ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A945L6G9 | MSVLRIEPFSGVSGDLFAGALAQLADAEPLISELPASLGLSGVATVWRTVNKCGVSCRKVSFVEKLEEPSKPGHGAHRHLSDIKHLISQADISKGAKFRALDIFQALGEAEANVHGIPLETVHFHEVGAVDSILDIVASALLLDRLGVTSAICDPVVTGKGFVEMAHGRYPIPAPATQKLLQGMVLEPGLEFGELTTPTGAAILRHLKPSFSVPQLRVLSTAVAGATKDFLHPNVLRLSLCESIATTGELLLIQTNIDDMPGELLGSDLLDLLLEAGAKDAWVSPIVMKRGRPAFKLEALCTRSEKDQVSAAILENTSTI... | Function: Involved in the biosynthesis of a nickel-pincer cofactor ((SCS)Ni(II) pincer complex). Binds Ni(2+), and functions in nickel delivery to pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN), to form the mature cofactor. Is thus probably required for the activation of nickel-pincer cofactor-dependent e... |
A0A946HLI4 | MGFATLSGSSRASAVTMGRVALPHMKRYKYADNLSTGSVAAGGTLDFLIPPSGGMILYAVLTEQSVGRLFMARVVQGIILTLLFIGAIYIVVARHPGVGPPGERASRADRQGSLLRAAPIPGVVLLTIGGMYMRFFHRLRPHPLAFS | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 147
Sequence Mass (Da): 15653
Location Topology: Multi-pass membrane protein
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C0P9R9 | MGSSTDHAAGARGKKQGSQLWKKALLHSSLCFVMGFFTGFAPSSVSDWTSAAAAAGGRVGSSHVVRALPAGGERHHQRNVALGHIEHHRLAGVVLFAGLGDVFDLRFFDELRGIRYQPAIIIACFTARTTCIVARAKLSSSLHK | Function: Involved in the synthesis of glucuronoxylan hemicellulose in secondary cell walls.
EC: 2.4.-.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 144
Sequence Mass (Da): 15354
Location Topology: Single-pass type II membrane protein
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A0A4V6EUD0 | MLLSHLRETPREARGWRLWFSAWAVGALGISRGLDEGIISGVLKQHSFVKTFGFDDNSPQEATIASQLQLGSVAGSAIAFFLCDRLGRLRTSMLACLLWIFGTAIWMTSAGIHGTHHPGNYHQLLAGRFIAGLGVGFTPVVAPVYLAEIAPKAIRGLCVCIFSGSVYIGILLGYLSNLGTSIQFNDARQWTIPASINFIFAGLTFIGCLFAKESPRWLIKQGRYEEGRKVLSYLRNLDEDHPFVVNEIEVMEQQIQAEKEALEGLNMFQILKKLVTNKNNQYILFLGLGIQVLGQLSGGGVYTIFAPKIFGLLGVPGGTR... | Catalytic Activity: H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in)
Subcellular Location: Membrane
Sequence Length: 548
Sequence Mass (Da): 60236
Location Topology: Multi-pass membrane protein
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A0A0N1MU75 | MKLVSRYTHIAEDFAVPDLPSPVVAPTLLLWNEAVAKQLDIQVSPSERASIFSGNTSNSTVAAVALGYSGHQFGHFSPRLGDGRAHLLGAVSDQHQQLWDIQLKGSGATPFSRGGDGRCAIGPAIREYIMSEAMHGLSVPTTRCLAVVASGETVYRQPPQQGAIVTRVASSHIRVGSFQYLATQGDVSALQALADSAIARHYPEIQSTGSDRYLAFLKAVIEKQITLVVSWMRVGFIHGVMNTDNTLISGETIDYGPCAMMNQFDFDTVFSSIDRQARYAFGSQPNIANWNCARLAESLLPLIHEDDEQAVELLSPLING... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
EC: 2.7.7.108
Catalytic Activity: ATP + L-seryl-[protein] = 3-O-(5'-adenylyl)-L-seryl-[protein] + diphosphate
Sequence Length: 471
Sequence Mass (Da): 51808
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A0A0P8AD67 | MTLNWLQIIRLGLVQMCLGAIVVLTTSTLNRLMVVEQALPAVLPGLLVALHYGIQMTRPHWGFASDRGGHRTRFIIGGMAVLGLGAVLAAFGVLLFAHSWWGGLALSILAYALIGLGVGASGTSLLAMLATATAAHRRAAAATITWLMMIFGIAVTAGVVGTLLDPYTPAKLMRIVTGVALGAVLLTALAVHGIEARVRSEQEPETASFRHGLAEIWAERRARNFTLFVFLSMTAYFMQELILEPYAGLVFAYSPGQSTQLSGAQNGGVFLGMLTVGIAATGLRIGALRHWVVAGCLGSAAALAAITMVGQAGAAALFVP... | Pathway: Porphyrin-containing compound metabolism.
Catalytic Activity: 3 NADP(+) + phytyl diphosphate = geranylgeranyl diphosphate + 3 H(+) + 3 NADPH
EC: 1.3.1.83
Subcellular Location: Membrane
Sequence Length: 819
Sequence Mass (Da): 86801
Location Topology: Multi-pass membrane protein
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A0A6N9BCX6 | MTLPNLIWHHQEKYPHTRSDQLAQLFYLNHSDDYTRFTQFLKGNIALSESIREAVNQIITGIVSEKDLALIAFTKKFDGVSLKPDELLLSEEEIEASVNTLEDSQKDMLKASFERLWKFHEKQIPTSQTWKDEDSVTLGWIWQPIQSCGLYVPGGTATYPSSVLMMGVPARIAGVKSIALTVPPSNALDPHLLYASRLVSVDRIYRVGGAQAIAALAYGTETISAVDKIAGPGNSFVTEAKRQVFGQVGIDMVAGPTEVVVVSDNNSRPDWVAADLIAQAEHDPLSRSILISDCEKFVSKVFSEVAKQAELLPRKEIILE... | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
EC: 1.1.1.23
Catalytic Activit... |
A0A2E0UMI8 | MKRNPTSELAKAQSQAGDFSREKLQALLAVCRNNLRSFDADLITRAFQFAADAHKEHRRKSGEPYFTHPYAVAMIVAQEIPLDDASVAAALLHDVIEDCEHYSYDDVAKEFGGTIADIVDGATKISNILKSREVTKAESYRKLLVSMINDIRVILVKFADRLHNMRTLEFVGTEKQKRISKETIEIYAPLAHRFGLARIKWELEDLSFKYMYPEDYRNLKEQVNQRRRERESFITKFCKPIAEKLEAKGLKFEMNGRPKHLHSIYKKMMDQNKTFDEIYDLFAIRVILDTKEETDCYVAYAVVSEIYTPIPERFKNYIAL... | 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: gua... |
A0A7S1YK36 | GLATMIFLWLSAATDPGIVPAVSSPVKPQPSPEWTIGGPTGHRYCGTCNIFRPPRSKHCNSCNVCVSKFDHHCPWTGNCIGERNHRFFFGFLLAIALLTILVTMTCFDVIVKAYQAFVLEKGVPPVVIDLSDTANLEENISQLPENAHYLWNVLLGMPLVVLFGTFTFLCAYSLVSLLVFHGMIITLAQTTNERVRNVFRGGSDNPYTHGCWSNWKTALWSERPVSRIP | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 229
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 25471
Location Topology: Multi-pass membrane protein
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A0A965D6N9 | MNAIDSPIKTITAPRLTRQQKAAIVVRFLMNEGADINLSQLPPALQANLTREIADLRLVDRATLTEVIEEFAEELDAVGFSARGGLGEALKLLDGKITPQTAKKLREDAGVRLFEDPWDRIKGLDLDDLIEILDQETAEVAAVVLSKLDVPAAAKILAKMPGERARRITYAISMTAQVTPTAVDRIGQCILSQIDNRPEFAFVDLPERRIAAILTAANDALRDEVLEGLRDTDKDFADRVERSVFTFDSIPERIAQNDIAKAIKTVPQSDLVVAFAYARNIDRGEIVDYMLGAMSKRMVERIEDEVKDLGKVTRKDGQAA... | 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.... |
A0A2A4QQV9 | MNDIETVKQTLTEEYDVSRETLSDLERLVELLVKWNKAINLVGKSTLDQVWSRHILDSAQIWSQRPADLRTWVDLGSGGGFPALVLAILAKKDAPNAVFHMIESDVRKCSFLRTVSRETFSKTEIHAVRIESAPDIQADVVSARALASVDQLLSYSEKFLGISGFCLFLKGQGCVTEVENAQESWKFEFSTTQSLTDLSAQVLKVWNIARAND | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.170
Subcellular Location: Cytoplasm
Sequence Length: 213
Sequence Mass (Da): 23... |
A0A1D6PUT2 | MIAFPLLLCLILSIFYMFWFSATLHLFSSGQVVRNDCNTDCCSYDLKLGKVNCDYNIHYTPHISIAILFHLFGCYWVTQFILTCS | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 85
Sequence Mass (Da): 9856
Location Topology: Multi-pass membrane protein
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A0A257TNE6 | MAEDPYLASSLVDHDIDVGAYHVGMVYGKALLAATEKAGNTDEVLAELDQLIELLARQPKVDGVMASGMIAIDQKVAIVERVFSGKVTPTFLNFLKVVVDHGRGGFLRAMRRAVRDLRDQQHGRVRVQVTTATPLDGELTERIHNQLKSMLGGEPVLTKKVDPDLIGGLVFRVGDTVYDGSVATRLTRVRSQMIDRSIHEIQRRRDRVSPTAGN | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
A0A1D6Q1T1 | MHMGNFEDAEGLLLESLNKDAKDTETLANLTVCSLNLGKPATRYLNQLKLAHPDLVKRMSSAAESFDRACQAMV | 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. The coatomer complex is required for budding from Golgi me... |
A0A3P9IGN9 | MNKSDYLKLIPLFLPGGGAVGSKGGSCPPLVPSIFESTIQAPLSICFIKHPNNNTKNMRIKLFEKPFFILSKIRRKDAPPPSSASLIPFQTMLDDLALIKTLHESRFDLVLADPCWGGGAILAKYLNLPLVYMGRWLIVEEAHFSIAPSPLSYVPVTGSGNTDRMTFLERVKNIFFYLLTYVQNDVLAKQIYQPTCDKYLGPDHDFNQIKTDADIWLMKTDFVFDYPRPTMPNVVYMGGFQCKPAKPLPEHLEEFVQSSGEHGVIIMPMGTFVSELPDDLANEIAAAFAKLPQKVIWRYKGKRPASLGNNTLVVDWMPQN... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 488
Sequence Mass (Da): 55153
Location Topology: Single-pass membrane protein
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A0A141CN78 | AFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLTHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPTAVTMYQIPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQ | 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-cytoc... |
E3HC20 | MQKQIEKAEMLVEALPYIKKFAGKTVVVKYGGNAMINDEIKDQVMKDIVLMKYVGVNPVIVHGGGPAINSMLAKIGKEAEFKMGNRVTDEETMEIVEMVLSGKVNKGIVAGINRHGGKAIGLSGKDGNLILARKKYLMDGKEKVDIGFVGEVKKINASIIEDLQKDGFIPVISTVGVDEDGNTYNINADYVAGAIAGALNADKFLFMTDVPGLLRDINDPSSKISVLKYNEAKDLIEDGTISGGMLPKIDACMTALDAGAENVHIIDGRVKHTILLELFTDSGIGTMIVKDYRIVR | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Function: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
EC: 2.7.2.8
Subcellular Location: Cytoplasm... |
A0A2N6D008 | MSRQASGLRAWALQRISAVYLGLYLIYMLGHLSFNAPETYEAWRAYVADPGVTIGMLLFVTALLIHAWVGIRDVLIDYIHPIMARVGLLSLFAIGFIACGLWFAKVVFLASVAA | Cofactor: The heme is bound between the two transmembrane subunits.
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Cell inner membrane
Sequence Length: 114
Sequence Mass (Da): 12589
Location Topology: Multi-pass me... |
A0A2N6D015 | MTTKNRPVYLDLTQFRFPIAAIMSVGHRASGVLMILAIPFLAYTLDLSLSGPEGFAEAKAILDSLFIKLVLFVVLWAMLHHLLAGIRYLLLDFHLGVEKEIETKSAQAVMVAAPVLAVLIGLVL | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 124
Sequence Mass (Da): 13573
Location Topology: Multi-pass membrane protein
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A0A7X4CDV5 | LAELKNNLSENNLEDAGQAIMTTDTFPKGAGIVVDCSDKPVAISGIAKGSGMIAPDMATMLAYVFTDANIDQTTLQSMVSELTETTFNSVSVDGDTSTSDTFMVAATGLARNKMIVNQETSDSRKFKAGLQSVMLSLAQQIARDGEGATKFVEISVVGAENNSDAKKVAKSIANSPLVKTAISGEDPNWGRVVMAVGKSGARADRDLLAIKFGDILVAENGQVADNYKEELGQDYMKKQEILITVDLGLGKGSSRFWTCDFSHGYISINADYRS | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and ace... |
A0A2E0UM29 | MLHTAGKDADPRAIAFAAEEIRDGGLVAFPTETVYGLGAEIYNEGAIRKIFEVKGRPPDNPLIVHIADPEQGIELMQQVPDRYNVLATAFMPGPLTLVVQRNASVLDVVTAGLETVAIRMPSHPLALELIRAVGAPLAAPSANVSGNPSPTTAEEAYEELDGKVAFILDGGRSDIGIESTVLDITGSKPVILRPGMITGEDISGALHEDVLHASEAGEVRSPGVKYRHYMPAVPMTLFAGQNAEDGIAAAAERLIAEGQRVGVLAPERMKRISHTLFYSLGKGATLDYAKYMYSGLRFFSAQQVDVLLCAGIEEEHQGLA... | 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 Len... |
A0A2E1RWL7 | MTKGHACPPSYCLGHLAVAHGGCLFLVGSWWMRIRTRLFVEDCLEVGAIVVPEQGQTHQLIHVLRVRAGEGVELFNGRDGSYHAQITELGKRHVSLHVTMKVHDQHCLPDLWLAFAPLKKARIDYVAQKVVECGYRHVCPVITNRTQAEKFNKDRFQANMVEAAEQCAINVIPGIDDPMSLESFVRLSLDRQIFLGDEGGEGAPAWEVLGRHQPGVPSVILIGPEGGFDNQELAWLRGLAHVHPMGLGPRILRADTAMVVAAALWQARLGDLTSPPRFALV | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A3R9QTT0 | MREFLSKITNSLDAIGFDDLILLPGMSSVEPSEVDLSTRASKGIWMKVPFISSPMDTVTESEMAIAMARSGGIGIIHRNCSKEEQVEMVKRVKRAESFIIRDVITIDPRSTIKEAAEIMEKNRISGLPVVEEGKLVGIITGRDVRFADPSLRVADVMTRDVITAKEGIKMEEAEELMKSHKIEKLPVVDEEGRLKGLITYKDIALRGRYGNATRDEHGRLRVGAAISPFDLERAKELSKIADLLVIDVAHFHSLRVMEATKKLLKEVDVDVVAGNIGTYEAAVDIISSMDVAGLRVGIGSGSVCTTMEVTGVGAPTPFAV... | Pathway: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.
EC: 1.1.1.205
Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XMP
Sequence Length: 475
Sequence Mass (Da): 51587
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A0A3G1KU11 | MKRSIVGAVGVVLVMNLVTKILGFARESFIAWGFGSDFHTDAYFIAYTLPYFLQAILGFALVTAVVPVLTRYLVDENYDEAWHVASTILNLTLVVLTLVTLLGIMGATVLVKITAPGFNPVSARLAVTLTQIMFPSVVFMGVGMVITGILNASYKFAVAAFAPGFSNLIIIFSVIFFSAHYGITGLAVGTLLSFLGFLLLQVPFLKSVKFKYSFVFDIKHPAVRQLMVTIGPIILGVAVNQINLALNRVFASWLAEGSISALNYAMKLMNLPQGVFVAAVASAIYPTLAAQAIKGDKKSLSDTMLRGLSMVSLITIPAAV... | 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: 518
Sequence Mass (Da): 55731
Location Topol... |
A0A7S1XYZ6 | QLPPSLVVDVLIFYLVLRALDTIEDDTTAFSQDPKLKVETLRTFHKTALVDEKWTLLPLVVGEGDERRLIENFGNCQRVYNQLLDAPKQIIADITQRMATGMAEFVDKDMGQGTTTIAEYNRYCHFVAGLVGEGLSRLFAASQLESSTLSRELHLSDQMGLFLQKVNIIRDYLEDYVDGRAWWPQEVWKKYATELGEFAKTSQNANNSQAALSCLNELVTDALELGPDCLHYMRNLQCKEVFSFCAIPQVMAIATLDKLYNNPDVFTGVVKIRKGLSCKLILQTKSLPQLHSIFYTFAKSIKEKALSVSNDPNQERTIKA... | Pathway: Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 1/3.
Function: Catalyzes the condensation of 2 farnesyl pyrophosphate (FPP) moieties to form squalene.
EC: 2.5.1.21
Catalytic Activity: 2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + NAD(+) + squalene
Sequen... |
H2MJ78 | MGRDSSEMNASPPAGSALAPGGATGPTTPKKGPPKFKQRQTRTFKSKAPKPGQKGFGDDIPGMEGLGTDITVVCPWEAFGDMELSDLAKYGII | Function: Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones.
EC: 3.1.4.35
Catalytic Activity: 3',5'-cyclic GMP + H2O = GMP + H(+)
Sequence Length: 93
Sequence Mass (Da): 9681
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A0A642URV8 | MFRVGVLRAPTLLLRRQFPSNVFVRFRSTLGDAVNQTPRKFSDEQPDPLDNSVENVERLRLTEKLERTKVEMEQTEETIKHLESAPQIEPVKIEPEASTQEEDKEAIKLEEDTDGDDIKGQAASLAAQAHESGKEPPNISQQINEEIHRQFKDLPSSQEARKSQWAKKISDQVESLHSVVLTATRALNDVTGYSVIEKLKQSIDNLEDDLKAAKQQVKECKSDYGDAIQLRSTSQREINELLTRKHNWSSKDLERFTDLYRNDHTNELREKEAAENLNEAESKVDAIQLKLTQSILTRYHEEQIWSDKIRRASTWGTWVI... | Function: Required for the maintenance of the structure of the mitochondrial inner membrane. Involved in mitochondrial morphology. Causes growth arrest when highly overexpressed.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 500
Sequence Mass (Da): 56811
Location Topology: Multi-pass membrane prot... |
A0A804PZB1 | MVVLYVLFVACLEGTAQSGEERNEEREHLHRPARQESMLIITQSIACSVPCRYGLPFVSPNNMLVSTINGAGAAIEAVYVVIFLAFASSQRTRLRMLGLASAVSAAFAAVALASMLALHGQGRKLMCGLAATVCSICMYASPLSIMRLVVKTKSVEYMPFLLSLAVFLCGTSWFVYGLLGRDPFVAIPNGCGSFLGAVQLVLYAIYRDSNSGGKQQAGDDVEMASDAKSSKKVADDVGGKEDRLV | Function: Mediates both low-affinity uptake and efflux of sugar across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 245
Sequence Mass (Da): 26176
Location Topology: Multi-pass membrane protein
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A0A2E0UM67 | MRAFCALYPDSEGLDQIFQVLRQLREHPFPIRWEKPDHIHVTLKFIADIDPAVLDQAIGDVSKTVTSMDSFRFRVDTLGAFPNPAKPRVVWVGSDSTPDKIATLHGLFEDACANYGVRKEQKKFTPHFTIGRTKKNGRVENLKNAFETISFQPFDVVFRAVRIMESTLTSQGAIHKEYRRLTFGNSE | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 187
Sequence Mass (Da): 21342
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A0A7I4XTX9 | MSRPEFKQKEKKARRKGRKGHGSREGSKEGGGSKEGRKEEKKKKSKEDAKKHKKKAEHKKSKEEAKIDEKEAEPKKSKEEVKANRKESTPKKSKEEERADKKEAEVVLQCFEKAPIQEVKCDEYSRDWLDHLCRLDIRDAPDKSRKTGIICTIGPSCRSVDMLKQMITCGMNVARLNFSHGTYEYHGGTIKNVRQAVEQMGGSLQIGIALDTKGPEIRTGLLSGGATAEVELVKGKSITLTTDEKYKESCTADNLYLDYKNIVKVVKKGSRVYVDDGLISLVVDEVKENSISCTIENGGILGSRKGVNLPGTAVDLPAVS... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 629
Sequence Mass (Da): 69217
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A0A0G1LWW3 | MPPRQEHNQRPRIRTLNDPPRLGEAGPPGRGHSDRRQHSAPRHNAASDRKFYKEGSLTGHEPHGHSKALKRDTVYYVPLGGLEEVGRNCSFFEYNDEIVIIDMGIQFPEEETPGVDWIIPNTKYLEKKKKNIRALLITHGHYDHFGAIPYVLERLGNPPIYGTRLIREIIQKRLSEMPNVPKMRFIEIKSHDKVKLSEHFTAEFFGVSHTVPDTTGVALHTPAGIMVHFADFRLDYDQEDTVQNLREFERLSGLGVHTLFLDSTNADFSGHSVSERTVEANLEASFREAKGRIILSTFSSMITRMAEIVKIAEKIGRKVV... | Function: An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 624
Sequence Mass (Da): 70472
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A0A1R3MNR5 | MDHVVGGKFKLGKKIRSGSFGKLYLAVNVQNGEEVAVKLESVTSRHPQLHYESKLYMLLQGGSWRILYLPNCSKIYQLPHLIFFWDRFPLDQGCRREALATGCCTSTANRGHRAGGQKQPATTVGHRRLEEGEEKGELGFILDGFPRTMRQAVENGRCRGYPAPRLRQRNWHGQGEPPAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQTVLSLYASGRTTGWEYSTDGKCE... | Function: Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth.
Catalytic Activity: AMP + ATP = 2 ADP
Subcellular Location: Cytoplasm
Sequence Length: 448
Sequence Mass (Da): 50573
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A0A161SEF9 | MAASSSSKKSRRAKTSSARSSGHPAGRSGNPQKPVVSGDPRQVAPATLRDWIGAARLRTLPLAVAPVVIGTGAALVVERRLHWVLALACLVIALALQIGVNFANDYSDGIRGTDDHRVGPARLTASRAVPAKTVLAVALVFFAIAAIVGIAVVFRTQHWWLLAVGAVCIAAAWFYTGGKRPYGYYGLGEVVVFVFFGLVATAGTTFVQIGVVPDEAWLGGVAAGFLACAVLLANNLRDIEQDRRAGKRTLTVLIGKRATQVLFTLFLLIPFAIAVVLATLYPIAWLSLLALLPALAAILIVWTYGHPRELVVALGVTSLT... | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
Function: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK).
Catalytic Activity: 1,4-dihydroxy-2-naphthoate + an all-trans-polyprenyl diphosphate + H(+) = a 2-demethylmenaquinol... |
A0A2E0BN50 | MKNTEENLSLHKKISQLDWSELFKTKNTPLNEEEYKSIKNLVENTSIDEVNNIYIPLSCLLNNHFSSLKGLSNSSDKSLGAVLQTPPFIIGVAGSVASGKSTFSKIMKEVMLIKYKNYKIDIVTTDGFLYPNSYLQERNLMGKKGFPESYDVNSLFKFLSKVKNSQEKVYAPIYSHQVYDVLPLEQLSVDRPDILILEGINVLQEQKIKENKSDTIFSDFFNFSIFIDARENYLSEWFLKRFLSLRSGAVNNKDDYFHKYASISDSDAISMAKTIWKKINLKNLNENILPTKKNADLILKKNKDHKINEIWLRNT | 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: 315
Sequence Mass (Da): 36308
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A7NSD0 | MTSNRFAFFNGEFVPIEQAQVSVMTAALNYGLGVFEGIRAYWNADDGQLYVFHLREHMERLRRSCNIMFMNLPYSVDELYDLTVELLRREAFREDAYIRPLVFKSDHTIAVRLNNMTDAFVLYAVPFGQYIPGTAVRACVSSWRRIEDNIMPSRAKVSGGYVNSALAKTEALLNGYDEAIVLGGDGQVSEASAANLYIVRNGALITPPITSDILEGITRRVVAHLAQAELGVPVIERPIDRTELYVAEEAFFCGTGAEVKPIIEIDRRPVGSGAVGEITARLAELYSAVVRGCLPAYRAWCTPVYIDEGA | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.
Function: Acts on leucine, isoleucine and valine.
EC: 2.6.1.42
Catalytic Activity: 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate
Sequence Length: 310
Sequence Mass (Da): 34374
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W7CEV9 | MTKRVGILGGTFNPPHFGHLFIAEQVFEAYQLDEIRFLPNAIPPHKAVVDGITDEARIALVKGAIANNTHFTIDTREITRGGSSYTYDTMLEMKQLEPDVQFYFIIGADMVEYLPKWYNINKLMELVTFIGVTRKGYRLQSDYPIETLALPLMDLSSSAIRAQLKAGQSVRYMVPENVYYAIKESQFYES | 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... |
A0A3L6FQS8 | MEEGCDVTSDWIISPNWLKESVREGQFVEEAQYVLEDEEYRMQYKSELRDAVMRAKERPNSLFAGYKHIQPSFDVLLAIIKSTGGNFIQAEKGIAAAKVPRSTLAAISLCQPGGGGEGDWDGACADVAACVPRSTHLCQHLVISEIDSSIATSLQAVKLLALYLTGDKEGAISSLKEWLSDSATGSNLVLRLIARIIFMREQDYNEALKHTHSGGTLDLYVYLFP | 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. The coatomer complex is required for budding from Golgi me... |
A0A367V6Q6 | MVAVAGSSSVALPMIQSAGLDPIWFGIYLVLVVEISQITPPVGFNLFVLQSMSGRDILTVTKASLPFFFLLLFGLILITIWPEIATFLPGLMINR | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 95
Sequence Mass (Da): 10339
Location Topology: Multi-pass membrane protein
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A0A7K6IKQ4 | VAYLVVFHVLFVLFVWTYWKSVFTLPIQPGKKFHMSYADQERYENEERPEVQRQILAEIARKLPVYTRTGNGGIRFCDRCQLIKPDRCHHCSVCAMCVLKMDHHCPW | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 107
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 12730
Location Topology: Multi-pass membrane protein
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A0A2E8SJJ5 | MKTELNNPRDKIKVVTMNGSLMPLNKAKVSVTAPGLSYAALVFEGIRAYWNDKLNELYIFRLDEHLVRFTNSMRLLKFSEFPDSSTIKEDILKNLKANNYQEDIYIRLQAYIDDWGEMALQTPVSTSIVSYPRPRAVAFKEGKNFTVSSWQRLDDNASPPRIKASANYLNSRLASIQAKESGYDGGIMLTANGKVSEGPGGCIFIIRNGTLITSSITSGILESITRDSIIEIAKKFKLKVESREVDRTELYXAQEIFYCGTGQEIMPILSVDKMLAGNGKPGEITRFLQNKFTEIVRGNNKEFNXWIYPVYQ | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.
Function: Acts on leucine, isoleucine and valine.
EC: 2.6.1.42
Catalytic Activity: 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate
Sequence Length: 312
Sequence Mass (Da): 35235
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H2LB94 | MTFGASCCCSLLLLSWAFGQTSITGGDRSPCQRCDLQLSCDCSHSGFSHVPMVTDQALRLDLSFNNITTITRDDLKGLSRLVALDLHGNRLSSIHPSAFDSLWSLEELDLSDNRLTVLDPRWFSELGALQQLNLLNNPYSRLGSSPLFEGLVRLRILEFGGPVQEELKTGDLKGVTQLDRLTVRANNLIRYERGTLAEIWPLGGVTLNLHRPFLTDPALVSAVLNDVLSPETHLTLEDVHLTSKIPAQVFRDTHINRIRYMSFRNVTISDESVVDFLTAINGSPLTSLSIDGLTVTGEGRWTRANWTDLRSMDEFLVRNL... | Function: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secr... |
A0Z7H0 | MIAERGSWVIVGSILIALLLVAIPVPVSWREYTPDWPLLFLFYWVLALPNRVGVLSACVVGILTDLLDGSPAGATAIGAVMAVLVILVSYQRIRQFDGLKQGLVMALLISLVHLVEQRLETFLGWQHSSTAFLMPAAVSFLFWVPVRNCLRFFRRYYEVQ | Function: Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 160
Sequence Mass (Da): 17948
Location Topology: Multi-pass membrane protein
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A0A2D5BEM6 | MRDELTYPPYNVVLLTLDRHAAGPAARALPKLAADFPGLHLKIHAAAEWAKDPEALALAKADIETAHLIVSSVLFLEDHVQAILPDLKARRASCDALVGIIADQEIVQLTKMGELDMMRPASGVMGFLKKLKPAKKSGSTGEGQAKMLRRIPKILNLIPGKSQDLRAWFLTMQYWLGGSDDNIESLVRFLISRYASRPEWRGVAAPAPVEYPEVGLYHPDLPGHHITTDIADLPQAGAGPT | Pathway: Porphyrin-containing compound metabolism.
EC: 6.6.1.1
Catalytic Activity: ATP + H2O + Mg(2+) + protoporphyrin IX = ADP + 3 H(+) + Mg-protoporphyrin IX + phosphate
Sequence Length: 241
Sequence Mass (Da): 26291
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A0A3C0PMH6 | MQLNVSRETQGRLEAFVALVEKWNPVINLIAKSSLPDIWRRHVEDSVQIIPMGQLGNFWIDIGSGGGFPGIVIAIILKESAPSTTVVLIESDVRKATFLRQAVATLGLNCQIHNARIESLNLPRGTTVSARALAPLPKLLSFVENLVEEGGVCLLMKGQSYQQELAAARQSWSFDCEVIKSQTNTDAAVLTIRNIQRATR | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.170
Subcellular Location: Cytoplasm
Sequence Length: 200
Sequence Mass (Da): 21... |
H0WX90 | QAEAEEDCHSDAVRADDDEENESPAETDLQAQLQMFRAQWMFELGPSVSSGKLENQPCRAARGSLLKAATDTKGKQEQAKEEKARELFLKAVEEEQNGALYEAIKFYRRAMQLVPDIEFKITYTRSPDGDGVGNSYIEDSDDDSKMADLLSYFQQQLTFQESVLKLCQPELESGQTHISGKLIPFDILCFALFFCISDFILILTISWLPEACKKMYALCTKDPEIWRLACLKVWGRSCIKLVPYTSWRQMFLERPRVRFDGVYISKTTYIRQGEQSLDGFYRAWHQVEYYRYIRFFPDGSVMMLTTPEEPQSIVPRLRTR... | Pathway: Protein modification; protein ubiquitination.
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins and plays a role in several biological processes such as cel... |
A0A973WDX1 | MDAIHLEDLTFFAHHGLFEEEAKLGQRFRVDLTCWLDLTRASNSDEIEDTVSYADLTLAIEKTVTSNRFNLIERLAGAVIQTVFETDSRIEEVRVRLHKPGAPLPTPTGQASVELKRKRSNT | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydr... |
B1HZW0 | MVTILLTLLSIYSAEEKIVQPITSSLLNQENSLHKEIMDESAVETKMNQDIVAQIKITDVREAKKKFINQSVIWMLIIIVAGIASIYVVAGRALKPVHDLRQKIGNISEHNLSQRIEHISTKDEMGDLTVSFNHMLDRLEKSFLYQKGFAANAAHELRTPLTTMMAGIQVLKLEKSPTVEDYKETLEVTEEGTQRLIQVVNDLLALAYEQTEHFTDDIELRTMLDTITQELQSLCLEKNITISVNIDVETIKGNQTLLYRVFYNMIENAIKYNHKNGMIEVRGRVKNGATHISIEDSGIGIPKDQLHYIFEPFYRVDHSR... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 363
Sequence Mass (Da): 41081
Location Topology: Multi-pass membrane protein
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A0A651EET8 | MLVETLVEGGDWAALGDAAALAEAAARAALAEAGVAAEGREISLLLTDDAAIADLNRRFRGKDGPTNVLSWPAGEGAAPPGEPSPLGDIALAAETVAREAAERGLALRDHVAHLIVHGALHLLGYDHEEDDDAEAMERLERRALARIGVADPYE | 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: 154
Sequence Mass (Da): 16045
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A0A0F6W1T3 | MVVGSGGREHAMAWKIAQSPQVHEVIAAPGNAGIAAVARCVDVRADDVAGIVALALREQVGLVVIGPEAPLVIGLADALRDAGVATFGPSRAAAQLEGSKVLSKELMAEARIPTAGFRIFDDADAAEAYVREARRPLVVKADGLAAGKGVIVASDTDEALDAIRTIMRDRAFGDAGARVVVEEVLRGPEVSYHVVCDGTRYVALASAQDHKRLGDGDRGPNTGGMGAYSPAAPVTPELEQQILARCVEPTLAAMRARGTPFVGALFVGLMIVDGAPMVLEYNVRFGDPETEVLMARWQGDVLPLFLGAAQGDLSGVRPSA... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Len... |
G1XYH5 | MPDAALLQVDEEKALAAALDAARTTSEPALAAEDYVGTMAALASLRGPVDAFFDKVTVNADDPALRANRLRLLAGIRRTLNHVADFSVIEG | Catalytic Activity: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
EC: 6.1.1.14
Subcellular Location: Cytoplasm
Sequence Length: 91
Sequence Mass (Da): 9607
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A0A1D6GGK0 | MAVLAITSKVRSLKWLPTRTLIANVLAASIMAVLAITSKVVDTKRSTTILSGIQLDFLGCLSTMSTFDAEVYTMRRSGQIARTLIYAASTFMLPFLLAQLSSWCPSRMLQAHRHLGQHTNILPHGFLHIIVIFVVLY | Function: Fluoride channel required for the rapid expulsion of cytoplasmic fluoride.
Subcellular Location: Membrane
Sequence Length: 137
Sequence Mass (Da): 15204
Location Topology: Multi-pass membrane protein
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H0WN12 | MLSIQVPFFFPAANVFLFVFTASTVFHLQQRLAKVQPLWELQSPAPTWMINTTGHMGNPIAPMWTINAIGRLGNQMGQYATLYALAKMNGRPAFILPEMHRTLAPIFRITLPVLPSTMTIIHWQNYHLNDWMEEQYRHIRGDYVRLTGYPCSWTFYHHLRHEILQEFTLHDHVREEAQTFLRGLQVNGSQPVTFVGVHVRRGDYVHVMPNVWKGVVADRQYLERALAWFRARYSSAIFVVTSNGMAWCRENIDASRGDVVFAGNGIEGSPAKDFALLTQCNHTIMTIGTFGIWAAYLAGGETIYLANYTLPDSPFLKVFK... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: a beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer(d18:1(4E)) + GDP-beta-L-fucose = alpha-L-fucosyl-(1->2)- beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<-... |
A0A1D6EIN4 | MAPLPWRQRHHTLLQAQLSKGPLSERDFRVVFAAISGKNPVQGVKFIRIHFLPKLLFSMHLYLAPWLTATHQQLLNNTLLKIKKDLAYLQLELRACVNQHDGMVYYGVVNNISYAIVGYRTPPQAGLVWASDGLFLTSEAGSVGMISHHVLSAMKPVSRLQAV | 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: Nucleus
Sequence Length: 163
Sequence Mass (Da): 18283
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A0A2E0BIY5 | MGRLTKITFDKKVLKKLKYKRYISGSFAFGLGSLAALGQAPWSIWPIALCALLLSFILAQKCGNFRLAGLVGFFTGLGYFTISLFWITEPFLLEGSNQGWLAPFALLLMSSGLSLFWALAYGLSVLLRYRGDIVLPLIVLLTTAELLRTKLFSGFPWSLIGYVWSDHPISQLSAVVGPHGLTMITLLISGLPLVLKSYKFIRVILPSFLLVGSWSYGYLILQTPDYPPTGKIVRLIQPNAPQNLKWDTEMVPVFWQRQLNFTKEPSAKPLDLIVWPETSVPFLLRESKESLQNISKAASDVPVIIGANDRVEGGIRNALA... | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipopr... |
A0A6L8C642 | MMDPIFLGLIGLGVLFLLIMIRMPIAYAMILVGGLGITFINGPALVLNQLKTLAYFQFSIYSLTVVPMFVLMGCLASRSGLSAALFRAANAWLGWLKGGTAMAVIAACAGFGAVCGSSLATASTMGRVALPELKRYKYSGALATGSVAAGGVLGILIPPSVVLIIYAVVVEANIVSMFLASIIPGLMATLLFNLTIAAYVIIVPESGPRGSKIERDEFIAATKGV | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 225
Sequence Mass (Da): 23367
Location Topology: Multi-pass membrane protein
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A0A804R5G4 | MFLRRILTGGGGLAALRAARAVKETTGIVGLEVAPNAREVLIGLYTRTLKEIEAVPKDEGYRKAVESFTNHRLQICQEEDDWKRIEDRIGCGQVEELIEEAEDELKLIAKMIVRFNVILCLNEWQNGIRGVSLMTTNVR | 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.
... |
A0A3F3HZ03 | MNKSESSSIEKRVSEKLKEYFPQKPNFVVGVSGGADSMALLYILKKLDIHALVVHINYEMRGEESNKDQELVEQMSFEWGFECCSVRLNSKEISSGNFQNWAREQRYNIFNGFLTEIEADGIAVAHHKNDQVETIIQKLLRGSSPEAWKGMDDWNNEIFRPLLEFNKAEILKYCKENSIPFRTDSSNIDSKYSRNFLRNEFSQKMDKLFKGWQENVMKLQEYGSLNKKMLDLLAKDYFDDEKLFIQPIKELDVILAQSLIKKFIEQFHIQISKGVLEQAYNLLSSQVGSELILSESVKLVRERESIIKVTGVVEFEEFQV... | 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)... |
H2M1L5 | MPEANYLLSVSWGYIKFKRMLNRELTHLSEMSRSGNQVSEFISNTFLDKQNDVEIPSPTSKAREKKKQQKQQLMTQISGVKKVSHGPLLSSSSISRFGVKTDKEELLSKELEELNKWGLNIFTVSEYSNNRPLTCIMYAIFQERDLLKTFKIPADTFVAYMMTLEDHYHSDVAYHNSLHAADVAQSTHILLSTPALDAVFTDLEILAAIFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEDNCDIFQNLTKKQRQSLRKMVIDMVLATDMSKHMSLLADLKTMVETKKVTSSGVLLLDNYTD... | Pathway: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.
EC: 3.1.4.53
Catalytic Activity: 3',5'-cyclic AMP + H2O = AMP + H(+)
Sequence Length: 384
Sequence Mass (Da): 43351
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O24596 | MAKALLGGLSAILVVAVVVGVVATVTRSGKKAGDNFTVPGEASLANVRQVGQVPVRAHPVQGVVREDVVPGHQWHREPQGGVPQRGQGGAGVGPDGGRAVQVDRRGQGSDSMTESAREDCKKLLEDAADDLRGMLEMAGGDIKVLFSRSDDLETWLTGVMTFMDTCVDGFVDEKLKADMHSVVRNATELSSNALAITNSLGGILKKMDLGMFSKDSRRRLLSSEQDEKGWPVWMRSPERKLLASGNQPKPNAIVAKDGSGQFKSIQQAVDAVPKGHQGRYVIYVKAGLYDEIVMVPKDKVNIFMYGDGPKQSRVTGRKSF... | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
EC: 3.1.1.11
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Length: 563
Sequence Mass (Da): 61712
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A0A2E9UFN3 | MTQLILASQSPRRKALLQKLGIPFEIQPARINEYSLTRDPTNLVKELSLSKAKDTAMNYSNAVVIGADTIVVHNKDILGKPTSEQEAVQILTRLSGTHHHVYTGVCLQYVDREGRLQEPVLFHERTKVWFHALSAYPIHKYVSSGRPMDKAGAYGIQDDWGAIFVKKIKGDYYNIVGLPLGRCYLELSSLKERYKLELQLSTP | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Seque... |
A0A2A4ZNK9 | MRTLLLTISLMVASPLAAQESCICLKCLLGQHRMVQAMSQNMAPALEPGDCRFARYLNEEFERLDYGDIIFFQHPVLDGEYLNRIAAMGGDTIQLIDGIIWLNGQPLRQEKIADYEIPFLPMGPNNSLPSCQNRPERGGFCRTERYIESMPNGKSYEILNIRDTTVDTTGVFNIPEGFVFVLGDHRDNSVDSRFSQTGSFPGVGLVPLENIIGIVEGD | 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: 218
Sequence Mass (Da): 24320
Location Topology: Single-pass type II membrane protein
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A0A6P3ZDI0 | HAYVHGFTDFTFLMLNTQKAGNTDIEGVDSTNACYGGTAALFNCVNWVESNSWDGRYGLVVCTDSAVYAEGPARPTGGAAAVALLIGPDAPIAFESKFRGSHMAHAYDFYKPNLASEYPVVDGKLSQTCYLLALDSCYKQFCKKYEKLEGKQFSVSDADYLVFHSPYNKVDDIVLIIYIK | Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
Function: Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form HMG-CoA.
EC: 2.3.3.10
Catalytic Activity: acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3-methylglutaryl-CoA + CoA + H(... |
A0A3G1L0V3 | MAALSFLIMLIEFPLPFMPPFMQIDLSEIPALLTAFSLGPGAGVLVELIKNILHLLKSQTAGIGELANFVVGIALVIPAGLIYKWNKSKKGAFLALVVGVVIMAAVASVFNYFVLLPLYARVLGFSTDAVISLGKQANHLIVDLKTLIAYGIIPFNIIKGFIVSVIVLVVYKRLSPVLHK | Function: Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex.
Subcellular Location: Cell membrane
Sequence Length: 180
Sequence Mass (Da): 19401
Location Topology: Multi-pass membrane protein
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H0WVP3 | MNSSGERRQEAAGPRDRRVHRREQDRDVHLSKALSYVLRHGALKLGLPMGADGFVPLGALLQLPQFHSFSVEDVQRVVDTNGKQRFALQPGDPSTGPLIRANQGHSLQVPELELMPIETPQALPLTLVHGTFWKHWPSILLKGLSCCGRTHIHLAPGLPGDPGVISGMRPNCEVAVFINGPLALADGIPFFHSANGVILTPGNADGVLLPKYFKEALQLCPTRKPLSLADDKDTEGQRGPKHSPRRRKMTQQ | Function: Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate.
EC: 2.7.1.160
Catalytic Activity: 2'-phospho-[ligated tRNA] + NAD(+) = ADP-alpha-D-ribose 1'',2''-cyclic phosphate + mature tRNA + nicotinamide
Se... |
A0A2E0BLU0 | MILSIIQYPDPVLRSLCTPILEVSKEIKTIINDMYDTLYEASGRGLAGPQIGISNRLFVMDINWKNGISEPVTMINPEILFKSNETQVNEERCLSIPETPVKVERPYTIEVMWMDEECKLNRNRFEGISAAIICHEIDHLDGKLIMDK | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
A0A2E0BG59 | MRDQEKITKLLEQLVTRSFKFNQNHNLFQRKTKEEIYKKDVLECLEINEHIIKDDKILDIGSGGGFPGLVIGITNPNNKIDLVESNQKKCYFLKQIQHDLGLKNVAILNKRIEKNNMFGEYDLITARAFASIEKITSLTKTNINQNTRYVLFKGTKIKIEEELLALNTNKFKYEIINQGNQKKERHFVKISLNE | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.170
Subcellular Location: Cytoplasm
Sequence Length: 194
Sequence Mass (Da): 22... |
A0A923Q4X6 | MASSKREKELARQRAERQAARRAAATQRTKQRNLVIASAVAVAVVAVAAISLGVVSRGGKTDVVATAGQSAEPVASVAPSADASSGASPAAGVSPAANAPGTCTYEPTSEPAAKKVGLPPTSDVEFKQEFTVTLATNRGDIVFDMPSAEAPCTANSLRSLAHFAYFDNTPCHRLTTQGISVLQCGDPSGTGGGGPGYQFADENLKGATYPRGTVAMANAGPGTNGSQFFLVYADSSLPPNYTPFGTITKGLDLLDTVAKAGSDDSNGAGDGKPKLPVEIKTLRVTPKAA | 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: 289
Sequence Mass (Da): 29412
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A0A1D6FIR4 | MKKIEDNNTLVFIVDLKADKKIKAAVKKMYDIQAKKVNTLIRPDGKKKAYVKLPCKHPSDFPSLPSMSLSPAGSNRPFHTPLAPHPRWCLGMGVAYETTKSGVGVASMGVMRLKLVMKSIVLIVMARVLGIYDLIIAAIISAGINPKAKPKPYFLDGYAHLSFELACSLAGLVAGMAISIVRDTRV | Function: Binds to 23S rRNA.
Subcellular Location: Plastid
Sequence Length: 186
Sequence Mass (Da): 20221
Location Topology: Multi-pass membrane protein
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A0A6P3ZF99 | MTGVIKKFFIVSMLIWIAPIAILFGFNQHWLAGSTHMSPYSLTLVSGLLAVVSVNIVIAFYIYMAIKEPSDKHEPDPSFLANAKATVSRSTVDTDISSQSSKKQE | Function: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 105
Sequence Mass (Da): 11548
Location Topology: Multi-pass membrane protein
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A0A6L8C2A9 | MIGKISGIIDFIGSDFVLLDVNGVGYEVYCSTNTLNSLPSPGEQITLFTDLLVRQDLLQLTGFKNLNERSFYRELLTVQGVGMKGALSIVDTIGVTASIRAISMDDWQPFKSAPTIGPKIAQRIVLELQPKISKLLILGGESVDSQTTRVQSGKNTESKESEESKKYNREAQIRTEALSALVKLGYSESVAAGVLTQIILESDEPTTESLIKESLQRLSSL | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A0A432Z8D9 | MSTAANSKAIEAGQIWDFPGGIHPPQRKELSNQTPIAKLPLANTYVVPVKQHAGAPAELCVSVGEQVLRGQPLTRAGVSLGLPVHAPTSGTVTSIGPGRIAHPSGMTDVVVRIEADGNDTPAPPQPLPDYRQAARADVLERLRNAGIAGLGGAGFPTAQKLALQRPIDYLIINGIECEPYISADDRLMREHAATILDGAAILMHLADAKKALIAIEDNKPEAIAAMKAELTDYPNMSLRIVPTKYPSGGEKQLIQLLTGRQVPSKGLPIDIGLLMQNVGTAYAVSRAIRQGEPLIERVVTVTGEAVEKPGNYWVRLGTPV... | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell inner membrane
Sequence Length: 537
Sequence Mass (Da): 57988
Location Topology: Peripheral membrane protein
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A0A257TMW5 | MAVMRPATRPSWRKGMDVPNNSETLVSHRGGRGRSAGRCWATALVLAAAVLGARNAPADEKAAPDKPVEKLNGKLVICGGGVLPVQLRNRFLELAGGAVARVVVVTTASVYADTDKMQAKLAFWHEQKLASLTVLHTRSRQTANEPTFAQPLREATGVWFIGGNQNWLTETYLGTLTEQEIRGVLCRSGVVGGTSAGAAIMSPVMIRRDKPQLEVGPGFGFLPGTVVDQHFLKRNRQGRLLKVLDLYRNLVGLGIDEGTGVVVEGKHISVVGESQVIVCSPATSNGPESVQSLDPGAEADLDELRTLVAQVVTKPQITTS... | Function: Exopeptidase that catalyzes the hydrolytic cleavage of multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer) into aspartate-arginine dipeptides.
EC: 3.4.15.6
Catalytic Activity: [L-4-(L-arginin-2-N-yl)aspartate](n) + H2O = [L-4-(L-arginin-2-N-yl)aspartate](n-1) + L-4-(L-arginin... |
H0WZC4 | MALSRGLPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSNIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIIAYHDSVMNPDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECHPKPTQRTFPGCTIRNTPSEPIHCIVWAKYLFNQLFGEEDADQEVSPDRADPEAAWEPTEAEARARASNEDGDIKRISTKEWAKSTGYDPIKLFTKLFKDDIRYLLTMDKLWRKRKPPVPLDWAEVQSQGEETNASDQQNEPQLGLKDQQVLDVKSYAS... | Pathway: Protein modification; protein sumoylation.
Function: The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2... |
W6K7T8 | MTQTAVLELGRDSMYVIFKLALPIMLAGMGIGLVIALFQALTSLQEMTLTFVPKIVVIFAALVMFLPFMMTTMIEFGNKIFDIIISL | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 87
Sequence Mass (Da): 9649
Location Topology: Multi-pass membrane protein
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A0A3S3SA32 | MNYAFYVLTSYGVAAAMTLCLIAWVWLDGRARRRELAELEASGIRRRSFQPKTEPAPPSNGRETKA | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 66
Sequence Mass (Da): 7446
Location Topology: Single-pass membrane protein
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A0A6B3C8H6 | MSATLASLLTTLEPTWCVEIHERLDAPALESSNPWNNAGTGHAALCELNYTPERPDGSVDISKAVRINEQYELSRELWHHLAAAGRLPGAERAVTTTPHMSFVRGAKDVEHLRKRWEALR | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; oxaloacetate from (S)-malate (quinone route): step 1/1.
EC: 1.1.5.4
Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Sequence Length: 120
Sequence Mass (Da): 13396
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W6K8Z4 | MRLKVLSVVSALMLVAACSSTPEESAKMEGTGGQSGAGNSGSTMETKPMGPMMGSADEFVVSVGDTVRFGYDRYDLDAAAQTTLEAQAAWLKRYPGVTVTIEGHCDERGTREYNIALGDRRASAAKDYLVALGVNGNRVKTVSYGKERPVALGHNEQAWGQNRRSVSVVTGGANS | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Subcellular Location: Cell outer membrane
Sequence Length: 175
Sequence Mass (Da): 18495
Location Topology: Lipid-anchor
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A0A314VR96 | MYGRTKGRRLSKKQKLFLRNHGKDLIFDDGKMEEFLYETFGPKENIFDNKKVYLEIGFGSGEHLAHKAERHKESKFIGCDYYLNGIASTVIKISEKELSNVSLFNGDAIKLLXKIPNKSLYEVYLLYPDPWPKVRHXKRRFISDQNLRLLASKLIDGGVLKVVTDSDXYFXHIKSVVLTQKXSKXFSFKGXDFSXPWKXWHSTKYEEKAKKAGRRSYYMVLKKXIVXSHI | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
EC: 2.1.1.33
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 230
S... |
A9F4S2 | MRFVFVMDPLSRVTHDKDTSFAFIRAAQARGHESFHCLPRDLSIEGGEAHASASPVLIGDAPPFISLAAGPERLRLADVDAIFIRKDPPFDRSYLYATLILERARRCPLIVNDPRGLRDANEKLYALNFPEWTPRTLVTADREQIHAFVRALGGTAVIKPLDGAGGLGVLQINERDKNARAIADMMTNEGHRLAMVQEYLPAVVHGDKRVLLLDGELLGAILRVPRDDDHRSNIHVGGRVVSTELSPRELDLVRAVAPRLRADGLFFVGLDVIGERLTEVNVTSPTGIQELGRFTGADPAARVIAWAEERARGQAARA | Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.
EC: 6.3.2.3
Catalytic Activity: ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + glutathione + H(+) + phosphate
Sequence Length: 318
Sequence Mass (Da): 34951
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A0A0G1IWX9 | MCLKNNMSQVFYRKYRPQRFEDVVGQENTIKILKNAVSKKRVAHAYLFSGPRGTGKTTVARILARETGSYEEDVIEIDAASSRGIDEARALREAVRTVPLRSKYKTYIIDEVHMLTKESFNALLKTLEEPPEHAIFILATTEPAKVPDTIISRTQHFQFNKVAIPDIVKELEKISLEEKLTTEDDVLKLIAFFADGSLRDAENILFQIASLGEKNIKEADVRTLLGAPEEESVEKIIKIAFEKNVEEVLKLLDKVLEEGIDPALLGKLLLRSLRAIYFLALDPKTERMLEREFSGDEITEFKKMVPSEAGRAEHALHQIM... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 347
Seq... |
A0A2D8CJ61 | MPDLLIQNISQIATPKPGVLRGSELRSLNVIQNGAIYISDGVIKSVGSLSEVLEQVEGHPTILDAEGKAAVPGFVDSHSHLVFGGNRADEFAMRSAGMSYEEIADQGGGIVSTVEATQLATKEQLKDVARIRLQKALKQGITTMEIKSGYGLNLDNERKMLEVINELKEEQPVELSATFLGAHAVPKNSTKEEYLEDVLAMIPEVAELADYCDVFCEDGYFTVDESRRILEKGLEYRLKPKLHTNQFNDIGGVEMALSLNAISVDHLEVLSEEDIERIARSNTVATVLPGVSYFLNIPYSPARKLLDRGALVALATDFNP... | Cofactor: Binds 1 zinc or iron ion per subunit.
Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
Function: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is t... |
A0A316FSB0 | MPNRSDERVVTPGLLRDWPLPSPGGDKTSRGTVLVVGGARCTPGAVLLAGVAAMRAGAGRLQLVVAEESAVPLSISVPEAKVVGLAPEGIPSDQVLEMAAGADVIALGPGLDDIDRALELMGSVLGAAGEDTAVVLDAYALGALSKDAGLLRQSRAVLTPNLVEAGHLLGREPGDDLAAAARELADRHDAVVSLYGHVAAPGGGAWREESGDSGLGTSGSGDVRAGIVAGLLARGAEPAQAACWGAFAHAVSGQRLAPRYGRIGYLARELLDEVAFTIASV | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
A0A2D7GD77 | MKVVLVNPEIPHNTGSIGRTCVALELELILIKPYGFSLEEKTVSRSGTRYWKNVNLSEYENWKQFLNCHQPRRDHLYFFEEYGKKSFYSPDYQLEAYLVFGCESVGLSKDILDGMADRMFQIPMLNHAVKSLNLANAATAAIYQAMKGQFSKR | Function: Methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH of the wobble nucleotide.
Catalytic Activity: 5-carboxymethylaminomethyluridine(34) in tRNA(Leu) + S-adeno... |
H0WNW7 | MASDGNQSIGATEFILAGFPNLNSTTKELFSVFLLIYLLTLTGNVLIVGVVRADTRLQIPMYFFLGNLSCLEILLTSVIIPKMLSNFLSRQHTISFAACITQFYFYFFLGASEFLLLAVMSMDRYLAICQPLRYPLLMSGPVCFRVALACWVGGLLPVLGPTVAVALLPFCKQGAVVQHFFCDSGPLLRLACTNTKKLEETDFVLASLVIVSSLIITAVSYGQIVLAVLRIPSAAGRQKAFSTCTSHLMVVTLFYGSAIFLYVRPSQSGSVDTNWAVTVITTFVTPLLNPFIYALRNKQVKEALKDMFRKVVGDFLGHFF... | Function: Odorant receptor.
Subcellular Location: Cell membrane
Sequence Length: 331
Sequence Mass (Da): 36526
Location Topology: Multi-pass membrane protein
|
H0XEI7 | ETSARSLAKGSAPPGPVPEGLIRIYSMRFCPFAKRTLLVLKAKGIRHEVININLKNKPEWFFKKNPSGLVPVLENSKGQLIYESAITCEYLDEAYPGKKLLPEDPYEKACQKMVFELFSKKMERCWRIKKKKNSNEIHSTVQKGNEKNNLTWLGAVLANKKTKFFGGNSLSMIDYLIWPWFERLEASELNECIDSTSKLGLWMAVMKEDPTASALLIDAKSYKGFIDLYLQNSPEACDYGL | Function: Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA).
EC: 1.20.4.2
Catalytic Activity: 2 glutathione + H(... |
A0A642UUM6 | MNDSLAKRTTASSRSFDPESLTSSSVAVSPAVPKPSWLVWFVTNWLVTDPELYERYNLAKRSYQTNQTRYIYICGGRWRSAKQKPINVACGVLIVAPGVLFFIFEASWMWHHINAAIPFIFAYLWLATLSFFLRSSMSDPGAFPKNIHLPQTPYEKKITIPDEYENIIKLPWIDRTKGVTVKYCPTCKIWRPPRVSHCASCDICVINHDHHCVFLNNCVGKRNYRYFLWFLLSAVVTTLFMAIMSFVHIFWYLISDNDTHTIKSFGGSLSKYPVSFLLVIYGILASGYPLLLLVFHLFLTAQNLTTREYLNYVRGDHDPD... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 371
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 42746
Location Topology: Multi-pass membrane protein
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F7UZM3 | MIIGIGTDILEHEQLAALDGKWDDAFFRRTFTPAEHAEALASTNPLHYFAGRFCVKESVIKAFNGWAETAQMKDIETLSDPTGEPRVYMRGALEGVLPDDTHVHVSISHDKHFSVAFVVGERP | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 123
Sequence Mass (Da): 13681
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A0A3B3IM82 | MRLDWMGPPRCVLLLLLLQLLQVQSRPTVEDPDPDAVKSSEDEEDDESSSEENKLSNELSASSENLQPMAPQWVMPEKMEKQLHAVPASMTVRFRCPATGNPVPTLHWLKNGEEFSRDQRIGGFKIKDHTWSLIMESVVPSDEGNYTCVVENEHGSLRHTYQLDIVERSPHRPILQAGLPANQTAVVGGDAQFVCRVFSDPQPHIQWLKHIVVNGSREGPEGHSFVQVLKTAGLNSTDKEMEVLTLRNVTLEDAGVYTCLAQNSIGMSYHSAWLTVLSEPPPSAVPSQTFLDIFFYCLGFSVIIVLAIAAVICRLYCTPK... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
EC: 2.7.10.1
Subcellular Location: Cell membrane
Sequence Length: 740
Sequence Mass (Da): 82931
Location Topology: Single-pass type I membrane protein
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A0A1D6EH22 | MASDNRASVFPFAAAVLVVLLAGGAAADDASSDDDAGTSRTPGCSNKFQLVKVKNWVNGTEGTTFVGLSAKFGAPLPRDIHEAKKSFAVLSNPIDCCSNLTSKLTSSVAIATRGECAFTEKANIAQASGSTGLLVINDNEELYKMVCGENDTSINVTIPVVMIPQSAGKKLKNLLHHGASVEVQLYSPNRPTVDLSACFLWIMAVGTIVCASLWTEFVTCEQVDERYNQLTRKDGPDTGTKYREDKEVFEISAKGAFIFIIVASVFLLLLFYFMSSWFVWVLIVLFCIGGIEGMHACLVTLLARIFKDCGQKTVQLPVLG... | Function: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane.
Subcellular Location: Endosome membrane
Sequence Length: 423
Sequence Mass (Da): 45798
Location Topology: Multi-pass membrane protein
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A0A2P7QFH2 | MLRPTPKRCGRCAAASRPARARPDSIEGQDQVTRIVVLPGDGIGPEVTNEAISCLEMLSDHFELGLRFEEHPFGGAGIDAHGDPLPETTLHACRNSDAVFLGAVGGPKWDKAEKRPEVGLLGLRSALGLFANLRPSRVIPGLESFSPLKASIATGADVLVVRELTGGLYFGERTQSDDFASDLCTYSRVEVERIAHVAFQEARRRGSKVTSVDKANVLATSKLWRRIVEEVAAGYPDVTLDHMYVDAAAMALVSAPGRFDVILTENLFGDILSDQLSVIGGSIGLLGSASRGADGPMMFEPIHGSAPDIAGLDIANPAGA... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylate... |
A0A0B4Y1S6 | MTQPSSTIPFQPVLIVAGPTASGKSALALDLADAFDGVVINADSMQVYKELRVLSARPDDSEIARAPHRLYGVLSGREACSAGKWRDMAMAEIAECHASGKLSIITGGTGMYLNALTEGIAPIPDIPAGIRDQVTAELEKDGHQAFFEAFAKRDPDTAATLDPSNTQRLIRAAEVLAGTGRGVAAWHREPMVTPPDGMVFKKLCYMPPRDILYDRCNRRFDLMIEQGAIEEVRGLLAENLPETAPVMKAVGVREIAAYLAGEIDLESAKEKSQRETRRYAKRQLTWFRHQMSDKEIIDTQYSESLAGKLRNDVHQFLLTT... | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylall... |
A0A142B714 | MKVGIAGCGQLSRMLALAGWPMGMQFSFLADPNEPVRCVEGLGEIVRQDGTMTARDIYGALGNPDVITIERESVCVPLLIQLKSFCQVYPDPDIVWTIQNRHREKTLVSSLGIPLSPWAVFREQESVNKAIASIGGLPVVIKSTEDGYDGHNQWVIDSDEQLQAFEKERDAQLADATYKGIHEWIVEKKIAFEREISVIGARSPDGNIVIYTPGQNTHSNGILIHSVIPAPGLPDSLHAKARDYVSRLLQDTEYVGVLAVECFVTGDELLVNELAPRVHNSGHWTMDGAATSQFENHMRAIAGLPLGDSAHCGDVMGMYN... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
Function: Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimid... |
A0A923RF76 | MIRRALLALLRGYKKYISPALGNNCRFLPTCSEYAMQAIQTHGVLKGGLLSLWRILRCNPLGRYGYDPVPPRGRWRSDERDLKKPR | Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular Location: Cell membrane
Sequence Length: 86
Sequence Mass (Da): 9944
Location Topology: Peripheral membrane protein
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A0A2D7TLJ3 | MRLTNYINNKLYFSSLDLASIASQFGTPAFVYCQDTIERNFLEYKTAFQNSNHLVCYAVKANSNLSILKLLKNLGSGFDIVSGGELHRVIQIGADPKKIIFSGVGKSAQEIETAIINDVGSINIESEDELDLVVQIAKQKQVQASVSLRVNPNVDPKTHPYIATGLKSSKFGVPIENAIDIYKKMAKNKYLKIIGVACHIGSQLQELNPFEQSIREIMQLVRKIEANGIKIGRVDCGGGLGISYSGEALPHIQELVAIMKKEIPSKHVIAIEPGRSIVGKSGVLLTKIEYIKQGSEKNFAIVDAAMNDFIRPSLYQAEHE... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
Function: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
EC: 4.1.1.20
Catalytic Activity: H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine
Sequence Le... |
A0A3B9K4W2 | MITRVLKVSDSDPFTKEDLRAIGAAAEVICHGGLVGFRTETVYGLGGNALDATASARIYAAKGRPSDNPLIAHVCDMAMVEEITEEIPETGKKLAETFWPGPMTLIFKKNDRVPLETTGGLQTVAVRMPSDRQAAELIRMAGVPIAAPSANTSGRPSPTRAEHVYQDLNGKIEMILDGGQTGIGLESTIVDVTGEVPMLLRPGAITMEMLREAVGEVAVDPAITGPMNPAVHPKAPGMKYRHYAPKADLTLVEGETEKVIARICALAA | Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate
EC: 2.7.7.87
Subcellular Location: Cytoplasm
Sequence Length: 268
Sequence Mass (Da): 28467
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A0A963UFL7 | GTLGILIPPSISLIVFGAMTDQSIGQLFLGGVIPGIILTAAYMLYIALRIRLSPTLVSGDVTARKQSWQACFRSLAKTWPVVVLFVGVLGSIYSGIATPTESAAIGCALTFAIAAVHRLLNRDVMARVLAGSVKTTAMVLCIYWAAKLMGIYLTYDQITARLSAVVLDLGLSPFATLLALVLFYLVLGMLMDGLAAMVMTLPLTFPIVVSLGFDPIWYGVLLTMLIECGLLTPPVGMNLFILQGLRPEYPFGVLVRGAFPFFVALLVVVAAVTAFPGLVTYLPHLFYH | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 288
Sequence Mass (Da): 30889
Location Topology: Multi-pass membrane protein
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A0A2A4ZNM4 | MPKHTVLIAGPTASGKTGLALKIAARNGGIIINADALQVYTKWRVLTARPTGAEMARAPHHLYGHVNEVQDYSVGRWIKEVSDLLNETEQSAIIIGGTGLYFAALLNGLSSIPPISAEIRSSGNEHREREGLAWFLEKLSQNDPETLLKLDQNNPARLQRAWEVLEATGRGLSYWHARPTRPTINIEETVPILLNWQVNDLNSRINTRFDNMIKSGAIEECETAKVAGFNAKLPANRAIGAKEIIDALDGKIAMQDAVIKSQTLTHQFAKRQRTWFRSKMKHWQHIEMSDAPDLDAIVSTLPR | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylall... |
A0A162ILW8 | MKLLDGKKVSAEIKEELKSKIREEKERSGRVPGLGIIQIGHNEAASVYVQSQLKGSRALGMESYLYSFDDSVEEETVLKKIKELNQTEEIDGIILQLPLPKHISHSRILQAIDVNKDVDGFKTENIGRLHLGEEGFNPCTPEGVIALLKKYDIEIASKNVTIIGRSNIVGKPMFGLFINHNATVTICNSLTKNLKEHTERADIIVVAVGKEKFLTADMVREGAIVIDVGINRSREGKIVGDVDFEAVAPKASYITPVPGGVGSMTVAMLFQNIWKAFIRNRRIINGEKNKGE | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate +... |
A0A1H4XTV7 | MLCAFRENGTELPDGSGASRGAGSGEPGAPGALWSAGVRPVRKAARTVVRAGAPGVMGAASARFAALHRNTTSLVNAVREELHDPLTPVLALGAAASAAVGSGVDSFLVVSVMAGNAVISGAQRLRAERSLRGLLLSERMNGRLVDWAPAMSLADGVAADREVFFAGLTAAPVRTVAAEELRVGDIIALRPSDVVPADARLLVSDRLELDEAGLTGESGPVAKDPAATPGADLADRSCMVYEGCTVLAGTGYAVVVAAGPQTEAGRAAELAGHATAPIGIEGRLAALTKVALPATGLGGAAVTLLGLMRGVPVREALSTG... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Subcellular Location: Cell membrane
Sequence Length: 664
Sequence Mass (Da): 66991
Location Topology: Multi-pass membrane protein
|
G9J4P6 | VTFINRWLFSTNHKDIGTLYLLFGAWAGMAGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGSPDMAFPRMNNMSFWLLPPSLLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTAINMKPPAISQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILIL | 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-cytoc... |
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