Datasets:
Synthyra
/
TremblNLP

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10
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A0A1Y1S259
MIPLTNYHTHNSLCDGTGELEEYLATARRKGFAALGFTSHAPLPFINDWTLAEADLETYCSRVRELQKNSDPELYLGLEIDYIPGRMGPAEERWKQYRFDYTIGSVHMIPVDGKAWSIDGPDDEFLHLYRNVYNRDGTAMAVEYYRLLEEMIHKGGFTILGHLDLIKKKNLKMHFLNEEAPRYTDAVLRVLDSLADSGIFMEINSGGLFRGATEGVYPSFSILQEARRRGIPLVINSDAHTPEALDFHFNEACDLARKAGYRRTMMLLNGDWREIPLGEA
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9. EC: 3.1.3.15 Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate Sequence Length: 280 Sequence Mass (Da): 31913
A0A6H2FUE7
MKKTNIRQVVLDTETTGMNLSYPYYIGHRIIEIGIIEIINRNITQNYFHTYINPQKIISKEAFSIHGISNKFLSKKPIFSDILDNFLNFIKGAELIIHNAQFDINFLNYELSLLKKKTPKIEDICIITDTLKIARNIFPGKRNSLNSLCNRFNINISKRNLHGALLDAKLLAHIFLFMTTKQNSFQLEFLKEKNSIFKNKIKFLNAKSKIKKTLVINASKKELKLHQLQLNLIKNKYGFSLWENKNK
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease. EC: 2.7.7.7 Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) Sequence Length: 247 Sequence Mass (Da): 28818
A0A9D8KAW3
MRSDLKDKKIGIVGGTFNPIHLGHLRSAEENREAFDLFRVIFVPSAEPPHKAGNIIDAKHRYRMVKRAIAANHSFSASDLEIKRGGKSYTIDTLIHYKELVGETGEIYFIIGLDAFREIGSWMRFRELFEYAHFVVTDRPDAGSKNPKFTIPGEIKSAFKKGAGGRGGFWTHTSGSKLYFQDISALDISSTTVRRLVKEGRSISYLVPESVEKYINKRGLYR
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). EC: 2.7.7.18 Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate Sequence Length: 222 Sequence Mass (Da): 25102
A0A366MJ50
MSGIAGIVDSRGVAYPLYYALHALQHRGQEAAGISTFDGRAFFMHKGPGQLSDVFCEKVLNRLAGNVGVGQVLYTQKAHRGRTENIQPFNFNFKDHQLSITVSVALINREALRSEYESKGHIFSSTTNAELIAAMIAHELIAGVSAEEAFVNTMQRLSGAYAGVAILDGVLYAFRDPIGTKPLCYGRTEFGHVVVSESVALDILSAAFEADVRPGELLTITEDGVSHRQVLESDHKAYCVFEYVYIARPDSVIDGVLVYDARRKIGACLATNPPKADLVSPVPDSGVAFATGYASESGIPYIEGLLKNRYVGRTFIMPTQTLRENAVRIKMNPVRRHIAGKSVILVDDSIVRGTTSLRIVDMVRDFGAEEVHLRVGSPPIVAPCYFGIDLATLGELIAAGLDVESIREKIHATTLQYVSTEDLVASIGIPAEDLCMGCSSGRFPLDIPGECTGCCRKITPVTK
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. Function: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. EC: 2.4.2.14 Catalytic Activity: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine Sequence Length: 463 Sequence Mass (Da): 50127
B1H0L1
MDNKIKTALTNSDKNNIWHPFTQMADWLNDDPCKPLIIDRAKGSYLYDVDGKKYLDGISSLWVTLLGHKNPRIDKAVKKQIDKVSHTTFLGLTHKPAIDLSEKLLKILPDNLKKIFYSDDGSTAVEIALKMAYQYWQFKNEKRSFFLSLKNAYHGDTIGAVAVGGTDLFHSRFRSLLFKSFFAMSPYCYRCVYRKKEIKFPVTAENFKDHNIQMHCRGQCIKEVESILVKNNKKIAAAVIEPINQAAAGMIIMPKGYLKEYANLCNQYGIPLICDEVATGFGRTGKMFAVEHENIKPDFICLSKGITGGYMPLAVTATTNEIYSAFLGKYEEFKTFFHGHSYTANPLACTAANAVIDTLNQNKILQKLQSKIKHLEKELTSLLEHYRVGNIRHCGVMAGIEIVEDKKTGKPYDSKLKTGAKICANLRKHGIIIRNLGNTLVLFLHLTMTNRETSKIISAIKIELDNL
Pathway: Cofactor biosynthesis; biotin biosynthesis; 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1. Function: Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to utilize SAM as an amino donor. Catalytic Activity: (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine = (7R,8S)-7,8-diammoniononanoate + S-adenosyl-4-methylsulfanyl-2-oxobutanoate EC: 2.6.1.62 Subcellular Location: Cytoplasm Sequence Length: 467 Sequence Mass (Da): 52732
A0A357LBR4
IAAQLAFPNLFYFPDLPWTSFGRLRPLHTSAVIFAFGGNVLIATSFYVVQRTCRARLWGGLAPWFVFLGYNLFIVIAATGYLMGVTQSREYAEPEWYADLWLTIVWVVYLLVFLGTLLKRKEPHIYVANWFYLAFIVTIAMLHVVNNLAMPVSLTSTRSYSLFAGVQDALTQWWYGHNAVGFFLTAGFLGIMYYFIPKRAERPVYSYRLSIVHFWSLIFIYIWAGPHHLHYTALPEWAQTLGMTFSIMLWMPSWGGMVNGLMTLSGAWDKLRTDPVLRMMVVSVAFYGMSTFEGPLMSIRAVNSLSHYTDWTIGHVHSGALGWVGYVSFGALYCLVPWLWNRERLYSRALVEWHFWISTLGILLYITAMWVSGIMQGLMWRAYNEFGFLEYSFVETVAAMHPYYVIRMLGGVLFLIGALLMAYNLWRTARGDV
Cofactor: Binds 1 copper ion per subunit, denoted as copper B. Pathway: Energy metabolism; oxidative phosphorylation. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O EC: 7.1.1.9 Subcellular Location: Membrane Sequence Length: 433 Sequence Mass (Da): 49810 Location Topology: Multi-pass membrane protein
R5FL66
MNEALFFIEIILTFGCVVAAKKIFGKAGLIAWIAIAMILANLTVVKTIDLFGIEATLGNIMFASTFLAGDMLNENYGRQAAHKGILVGLAGVLVFMVCTQISLLYTPSTSDISQEAMVLLFTLNLRTSIASVAMCVLANWLNVSLYAKIRELTNGKYLWLRNNVTTITCNCIENFLFVLLAFGGIYSMEQILAIALSTCAIEIFLALCDTPFLYLSRGESKLLSKVTASH
Function: Involved in the import of queuosine (Q) precursors, required for Q precursor salvage. Subcellular Location: Cell membrane Sequence Length: 230 Sequence Mass (Da): 25102 Location Topology: Multi-pass membrane protein
A0A1G1LV54
MQLSKLLQNITKEKIPSDVAHYDIRNVCSDSRKVIPNSLFIALKGFSQNGEDFIPDAVKKGAVAVIKSPSGSQSKSLTSRLPKDPNVFILEVEDTNKTLREIAAKFYDHPSSKVRTIGVTGTNGKTTTTFVIESILQKAGQACGVLGTINYRINREVFPAPNTTPDVIGIQQFLYNLMQKNIPYCVMEVSSHGLDQGRVDLIDFKVGLFTNLTSDHLDYHQTTEKYFLAKAKLFQNLSKGSHAIINGDDPLAKQLKAMTKAKVYTFGVSSDSDFKAVDITTDISHTSFQIKCPQGKMINIRSKLIGLHNIYNILGAVAACYAEKIPISSIEKGVEELAMVPGRLEKINCGQDFHVFIDYAHTEDGLKNVLSCLQDIKTRKLIVVFGCGGNRDKTKRPKMGKVASQLAEIVILTSDNPRTEDPQDIIDEIIVGCSKENYAVSAERKEAIYYALHLAQKDDVVLIAGKGHEDYQIFKNQTIHFNDKEVIQEFFAARKLVNKA
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: 500 Sequence Mass (Da): 55480
A0A9D6KDK9
IPIFGLPGNPVSAMVTFDQFVRPALLHAQGGFRWLRPAIYATLTANIQKEPGRSHFVRGHLTIENGEYKVAPTGDQDSSNLVSLVKANVFIVLPEACGDLEAGKKVLVQIMTAPLF
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis. Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. EC: 2.10.1.1 Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin Sequence Length: 116 Sequence Mass (Da): 12586
A0A9D8KGZ9
MLATINWLRDFVDIDMDVEKLADLLTMSGLEVDSVTKIGDDLKGIVVAEIMDVSTHPKGGNLYVAKVSNGAETFQVVSAAPNTKVGLKTALAPPGVVLPTGLKIEKRDFKGVESTGVLLAEDEMGLTHDHTGLIELDPKAAPGKSLAETLNLSDYLIDIDLTPNRSDCLSVIGLAREISALTGAPLRLPKTDVKEEGPDINELTSIEVIDKDLCPRYVARVVQDIKIRMVPFWMRLRINQLGMRDINNIVDITNYILMEYGQPLHAFDYDLLSGNRIVVKRAKEGEKFFTLDAVERTLNKDVLMIADAERSVAIGGVMGGANSEIQEDTANVLLESAFFHPPSIHKTARELGLLTDAAFRFERGIDPEGCKTAADRAAALMAEYADGTVAKGYIDVKGDVPKRPTLKIRTSMTNKVIGFKADTKEIRKYLESLFIKVEDESKDELLVTPPSYRLDLEREIDLIEEVARLKGYDNIPETLPNISMDFSKTSEIKTLIDLVSDAVLSEGFNEIITYSFIGSVSFDKMRLSPKDPMRKATPLKNPLSEEMDVMRTTLVPGILQTAETNINYLSYDLRLFEIARVFMPRNSKGGKGEGEGGDNGLPDERFHLSLLISGKRRPKQWGADAPEVDFFDLKGVWEKITDEIGFVSIEYEMNKDVEYLDKTQSCVIRGGGETIGVMGRIDPDVMDNFNISRDTYILEADLNKLIKLDTKVKTFSQVLRYPPVMRDIAIVIADDVNSDRIVKTVEGAAGELVKEVTIFDLYQGEQIERGSKSIALTVKYQSDNRTLTDDEVNKKHGEVLDILKKKLGAQIR
Cofactor: Binds 2 magnesium ions per tetramer. Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe) EC: 6.1.1.20 Subcellular Location: Cytoplasm Sequence Length: 812 Sequence Mass (Da): 90150
A0A969KAZ6
MSIVENKVLAPYTSWRVGGPARFFTEATTTSEVRRALRWSQERTLPVLLLGGGTNLLICDEGFDGLVLRYRARSWALENQGTTGLLSLAAGTPIGHLAWIIGSQGWSNLEWAAGLPGSVGGAIYGNAGCYGGSMAGVLRRAWLLIEDQVQEWSVEHFAYGYRSSVLKQPRRFSSRRSEEGEGAPASDPDRTCPRPGAVMPAVILSAELVLKRQDAGSVEETMKAIIANRKERTPVGHSCGSVFKNPPGSQVTAGQLLDQAGLKGTRIGAAEISQRHANYLLNLGGARSDDILRLIELARNTVLRQFGIALELEIQVVGPVRP
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis. Function: Cell wall formation. Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine EC: 1.3.1.98 Subcellular Location: Cytoplasm Sequence Length: 322 Sequence Mass (Da): 34760
A0A366MDC6
MDDRSLLASIRHLIGEEETADDCAAFDLGDGRILVSSTDMLHETTDFPKGMTEFEKGWMSAAVTLSDIASCGAQPVQLLVAVGLDDPSRLVPFMEGAVSCAERFGAKVAGGDIDSHTELTVVTTGFGIVEKAHYCRRSGASPGDVVCITGTPGLAMAALEGDERYRKNLLNPGPQVDAGQKIAAVGASSMMDVSDGLAISLYDMAEASGVGFALDSAKFNLPDVRPGSAREYYLYGGGDFGLLFCISRERLPALDAEYTVIGTVVEENGVWYDGNVAEKRGYAHSW
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1. Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1. EC: 2.7.4.16 Catalytic Activity: ATP + thiamine phosphate = ADP + thiamine diphosphate Sequence Length: 286 Sequence Mass (Da): 30336
A0A671S4P0
MAPFHAVKCCQRGLSWIPVIFINLVVCWSYYAYVVELCIYTISNTEEQVIYLLVFHVFFFMFIWSYWKTIISKPASPSKEFCLPKVDKELYEKEENPEAQQEILKRVARNVFIYTCTGSGAIRYCDRCQLIKPDRCHHCSTCDRCVLKMDHHCPWVNNCVGFSNYKLFVLFLAYSMLYCVYIAATVLQYFIKFWTNHLPDTHAKFHVLFLFFVAAMFFISILSLFSYHLWLVGKNRTTIEAFRAPVFRNGPDKNGFTLGFRKNVTQVFGDQKKCWCLPIYSSLGDGYTFPTRLVNADSEQGNAEHQAIKCTVDGQTNPRPLSESQNHLLGNDMHSEEQKDSSPTNIEVCQPVSITMENES
Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] EC: 2.3.1.225 Subcellular Location: Membrane Sequence Length: 360 Domain: The DHHC domain is required for palmitoyltransferase activity. Sequence Mass (Da): 41708 Location Topology: Multi-pass membrane protein
A0A968NBI3
MTDTGVILRAQSGFFWVQTADAVLRCRLRGRLKKDRQSSDIAVIGDQVDVEPTSPNEGAITHVHPRQSSFSRQQPGPRGQWREDVLIANLDQVVLVMACANPDWNARMLDRFLMIAEHNQIAALIVANKTDLLAPAQVAAMVQPYEQIGYPVFATCTPTGAGIASLREHLAGRVSVFTGMSGVGKSSLLNALQPGLQLATGAVSATLNKGRHTTVVAELHALPDLGGGYVADTPGIRELAAWRIPDADVAWCFREMRPFLGQCEFNNCLHTHEPNCAIQAAVATGEISPTRYESYVRILEKQERSG
Cofactor: Binds 1 zinc ion per subunit. Function: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit. EC: 3.6.1.- Subcellular Location: Cytoplasm Sequence Length: 306 Sequence Mass (Da): 33280
F2I4T1
MLLTDSETLSVLKEIMVLFPDAGPSLNFNSVYQLLIAVMLSAQSTDKKVNEVTPDLFKAFPTPKHLAKASPLDIEPFINKLGLYHSKARYLHAMGQQLIDKYSGQVPSQRKDLESLNGVGRKTASVVLSLGFDQPAFAVDTHISRIAKHHHFVDPNATVREVEKRITKVLPASEWKDAHHALIAFGRTICTARNPQCYRYPQLLPHQEKETKRND
Cofactor: Binds 1 [4Fe-4S] cluster. Function: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. EC: 4.2.99.18 Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+) Sequence Length: 215 Sequence Mass (Da): 24167
A0A101SXA9
MSSTSRRRTSHTPHHRTATLALAGVAALIAAAVQAGAASAAPAAAHRAGRIDPAHAALRLTPSQRAELLRHADAGRAATARSLGLGGKEKLVVRDVVKDADGTLHTRYERTYAGLPVLGGDLVVDTTGSGATRRVVRASNAVLDVARLTPAVPRADAGKQAVRRAEALGSTKSAEVSVRKVIWAATGRPVLAYESVVGGLQDDGTPNELHVVTDALTGKKLFEYQGVRTGIGNTQYSGQVTLTTTQSGSTYTLTDGARGGHKTYNLNHGTSGTGTLFSQSSDTWGNGTTSNAATAGADAHYGAQETWDFYKNTFGRSGIKNNGVGAYSRVHYGNSYVNAFWDDSCFCMTYGDGSGNADPLTALDVAGHEMSHGVTSNTAGLDYSGESGGLNEATSDIFGTGVEFYANNASDPGDYLIGEKIDINGDGTPLRYMDKPSKDGGSADSWYSGVGNLDVHYSSGVANHFFYLLSEGSGAKVINGVSYDSPTADGLPVTGIGRDKALQIWYRALTTKFTSTTNYAGARTGTLAAAGELYGTSSAEYKAVQDAWAAVKVGSRSGGGGGGTSYENSTPLSIPDNGPAVTSNITVSGRSGNAPSNLQVSVDITHTWRGDLVIDLVGPSGTAYRLKNFSSSDSADNVNETYTVNASSEPANGTWKLRVQDQATYDTGTLNDWKVTFP
Function: Extracellular zinc metalloprotease. EC: 3.4.24.- Subcellular Location: Secreted Sequence Length: 678 Sequence Mass (Da): 70639
A0A1F7G403
MDILLHTCCGPCLTGSYPLLEAGVGAGKAALFWENPNIHPFIEYQQRLASFKTAADHFKLEVIYGDASYGLEKFLRALDNEFGPARCATCYRLRLEATARAAAKAGIAAFTTTLLISPYQNHELLIKTGQEAAAQNGVSFHYTDFRPGFRGSQATARELELYRQKYCGCVFSEHDRYKNDKKYLNPVGAAGV
Pathway: tRNA modification; tRNA-queuosine biosynthesis. Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr). EC: 1.17.99.6 Catalytic Activity: AH2 + epoxyqueuosine(34) in tRNA = A + H2O + queuosine(34) in tRNA Sequence Length: 192 Sequence Mass (Da): 21254
A0A969FQC5
MMMRGRADVLLLALALDWLVGEPPDTLHPVVWLGRLAAALEQRAPRGSPPRELLYGAGMAAACLGVAALPALLVTALPLPAPLCLLEATLLKTTFSWRTLHHAGERVRQPLVAGNLEEARAGLRGS
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis. Subcellular Location: Cell membrane Sequence Length: 126 Sequence Mass (Da): 13400 Location Topology: Multi-pass membrane protein
A0A2G5IJ77
MLQGSSWQQTSRQATCLGIDVVFVLPFTDLLANTTAEAFASKVIAERLRASVVVVGDNFRFGKGGRGDVDTLKRMGASNGFTVEAVGAVEYDGQTCSSTLVRNHLDIGDRASAEKLLGRPVTWRDACVTPTAAER
Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. EC: 2.7.7.2 Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD Sequence Length: 135 Sequence Mass (Da): 14451
A0A2H1W7H0
GVGLLPYTGHNSSLRAATEKFSKNRKKSSNTLPDTGIEPETSCPAVALAPTQPTRQSTYCLDAQVPDSACTATSYLTGVKTKYGVIGLDGNVTRGSCYSQLHEPNWSESIGQWALEQGLDVGLVTTTRVTHASPAGMYAHTSERNWESDADVPEECLAAGCRDIAYQLVTNSPGRHFKVIMGGGRREFLPNTTNILGSKGRRLDGVDLTDLWHVDKLNMNATHQFVTDRLELLKVFNSDDLPEYLLGLFRDDHMEYHLKAQNQPSLEEMVEVAIKMLSRSSKGYFLFVEGGRIDHAHHDSLAHLALDETVEYSKAVKKARSLTSEEDTLIVVSSDHAHTMTVAGYPSRGNDILGTVDTANGMDGKPYTTISYANGRAKSIGADGRVDVTQDKQFTS
Cofactor: Binds 1 Mg(2+) ion. EC: 3.1.3.1 Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate Sequence Length: 396 Sequence Mass (Da): 43285
A0A671RCF5
MRHQHLLSNYNSHDTRNRTTEANMAAVGRFLKNAWNKEPVITVSCGIGLLACLLPALSPLTKYTGMMNRAIPYNYPVPVRDDGNMPDVPAHPSDPQGKNLDWLKNL
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Subcellular Location: Membrane Sequence Length: 106 Sequence Mass (Da): 11856 Location Topology: Single-pass membrane protein
A0A2T2SGM7
MDDNALPQNGTLQSGSFSENGEGPANNEQIVVGVDIGTTKVCAVVASTDARDRVNILGVGMAESKGSNRGVVVNIDKTVDAVQEAVGEAERAAGISVESVIVGIAGDHVQSFQSRGVITISRRNGEITQDDVQRLLEDTMHVAMPADREILHVVPQEFIVDGQDGVADPVGMSGVRLEANVHIITGLVSAAKNVFRCIEKAGFEVADIVLEPLASSFAVLHDDEQEVGTALIDVGGGTTDVAVFEDNTIRHTAVIAVAGDKVTDDIRKGLGVMREHAERLKRRFGTSLIDYAGEDEMITIPGIGGRSEKSIGRSALAQIIQPRMEEVLEIAQIEIKRSGHARHLAAGAVVTGGGSLIDGTDDLAADVLGMEARVGRPMGLDGGLVEEVSDPKFSTAVGLVLYGMRPEVIGGEPLSDDMGRRAHVDADGGTAPGDTLFARIADRMRAWFDEL
Function: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring. Subcellular Location: Cell membrane Sequence Length: 451 Sequence Mass (Da): 47554 Location Topology: Peripheral membrane protein
A0A1Y4BBF4
MLSLDGWTLFFTVLNVIVLFVGLRLLLFKPVLKIISQREEMIKTQLKEAAAKEQQAEQLKNDYQEKLKDAGHKAEEIIAQAKSRAAREQSEAAVKAKEEAEKMLEKAREEIRTEQEQARKEVQADIAILAMEAARKIMKTGDVHDAAGK
Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). Subcellular Location: Cell membrane Sequence Length: 149 Sequence Mass (Da): 16847 Location Topology: Single-pass membrane protein
A0A366MH62
MKSLLISGDRSGAGKTSITLGLAGLLAKDAVVQTYKVAMDYIDTSYLSGVTGRPSYNLDTFVQTDEELAGLFSYGAKGADIGIVEGVRGLYEGRDSFTDVGSTAAIAKRFSLTTILVVDARSITRSAAALVKGFQAFDPDVRIKGVILNNTGGGHHVTKATEAIEYYCGIPVLGAVPRSPEMDLSMRHLGLVPFVEGMRDPGFAKTIEGIIRHVGAHVDLEAVKAIAEDVTPEPNLVTESLASRPAASRRIAVAFDEAFTFYYGELEAVLRSQGCDVVRFSPLHDTLPEADGYIFGGGYPEMFAEELSKNVPMREAILAKAKAGVPIYAECGGLMYLTRSITLKKGWLGRGEDAVYPMCGVFSGDTVMPAGKTLRYVEGTAVLSGNSYPFKGHEFHYSGVVMDSGTRFVYTLSRGTGIIDGKDGVVFNNTLGSYTHLMPVSAKGILAEIFSAERGKQYIKADSPQTL
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10. Function: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source. EC: 6.3.5.11 Catalytic Activity: 2 ATP + 2 H2O + 2 L-glutamine + Ni-sirohydrochlorin = 2 ADP + 2 H(+) + 2 L-glutamate + Ni-sirohydrochlorin a,c-diamide + 2 phosphate Sequence Length: 467 Domain: Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP, and cobyrinate or Ni-sirohydrochlorin, and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate. Sequence Mass (Da): 49987
A0A671MT42
MSELSSKKQGFKKCRSATFSIDGFSFTIVANETGESSARPLARFARSKSQNALWNAITAGIGIKDKDKRGILIDPRSPEEILADDLPSVDSPDAMEKTAIRLRCLVKQLERGEASVVDLKKNLEYAASVLESVYIEETRRLVDTEDELSDIQSDSVPSEVRDWLASTFTRQMGLMLRRSEEKPRFRSIVHVVQAGIFVERMYRRTSNMVGLSYPPSVITALKHVDTWSFDVFTLNDASGDHALKFIFYELLTRYDIINRFKIPVSALVSFVEALEVGYSKHRNPYHNLIHAADVTQTVHYLVLKTGMVHWLTELEIFAMLFAAAVHDYEHTGTTNNFHIQARSDTAILYNDRAVQENHHVSAAYRLLQEDDEMNILYNLSKDDWRELRALVVEMVLATDMSCHFQQIKAMKNFLQQPEAIDKPKALSLLLHTADISHPAKNWNMHHRWTTSLLEEFFRQGDKEAELGLPFSPLCDRKSTMVAQSQIGFIDFIVEPTFTVLTDMIEKIVTPLIEEASPSGLAGFRRSSLNNIPSDGKRSTVRGTGSEGGTSLNCSVNAVDFKTFKSTWNEEVHKNREKWKAQAAKDLEEKAKQEENEEKDNKTDTDTRQEKDSKTDGEATGDNEEPTEQQPREEEGNKDPGGVNGAQTPASDAKEPETSSDTDNSQRAHNGERQSFQICGFFFLFDFIPILLFLNYF
Cofactor: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions. EC: 3.1.4.- Catalytic Activity: 3',5'-cyclic AMP + H2O = AMP + H(+) Sequence Length: 696 Sequence Mass (Da): 78808
A0A6V7XAF6
MFPDLEYCIPVESSSIHFLKLPDEFYQEILKRISASKSRIVFAALYLGAGQKEQQIVSRLQTACSENVELEISFLLDYFRGTRGEPNDSSTSILKPLLENRNVQVSLFHTPEMRGLLKFLLPGRLNEIIGVQHMKFFIFDDSIIISGANLSDQYFDNRQDRYLVVENCPRLADFFHSISTIMAKHSMQLDKFGKLNFSGSASIHPFTGSNEEIQKSIKTEIFELFDKCKDNVNNLANDTFIYPFLQMGVFDIKQEENIKEINLITAYFNLCDEYADWMLQKRSFLVNIVFGSPRTNGFYGGTGISGSVPLLYLQNSLDFIRKSKEQGFEKSPFTFMEWDRDSWTFHAKGLWIDFLNEKRIGTVIGSSNYGFRSSQRDLEAQVLLVTENDALKQKIIEERQYLLEHAQSIEIDAFFKRDILVSNWVKYFARIFRNFF
Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2. Function: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin. Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+) EC: 2.7.8.5 Subcellular Location: Mitochondrion Sequence Length: 436 Sequence Mass (Da): 50557
A0A2K6QAX3
MFVSRNALIETAIFLFQISDDEPGYDLDLFCIPNHYAEDLERVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLLVKRTPRSVGYKPDFVGFEIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA
Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1. Catalytic Activity: diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine EC: 2.4.2.8 Subcellular Location: Cytoplasm Sequence Length: 226 Sequence Mass (Da): 25663
A0A7S0X5K7
DDVERAPLPSPRTGPDRPGRGSVHGKSPRITRQLVMWLAAARPKTLTAAVVPWLVGSALAAAGGGETQWLHSLAALLAYFFIQIGTNLVNDACDFDRGADTKERTGPIRVTQAGMFTSRTVHAAGVGCFLFAGVAMSPAIFHRGWPLALLLVSSCAAGYAYTGGPYPLGYHGLGDVTVVVFFGIVATGGIRYIHGGGDFLSVPIAVASVQVGL
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis. Subcellular Location: Membrane Sequence Length: 213 Sequence Mass (Da): 22188 Location Topology: Multi-pass membrane protein
A0A6V7W2R1
MINNKKILFFVNNQIIKLINNNNLKFQYKYFSTTNLIKNEVKQNFKENSSLIDSFGRFHNYLRISIVEKCNLRCKYCMPEEGVKLTPSSDLLTKDEIIRLAKLFAFEGVNKIRLTGGEPTIRKDLVEIVSELSKIDGIQEIGITTNGIVLNRMIKPLIDAGLTNLNVSLDSLSAQKYAEITRRDGFQKVWRGLILSEQLMPKGKVKINCVVIRGINEKEVISLVEIGRELSFNIRFIEFMPFAGNNYEMKKFVPYREMLENIGKYYGVENIERLIDGPNETSKSYQVKGFVGKFGFISSMSEHFCGGCNRLRITADGNLKAIN
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis. EC: 4.1.99.22 Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine Sequence Length: 323 Sequence Mass (Da): 36924
A0A4Z2CUY0
MLIRLWDWENNWTCAQVFEGHNHYVMSLAFNPKDNNTFASASLDHTVKVWNLGSGTPNFTLEGHDRGVNCVDYSTSGDKPYLASGSDDRTVKIWDYQTKACVQTLEGHAQNISSVLFHPELPIILTGSEDGTVRFWHANTYRLESTLNYGLERVWTMTCQRGKQIVGIGYDEGTIAISLGRDEPAMSMDASGKLVCARHAELVQANLRSLNFSGEGGEAIQDGERLPIAFKEMGTSDIYPQTIEHNANGRYVVVYGDGEYIVYTAMALRNKTFGQGLEFVWCQSDAGVYAVRESNAVIKVYKQMKEIRTFKLDYGAEQIFGGHLLGVRSLTGLTFYDWLTGRIIRRIDNCPKGVYWSESNQLVALCTNDAFFILRYSADAVPDSSNSSVNNNYEDTDGYEKAFQLVPNGEVNIQVLNGRWFGDAFIFTTQTNRLCYFVGGEVVTLALLDRPMYLLGYLAKENRLFLGDRDLQIVSYTLLLSVLEYETAVLRGDFTSADAILPNIPKDQYIKIAQFLEKQGFRKQAMLVTTDMDHKFELALQLGDFELCQQIAMDGDPKTNENKWKQLAEAACKVCKFKYAEEYLSHTEDYASLMLLATSSGNRKLLEWIGKEAAIKSNDNIAFLARFLVADLEGCLELLTNAKRFPEAAFFARTYLPSYMPEIVEEWRNWLDKSNKASAKIANSLANPKDYPNLFPDLEEALSTEKWLKADRKARLNLPASAYPTQVLPGDRDLHIEMQNEPVPMVEPSLLNKMSHLGLTPTTMDNVSAVTEHQQQPRSNSPSVDQELQFRNNENDSGDSELDSVKLIGDEEEEEEEDENDDVEDVQEDLEAEHEESWYDDDDEDDDEVNNQLRSGTKTALNGKGK
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. Subcellular Location: Cytoplasmic vesicle Sequence Length: 866 Sequence Mass (Da): 97712 Location Topology: Peripheral membrane protein
H3CI64
ALDPGGCLQVSETGKESLPGWLHWNASSGTLLGVPLEEDRGVHHISVSTYSDATSSSSEVFSIEVHPEDVLEPDSSLRASADAQTFLCEGEEPVTVLTVIMDADLNKMSSGQRVALLDNMRKFSGVDLQHMKMLPVVNNRLFDMSAFMAGPGNAKKVVENGVLLSWKLGCSLDQTTVPDISSIQGPAKAGTMSAKLGYPVVGWHVANKKQHLPKRVRRQLSNTPTPVLVVPPPTTVVEPPVRIVPTLSSPSAAAPTETSAPPVRGPVPLPGKPTSRFREPVAHTPTLAPPQPTRVAETTSTLPIQPTMTRPTYVEATATPPTPTPTPTSTSTSTRRTTKKPKRVKTTPAPKETKSSTAKPSRRTTPSPALVPDPYNTKPELRNPIDQVSALVGTYFEVKIPSDTFFDRQDGTTDKLRLTLRQNNNEVVGEGSWIQFNTTSQLLYGLPDAQHAGKHEYFMQATDKGGLNAVDAFEVRVDRWPVNDKTPVVFTARFEGEPRALTNDIHKKILLVKKLAYALGDRNSSTVSLRNVTKGSVVVEWTNTSLPQHPCPRDQLATMSQRLASPDGNPSPDFRFSMEPDFRPLDVKVRGKASCRTYSFIPPGEVDSPEPAAVTPALGTGRQSTDDVYLHTVIPAVVVAAILLIAGVVAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSTVPLILQEEKPPLPPPEYPNMAPPESTPLNQEVLGTYTPLHDEDPNAPPYKPPPPFNTPLEGKGSRPKNMTPYRSPPPYVPP
Function: The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization. Subcellular Location: Cell membrane Sequence Length: 774 Sequence Mass (Da): 84056 Location Topology: Single-pass type I membrane protein
A0A6N4R9C1
MSSGTQSQTTNKLKAPKPAAKVVAPARPSSLLEDYPKLNGLTPAQYIKLQTLCGPRWIDLLFHLPTKMLDRSATPTIAAAPVGETVTLIVQVTRRQPLPPRHIKRPMTIDVTDGSAPLRVMYFNPGYWLERAYPVGETVILSGKIEVDNKGRKLIHPDVWSLPKSEDTASNKINHVARIWPLYPLTAGLGQGWLSRAILTALEVAEDCPLPEWLPASLREQHNLPTFTDALKAAHNPQTEADLQPNSPARTRLALDELYATQLALQHARAANRGQRGIAHGKSDTLTQRLLQSLPFPLTGDQQNALTEIRADLSAPRPMLRLLQGDVGSGKTLVALFALLKVIENGHQGVLMAPTEILAQQLYANAVKYLQPLGITVGLLTGSQTAAQKKRLKDHIRQGFVQLTVGTHALTEDSVVFDKLGLAVIDEQHRFGVKQRVALSANQPLAPDMLIMTATPIPRTLALTAFGDMDTSILAQKPPGRTPITTLVMADDKLAQIAQRLQGVIAKGEQAYWVCPLVEESEESDLSDATSRHKWLKRVYGDKVALLHGKMKPKEKDEIMQAFKRHEYSILVSTTVIEVGVDVPNATVMVIEHAERFGLSQLHQLRGRVGRGALASHCILIYTSPLTPFAQERLQALKDSEDGFYLAEKDLELRGPGEVLGARQSGEMKTRLADLHHHKHLMPVAHQLGATALTRPLNAAQRNALALLLTTFHKETAADWLRGG
Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA). Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate EC: 3.6.4.12 Subcellular Location: Cell inner membrane Sequence Length: 724 Sequence Mass (Da): 79514 Location Topology: Peripheral membrane protein
A0A931FBA7
MADKEILVITGETSGDMHAAKVVARIKELTSGVKFSGLGGRELDYLKLENLLPSEEIKTGSHGFASGITGLFSHIKLAHKITDLVADRDIAVCFLVDYSGFNMYLGRRLRKKLDLPVIHYFPPTAWIWGRWRAKWLASAGVKVAATFPKEADVYREAGAEVKYVGHPLLDEIPESRDQADAREELAELIKLAGRRELQLGERLLAIMPGSRPKEVETHLGPMLAAADQLAHDFALRPVIPVARGIDIEQVEEKIENHRINPVLLSGYSRELLAAADLALVVSGTAVLEAALLGTPQLLIYRADKLTAFLGKYLIGPEYIGLPNILTDQELVPEILQDDVDGAEIAKRAVPYLTDPKVIRKQVEGYNQLRELLGEPGAIDRTARFLLEEAGIFNGE
Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. EC: 2.4.1.182 Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a lipid A disaccharide + H(+) + UDP Sequence Length: 395 Sequence Mass (Da): 43536
A0A0G1WQ52
MALSEKEVIRTAELARITISEDEKKRFGDELTAILDFVRELNEVDTEGVSPMTGGTREENALRPDEPLSDALEGAGADLLNAAPGKKNRYISVPAIFE
Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln). EC: 6.3.5.- Catalytic Activity: ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+) + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate Sequence Length: 98 Sequence Mass (Da): 10704
A0A1W9VM55
MEDFKDKNVTIMGLGLHGGGLATAKFFLAEGANITITDLRTKEILKQTIEQLKGEKINYTLGEHIDSDFTNADIVIKNPGVPKTSKYLKLAKRVESDISIFLQRVNTPIIAITGSKGKSSTVSAIYHVLKKFNPKTRLGGNITVSPLTFINDVDETTPVILELSSWQLADLNGKGCLKPKIAAVTNIMNDHQNAYNSLDEYAEDKAVIFQGVTDYAILNYNDKYRDFFKSRLNIKPLYYSNTEEPSHINGIYLDSANQGWSNIEGKRELLLDPQLTLKGEHQRENLLLAALILSLYGVDKKSIRTGLQEFKGIAHRMELFHEKNGVKYYNDSAATIPEAACAAINSFKTPIHLISGGTDKALEFSSIKNYFSKPKSIYLLAGTGTDKMMEVLNSNNIDYFGPYKSLEKLISELKPNIEPGDSVLFSPGATSFGMFNNEFDRGDQFKAIISKI
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis. Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate EC: 6.3.2.9 Subcellular Location: Cytoplasm Sequence Length: 452 Sequence Mass (Da): 50247
H3CZE8
MAKGKFFYAVKKGLQPGVYTTWDECKSQVDKFPSASFKKFASEREAWAFVRGAEPSAPPGTNKAVESGVGLLPKRGPEALEYIPLGKKRSHSGEDEEEAQAKKVKHSGTSSSESTDGFTYMGDAVVVYTDGCCSANGKVGARAGIGVYWGLNHPLNVAERLPGRQTNQRAEIQAACRALELAKEQNIKKLVLYTDSKFTINGVTCWVKNWKLNNWRLKSGGSVTNKEDFEKLERLNAGLDVVWMHVPGHAGYHGNEQADRLSREGAAKPEVQQGNG
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. EC: 3.1.26.4 Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester. Sequence Length: 276 Sequence Mass (Da): 30178
A0A1V5W8R4
MKFTVKIAVFSLFISACSDKQDRINTNIHHSQITITYLPPVQKKNKLLPFEVLLVNHGFVNMQHIDSSIQCDLRYSTTHNFVGIDMYGDFNACYVPRDIALRLHRVQKQLQAIDSLYSLVILDAVRPLHIQQIMWDSCSYSGRQKKNFLAPPSQTSLHNYGAAVDVTLAYNGSEVDMGTAFDYAGEAAYTYIEQELLTYNKITREQLYNRTLLRSVMKQQGFIENKYEWWHFGACYRSQVAKKYPLVLSFDSIVPNHQF
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): 29923
A0A1V5W610
MNLTSLYAIIVAGGKGMRMQNDIPKQFLILSGKPVLQHSLEAFYRYNNSIQCIVVLPKDQISYWQQLCVDYNCMVPHTIAEGGSERFFSVLHGLQYITSHGFVAIHDGVRPLVSNEIIAQGFAYAQQYLAAIPVIDSVDSLRYVEKNTTYVVNREPIKRVQTPQVFETKTLLHAYTLGYDLHCTDDAAVWEKAGNTVFCYKGDEKNIKITTPLDLCTAELLINM
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). EC: 2.7.7.60 Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate Sequence Length: 224 Sequence Mass (Da): 25257
A0A9D8PNC3
MEIVMPDIQLLALAPEIILIIVAFLMLFFGPLVGGPNTKGGPKVGGIVSLVALTGAFLINLYIGQDEIVTLGGMIVKDAFSLYFNALVIIAAAFSIIISFGYINRFGIKEGEFYLLILFSTVGMMLMGSSADLLSIFIALELMSIPIYVLVGFRKENLRAREASFKYFILGAISSGIFVYGAALVYGSLGTTNLTAMAEALGSNISPVFLLGSAFIISGFLFKISAVPFHMWTPDVYEGANLPITAYMSVGVKAAAFSAFLRFAVVDLANTGDSWVLAIGFVAVATMSLGNTAALAQKNLKRLLAYSSIAHVGYILVALVAGSEYGISSILFYLFIYIVVNLGIFSLLVYFSKDGKECETMDDLAGFGYAHPLMAVCMGIFLFSLAGIPPTGGFMGKLFLFIAAVKGGYVGLVIVAVIASGVSVYYYLKVMMAMFEKGKDKAQKIKNPAAAFVVVLAAIITLYLGVMPGHFMELARICAAALF
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+) EC: 7.1.1.- Subcellular Location: Cell membrane Sequence Length: 483 Sequence Mass (Da): 51535 Location Topology: Multi-pass membrane protein
Q4RQD8
MERFALKQSQLCGSWEMKERLGMGGFGHVYLYQHLESGEKMAVKLCRLELNSKNRERWSREIQIMKKLKHTNVVQAREVPEELTSISINDLPLLAMEYCSRGDLRKVPSGYFIIENHVVVFSEVASLSFVYSFFQILNKPENCCGLKESEVLSLLSDIGSGVQYLHDNKIIHRDIKPENIVLQENDGKLVHKLIDLGYAKDLDQGSLCTSFVGTLQYLVVRETKTQLPLTALRKVWGEAVSYICGLKEDYIRLYSGQRAAILSLLRYNTNLTRYKNLLFSCSQQLRAKLAFFKTSIQQDLEQYSKQSQSGISSEKLLRTWQENQEKVDEFMKVADVVHLDEEIVAVHFEIVELQRSPFARKQVDVMEQLSVSLELMPTCPSTTTDCLSVFPSEEKAIELYKQLKAKCKSPDPPHGYSDSSDMLKIILQMVQNQDRVVKDLYTHLSTILVCKRRIVDLFPKLETAVTDIKSAETGVMQMQMKRQKEFWFLLKIAC
Catalytic Activity: ATP + L-seryl-[I-kappa-B protein] = ADP + H(+) + O-phospho-L-seryl-[I-kappa-B protein] EC: 2.7.11.10 Subcellular Location: Cytoplasm Sequence Length: 494 Sequence Mass (Da): 56797
E1QZZ5
MEELKDIREEIDRIDDGIIDLFMRRMDCAEHVASYKAAHHMPVLDKSRERDLLAKVAERVPHEMRSYIEVLFQLLMEASRNRQDRRLGRQSATADDIERALGAAPELFPARAFVACQGVEGAYQQMAADRIFRHANLAYFDTFDAVFRAVEEGFCRYGVLPIENSTAGSVNQVFDLMMRHNFHIVRTCRLKIDHNLLAKPGTGLEGIHHVYSHEQAINQCGEFISSLRGVQVHACENTAMASRMVAESERSDVAALASRTCAELYGLDVLARSVQDQGNNYTRFACIARDLAIYPGADRSTFMLVVSHEPGALYKILAKFYALDINIIKLESRPIPDRDFEFMFYFDVDCPAAAPEFLTLVRSLDGACEELRYLGSYREVV
Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1. Function: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate. Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O EC: 4.2.1.51 Subcellular Location: Cytoplasm Sequence Length: 381 Sequence Mass (Da): 43161
A0A9D8KDX0
MSVINVAIAGNPNSGKTTIFNALTGSRHMVGNYPGITVEKKEGKIKIEGREVNFIDLPGTYSLTAYSLEELVARNFIVEEKPDMVVDIIDSSNLERSLYLAVQLMEMNVPLILAFNMTDLAELRGIEINVEELSGLLGIPIVKTIGNKKTGLDQLKRTIVMVAEGKIESTPSKIYYEDRVEEEIARLAEIIEKSSLSESGFSPQWLAVKLLEHDTEVEKRLSEDEKWEEIETALEGSRENLLKVLKEDSVNLIAEGRYGFIKGTMKKAVRHIREDHIIVSDKIDKVLLNNLLGIPIFVGVMYIVFQGVFKWAGPFMDLIDAFFGWMGSVAALIIPEGLIQSLVVDGIIGGVGGVLIFLPQILFLFFFIALLEGSGYMARAAFIMDRVMEKFGLNGKAFVPLLSSFACAIPGIMATRTIESEKGRLVTMLLAPLMSCSARLPVYTLMISALIPQKKIFGGLIDAQGFTLFSLYFGGILVAMVMALIFKATILKGESPPLVIELPPYRIPTLKEIFVQMWDRSKHYVQKAGTIILAISIVIWFLFTFPRNPDTKVDYDKLRENRKTEFVQETGFKPGALEEGGDLYDKYLPYAEFDKAVEEGGFEEGDEGYKSAKDTLDKELSVLKAESPDLFDAVSVYREKYLPDIEEIDNKEAMELFSLSYGGKVGRGIEPVFRPLGMDWRLSVAMVASFAAKEVFVAAMGTLYSLGGEVGAESKALIQSVRDDPLFAGRAGILLAIVVMVFSLLSTPCMATVAVVKQESGSWGWAGFLVLYTLVLAWIVCFTIWQGGRLVLEL
Function: Probable transporter of a GTP-driven Fe(2+) uptake system. Subcellular Location: Cell inner membrane Sequence Length: 794 Sequence Mass (Da): 87940 Location Topology: Multi-pass membrane protein
A0A0K8MED0
MRFGALLYRYFFRHSSKNAKLLFVMLFFVTSVFLAVVVDYFFPVDTSRFQDISIVVAAEDKPLAHVFQTKDEKWRLGTSLKDVDSCFIKQILYREDRYFWLHNGINPFSLLRATSQWLINGKVISGGSTLTMQVARLLEPRPRTLSSKFIEIFRSFQLEWHFPKSQLLQMYLTLAPYGGNIEGIQAASWRYFGKSAQHLSPSEAALLIALPQAPRRYYHHSFTLSALQARNRILVQLHEAGFFDKATLMAAQDEPLPGQRFALPRYLPHLAYRLKRLLPQQKKIETTVQISLQNKIQHLASQALNIYPSGVNIAVLVVHHPTHNVLAYLGSIDFFSVPRQGQIDYIRALRSPGSTLKPFIYGLGFEEGIIHPDTLVRDDEKTYGNYKPSNFDKEFHGMVTIENALLLSLNIPVVTTLQSLGPLKFLGILEEVGITPVFPDPLKPPGLSLALGGVGMTLEQLTVLYQSLADRGEIASLRFTHNQPKGEAYQLFLPQTAALLTQILQKSSEIEGDSSLSSISFKTGTSYGHRDAWVVGYNASHVVGIWIGRPDGAPFGTGTGASLAVPLMKQIFQILPAPRFSRKDLFPVKNASFQIREVQKVGFRDPAVSSQAVPLQLLFPIHDTTIEAFAGNSSFGSVSLQAVGGKRPYTWVINQVPYACQVWRPKTVWTPSQKGFYTITLLDAQGQSKSAHVEIN
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis. EC: 2.4.1.129 Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+) Sequence Length: 696 Sequence Mass (Da): 77971
A0A1V5W9B3
MTRYKLAIEYDGSQYKGWQILHNEPTIQGKLIEICSKICKTNTIEVYGAGRTDAGVHALGQVAHVDADTNIPPNEFHNQLQAFLPSNISVRAVEIAHNRFHARHHATYRSYLYCITKERTALFKRYVWWIKNSLNVEQMNIAAQEFKGFHNFKSFGKSSKNEESTMVEISHIHIYEVQNCIWIHIVGSHFLWSMVRRMVGTLAEVGKGTLQPNDIKTFLQESSNFPARHTAPPSGLFLEQVYYSKHIDIQKPQFPFII
Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. EC: 5.4.99.12 Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA Sequence Length: 258 Sequence Mass (Da): 29735
A0A5C7EZ96
MHITFIGGGNMATALIGGLLAKDWSASQIRVVEVDAAARERLTGRFGVATTEAPEVDGSDTVLLAVKPQQMHEVARRLAGRLGSQLVLTIAAGIRLDDLARWLGGYQRLVRCMPNTPALVHCGVTGLYALPQVSREERQRAEAILGAVGRTVWLDREELLDAVTAVSGSGPAYVFYFMEALEEAASSLGLSREQARLLVVETFLGAASLARQSEEPLAALRARVTSKGGTTERAVAVLEEARLRDHIAQAVRAAHARSRELGDEFGKLG
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1. Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH EC: 1.5.1.2 Subcellular Location: Cytoplasm Sequence Length: 269 Sequence Mass (Da): 28836
A0A4S4BPT7
MLWMVTGGVGCGKSVYAERWAASLAREAILLSCPTWPNEREDLVGGRPDESALMEEERVVWMRWKADEKLSDRIDQINLKSNPFRADNRVIVLDSLSGWLRRAVREVRQMTLPPAPAEPPRRGRPKRIPETEDLFALRTDRAGKEFRRVVDALLRYHGRSIVVTEQPAPGLADDPWERWYARELAEANRRLAERSAELRMLVSGVAVEIRGPRMKRGNGNDEDLYSNRR
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: 229 Sequence Mass (Da): 26315
A0A381H8C3
MIYSLATGGTVSIAALFIAGILPGLLLSFTLMVMCVGFAHKARYPKGERVPFRQALKIFVDTLWGLMTVVIIMGGILSGIFTRDGIGGDRLSVGLLRHYVYLPRLQMV
Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system. Subcellular Location: Cell inner membrane Sequence Length: 108 Sequence Mass (Da): 11773 Location Topology: Multi-pass membrane protein
A0A4S4NN58
MSRPLFIVIEGLDGSGKTTQLEMLRDYLQSRGESCRLTAEPTDLPTGRLIRSILQKEISVDPRTLAALFAADRVEHIFHPESGILDLLAAGHHVIASRYYFSSLAYQSEFVDPGWIAALNRQAKTALPADLTIFLDLEPTESMQRIAGRNGEDELYETLEKLTHVRESFLAAFSVFGEGENIQYVDAGQPVVAVADAIIEHVEALR
Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. EC: 2.7.4.9 Catalytic Activity: ATP + dTMP = ADP + dTDP Sequence Length: 206 Sequence Mass (Da): 22842
A0A2H6HXQ1
MNGKNGQTDGNGINGSNGHGIGGGNGHGGSRRALITGVTGQDGSYLAELLLAKDYEVHGLIRRSSTFSTGRIDHIYDDPHRAQVNLKLHYGDLTDSTGLRRIIEEIEPHEVYNLAAQSHVRVSFDQPEYTADVVATGTLRLLEAIRDYMAISNNRPRVYQACSSEMFGSSIPPQNEMTSFHPRSPYAVSKVASYHYAVNYREAYDLFVSNGILFNHESPRRGGTFVTRKITRALTRIKLGLQEKLFLGNLDAKRDWGFAGDYVEAMWRMLQHDRPDDFVVATGETHSVHEFLESAAGVLDMDWRAIVEFDSRYLRPSEVDVLQGDASKIHRELGWKPTVNFERLVRMMVDHDLNLAQREQTLVDAGHVTRMQASGDE
Function: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose. EC: 4.2.1.47 Catalytic Activity: GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O Sequence Length: 377 Sequence Mass (Da): 42265
A0A2H1X0S9
TDIKFFFKILALCHSVQVSNEDMKKLSARLSVTGNMQLMNFFKRKKIKTNNTNGSVVDNVTWNSIINENGNKIDYQASSPDEKALVEVAERFDITFLGEEGNDLVLKVGEHTEMYERLQIIEFTSERKRMSVILRDRDGKIWLYCKGAESSVFPLCTNYSCVQETDRDINIFANKGLRTLAIAYREVPEEEYEKVAEAIKRLDGKSAEALQQVTQQYRTLERNLTLLGATGVEDCLQDNVADTLASLRAAGVKTWVLTGDKVETAINVAQSCAHISENDRRMFMIGIEDSTTLQAHIGECSRIINEPSYRDLTLVVDGTSMTQVLDTAYAPAFVNIAIKCHAVLCCRLSPIQKAKIVKLIKESDERPITAAIGDGANDISMIQEAHVGFGILGREGHQAGRSADFAITKFSMIKKILLVMGHWYNQRLATLIQYFFYKNLVLGNIMFLFQIHTVFSTQSIFDSMYLTFYNLVFTSVPVLLLSVTEQAWSSDVLYKDFYTLLHSV
Catalytic Activity: ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2. EC: 7.6.2.1 Subcellular Location: Membrane Sequence Length: 504 Sequence Mass (Da): 56835 Location Topology: Multi-pass membrane protein
A0A932QW80
MNVADSELIRSILIAKGHQMTSSANDAEVVLMNTCAIRENAHRKIYGRLDILRPLKKQREAEHRPFVVGVLGCMAQNLKEELLMHPVANLVVGPDNYRALPNLIDRIVQTNHHEVEASLSEYETYSDIAPTRIEGVNAWVTIMRGCDNFCAFCVVPYTRGRERSRSIPSILNELEQLVAAGYPQVTLLGQNVNSYCHEGETFADLIVKAAQIPGLKRIRFTSPHPKDFSEKLLYAIAEYPNICNHIHLPLQSGSDRILNLMNRTYTSAEYLGLVKTIRRVIPTTTLTTDMIVGFPTETEKDFQETVQLMDAVQFDNAFIFKYSERKGTIAARDYPDDVAEVDKTNRIVRLNNIQHEIAFAKHRCYSGQTVRVLIEGSADKGINQQMGKTEGNLTVVFPKTAFNPGEFVSVRVTETTTGALYGEVIE
Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. EC: 2.8.4.3 Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine Subcellular Location: Cytoplasm Sequence Length: 426 Sequence Mass (Da): 47847
F9ZAF5
MADTSNKKNIREESLRDLSDFLTAQGEKAFRAKQIWQWIWQRGVTDFAEMSNLSKATRELLSRHYFFDSLFPQQVQTASDGTEKTAWRLTDGEIVESVLIPGNQKFTVCVSSQVGCQLGCKFCATGTLGFKRNLTAGEIFEQVVRAQQAAEAQGQPLSNIVFMGMGEPLLNYEQVLRAIERITAQDGLAMSPYRITVSTAGIPEKIRQLADDGVRFNLALSLHAAKETTRTFLMPVNKAYPLSEIAGSLKYFVEKTGTRPTFEYLLLKDINDSLEDAKALALYCRQFPIKINIIEYNNVEGSGFHHSPDKNRDAFIRFLEGCNMVVNVRRSKGKDIDAACGQLAGKQESNL
Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. EC: 2.1.1.192 Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine Subcellular Location: Cytoplasm Sequence Length: 351 Sequence Mass (Da): 39272
A0PZR1
MSKVKVARFASQVMIITILSKLMGFWRDALIAKEFGTTYETSAYMMSLNVSSILFGLMGLAITTTFIPMLTRSLREKGKDDMYEFGNTVINIIIILTTIIGVLGWKFAPQIVKIVACGYTGEIYDLTVQLTRLSVINVVFIGLTSGYTAILQTMDNFAAPSLVGVAMNICIIIYLLFTKNTTIEGLTIATIIGNGSQILVQIPWLIKNKYKYSCKINFKDPRLKEMMTLILPVLIGIGINQINTLVDNNVASNLNEAAVSVIQYANRLNSLVYGIFATSIITVIYPTLAKYINAGEIKEDFKKYLSKAINNINLIMFPATVGIIVLRTNIISVAFKRGVFDEKSVEATAIALLFLAIGTGVLGIRDIYNRAFYAIQDTKTPMKNSAIGVLTNVVLDITLVKFMGVGGLTLATTISIFVSTVLLALDLRKKIGNIDAVSVLKSGFKILVSSVMMGLVVYIINTNILKYVSGNKGNMLSLMICAVVGSIVYAIAINILKVEEYHDIKKYLLSKIKTK
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis. Function: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane. Subcellular Location: Cell membrane Sequence Length: 515 Sequence Mass (Da): 56524 Location Topology: Multi-pass membrane protein
A0A4R1HAJ2
MSIRAVSFLALALLLATACQPQPEVVYRQQLFAFGTLIDITTQGVDAAQSRAAVQAVDAMYQQQHRDWHAWQRGALDDLNNAIAAGKSWQTDSSIVKLIRMGQNFERLSGGLFNPAIGELLALWGFQQDEPEGPPPSPQRINAWLSHKPSSLQLTIDGNIVSSQNPHVRLDFGGFAKGYSVGKAVELLEGRGIHNLIINAGGDLCLRGNRGGNKPWRIGIRHPRNTGTLATLELQGAACVFTSGDYERYYIYQGRRYHHILDPRSGYPATATRSVTVIADDPALADAAATALLIAGAEHWQSVAVNMGVTDVLRIDDQDVAWVTPRLAKQIVFDPAWKSVRVVSLKH
Cofactor: Magnesium. Can also use manganese. 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. EC: 2.7.1.180 Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+) Subcellular Location: Cell inner membrane Sequence Length: 347 Sequence Mass (Da): 37963 Location Topology: Lipid-anchor
A0A1H4CIQ7
MPKGFSLQELAEYTDSDIRGDAQLRLYSVASIEKAVSGDLSYIRDAKYRHYLQTSEASALILPTDMAQTYQGNCLVNPNPYLAYAKAVTLLYPAVRPAVLIHPSVVIGDGVELGADVVIEAGCVIGDGCVIGDGSWLHANVTLYADTYIGKRCIIHSGAVLGADGFGFAPDQKTWFKIPQVGNVVVGDDVEIGANTTIDRAAMGSTVIGNGVKLDNLIQIGHNTQIGDYTAMAACTAVAGSVQIGRYCQIAGMCAIAGHLSITDHVVVTGTSMVSHSITKPGVYSSGTTIEENAVWRKNAVRFNQLDKLARRLQELEKQLTALQNKGST
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. EC: 2.3.1.191 Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP] Sequence Length: 329 Sequence Mass (Da): 35023
L2GW45
MSSTVYASFVNSILSTLYPILTIYSYYVLVGKYCIDAKRFDSVVVLIMFLIYHVLLIYTLIFYMRILAIDDTSTANRFPSKVANKQAITSRYFNPFIEEEIIQKRLKMLKTCNICVTYKPPRTHHCSICQKCFLRFDHHCGLLGVCIAFHNYKFFYLFVIMNIIYCLFLIILLMFELIKNRQLPTASFSHFIVLTSLLFVEMCVSLQMFIYHTILIRKNETMIENKALNAFLRGDQGVRFVYQEGPLVNEEEVLERDEMNPYNMGVYENWEQIFGKNTWEWFLPTFTTLGDGINFPKKIGRD
Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] EC: 2.3.1.225 Subcellular Location: Membrane Sequence Length: 302 Domain: The DHHC domain is required for palmitoyltransferase activity. Sequence Mass (Da): 35573 Location Topology: Multi-pass membrane protein
A0A6V7V4Z8
MDEKHQQQSPIIMDNLINNNGENSSSKISSPLLDTGQSEDPSICPYCNKKFRKPRVLDCLHSMCEDCIIAQLDDGRNNQQRNSKNILNSFMELELEDSVAGRRPTPPGVICCSVCNQETHIGNDPMFVNLMLLDFVKIREYGFNDANDTGRICEACKSEEKAVANCIHCCSDLCPKCVQVHRDMKMFDGHKVVMFSEKDKLSNQQEGLLKEGGMETIKLALCNKHKGDFELICPSCDELLCKQCAFEHVEHNVSPLNDLVFKWYKQSIHDLAKQAENKGRTTLDARSAIPDRKFLLQQSYHKCRDKIEDAFQFYARVIDEVKLDLLASLDKNRDEKEEHLDSLYQKIDMQTSRLQDALSYTNNLLEKGTIVDLCLNRKKIWQQLKLLMHSMPDVNEEVDLDFDILSQHEFKKKFESVIGGIKCRITGPPKEPAVIMNALLGNSPSNKLDTFDDFDNKLKQQQQLILSSAINNCQSLANNSSIDWTDSSNLFAQHSNTSSIITAAIPTTTTNSGPGTIGMERRQNRNSNGNSYLSGDSGIYSSASDMTISSPIQQHQLGGTPETFNMGRFGIPESFGSAFRAPATTLDSGQQLDPGNLIFSDNYFGNTQSKIWSANYSTTQNMFGNFDASRPRELMDSRFGLNDFPPLGSDPSGFRSRSSLCTTPSIDTFVPSMSIHQNYQPMVAAGRHYGINSQQQIEMQILYTFCSNTLSTQDTFNTPQGLALGLDNEVAISDTNNHRCVIVDVKGNFLRFIGSSGTEEGHVYYPKKVVSLIRNRDCRYIVLDRGTNQQFNRLQLFKNSGEYVCRLSLPCQIDQVSVMTVNKENEQLIIVDNKNLVHAFEFETFNQLTLVRQFSISGNVHEPSDLGVYKGYYYITDYKMHGVVVYTLEGKLHRKFGGLDTTPYPVGIDFSKSGDVLVGDSHGNHFHIVVFNLQGQPLHHYRCYQQKVSRCTGLKINSEGHIVTMSRQNSAVIVFNTLYIPSA
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: 983 Sequence Mass (Da): 110621
A0A9D8KFE6
MSEILKFKSPAKVNYFLKVGEKLPNGYHKIATVMSAIDIYDHITVAFEGSRIEIESDNTKVPQGPSNTVYRAIEALLKEANVDIGIKVNIQKNIPLESGLGGASSNAASVMLKLNDHLNLGLGLDELLTLGVKIGSDVPFFIFGSPALVTGIGENLKKIEGIPETWMVVVKPPGSVSTKLAYKMIDLVLTFNKKSIIIPKFNGTLGGLIEGMVNDFETVVGVEPIVNDKRNDRDRDGGGYSVYLPEVGRIKREIERLGSLKAMLTGSGSSVFGVFGNRIEAKRAFEEIRSKNDWTVFLAQNLFY
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-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+) Sequence Length: 304 Sequence Mass (Da): 33208
A0A951BRS6
MTGSTSRSTRRAPSACSTASWKRRERTGAEASVSGLGPALESVALDVPEAAVPAYEAALRTACGSVGLFRDEASGTWRLEGVKPAGAGEAALAAGLALAAAATGVDARARRGPIAAEGWLARSMAGFPEQTVGRFAIRGSHLPDRPRAGRITLRLDAGVAFGSGEHGSTRGCLLALERVARRRPGRTRVWRILDLGTGSGVLALAAARLLRRPVLAVDVEPWSVRTAAANAGRNGLRPRIRCRLGDGWRDRAVRAGQPYDLVFANILARPLCAMARDLAAGLAPGGRAILAGLLVSQARQVLAAHRRQGLVLEWMVNEGGWTTLVIRRGDAKRRA
Function: Methylates ribosomal protein L11. Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine EC: 2.1.1.- Subcellular Location: Cytoplasm Sequence Length: 335 Sequence Mass (Da): 35275
A0A671Q3P0
KKHLLLSILKTVVVIKNLLQFEDMIKCTVPDSSPLLDFADYGCFCGLGGTGTPVDQLDQLVSFVIFSENVYIIYIYITLFVLNHFVLIIFFL
Cofactor: Binds 1 Ca(2+) ion per subunit. Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+) EC: 3.1.1.4 Subcellular Location: Secreted Sequence Length: 92 Sequence Mass (Da): 10435
A0A0N1CTT3
MIEMKDIMKKYSNGTTAIRNLSISIDQGEFVYVVGPSGAGKSTFIKLMYREEKATKGVLNVAGYDLVGMKSREIPLMRREIGVVFQDYKLLPRKTVFENVAYAMQVIGRKPRDVKKRVMEVLDLVGLKHKVRVFPSELSGGEQQRVSIARAIVNTPKVLIADEPTGNLDPENSWEIMKLLDRINAQGTTVVMATHNSTIVNTIRHRVIAIENGRIIRDQAEGEYGYDD
Function: Part of the ABC transporter FtsEX involved in cellular division. Subcellular Location: Cell membrane Sequence Length: 228 Sequence Mass (Da): 25641 Location Topology: Peripheral membrane protein
A0A1Y1RZY8
MSAIPPERLVFHSLHAAVDWILKHPNAREDLQKAIDKGALSLRQGKLTAFPTETVYGLGADALNRDAVKLIFKAKQRPFYDPLIVHISELQQLDTLVLEFPEKARRLAEAFWPGPLTLVLKKDSRVPDIVTAGHPTVAIRMPSNPWARELIHRAGTPVAAPSANLFGRTSPTTAAHVAEQLSGSYEVLIDAGACRVGLESTVLSLAGERPLLLRSGGVSREQIEEIIGPVEVPAKTRAGDAESPGMLPNHYAPVTPLLMVEDVRDYAENRDIGCILFEKPDIDFQGPTVQVSGNRNADEIAVNIYAALRSLDGKGLRLIVCEWCPESGIGAAVNDRLTKASAKPQG
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. Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate EC: 2.7.7.87 Subcellular Location: Cytoplasm Sequence Length: 346 Sequence Mass (Da): 37499
A0A109ULC2
MQRNQLADAGIGLGETLGQVVALHGPTGNADQGRRLVLNELRLRALDLHDDPALEVLDLRGCGRQHYLHLQLDRLPHLREIYLPCLAEGAILHLFNLDVPASLTVHGRVREIDADWQKGTLRLTHRQRSWEGVQLLGHDAKPDDLVDPPLAFPLNVVLSSELLQAATMDGALCLSGQGEWMDGFQPLRMGQRLWIVPSWHQPPDPDAVNLHLDPGLAFGTGTHPTTALCLEWLDGLSLTGELDERAVLDIGCGSGILAIAALKLGAGQAIGTDIDPQALQASRDNAARNAIADEDLRLCYPEELAESGTATTFPVVIANILAGPLIDMAATVAGHVAPAGRLVLSGILESQAGEVLEAYREQGLVMDEPEIREGWVRLSGQRPI
Function: Methylates ribosomal protein L11. Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine EC: 2.1.1.- Subcellular Location: Cytoplasm Sequence Length: 384 Sequence Mass (Da): 41441
A0A1F3EPK3
MAHSDGDVLLHALCDAMLGAAKMGDIGRHFPDTSSDYKNIDSKILLAQTNELIAAKNYRVGNLDVTVAAQQPKLKPFIPEMEETIARILGIDVDAVSIKATTTEQLGFEGREEGISVHAVVLLETLS
Cofactor: Binds 1 divalent metal cation per subunit. Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). EC: 4.6.1.12 Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP Sequence Length: 127 Sequence Mass (Da): 13690
F9ZC24
MIQETIKNFLQQHHISRDAGFILAVSGGADSICMLHAFKYLNLKMLVLHCNFSLRGKESDMDEQFVKRFCDSYGIAHSVKKFDTLKYARENGLSVEMAARELRYTWFREMKEKKKMDYIVVAHHADDVAETVLINLCRGTGIKGLTGIKSINGDILRPLLPCSRTDILKYIEDHQLGFRTDSTNNSLDYVRNKIRHQIIPVLKEINPSFLDTMTENCETLKETEEIFQYGIHRFQEEILDCEEDELLIHISKTLATPAPYTFLYETLKPFGFNKVQIRDILNTHTAIPGKQFIAGHHTLERGRIFWRLYDNSKCSRTIVSIPTTGIYTIGKLKVEFTLFPRTEEFVIPQQPDIACLDADKLQFPLLIRNWQAGDYFCPIGMKKSKKKLSDFFRDQKFSSKQKQECLLLLSDEKIAWIIGNRPDDRFKITSFTSNILQISIL
Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2) EC: 6.3.4.19 Subcellular Location: Cytoplasm Sequence Length: 441 Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding. Sequence Mass (Da): 51055
A0A0C1S0S2
MNIKIFSGNSVIKLSKNISKHLHTNLGDASVGKFSDGEINVQINESVRGKDVFIIQSTCYPANDHLMELILMIDALYRASSKRITAVIPYFGYARQDRRVGSSKTPITAKIVANILSCVGTSKILTVDLHTDQIQGFFDIPIENISGNDVILKDIESKKLYDPIIVSPDIGGIFRARMVSKLLNNMEIAIIDKIRSRANVSEMVHIIGNVKNRDCIIIDDIVDTGSTLCQAAEILKKNGAYKIFIYVTHPVFSGNSLKNITKSSIDEMVVCDTIPVSEKINGLGKIRSLTLSFMLAESIKKINNEASYCSIKTFNK
Cofactor: Binds 2 Mg(2+) ions per subunit. Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1. Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P). EC: 2.7.6.1 Subcellular Location: Cytoplasm Catalytic Activity: ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+) Sequence Length: 316 Sequence Mass (Da): 34932
A0A101ST62
MSELAVRAEKLDGADELAPLKSRFVLDGAVYLDGNSLGALPAHVPGRVEDVVRRQWGELRIRSWEESGWWTAPERIGDRIAPLVGAAPGQIVVGDSTSVNVFKALVAAVRMADEGRDEILVDATTFPTDGYIAASAARLTGRTLRAVTPAEVPAALGARTAAVLLNHVDYRTGRLHDLPALTAAVHAAGALAVWDLCHSAGALPVGLDEHGVDLAVGCTYKYLNGGPGAPAYLYVRSDLQDRFDSPLPGWNSHADPFGMDPSYAPAPGAPRGRVGTPDILSMLALEAALEVWDGVSVEAVRRKSLALTDFFLECVTACTEPGRVESVTPAAHEERGSQVALRCADAGDVMKRLIDRGVIGDFRHPDVLRFGFTPLYVGFAEVERAARILGEVLG
Pathway: Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. Function: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively. EC: 3.7.1.3 Catalytic Activity: 3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + H(+) + L-alanine Sequence Length: 394 Sequence Mass (Da): 41914
D8IGA2
MNDTSIIVLVQQTLWTFMLLSAPVLGVSIIVGLIISIIQATTSIQEQTLTFVPKMIAMLAVIYFLASWMINYISGFTVRLFNILPTIAR
Function: Role in flagellar biosynthesis. Subcellular Location: Cell membrane Sequence Length: 89 Sequence Mass (Da): 9920 Location Topology: Multi-pass membrane protein
A0A317PNI2
MSTLLLALGLIFVLMALRVPVAVSIGLAAMTATAAELGWRVFPVSAQVMVDGISSFVLIAAPFFMLAGEIMNRGGLTQRIFRLANALVGSLPGGLGQVNVMASMLFAGMTGSAISDAVGLGTMEIRAMKERGYDARLSASITAASSIIGPMIPPSVPIVIYGALAGVSIGSLFLAGLVPGILMGVALMLAILVYDRLGLCPREPRAPGSELRAAALAAVPSLALPVLVVGGIYSGLFTPTEAAVVSSAYAAVLALIYGELRIADFKQIITGVASATGALFLIVATTALLGWIVTRSGVMIEVALWLGGAVDSQTQLLLIVAGLCLVVGLFMEPIAALVLLVPILLPAVKILQIDLVHFGIVLILALMIGLLTPPVGLILFVVARIAEISITQMIRGIAPLLLVLVTVLLLIIVFPTIVMFLPRLAYGLPPFG
Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system. Subcellular Location: Cell inner membrane Sequence Length: 432 Sequence Mass (Da): 44676 Location Topology: Multi-pass membrane protein
A0A2X2WNH6
MVSFRKEMLSNISDLLKHQDAIKFMTEEKKGKVCVFGSFNVDIVSYVARLPHPGETIVSQSCSFGPGGKGANQAIAASNAMCKVDFITKVGNDQLSSHAYSHLEASNIDSLTIYVSDSAPTGNALIYVSELDGENMIAINQGANVTIIDEEIINSHKNILNSNILLVQLENNLSATINAIKYARENDVTVILNPAPFTSDAKIMLPFVDIVTPNQTEATLLSGINITDIETAKKAAERIAQMGPQCVIVTLGNKGALLYDKGQFYMIPAYPAMVVDTTGAGDAFNGALAASLSKGETIKHACHYAAAFSSLAVELNGASNMPEHKNVLIPIERIKLFKNVTREKP
Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate. Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2. Function: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway. EC: 2.7.1.15 Subcellular Location: Cytoplasm Catalytic Activity: ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+) Sequence Length: 345 Sequence Mass (Da): 37106
A0A0X8HCA8
MTRRLLIRATGAARPGQLAGLGQAMARSGARLLDINQSVTFGMVSLEALVGLDRESDLESALSAAGDTLGLEIQAIQVSAEDYQRWSVQASEPRLILTLLAPHLPAGILAEVGALTAEHGLTVELIHRLSGREPLDGGVPRDHHTQGACVECWLRGEEVDLDALREKALALGAMHGVDIAIQEDSIWRRHRRLVCFDMDSTLIKAEVIDELARRHGVYDEVAEITERAMRGELDFQQSFRERMAKLKGLDETVLAEIADTLPMMDGVERLMYHLKRLGYRTVILSGGFTYFARHLQEKLGFDEVHANELLIENGKVTGEVREPILDANRKAALLREIAEREGLTLEQTIAVGDGANDLKMLATAGLGIAFRAKPLVRSQARQSISTLGIDAVLYLMGYRQVDLEDERR
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3. EC: 3.1.3.3 Catalytic Activity: H2O + O-phospho-D-serine = D-serine + phosphate Sequence Length: 408 Sequence Mass (Da): 45026
A3DVI8
WXAGMIGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTIEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINMKPPTLSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPV
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: 206 Sequence Mass (Da): 21856 Location Topology: Multi-pass membrane protein
A0A6N4R9U3
MKFSTGTLVVVGVIVLGLITAVTGGIGVYMAQRGPLEQPVKVIVDQGMGVRAIASRLGQANVIAHPDAFVVMVKATGMAGTLKAGEYAFEPGISLRAVVNKLALGDTENRSVTIPEGWTVKQAIDRLEAVEGLTGHAVRPEEGRIFPDTYAFRFGAERAKVLDTMTARMDKELANAWAARDTTLPLKSPEELLILASIVQKEAANDDEMPMIAAVFYNRLSKGMRLQSDPTVMYGAELEGDRLKRKDLTEPHPFNTYLFAGLPPTPISNPGKSALMAVARPARTEAIFFVADPSLTMHVFSVTYDEHRRNVARYWKDVKKTLQPKSVANVIEGALVTPTNVVSGTAKEN
Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. EC: 4.2.2.- Subcellular Location: Cell inner membrane Sequence Length: 349 Sequence Mass (Da): 37834 Location Topology: Single-pass membrane protein
D8IDD5
MKKVNVCLLGASGAVGKEMLKILQERKFPVNELRLLGNKTAGQKVIFNNKEYTIEKPTKDSFKDMDITLVAVGSDESKKLSPLAAKAGSVVIDNSSAFRMDKNVPLVVPEVNPEDVKLHKGIIANPNCSTIIALVALAPLHKFAKIKRVIASTYQAVSGAGKEGMEELQQQVYDYAEQKKLNIKAFKYQILFNLIPQIDAFDSKTGYTKEELKMTNEGRKILHAPDLQVSCTCVRVPVLRSHSESITIETEKKLTAKKAKELLSKAKGVKVVDNPSQFKYPMPLDTTDQDNIFVGRIREDISAKNSLTFWCAGDQIRKGAATNAVQIAELVLPLLDKESKKEEAPKKRVCKPKKAAAKKEVKKTDK
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. Function: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. EC: 1.2.1.11 Catalytic Activity: L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-L-aspartate + H(+) + NADPH Sequence Length: 366 Sequence Mass (Da): 40523
A0A1W9VIL2
MVLLLAPLLLYLLLKSGKVKLALGYFTQKDLDYAKKCKKDKVLKKKESKRLRKERNVFQNIWFELLDPLFWAIIWVLILNNFIAQLYVIPSSSMVPTFLEKDRVVASKLFSGPGIPLTNYQVPEVSNPKPGDIVTFNNPKVDDSTSDIHYKNVFTRIFQPFVYMLTLTKLDIDADVNGNPKVRQLVKRVIGVPGDKLCMVNDKVYKKVDGGEWFLMSDIPGQKEWGQNALFSLTNKNSMMEIKISFCFGY
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: 250 Sequence Mass (Da): 28696 Location Topology: Single-pass type II membrane protein
A0A8H2QYN3
MKTIGVLFGGKSVEHEVSVITGVQVMENLSKDYCVVPIYVKKDGQWLGGESLKDFKSFKNQDFSQAYPVYFKAGIPSLFHLQRQKGGLLKGDQLVEEERKIDCIINALHGTNGEDGSMQGLLEQWSVAYTGCQVPGSVLGMDKVLMKERFSHCGIQQVAYTWFKARDWKENRDQVMEKIEKIGYPLMVKPSTLGSSIGISKVKEEKDLEAAVDLALSYDKKVVIEHAVDHLRELNISVLGANGSYDLSPIEEPKSINDLLTFDEKYIHSNNKAGGKTSGKGGRNIVVPEEKVLEAIHTMARSAMDAIDGAGVVRIDFMMEGDQVYLNEINTQPGSMAFYLWEEAGLSFKDLLDRIIDIAEEKKRERDQIIYSYESNLFQRSGFGSKL
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: 387 Sequence Mass (Da): 43297
D8I9T8
MSISSKPIAVFDSGFGGISVLKKLLNILPNENYIYLGDNHNIPYGDKSKEEITQLSIKILDFLIKQNCKMAVIACNTITASSYDVLKEKYNIPIIEIISNGVEDIIDNTKNNNISIMATEFTVHSNMYHDKILDYNDKIKVTQVACQKLCPMIENNWYSYDDRILVLEEYVKKIDDNSDTLLLACTHYPFIIDDIKSVVNRKKTNIKNIIDPSTKIALSIKKYLIDNNLLNTSGGKLKFFTTGDKKDFNDFVSRYIKINYELERIVL
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis. Function: Provides the (R)-glutamate required for cell wall biosynthesis. EC: 5.1.1.3 Catalytic Activity: L-glutamate = D-glutamate Sequence Length: 267 Sequence Mass (Da): 30558
A0A0N1LZ49
MKQSKLLIPTLRETPSDAETLSHQLLVRAGYIRQAASGIYVYLPLAQRVLEKIKTVIREELAAIDAIEMAMPALLPFEPWVASGRAERYGRALYHLEDRNAREMVLGPTHEEPFMELIKNEVTSYKKLPLNLFQIQNKYRDEQRPRFGLIRSREFLMQDGYSFHADAESLDTTYRQYEAAYHAIFRRCGIDYRTVLGDNGVMGGHDSKEFLALSGIGEELLCYSTESDYVANWKLATSLYASKKSHETFLPLDTIQGNKEWSIDEAAEAAEIDDSKIVKSHVFLVDEQLVMVLIRGDHTINETKVKLFLSGEQITPLSAADVSSIEEVGQVRSPIDLSDAIALYADQHVQDMTNVLVAGQDDGTYVRNANIGRDFQPIAFADFRLVQEGDPSPDGQGVLTFTRGIEIGHIFKLGTKYSEAQQATILNEYGQEISVLMGCYGIGVSRLLATIVEQHGSDNGIDWPQEIAPFDVHIIQTAIEDPYQISLCQEVEAMMTQVGYDVLVDDRNERAGVKFADADLIGCPIRLTIGKKATDGIVEIKIKHSGATIEVRKDEVASTLTILMSDQA
Function: Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS. Catalytic Activity: ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro) EC: 6.1.1.15 Subcellular Location: Cytoplasm Sequence Length: 568 Domain: Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain. Sequence Mass (Da): 63404
D8IAD0
MNNNKKIMLSGIQPTGSLHIGNYLGALKNWADILDDYYGFFCIVDYHAITIEYDVKEMQKRIINAAVEYLASGLDPKKCSIFVQSDVRAHTELAWIFNSIIPVAELERMTQYKDKSRKNVENINAALLTYPSLMAADILLYHPDIVPVGEDQEQHVELTRMIVRKFNNRFGEYFKEPDTYHGKVLRILGLDGVNKMSKSLNNHIALSLTAEETEKLIMQKAMTDTNRKLKTDKGNPDICNVYSYHKIFSSEEEQKEVCEGCKNASIGCVQCKRMLAANINKELAPIRENINKYSNDLDYVYDVLKEGAKNASEVAEKTLYEVRDLMGLNDRKRK
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: 334 Sequence Mass (Da): 38194
A0A4R1HNW4
MVARAETTTSNDGQLPDVDAWLSSVSFGRDESAQQMIRAALDRAQKAHRDQTRASGEPYLVHCLAVAEIVHHLQLDHEAVTAAVLHDVVEDTDVSLDDIREEFGEKVAHLVDGVTKMGRISEIREPLSLQQQLDHGRAENVRKLLLAMAEDVRVVLIKLADRLHNMRTLRHLSEERQKRIARETLDIYSPLANRLGIWQVKWELEDLALRYLDADAYHRIAALLDGRRIDRERHIELVKESLIEEFDRAGIQADVVGRPKHIYSIWRKMRRKNVDFHQIFDVQAVRVLVDTTAECYTVLGIVHGLWRHVPHEFDDYIANPKANNYRSLHTAVIGPEGKPVEVQIRTREMHEHAELGIAAHWRYKEGSRYDEGFEKKIAWLRQLLEWKDEEPSAHEFVDRFKSESVEERVYALTPQGEVIDMPAGATALDFAYHIHTDVGHRCRGVKVNGRIVPLNYVLKNGEQVEVLTARQAHPSRDWLNPHLGYLKTSRARAKVRHWIKLQDREINIAAGRTALERELHRLGLSAKRMAEVAEKLNFSNVDSLMASLGRGDLPYGQVVSVLLDLERTEDEPLTLPTTGRRNEKGTQDGFRILGVGNLLTTTARCCNPVPNDSIVGYITRGRGVTIHRSDCSNVLRLKEEDRDRLIEVEWGALPDRVFPVDIRIQAYDRPGLLRDVTAVLANDRINVTGISTNTDGKELIARMDLHVEVTDIGQLSRILSRIGQLPNIIEVRRKT
Pathway: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step 1/1. Function: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. EC: 3.1.7.2 Catalytic Activity: guanosine 3',5'-bis(diphosphate) + H2O = diphosphate + GDP + H(+) Sequence Length: 735 Sequence Mass (Da): 83754
A0A7J8E4V4
MEPSPATVGSETTRLVSPRDRGNAGGGLRLKSLFTEPLPEEPKSVEMASHHCHRDPLPQGLTPERLRAQRQLCAACAVCCIFMAGEVVGGYLAHSLAIMTDAAHLLADVGSMMGSLFSLWLSTRPATRTMTFGWHRSETLGALASVVSLWMVTGILLYLAFIRLLHSDYHIEGGAMLLTASIAVCANLLMAFVLHQAGPHHSHGSRGAEYAPLEEGPSEPLSLGNTSVRAAFVHVLGDLLQSFGVLAASILIYFKPQCKAADPISTFLFSVCALGSTAPTLRDVLRVLMEGTPRNVGFEPVRDTLLSVPGVRAAHELHLWSLTLTYHVASAHLAIDSTADPEAVLAEATSRLHSRFGFSSSTLQVEQYQPEMAQCQRCQDPPQA
Catalytic Activity: 2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out) Subcellular Location: Membrane Sequence Length: 384 Sequence Mass (Da): 41327 Location Topology: Multi-pass membrane protein
A0A9D8PRS8
MFNETVIRDTRAVVDLDRIRESVSGIRKLVGDGVEIMAVVKADGYGHGAVRVAKKALRSGAESLAVAYPEEGAELRDNGITAPVLVLGLTSPKIKGAMEKVVGCGLTQTVADTELPRALNAATPEGKRVPVHIKVDTGMGRIGIGIEDVIEYILFLKGLKKIEIEGIYTHFPSSDEADKGFTKRQIEAFLRLLKELKGMGIDIPKAHMANSGGILAHPKSHLTSVRAGIMLYGLYPSGEVERSIPLTPAMSFITRVRYLKKVPKGTTISYGRSFVTERETAVATLPVGYADGYLRILSNRRHVLVGGKQAPIIGRVCMDMTMVDVTDISGVEVGDEVVLFGRQGESEIHIDQMAEWLNTINYEVTCIVGKRVPRVYINE
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: 379 Sequence Mass (Da): 41270
F9ZBY2
MIHSIGLTGGIGSGKSTIAGILKQLGYPVYLADPEASRLINRSVEIRNDLTGLFGADLYTPRGMLDKKLLADIIFKNPQALSQVNRIVHPRVIRDFQHWREQQNSPLVFFESAILFEAGLTRHFDFIICVTASEATRLKRVILRDATNEDKVKERMQNQAADTEKCKNSDFIIYNDEDHMVVQQVLDVLNKLNLKIQ
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5. Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+) EC: 2.7.1.24 Subcellular Location: Cytoplasm Sequence Length: 197 Sequence Mass (Da): 22351
A0A968NCZ7
MDCAIPIDSTDSNRPDPLAQIVVVLHRPQAVVNIGATVRAMKNMGVGQLRLVQPVAYTPDQISALAHRSADLLHGTHHYPDLASAIGDAVYVVGTSARQHRDYPVQPDLRRAAHTLLQATQRGTVALVFGTEDNGLQRAELDLCQQVLHIPTDPAYASLNLAQAVLLVLYELRMAAVGMPAPAVPAAPAPTAAELADLEQAWVTALTELDFFETRNPAIPLRRLRRLLHRAQADRREVAMLRAIAHRITRRLRERGQ
Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA. Catalytic Activity: S-adenosyl-L-methionine + uridine(32) in tRNA = 2'-O-methyluridine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine EC: 2.1.1.200 Subcellular Location: Cytoplasm Sequence Length: 257 Sequence Mass (Da): 28195
F9ZA27
MNLVIDIGNTRSKYAFFQEDRLIGVNYRLDSILEDIRVWKEKGEKVWIFLTGSGHIDSEMQLAIKEQADYWLEASPALEVPLKIGYATPETLGFDRIAICVGAKSYYPGASLLVIDSGTCITYNYVSAEGVFLGGNISPGLEMRFNGLHRFTARLPLVTPTETYGGIGQSTEEAIRNGVMSGMLFEVQQYIECFLGQYPEGHVLITGGNAHFLERHLTPDILFCKYLSFVGLNEILKYVKKSNY
Cofactor: A monovalent cation. Ammonium or potassium. Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. EC: 2.7.1.33 Subcellular Location: Cytoplasm Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+) Sequence Length: 244 Sequence Mass (Da): 27330
A0A931ANW0
MNNKMPEMIQLVIFGGTGDLSRSKLIPGLYKLYKRNSLPDQLSILGLARSFSSRKAYLQSLEQSLKEENPEIYTKESWNNFKEYLDYLQMDFTEDIGYNKLYHHLNDQEGNQAGRHCIYYLATAPEFFPMITENLKEHRLSKSREPGWPRLVIEKPFGYSLSSARDYNSQICQVFPEENVYRIDHYLGKEMIQNILTMRFANMFFEPIWNKHYIDNIQIVSTETSGIKTRGKYYDNAGALRDMVQSHLLQMLALITMESPADMSTESIRQEKIKLLKTLADSPSLGDLRDNLVIGQYKSGIIGDRTVPGYQDEDNIASNSRTETFAAVKLNINNLRWRGVPFYLKTGKRLHKKSAKIYVQFKDDFHPALSKDKNPEANLLIIKIQPEEGVSMQFNAKEPGSQDKITSVFMDFCQQAPDLQNTPEAYEELLLALFKGDQSLFTHWDGVKNSWLYIDKLRDYIEANRLEPEKYNPGSNGPTSSEEMLNRDGRRWWDEEEFNANT
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3. Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone. EC: 1.1.1.49 Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH Sequence Length: 502 Sequence Mass (Da): 58161
A0A2N2KYM3
MPKGRLYLVPTPVGNLGDMTLRAIETLRNVALIAAEDTRTARKLLNHFEIAAPKLISYHKFSEKSRSPEILGVLTRGEDVAIVSDAGSPGISDPAEIIVKDAIARGFEVIALPGATALIPALTASGLPCGAFLFLGFLPTHSRERKDILKQIKDSPVTAILYEAPHRLRTTLTELYKAIGKRKVVIAREISKIYEEYIRGNLDDVLEDYQVTEKGEFVILIEAIAPDSAPDPLALKSLILAELESGKSPSEIVKALSPDYPKNLIYKLILEMKEHKA
Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine EC: 2.1.1.198 Subcellular Location: Cytoplasm Sequence Length: 277 Sequence Mass (Da): 30359
A0A1G1LN04
MSRHKTLHLHSPAKLNLYLRVLNKRKDGYHNIVTLFERIDLFDVLTFRCNAGGGIKIYCDHPDVPKGAKNLVYKAAQMLKKEHRVSAGVDIRIKKQIPVAAGLGGGSSNAATALLALNRLWRLSLTQKELLGYAKRIGADVAFFIHDCRWALGEERGDEIRRIPLKTRLWHILVVPRIKMYTKAVYEAFQPAKTDITYRKSEGYSTGPVPRNLLTNQKQNVNILIRHLRQNDLRGVGQFILNDLESSSFRLCSNLKELKETVLNHAPLGGLLSGSGPSIFGLVKTKKEAEKIRSVLRKKYSQSFVVGSL
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-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+) Sequence Length: 309 Sequence Mass (Da): 34791
F2I8Q2
MAESLTDRFIRYAKVNTRSDMYSETFPSTQSQLDFLEVIAGEMEELGLSQVDFDRQRACVTATLPATTEADLPVIGFVAHVDTADFNAENIQPQVHEDYDGQDLVLNEAEGIVMEVAEFPFLKDYVGQTLITSDGTTLLGADDKAGMVGIIGAMEYLLAHPEIEHGKVRIAFVVDEEIGLLGAYRFDVEGFGADFAYTPDSGRVGKIEGETFNAAQVEVWIEGKSVHPGSSKGNAINPLHLGAQIVNDLPKDQVPEKTDGYEGYFMLTQQNGDLGQVHQVFIIRDHDEAKFQERKEIFAQVVDKINSQYKRPRIRYEISDQYKNIKEVLDHHPYVMERALKAYRDCGIEPDIQPFRGGMDGCVFNFKGLPTANIFTGGENLHGQYEFVSAQGLQALQDVIVAIIKG
Cofactor: Binds 2 Zn(2+) ions per subunit. EC: 3.4.11.4 Catalytic Activity: Release of the N-terminal residue from a tripeptide. Sequence Length: 406 Sequence Mass (Da): 45128
D4G7K8
MQKKLSWKTVGFGKQNIVLIHGFGFNSEVWKNTIHQEDRNFRFHLIDLPGHGCNHQVLIESVDQVIEKIWENSPKRAIWLGWSLGGLIASEIALRYKDQVRALITVSSSLYFIQEKKDHLLWPGITEKSLKNFKNQLSENFEETIRRFLFIQNLGSNLLKKDLKSLKNSILSYPRPNLESLSFWLNVLRKIDLRKVMSKFKKPFLRIYGEFDQIVPKSVIPLINFLIPNSQSVLIKGSSHAPFISHSEIFNKIIFYFYRNHR
Pathway: Cofactor biosynthesis; biotin biosynthesis. Function: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. Catalytic Activity: 6-carboxyhexanoyl-[ACP] methyl ester + H2O = 6-carboxyhexanoyl-[ACP] + H(+) + methanol EC: 3.1.1.85 Subcellular Location: Cytoplasm Sequence Length: 262 Sequence Mass (Da): 30726
A0A0C1RZP5
MNIKQIIQEKIRSIVTFENFCDSVEVRVRFSKNRKTFGDYQIEGLSNILKSNRISLETFKRKLCYLFSKEEYIKSIKIIEPNFINIFLHERWISRQIDTIFSKDRLGISQDNYQKKIVTIIDYSSPNMAKNMHVGHLRSTIIGDTVVRVSKFLGKKVIKANHIGDWGTQFGMIIAYLKEILRKNCVKNITLEKIEDIYQRSRKIFDQNGRFSHISRRYIQQLQSGDDELLTLWNDLVQITILENQRIYDLLGVSLNKGDIVAESFYKDMLQDIVEDLKQKKIAVIHNGAVVVYLDDFKNHHGRSSAVMIQKSDGGYLYATVEIACLKYRCEKLKADRIIYYVDSRQTRHLQQSWAIARKAGYIKKRVKLEHHQIGMILGEDKKPFRTRSGRNIKLFDLLKESITRARKFIVDKNSEHLNKRSISRTARKIGIGSVKYSDLSKNRKTDYVFDWNNVFSFIGNTSSYIQYTYSRTKSLINRSNISPKELKNDFYLSDRYERELSIQLLRLEEVLQDVSKMGLPNILCCYLYELSNIFSKFYEHCAILHSIDDIQKENRIKLVFLTERTIKIGLNLLGIQTVSKM
Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg) EC: 6.1.1.19 Subcellular Location: Cytoplasm Sequence Length: 582 Sequence Mass (Da): 68229
E1QXY9
MAMEPEAWTIRRMLDWTIGYLERRSDGRPRLSAEWMLSNVTGLSRVQLYTSFDRPLSADELARMHDAVVRRGAGEPLQYVTGEMPFRHIVLHCEGGVLIPRPETEVLVDAVLAHVDVAAAAGHDAQVLEVGTGTGCIACSIASERPGSHVVATDLSPAAAALAMRNRDALGLARAVDVITCDLASGVDPALKGTFDVLVSNPPYIPSDVVPTLPREVVGFEPHLALDGGADGLDVFRRLLEVAPDMLRPGGMLACELFETNAEVAAELCRRQGGWARVEVREDLTHRPRVLVAVREGDLAAGGVMVRPRKLLAVDQDRPERMVVRDVARVLLDGGVIVVPTDSVYGIGCAATPGNPGHARTFQIKRRALSQTLPWLIADVQDLERFGHRVPKWAYALAREFWPGALTLVVRASPLVPAEYRRSDDGTIALRLPDSNLVREIAREVGAPLAITSANTHGASSATSGEGIEGRIAGEVDLVLDGGPSPLAAASTIVDCTGADPRVLREGAIPSVGIMRVADPDAWA
Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif. EC: 2.1.1.297 Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine Sequence Length: 524 Sequence Mass (Da): 56087
A0A2H1VBT9
MCEVVFQCSSDTELALELNEPVFLEDDDYATRAPASPTTVPNVRPYRPPSTGSNILKSPRARRVRTTSMSQPNKRTTAESILHADRRTIYTAGRPPWYNCTGGQEVEPFLIGICGASASGKTTVATKIIESLNIPWVTIVSMDSFYKVLNEKQHQAANRNEYNFDHPDAFDIELLISVLQRLREGKKVEVPIYNYVTHSRENRTKTMYGANVIIFEGILAFYNAEVTKMLDMKVFVDTDADIRLARRLRRDIVQRGRDLEGVLKQYMTHVKPAYQSYIAPCMAHADIIVPRGGENKVAIHLIVQHVHKQLQLVSYCNTFWGGGISSNEFSRLGRSECQTLTD
Pathway: Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3. EC: 2.7.1.48 Catalytic Activity: ATP + cytidine = ADP + CMP + H(+) Sequence Length: 342 Sequence Mass (Da): 38662
H3D6L8
MVRRVAVIGAGSSGLACAKACVEEGLEPVCFERGHDIGGLWNFREWSEPGWAGVYRSLVANTSKEMMCFSDFPMPADYPNYPHNSQMLQYLRLYAEFHLLPYIRFQTTVTRVTRRPDFSQSGRWDIETVTSDGEEEKHVFDAVLVCSGQFGYPSSPLEDLPGHQDFPGERLHSRDYRDPEAYRGKRVLVVGIGNSGGDIAVEISRCAEMTFLSTRRGAWVISRMSRQGLPVDISSITRFNQVLMELLPWSLLNGLLERALNQKYDHRLYGLQPHHRFLDRKVLINDELPGQILKGRLSVKADLRAFQGSGVLFEDGSVEENIHAVVFCTGYRSGFSFLPPDLGGGPHGDPALYRRVFPPSLLPPTLAVVGLIQASGPIFPLVEMQGRWAVRVFAGLSFLPPKDRMLEVMEGDRRRNSGRHSCHRTAALTVSYIPYMDFMAEQVGVRPSLLGLFLTDPVLWVRTLFGPCTPFQYRLSGPGQWSGARQAILTQWDRITGPIRTRAVPEPESSLTYGFFPFLCVFGGVTVAIMYTKLKLF
Catalytic Activity: H(+) + N,N-dimethylaniline + NADPH + O2 = H2O + N,N-dimethylaniline N-oxide + NADP(+) EC: 1.-.-.- Subcellular Location: Endoplasmic reticulum membrane Sequence Length: 537 Sequence Mass (Da): 60277 Location Topology: Single-pass membrane protein
A0A1M5R7R3
MGPVPVRSASPGAARRPGRRGPADYRRARRAARARPDRGAPLSEQPEDAARATPARRPRTRLLLTLAALLFLADLATKLLVVATIDRGENIRLLGGLVYLTHARNTGAAFSFAEGFTVVFTLIAVVVAVVIVRAARRLFSTAWAVALGLVLGGALGNLVDRVFRDPGFLRGGVVDFVSVFAPNGEFYPIFNVADSGIVVGGLLGAYLALRGVEFDGTRSRDRGDGAVTSS
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage). Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins. Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains. EC: 3.4.23.36 Subcellular Location: Cell membrane Sequence Length: 230 Sequence Mass (Da): 24336 Location Topology: Multi-pass membrane protein
F2I584
MAFNNMYHIIDRDDWHAYRDEITSDINVKLTEKQLEALLAFNDHLTLEDANDIYQPLTQLISIYFKNYQSLIIERNQFLGINDKIPPFIIGISGSVAVGKSTTARLLQLFLSQFFPYLDVELITTDGFLYPNEQLEHWDLMHRKGFPESYDMHELKKFFMAVKSNKQRLKVPLYSHESYDRINAYREIKSPHILIVEGINVLQFLGSDQFFIGEYADLSIYVDADTELIEKWYMERFILLRENALKDPDHYNQRYSKMSLDDALRSAKRTWENINLVNLEDYILPTRDRADIVIHKIENHYIDSIRMRRY
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+) EC: 2.7.1.33 Subcellular Location: Cytoplasm Sequence Length: 310 Sequence Mass (Da): 36851
F2I5J0
MKDNKHSGRLSNILNQSNIFVPLVIAAILVFLAVGMLMHNNPLIALISFLLVIFAIILVYVAFRLIEQELNKQVYDLTDDIQTIENEILLQIPLGIILFEEDDTIRWMNPYMQNYFNSSDTLGNKIDDVDSVLSDIYHQLKERDEDDVTGHPISWDDHYLSVGLLEDQNAMYMLDITEYGRIADVADKNRLVIANILIDNYDETIASYSDRRKSTVDNFMTKQLFAWAKKFGSFIKRLDDDRFLLVTTYGELMEMEEDRFSVIDTIRETTSKGNFPLTISMGISYQEEDDEAPDIGKINEIAQSNLDLALSRGGDQVVIKIESEKARYYGGKTNPMVKRTHVRSRQIATTIAQMMQQNESIFVMGHDYPDMDAIGACIGIRRIAEMNDRKCHIIIDESRINSDIEKLLVELRKDEVINEAIISPQEAEELIEHNSLLFIVDVHRPSITTAPKLIDMVNGVVVIDHHRKGEEYPENVLLEYIEPYASSTCELITEFFEYQNASSKSINRIEATTMLAGIIIDSRNFTLRTGSRTFDAASYLKSCGADSILIQEFLKEDLSEYIKRNQLIESVDIMPPYYGIAAGDDDTVYSTVTAAQAADSLLSMNGIVASFVVFLREDKRVGISARSMGNVNVQTVMEELGGGGHLSNAATQISDVSVSQARELLVDVIKKQSEED
Cofactor: For phosphodiesterase activity, probably binds 2 Mn(2+) per subunit. Function: Has phosphodiesterase (PDE) activity against cyclic-di-AMP (c-di-AMP). EC: 3.1.4.- Catalytic Activity: 3',3'-c-di-AMP + H2O = 5'-O-phosphonoadenylyl-(3'->5')-adenosine + H(+) Subcellular Location: Cell membrane Sequence Length: 676 Sequence Mass (Da): 76329 Location Topology: Multi-pass membrane protein
Q3YRP0
MLCKLKYIVSNFGEYRLLLRLHSVEIIFLAMFPALASIALVSHSVLRACGYMILCVIGAFIMRPAGCIINDIFDRKIDSKVKRTRNRPLANGNLSVVQALKVLGVLLACACLLLACTNMYTVKLSIISMILIVLYPLSKRFFTWPQLLLGIVFNSGVLLGCTMTIGHLTLSAVLLYIGCVFWTIGYDTVYAAQDKEYDIELGLQSTAIKFGNDIRLWIGRLYIITITMWISAGIISMLHPIFYIAILIIGAIFYYQYKKSDFDNPEKCMYMFKVNVYVGLILFLGIVLGRVI
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 ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate. Catalytic Activity: 4-hydroxybenzoate + all-trans-octaprenyl diphosphate = 4-hydroxy-3-all-trans-octaprenylbenzoate + diphosphate EC: 2.5.1.39 Subcellular Location: Cell inner membrane Sequence Length: 292 Sequence Mass (Da): 32861 Location Topology: Multi-pass membrane protein
D8IAW5
MSENQNNSENTQNEKNSSVEKNAEKENRKEKLNTLRNMGINPFPNSYDVTYKSKDIAEQFEELEKNETEVAVAGRIMLYRVMGKSSFLTIKDSKGTIQAYIQKDKLGDEFYNTVFKKLIDIGDIVGVKGTVFKTKTGEITIYASELKLLTKSLNPLPEKFHGLTDTELRYRQRYVDLIMNDDVKEAFIKRSKMISAIREIMIENNFLEVETPMMHPLIGGAKAKPFVTHHNTLDMTLYLRIAPELYLKRLIVGGFDKVFELNRNFRNEGISTRHNPEFTMMEAYMAYANFHKVMELVEEVFSKVCFKLNGKYTSQYKDYEINFKPPFARVPMVDLVKEHSGLDFNSIQSDDEAISKAKSIGVEIDTSKGKPTKWEVMVAVFEEKVEEKLIQPTFVINYPKAVSPLSKSYPDNPDITERYELFIGGMEMSNGFSELNDPIDQKERFEEQLKAKARGEDETMDMDLDFINALEYGLPPTGGLGIGIDRMAILFLNVPSIRDTILFPQMRKLE
Cofactor: Binds 3 Mg(2+) ions per subunit. Catalytic Activity: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys) EC: 6.1.1.6 Subcellular Location: Cytoplasm Sequence Length: 510 Sequence Mass (Da): 58568
A0A2H1VZ36
MLLIKLWLWLLFLFKTNEALLCYNCSTTQREWSRCGGDFVPTNLGFNSTRMFLVNCTGENAMCFVRSWNARARHAWIVQRGCYLPTGDDTLPRSVNIPTRAMSCKHERHAEAEYKVCLCRADWCNSASSLVPSIAQYFYKSLTYIVGNIIIIFWTNKLPIFI
Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excitability. Subcellular Location: Cell membrane Sequence Length: 162 Sequence Mass (Da): 18750 Location Topology: Lipid-anchor