIDINVNTTAFAEITEISAMNEGREVLFNPGAIFKIDHVKYDHTDKMWRVRLSSREKDFMVGQHYIKICMLERSSMNNLPLFASLLLEAGQIHKAEIFIARHFSENKPIDKETAESSNETLFLLGQLLREKGDYIGALDTYNKALDIWKETLPENHPDIAKSYNNIGLVYHKKGDYDNALDYYSKALHIWKETLPEKHSNIAKSYLNIGLVYHNKGDYDNALDYYSKALHICKETLPEKHPAIAKTYNNIGIVYHNKGDYDNAHDYCNKALDICKETLPEKHPDIATTYNNIGSIYQNKGDYDNAHHYCNKAVDIWKETLPENHPHIATSYNNIGSVYRDKRDYDNALDYFQKALDIWRETLPQKHLDIATSYNNIASVYRDKGDYDNALDHLQKALDNRKQTVPEKLADIAKSYNDIGSVYEDKRDYDTALDYFQKALDIWKETLPEKHPDIARSYSTVGLTYQNKGDCDNALDYLQKALDIWKETLPERHPRIAKCYNSIGLAYHIKCDYDNAHDY | Catalytic Activity: L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide
EC: 2.4.2.31
Subcellular Location: Cytoplasm
Sequence Length: 859
Sequence Mass (Da): 100038
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A0A8S2ECS6 | MMNMKVRRLVFRLVVIIPFIWLIIILALLQTGDNNKNTINENQRVHRAGRDADNIDAFGGADIKIRKPNIDKLLNNFNNQSVSSVLNDNIRVIHDKHEQVAAPQIDKHDINGPGEMGKPFEVDKEKLSPEERQKYDKGFQENAFNQYISDMISIHRSLPDVRDPGKMQYLDNLPSASVVMCFHNEAWNVLLRSIHSIIDRTQPNLLKEIILVDDFSDMDHLRKPLDDYVAPLKKVFIVRQQKREGLIRSRLAGAKTVKGDVIVFLDSHIEATEDPIARNKSTVVTPVIDVIDDTTFKYNYGAVTSLSVGGFDWNLQFNWHAVPESERKRRKHELDPVRTPTMAGGLFAISRIYFEESGTYDAGMDIWGMLFNTILIIWMCGGELVTAPCSHVGHIFRKRSPYKWLPGVNVVKKNAVRVAEVWLDEYKKYYYERFNYDLGDYGDVSNRKLLRQKLECKSFKWYLDNIFPEQFIPGDAVASGDIRNAAAAFCVDGSTDHKNYHKPVIGYSCHSQGGNQFFMLSKLGEIRRDDGCLDFSGGVHEVGKDDKIIVYPCHGMKGNQHWAYKENGHIFHQVSSLCLALSTDNKHIQMEKCDESNLRLKCFLFQDKMSLDDDLTTIYKQQYFTTQLPSTFLAWNLNNNKNHDDFMKKILLLQRLIRRHYIRKQFDHVQDEYLKTLNDIENVFVSSFPSYMKPKDDITSNHTSKNEVIIKPIPMISSIIQKTTTTKELPPVETVTSIVCPISSLSGKIVNNRHQQLESPVVRNEETKHTGIDQHDSIDFENQLNDMDDTKRLTRNELLRKRESLAIELVWIEQAIKSRKDYLKLKTRYTSVNS | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 834
Sequence Mass (Da): 96136
Location Topology: Single-pass type II membrane protein
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A0A846Q7V2 | MDRVSGLLNNGIIRKIAFLVNQRSTRYRKVALIGAKVPEKSILKAVSTINSRKVVAHNYLRNHERYNVWFTFKAETLDELYEGVEELMAKAEIRDFVVLPSKRVYKISYIKYDLENGVPRCPTRIEPVSVPTLEELGVDVSLALSLAMGIKAEKNPLGSLARRHGIGEGELLDLLHELAHKGVIRDWGAVLDGGRLGFVVNAMVVLRLPVERVVDICLEIVKRFEEVSHCVEREVAPGRWEYPAYFVTHARERKTIDLFVERVRDALRLEECLPLYSVANLRKARPIVM | Pathway: Porphyrin-containing compound metabolism.
EC: 4.1.1.111
Catalytic Activity: 2 H(+) + siroheme = 12,18-didecarboxysiroheme + 2 CO2
Sequence Length: 289
Sequence Mass (Da): 32911
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A0A936US01 | MSAHLPPPHTHDALPLTTAQQTGRRHWLRALRTFWPCVALTLAGWLGWRELSGLDLHALHGITRDLSDLDLIGLQVLAVLAVLVMCGYDLLLSRWLAIGLPSRQVLRYAWPACTLANLVGLSGMAGSGVRYLALSREGVGGRTIAIYAGVQLLAVPVGLGGLCAVMLAIALQQATTLPHGLPQLALAAFAVYVPAFFLLTGSGALHRRFFHELPPLTAGLRLKLIAISCAEWALALVVLGAALALAGVRPEPEELLFAFALAATAGIASQVPGGLGVMDGTLLVILGRLGYAQEGVLAGVLLFRLSYYLVPALLGLAIGARLFVPDENLFVRVLRRAEAHPLFGVLRLPVELIGALSVRLLGYLTFLAGVVLLVSAAYPTLSERSALLHDYLPHTVLEGSHLLSVVAGVVLLSLSRGIAGEVRRAYQLTLLALLAGALLSLVKGLDYEEAIYLLALAALLGTRRERFDRHAYPLLSRRNLLWLAALAAALGGYAWLGAALYGDEAWAASLLHVAPGAHAPRFARSLLAVVVTGIGMLGWLAFSMPKPRLLRPDAAALEQARTFYADHGGHEFAHLTLLGDKYLFYTRDRDALIAFGAIRNRLVALGDPAGAPSAVEGAVLAFRQFADRYGCVPVFYEVSETNLHLYHDHGFGLFKLGEQALVPLADFSLRGKKRDDLRSAVNRAARDGLEFCMLEHPLPEAVWAELQGISEQWLGKKTAEKGFSLGRFERAYLSQTPIAVVRRAGTIVAFASLMPDYRQRQELSIDLMRHGTAAPPGCMDFLFVRLMEYARDAGYARFNLGIAPLAGVGENEYARPAERFARLAYEYGNRFYNYKGLRRYKEKFQPEWRGAYLAYPYQMSPRLLLLDISALIAGGYRRVFSRN | Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys)
EC: 2.3.2.3
Subcellular Location: Membrane
Sequence Length: 883
Sequence Mass (Da): 96164
Location Topology: Multi-pass membrane protein
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A0A0N4Y8H8 | MKFILNGGELTIGTLDGANVETAEKMGRENIFSFGVNVGEVEQLQKRGYNAEDYIRKSLALEQAIEQIDAARSAKMVLMTLMNIASTGEFGTDPTIFGYAREIWGIAPGETSPPATYDHPDGVESSR | 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 = [(1->4)-alpha-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate
Sequence Length: 127
Sequence Mass (Da): 13819
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A0A183AKH1 | MAKMVEENSVLVQKRIKSWLLLKEKQRGYQAVARHYKHALNRMFLQLNHSALIIVEDDLDVASDFFQYFAGTLPLLMANQNLFCVSAWNDNGRPDLIDLKRSDLLYRTDFFAGLGWMLLRSFWLEIHAGWPDIFWDEYLRKPYVRKNRACLRPEVGRTTTFGRMGISRGQFFDKYLSTMRLNHDWQNFVQMNLTYLHEPGDLPNISTTPTERIRVTYHSQADFDRIAIKLNLMRDIKSGVMRNAFAGVVPTKWKDQWIYINKVFSANPVSTIDNRRNKITKGIICEQQLDESTVIEVIFWFRMRDQIANK | Cofactor: The cofactor is mostly bound to the substrate.
Pathway: Protein modification; protein glycosylation.
Function: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
EC: 2.4.1.101
Subcellular Location: Golgi apparatus membrane
Catalytic Activity: N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP
Sequence Length: 310
Sequence Mass (Da): 36554
Location Topology: Single-pass type II membrane protein
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A0A814TF08 | MDSNINKNARRIDIHHHIVPDFYAKAIEENGAYSNKWPVPTWSVEQAKEHMSILGIETAIVSVPTPGAKIYEDNKEKRRILVRKLNEFMGDLVKNNPKEFGFFASLPSLTDVEGTLNEINYVHSTLKPDGYLLFTSYGNGQYLGHPSFKAIWTKLNELKAAVFIHPCEASTTVAIEYLPPPLLDFPHETTRTASDIVLSGTRAACPDIKIILSHAGGTLPFLARRITMAGAIPSLHCPRQPEQILSDFRSFYYDTALSSSVPQLQALLHFADPSKIIFGSDIPYAPLSVTLDYSKSLDTFFLNQFQNFSQAINRENAKKLFPDKFTD | Pathway: Secondary metabolite metabolism; quinolate metabolism.
Function: Converts alpha-amino-beta-carboxymuconate-epsilon-semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS).
EC: 4.1.1.45
Catalytic Activity: 2-amino-3-carboxymuconate 6-semialdehyde + H(+) = 2-aminomuconate 6-semialdehyde + CO2
Sequence Length: 327
Sequence Mass (Da): 36664
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A0A661C4N9 | MHEVDRKIINHLQDNFPVCERPFARLAEQLNMEEKELLKRVQSLLDDGTLSRFGPMYNIEMLGGVYCLVAMSIPEQDLEQVVKKINTYPEVAHNYEREHEFNVWFVLAAENEMQLKNILKDIEKQTGYPTYEMPKLDEYFVGLKFDA | Pathway: Porphyrin-containing compound metabolism.
EC: 4.1.1.111
Catalytic Activity: 2 H(+) + siroheme = 12,18-didecarboxysiroheme + 2 CO2
Sequence Length: 147
Sequence Mass (Da): 17316
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A0A183TMU8 | MPYSRQEYKLKAQTRVSPMFLLLREAAPKSSAPQRVLQRLKHVRGILLYGPPGTGKTLMARQIGNMLNAREPKIVNGPSILDKYVGESEANIRKLFADAEEEEKRMGPHSALHIIIFDEIDAICKTRGSVASGASVHDTVVNQLLTKLDGVDQLNNILVIGMTNRRDMIDEALLRPGRLELSLEISLPDEDGRLQILSIHTSKMAAAKKLSPDVNLKELAARTKNFSGAEIEGLCRAAAFTAMYQLVRPSGKEKIDPNAIDNLVVKRADFMYALENDIKPVCPSDPVLLDLNQLSGRLCA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
EC: 3.6.4.6
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 300
Sequence Mass (Da): 33119
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A0A814UL92 | MAFLVIVVVFYITVPAFFTGNYEEYTNNVCWVRNTYYVDENSQIPDDSQTRHDNSIRYYQWIPFILLVQAFFFFLPYVLWRALSQRSGVDVRDIVEAAALYKKSSDEKARDRLMRFIISAIDQYVDDPRRQSESRIDNPFTKVLLILCPPVGRYMGDYLRNLFLFIKVIYLLNVLVQIALLSVLLGHPFYSLGFEVLKILYEGKGWDYTSRYFPKVTFCIHCDKEHNDRLLRILSRDESTIDPTYIPNDGKKIHHYSRLYPVPERFLVNKLTLFDYFNDEYLEADGVFILRIIGTNASDFVSTRIIHELYERCCAKRFTPNPVSRQRETAKTTLYKYVIVPKVSADEKENHTDTNPFHKRDVNSFNFTSNDHKKIGDIEEEQEETHHEQQQQQQQQQQQAPETKRRTLRNTTNISESGSDRMRSGTLPFIHSPKESSQE | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 439
Sequence Mass (Da): 51740
Location Topology: Multi-pass membrane protein
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A0A3L7Q6A9 | MSARVALLGSGAFAIPSFSALAATRGLEVPLVITQPDRPAGRGRVLEPTPVGAWAAREGLCVVKPEDINAPEWVELLVRERIDALAVIAFGQKLSPAVLDGRVACNLHGSLLPRWRGAAPIQRSVMAGDDEVGVTVISIASRMDAGLVYARVATTIGASETSGDLHDRLAQLGVPAMVEVVRGLLDGTARGTTQDESLATRARKLARADAWVDLRGSARDVCARINGLSPWPGTDCMITGEGHEPMPIKLLRCRAVDASLPVGSVATSGVVGCGEGAIDVLEAQLPGGKPMQLVDLMRGRRWSRATLASEPHAPAAH | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Length: 317
Sequence Mass (Da): 33211
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A0A1B0GK16 | MRLTSYKSILRDRRVFVDFLAILFGIGSWIGINSTFVQFPLLVASAPERWDLPSFIVVIIQLGNLGPLAYTLIQKYSPKKILDAHVIYGILGIGCMAALAMCFVYDITAYVAGMQRSVWLFVVVFFLALVGCSSSVLFMPYMGRFREIYLITYLIGEGLSGFLPSTLALIQGVGGNDQCVLRNTTDGGQEYELYTPPPRFGTAQFFAFVTTFMVVSLGAFVLLENLSVCKKEYAAVKIDRGNKYTYDESSKINESGEQLTLQEDSGFTNLSVTTYRALLVLMGIICMFGNGIFPSIQSYSCLPYGNIAYHLTVTLSSIANPLACFLAVFLPHTSIRMISILSSIATAIGVYAVATAVMSPSPPLLGNIGGEILVVLSWTVLNGLISYMKLSITTIFRQQGGKSLVWVGGVSQIGSFSGAILAFVLINNAELFTSYTPTCPATP | Function: Plasma membrane transporter mediating the uptake by cells of the water soluble vitamin B2/riboflavin that plays a key role in biochemical oxidation-reduction reactions of the carbohydrate, lipid, and amino acid metabolism.
Catalytic Activity: riboflavin(in) = riboflavin(out)
Subcellular Location: Cell membrane
Sequence Length: 443
Sequence Mass (Da): 48233
Location Topology: Multi-pass membrane protein
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A0A183B2C7 | MKINFISKKDPSDITIFSLTTKFSPLTSPTLYCIIRFISFVFEKSHQIGYYLDEEHEWGLNVDQLEATLKEHSKNCFPRALVVINPGNPTGQVLPEKVIKRVLEFAHRHSLVVLADEVYQHNIYTPDRKFVSFKRALHDIGGAIAKEVQLASFIKHERCRKMVKGMCIEPLKGLFSFECTYLFNEHRIHFLDVFIFQHEETNLFL | Pathway: Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.
EC: 2.6.1.2
Catalytic Activity: 2-oxoglutarate + L-alanine = L-glutamate + pyruvate
Sequence Length: 205
Sequence Mass (Da): 23905
|
A0A2P2ICL3 | MRSMLFQRAIVLVALSIAMVVIVGITFDMTNYNISSSPVRSDNSSQYLDIVNENVNRLMITMNEKMHDETLEQLVRLIVELGHIERPFIMQLLKETLNNKDVDVQLMLAELQDFRKRNETKGIPKIVLSIKTALKYNDTWQNYSLPVLVARSLGGVGNVMGQYATVFTLSRIFNMTGLMATGLRGNLVRFYDHLSMDPIDVGPTRNLTLNGWVRVFKDHNTAPSTYNALQFAAAGLLGPKRFITTFCPIEVQLFGRFQDELRKEFTFNDYLLDKANTVLGGFASMAVIKRKDGPPTYIGVHVRLQDYVSHAKVRWGVRNIRYKYKPYLRRAMQYYKDRYKNTVFVMASDDPEYVEIFLKEEGERNGFLTHGTQGEDMSLLTRCNHSIITLGTFSFWTGFLKPSGKTVYPDVKGWRARTYHFARKTIEDAEVQNFIPLEF | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 439
Sequence Mass (Da): 50463
Location Topology: Single-pass type II membrane protein
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A0A814WZQ3 | MGNTFRISISKCPPITQRKRLSPASLQVPSAIPHWNADVKLDKEETQREVSHDSFWVNRTISNTQFDENDTEKELHHGVIQHTPEIHSLGWARIACYVLVAIMNLSAWIDMQGLFVELPLIVPFTPERWTLPSTAAMCVCAANIVPAVVIVLRWRQGKKFSEIPYIYMIIIVGIVACFIVALSWQQTIFLFGRQRSVWLLASIFILSMLDCTSSLVFFDYMKRLRAQYLSAVFLGEALTSVIPTLLVLAQGVGGETICINTSNSTIPEARFTQPRFSVRIFMLCIAGIITASLIAFVLLRWTNVIALADAAQMDDSIYDSQIKIIFNQTKNNLDTWKEKWLKASFIIKQLDQAFIELMEFIKSGFEIMSTVFRQVTVKINKFGQIIETIQCENTDLKSKVKKCEENELKRTKKKQIREQRLLIRDLFVTARQRLTQEQLI | Catalytic Activity: riboflavin(in) = riboflavin(out)
Subcellular Location: Cell membrane
Sequence Length: 440
Sequence Mass (Da): 50375
Location Topology: Multi-pass membrane protein
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A0A8S2HDV1 | MSSKFTLVNSPIFYNEDYNNYAIFNAVDMDTSPMIQVEIRNSHGVFLFQTLINTRVSPKTVGLNDRQQKRYKLKLYHKYSVQIHVHQHNLLTIINQKFNVDKTVGGYNHVFERIFGNILLSRLYPQNFIRKTGMKHSRGILLSGPPGTGKTLIARTICEVLRVKPKIVNGPETYNHLLRESEAKIRHLFDESEFDAEKYGANSDLHIIMVQNCEEQAQDPEAPPLTRALARAQQLYNIAILNFGVADLRSITRLLRCSLSGTYKVDRQTLVVLGGAVIYVAMPCDAIPDFIPVLGYLDDAYILRQAITTCLSEIRRFQQWEEEQQRNK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
EC: 3.6.4.6
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 328
Sequence Mass (Da): 37633
Location Topology: Multi-pass membrane protein
|
A0A2N7W466 | MNQIDLNSDLGEGFGVYKLGDDEAMLDIVSSANIACGFHAGDPDVMHKTVVAAMKRGVDIGAHPGFNDIWGFGRRTIVGDSMRTIENLIAYQIGALQAIARAAGANVSHFKVHGALGNLMFTDREISDAVVRAVKAVDRELLFVVPPNTEGESAAERGGLNLVREVFADRAYTDEGHLVSRRLPGAVIHDAELAAQRVIDMIDHKCVTSISGKKVAVKLDTVTVHGDTEGAVTMAKIVRSRLVENGIVVQPVSRTFAR | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
EC: 3.5.2.9
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Length: 258
Sequence Mass (Da): 27684
|
A0A814NI28 | MMGSETVEKADLRIRKDYRFDAVECQNPYEFTIDQWKKVFNEEKRPKWVLINSPPLFDQPQTISTFDQYRQHILDKTLDYAKELKISKVHLVMNDVSNSSQIPSVVNLLKLAAQYFAPHNIMCLIEPLSTRSDYYLRSYYLAADIVREAKQSNLKVMLDSFHLQRLHGNLTENIELLAPFVGHVQISQTPLRDCPMNNGEVNHKYFLQKIATFYHDYIGLEYICVNFALIIDILGTMFVYMKLLKFK | Function: Catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde).
EC: 5.3.1.22
Catalytic Activity: 3-hydroxypyruvate = 2-hydroxy-3-oxopropanoate
Sequence Length: 247
Sequence Mass (Da): 28970
|
A0A0N4XSY2 | MLLLLLFHYVVCVTTYKILVFSPTISRSHMISNGRIADELAKAGHDVVLFEPDFLNISAAVMSSKIARRWTVYGFAPALRNVLQGFSETAFEQFSLLEEHRGLLLYSRAYNELCEDLINRDELIDALRAEKFDGYFGEQINLCGNGLAHVLGIKSHFWVSSCPIGDHMAWILGMPQPSSFIPSLIAMDITHRPSYIERVQNVWATFLPNFPSLEDIAADSDMVFVSTDEFIEFPRPSLPNIVHIGGLGLGTSKETSPLNKVFAEQMEMGANGVIYFSLGTLVNTSSLPAFAMEAVIETARRTPDHHFILVADRHDQKCLSVISDKLNHFQHTRQLAEHLKNVFVCSWAPQPAILGEPMASFLQLPNLQYRTCRFVKK | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 377
Sequence Mass (Da): 42377
Location Topology: Single-pass membrane protein
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A8BD08 | TLYFLFGMWASMLGSSLSWIIRIELGLPGSFINDDQTYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSITLLCMSSVVESGAGTG | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 109
Sequence Mass (Da): 12005
Location Topology: Multi-pass membrane protein
|
A0A183AF88 | MWSSLCVAIFILPFLSECLTESKGPKVTHKVYFDIESGGKPLGRIEIGLFGGTVEKTVKNFVALFGEKVMGYKGSKFHRVIKDFMIQGGDFTNGDGTGGMSIYGEKFKDENFKLAHYGAGWVSMANAGPDTNGSQFFITTTKTSXDGKHVVFGKVLSGMVILFTFY | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 166
Sequence Mass (Da): 18150
|
A0A0N4XGQ5 | MMLITSFFCALLVSVYSVEIDPKGYIIFCPCMGRYGNQVDQLLGVMRFSKELDRTLVLPNFIEYPFPNTVMVPFESVFSVTEIEKYMKVIKMVTFIRDVMPVIWPPERRTAICRTPRMSIYDENAPTGCHPKEGNPFGPYWDKVGISFVDDAYFGDLPGGYDLTVSGSKAAWLERFPSSIYPVLAFPSPPAPSPSRSTTWELQRYLKWSTRILEKAGQFMRTNLVRPFVGIHLRSDNGWVSCSLY | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.221
Catalytic Activity: GDP-beta-L-fucose + L-seryl-[protein] = 3-O-(alpha-L-fucosyl)-L-seryl-[protein] + GDP + H(+)
Sequence Length: 245
Sequence Mass (Da): 28006
|
A0A946DCF6 | MLITCIDVVGRYVFNSPFTGSTELTEMAVGIVIFSILPIISWRNDHVVVDLLDQFVSPRVHMIRNMILNILISIALTFVGYRIMVLGERSLSYEEVTEYLEIPTGWMMYFIGIACWITAVMVITLGIYRSYREYRLTIVSISQAD | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 145
Sequence Mass (Da): 16625
Location Topology: Multi-pass membrane protein
|
A0A2D7I724 | MKLAYEQAEISELNGEVPVGALFFDEGQVIAVSGNVSIANHDPSGHAEIDVLRKAAKIKKNHRTGGTLVVTLEPCVMCMGAIIQARVDRLIFGAYDPRSGAAGSAFDLSNSSKLNHKVNVIGGVMDKECKALMQNFFKSRRKN | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).
EC: 3.5.4.33
Catalytic Activity: adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+)
Sequence Length: 143
Sequence Mass (Da): 15432
|
A0A813VCK2 | MLFGRPIYTIVMNKRRTTYDEHFRNNHHSSNNNNNDDDDDHHRHYNRNSIENRRNNSEDQIKINDIHSSRDQKRGVVLDIDMRDADSAETMLDDDVTYEKEVDMSELWVEQGIHTIEYFLSCISHTASYLRLWALSLAHAQLSEVLWHMVLYNGLVMPGFIGSVATYVVFIPWAVLTVFILLLMEGLSAFLHALRLHWVEFQSKFYKGEGYPFVPFSFRLMEDQLTD | Function: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Subcellular Location: Membrane
Sequence Length: 227
Sequence Mass (Da): 26705
Location Topology: Multi-pass membrane protein
|
A0A946QAJ3 | MVRVALLGPRGSGKEEYAEQLAERFGLPMISIGALLKLEVDSGSSLGVDILKGQKGKRPVHDDLIMQVLQTRLREEDVAAGFVLEGGPRTDAQAKGIDAFLLRHGAAFAGVVLLKYDYDEFMEAMTGQRSCRECGSQFNIYTNPPVVERICDACGGRLHSRVDDREEKISRRLRDYESIEAPLAKYYEGRLKIVQGGFEQSRVFKMVAQAAEQLKKAAPEFQVSSIQKEEEVVMAKAEKKKKKAAPKKKAVAKKKVAPKKAVAKKAATPKKSAPGKKAAPKKAVVKKKVAAKKAAPKKAVAKKKVAAKKAAPKKAAVKKKVPAKKAAPKKAAVKKKVAAKKAAPKKAAVKKKAAAKKAAPKKAAVKKAAAKKAAPKKAAVKKKVAAKKAAPKKAAVKKKVAAKKAAPKKAAVKKKVAAKKAAPKKAAVKKKAAAKKAAPKKAVVKKKAAPKKAALKKKVAVKKAPVKVKRAAPKKKAKR | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence Length: 479
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Sequence Mass (Da): 51106
|
A0A0N4YVK1 | MRNREPFSLFIPLNVWNFILATFSIMGMIKLTPEFWNTLFDKGFQNSYCYAYDFTKGENGYWVFLFIVSKLFELLDTVYHHILTGIYAFYSHPHTPGFNRYGIYLNYTVHAFMYSYYFLRSMKISVPGIVAKFITTLQILQFVISCAILAHIGYLVHIAGVKCDFDDNIFVLATFMDTTYLILFINFFLKSYVLRGGKAKYQSIQKSKKSN | Pathway: Lipid metabolism; fatty acid biosynthesis.
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: 211
Sequence Mass (Da): 24711
Location Topology: Multi-pass membrane protein
|
A0A816AXT3 | LQITDFENAALSVFLILLTRTIVTYELNLLIPISKVDENMQNAQKRDAIHTEKFYFRRKISRTGYVGK | 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: 68
Sequence Mass (Da): 7946
|
A0A817VJH9 | MTNWSDYLCFPIPPWLRIVSMTFTISKIWEWFDTAILISKGQSLKKIGFLHIYHHATTFLLFLCVMNFPGGEKSGMLLNGFVHTLMYYHFAFRLPKLLRPIITTLQIIQLITVTYIWHVVPTVCSSYKHFPKRSFLEFLLPYALVPVYSLFFFKFFIEQYLMPSNKKVKASSHKQE | 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: 176
Sequence Mass (Da): 20814
Location Topology: Multi-pass membrane protein
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A0A8S2HZK0 | MGVLWASRVTYLLILILNLSTWIDLLGIWAELPLIIAHLPEDSSSSLIYFDYMKRFRPKYLNAMFFGESLTCFIPTLIAFAQ | Catalytic Activity: riboflavin(in) = riboflavin(out)
Subcellular Location: Cell membrane
Sequence Length: 82
Sequence Mass (Da): 9474
Location Topology: Multi-pass membrane protein
|
A0A158R314 | MVPIYPILKGWKAWLAGASIDPSTVPVPVAHHPLCYDPYYEMISETFKSVMKTPWDIVILDELFASAQGAMAMQLREKYGTKVATFATTEFSSQFSFYRGFSRNPVTTPNYYTKGYDMMSYDVGNFFGRLKTTRDVIYEQLSRFTFTDFPSHYGVASPQGHDLISVGEHCKEMNEPGHHGTVLICSFLALYLASPLNLMMRIVEAKPLADELRTFVEDPDSKGTIYIAFGSIVITAFFDVINSIDEYRFIFSYGGAEVKNLKPHVKILRWAPQNDILHHHKTVLFFTHGGLKRFASVRQLRVEVERERECEEREKEKENEKEKVKKQSDEKENEKALAVVLVKEKENMEEKIENEKEEERETEEKQSSEKIQMKEKENLKEGVCSDTAMLFLPFFADQCRNALLAKHHGIAEVIYKKNITKEELRTKMYQVLIDEQYTVRTKKVDVTQRDVVRRRLPSNTVERDEQDELEELGGKEFQEIHMNFEEKPKTAPQGNRENAVAHTLPRRAPSRRAKPAQSKSPRRAPSKKGSLARKRKSSKVKARNIASKKKAGSKSVIETKKVGY | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 564
Sequence Mass (Da): 64860
Location Topology: Single-pass membrane protein
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A0A0X3P611 | MQISRTPASRCVLYIVIIYSLFIFFLLLIKFTPENSPKICKISGSRGHFQRQKALVLPKIFLITATYNRLEQTAELTRLCHTFLHVPNIHWLVIEDATNISSKVSKLLGRCGVPFTLLHAKTPAAEVQRPEEPRWRHARGVAQRNRGLRWLRENLVQNQDKGVVYMADDDNTYSLQLFDEIRTTKRVSTWPVAFVGGLPWEGCVTKPDEPHVIERMWSIFKPWRVFPVDMAGFAVNLDLILSHPTAEFVYHKKPGLLETEFLKQLGLRNFTEMEPKADGCKRVSACHMFTFSSMKN | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP
EC: 2.4.1.135
Subcellular Location: Golgi apparatus membrane
Sequence Length: 296
Sequence Mass (Da): 34113
Location Topology: Single-pass type II membrane protein
|
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