ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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D2Y499 | MKLTTVLIVAVLVLAACQFTVTDNSGDDTENPSLRSAGENQNPDSTKTITARATRARTNMRRGLSRPSKGCIGGGDPCEFHRGYTCCSEHCIIWVCA | Function: Probable neurotoxin with unknown target. Possibly targets ion channels.
Sequence Mass (Da): 10448
Sequence Length: 97
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P0DQD4 | CKGKGASCRRTSYDCCTGSCRLGRC | Function: Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels. This toxin blocks N-type calcium channels (Cav2.2/CACNA1B). It shows a higher potency when Cav2.2/CACNA1B is only expressed with the ancillary subunit CACNB3 (IC(50)=0.1 nM) than on Cav2.2/CACNA1B expressed with... |
O06994 | MSEWWKEAVVYQIYPRSFYDANGDGFGDLQGVIQKLDYIKNLGADVIWLSPVFDSPQDDNGYDISDYKNMYEKFGTNEDMFQLIDEVHKRGMKIVMDLVVNHTSDEHAWFAESRKSKDNPYRDYYLWKDPKPDGSEPNNWGSIFSGSAWTYDEGTGQYYLHYFSKKQPDLNWENEAVRREVYDVMRFWMDRGVDGWRMDVIGSISKYTDFPDYETDHSRSYIVGRYHSNGPRLHEFIQEMNREVLSHYDCMTVGEANGSDIEEAKKYTDASRQELNMIFTFEHMDIDKEQNSPNGKWQIKPFDLIALKKTMTRWQTGLMN... | Function: Hydrolyzes various disaccharides such as sucrose, maltose, and isomaltose with different efficiencies. Also hydrolyzes longer maltodextrins from maltotriose up to maltohexaose, but not maltoheptaose, palatinose, isomaltotriose, or isomaltotetraose.
Catalytic Activity: Hydrolysis of (1->6)-alpha-D-glucosidic l... |
O34364 | MKTDWWKDAVVYQIYPRSFQDSNGDGIGDLRGIISRLDYIKELGADVIWICPIYPSPNVDYGYDVTNHKAIMDSYGTMDDFHELLDQVHQRGLKLVMDFVLNHTSVEHPWFKEAELDKNSKYRSYYYWRPGTKNGPPTDWLSNYGCPVWQYEEHTGEYYLHMNAVKQADLNWENPEVRQAVYDMMKFWLDKGVDGLRIDQLHLISKKEYLPSYEDYINQQAEPKPFQPNGERIHDYLKEITDEVFSHYDVMSVGEVGSVTPEEGLKYTGTDKHELNMIFHFQHMELDQQPGKEHWDLKPLELSDLKSVLTKWQKKLEHQG... | Catalytic Activity: Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
Sequence Mass (Da): 65816
Sequence Length: 561
Subcellular Location: Cytoplasm
EC: 3.2.1.10
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O05242 | MKKAWWKEAVVYQIYPRSFKDSNGDGIGDIQGIRTKLSYIKELGADVIWICPLYDSPNADNGYDIRDYQNILSEFGTMEDFDELLGDIHDLDMKLIMDLVVNHTSDEHPWFIESRSSIHSEKRDWYIWKDGKNGKTPNNWESIFGGPAWEYDQKTSQYYLHLFDKKQPDLNWENEKVRNAVYDMINWWLDKGIDGFRVDAITHIKKKEGFPDMPNPKGLDYVPSFPYHMNADGIMDLLTELKENTFSRYPIMTVGEANGVAAKEAADWAGEKNGIFSMIFQFEHLGLWDVEINESIDIVAFKRILTDWQDSLEGIGWNAL... | Catalytic Activity: Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
Sequence Mass (Da): 63969
Sequence Length: 554
Subcellular Location: Cytoplasm
EC: 3.2.1.10
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P21332 | MEKQWWKESVVYQIYPRSFMDSNGDGIGDLRGIISKLDYLKELGIDVIWLSPVYESPNDDNGYDISDYCKIMNEFGTMEDWDELLHEMHERNMKLMMDLVVNHTSDEHNWFIESRKSKDNKYRDYYIWRPGKEGKEPNNWGAAFSGSAWQYDEMTDEYYLHLFSKKQPDLNWDNEKVRQDVYEMMKFWLEKGIDGFRMDVINFISKEEGLPTVETEEEGYVSGHKHFMNGPNIHKYLHEMNEEVLSHYDIMTVGEMPGVTTEEAKLYTGEERKELQMVFQFEHMDLDSGEGGKWDVKPCSLLTLKENLTKWQKALEHTGW... | Catalytic Activity: Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
Sequence Mass (Da): 66013
Sequence Length: 558
Subcellular Location: Cytoplasm
EC: 3.2.1.10
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Q60881 | MANKNNVTELIFTGLFQDPEVQKVCFVLFLPVYLATLLGNSLILVAVSISKTLHSPMYFFLSSLSLVEICYSSTIVPKFITDLLAKVKTISLKGCLTQIFFSHFFGVVEVILLVVMAYDRYVAICKPLHYMNIMSRQVCHMLVAGSWLGGFIHSIIQIIITIPLPFCGPNVIDHYFCDLQQLFKLACTDTFMEGFIVMANSGLISIVSLFILVSSYAVILISLRKRSAEGRRKALSTCASHITVVILFFVPGAFIYMRPSSTFTEDKLVSVFYTVITPMLNPIVYTLRNTEMKNAIRMSWKQKDS | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34312
Sequence Length: 305
Subcellular Location: Cell membrane
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Q60878 | MDSPRNVTEFFMLGLSQNPQVQRMLFGLFLLVFLVSVGGNMLIIITITFSPTLGSPMYFFLSYLSFIDTCYSSCMTPKLIADSLHEGRAISFEGCLAQFFVAHLLGGTEIILLTVMAYDRYVAICKPLHYTTTMTRHVCIVLVAVAWLGGILHSTAQLFLVLQLPFCGPNVINHFVCDLYPLLELACTDTYVIGLLVVANSGVICLLNFLMLAASYIVILRTLRSHSAEGRRKALSTCGAHFTVVALFFVPCIFIYMRPSSTLSIDKIVAVFYCILTPMFNPLIYTLRNAEVKNAMKNLWRK | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33734
Sequence Length: 302
Subcellular Location: Cell membrane
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Q8NGJ6 | MSIINTSYVEITTFFLVGMPGLEYAHIWISIPICSMYLIAILGNGTILFIIKTEPSLHEPMYYFLSMLAMSDLGLSLSSLPTVLSIFLFNAPEISSNACFAQEFFIHGFSVLESSVLLIMSFDRFLAIHNPLRYTSILTTVRVAQIGIVFSFKSMLLVLPFPFTLRNLRYCKKNQLSHSYCLHQDVMKLACSDNRIDVIYGFFGALCLMVDFILIAVSYTLILKTVLGIASKKEQLKALNTCVSHICAVIIFYLPIINLAVVHRFARHVSPLINVLMANVLLLVPPLTNPIVYCVKTKQIRVRVVAKLCQRKI | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35256
Sequence Length: 313
Subcellular Location: Cell membrane
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Q9Y5P1 | MWPNITAAPFLLTGFPGLEAAHHWISIPFFAVYVCILLGNGMLLYLIKHDHSLHEPMYYFLTMLAGTDLMVTLTTMPTVMGILWVNHREISSVGCFLQAYFIHSLSVVESGSLLAMAYDCFIAIRNPLRYASILTNTRVIALGVGVFLRGFVSILPVILRLFSFSYCKSHVITRAFCLHQEIMRLACADITFNRLYPVILISLTIFLDCLIILFSYILILNTVIGIASGEERAKALNTCISHISCVLIFYVTVMGLTFIYRFGKNVPEVVHIIMSYIYFLFPPLMNPVIYSIKTKQIQYGIIRLLSKHRFSS | Function: Odorant receptor.
PTM: Ubiquitinated by the CRL2(FEM1A) and CRL2(FEM1C) complexes, which recognize the -Lys-Xaa-Xaa-Arg C-degron at the C-terminus, leading to its degradation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35373
Sequence Length: 312
Subcellular Location: Cell membrane
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Q9Y5P0 | MWYNNSAGPFLLTGFLGSEAVHYRISMSFFVIYFSVLFGNGTLLVLIWNDHSLHEPMYYFLAMLADTDLGMTFTTMPTVLGVLLLDQREIAHAACFTQSFIHSLAIVESGILLVLAYDCFIAIRTPLRYNCILTNSRVMNIGLGVLMRGFMSILPIILSLYCYPYCGSRALLHTFCLHQDVIKLACADITFNHIYPIIQTSLTVFLDALIIIFSYILILKTVMGIASGQEEAKSLNTCVSHISCVLVFHITVMGLSFIHRFGKHAPHVVPITMSYVHFLFPPFVNPIIYSIKTKQIQRSIIRLFSGQSRA | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34912
Sequence Length: 310
Subcellular Location: Cell membrane
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Q9H339 | MSSSGSSHPFLLTGFPGLEEAHHWISVFFLFMYISILFGNGTLLLLIKEDHNLHEPMYFFLAMLAATDLGLALTTMPTVLGVLWLDHREIGSAACFSQAYFIHSLSFLESGILLAMAYDRFIAICNPLRYTSVLTNTRVVKIGLGVLMRGFVSVVPPIRPLYFFLYCHSHVLSHAFCLHQDVIKLACADTTFNRLYPAVLVVFIFVLDYLIIFISYVLILKTVLSIASREERAKALITCVSHICCVLVFYVTVIGLSLIHRFGKQVPHIVHLIMSYAYFLFPPLMNPITYSVKTKQIQNAILHLFTTHRIGT | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35241
Sequence Length: 312
Subcellular Location: Cell membrane
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Q9H340 | MGLNKSASTFQLTGFPGMEKAHHWIFIPLLAAYISILLGNGTLLFLIRNDHNLHEPMYYFLAMLAATDLGVTLTTMPTVLGVLWLDHREIGHGACFSQAYFIHTLSVMESGVLLAMAYDCFITIRSPLRYTSILTNTQVMKIGVRVLTRAGLSIMPIVVRLHWFPYCRSHVLSHAFCLHQDVIKLACADITFNRLYPVVVLFAMVLLDFLIIFFSYILILKTVMGIGSGGERAKALNTCVSHICCILVFYVTVVCLTFIHRFGKHVPHVVHITMSYIHFLFPPFMNPFIYSIKTKQIQSGILRLFSLPHSRA | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35269
Sequence Length: 312
Subcellular Location: Cell membrane
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Q8NGF3 | MQKPQLLVPIIATSNGNLVHAAYFLLVGIPGLGPTIHFWLAFPLCFMYALATLGNLTIVLIIRVERRLHEPMYLFLAMLSTIDLVLSSITMPKMASLFLMGIQEIEFNICLAQMFLIHALSAVESAVLLAMAFDRFVAICHPLRHASVLTGCTVAKIGLSALTRGFVFFFPLPFILKWLSYCQTHTVTHSFCLHQDIMKLSCTDTRVNVVYGLFIILSVMGVDSLFIGFSYILILWAVLELSSRRAALKAFNTCISHLCAVLVFYVPLIGLSVVHRLGGPTSLLHVVMANTYLLLPPVVNPLVYGAKTKEICSRVLCMFS... | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35839
Sequence Length: 324
Subcellular Location: Cell membrane
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Q8TCB6 | MVDPNGNESSATYFILIGLPGLEEAQFWLAFPLCSLYLIAVLGNLTIIYIVRTEHSLHEPMYIFLCMLSGIDILISTSSMPKMLAIFWFNSTTIQFDACLLQMFAIHSLSGMESTVLLAMAFDRYVAICHPLRHATVLTLPRVTKIGVAAVVRGAALMAPLPVFIKQLPFCRSNILSHSYCLHQDVMKLACDDIRVNVVYGLIVIISAIGLDSLLISFSYLLILKTVLGLTREAQAKAFGTCVSHVCAVFIFYVPFIGLSMVHRFSKRRDSPLPVILANIYLLVPPVLNPIVYGVKTKEIRQRILRLFHVATHASEP | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35271
Sequence Length: 317
Subcellular Location: Cell membrane
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Q9H255 | MSSCNFTHATFVLIGIPGLEKAHFWVGFPLLSMYVVAMFGNCIVVFIVRTERSLHAPMYLFLCMLAAIDLALSTSTMPKILALFWFDSREISFEACLTQMFFIHALSAIESTILLAMAFDRYVAICHPLRHAAVLNNTVTAQIGIVAVVRGSLFFFPLPLLIKRLAFCHSNVLSHSYCVHQDVMKLAYADTLPNVVYGLTAILLVMGVDVMFISLSYFLIIRTVLQLPSKSERAKAFGTCVSHIGVVLAFYVPLIGLSVVHRFGNSLHPIVRVVMGDIYLLLPPVINPIIYGAKTKQIRTRVLAMFKISCDKDLQAVGGK | Function: Olfactory receptor . Activated by the odorant, beta-ionone, a synthetic terpenoid . The activity of this receptor is probably mediated by G-proteins leading to the elevation of intracellular Ca(2+), cAMP and activation of the protein kinases PKA and MAPK3/MAPK1 . Stimulation of OR51E2 by beta-ionone affects m... |
P14803 | DDIKLSQQYDVLDLFKYMHQ | Function: Putative receptor for octopamine. Octopamine (OA) is a neurotransmitter, neurohormone, and neuromodulator in invertebrates. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 2500
Sequence Length: 20
Subce... |
Q60856 | MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEA... | Function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA . The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L . The truncated form of the protein lacks antiviral activity .
Location Topolo... |
P00973 | MMDLRNTPAKSLDKFIEDYLLPDTCFRMQINHAIDIICGFLKERCFRGSSYPVCVSKVVKGGSSGKGTTLRGRSDADLVVFLSPLTTFQDQLNRRGEFIQEIRRQLEACQRERAFSVKFEVQAPRWGNPRALSFVLSSLQLGEGVEFDVLPAFDALGQLTGGYKPNPQIYVKLIEECTDLQKEGEFSTCFTELQRDFLKQRPTKLKSLIRLVKHWYQNCKKKLGKLPPQYALELLTVYAWERGSMKTHFNTAQGFRTVLELVINYQQLCIYWTKYYDFKNPIIEKYLRRQLTKPRPVILDPADPTGNLGGGDPKGWRQLA... | Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response . In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates (... |
F1N3B8 | MGSRESHLYEKPSEKLEEFIQNHLRPSEDCQKDIDQSVDTICEVLQEPCPSLTVTGVAKGGSYGRRTVLRGNSDGILVVFFGDLEQFQDQEKRQYELLSKIWAQMKHCESTWKLAAKMELQNTNRSSRVTIQLSTKQQSITFNVLPAFNALGLSEKSSLWSYRELKRSLDMVKARPGEFSVCFTELQEKFFSNYPSKLKDLILLVKHWFQKCQEKLINSSLLPPYALELLTVYAWEQGCGAEDFDMAEGVRTVLRLIEKQEQLCVYWTVNYNFGDEIVRNILLSQLQAPRPVILDPTDPTNNVSMDNTCWLQLKHEAQNW... | Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L ... |
P29728 | MGNGESQLSSVPAQKLGWFIQEYLKPYEECQTLIDEMVNTICDVLQEPEQFPLVQGVAIGGSYGRKTVLRGNSDGTLVLFFSDLKQFQDQKRSQRDILDKTGDKLKFCLFTKWLKNNFEIQKSLDGFTIQVFTKNQRISFEVLAAFNALSLNDNPSPWIYRELKRSLDKTNASPGEFAVCFTELQQKFFDNRPGKLKDLILLIKHWHQQCQKKIKDLPSLSPYALELLTVYAWEQGCRKDNFDIAEGVRTVLELIKCQEKLCIYWMVNYNFEDETIRNILLHQLQSARPVILDPVDPTNNVSGDKICWQWLKKEAQTWLT... | Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response . Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L... |
Q59327 | MSNVKKHVSTINPVGEVLDVGSADEVQWSDASDVVVVGWGGAGASAAIEAREQGAEVLVIERFSGGGASVLSGGVVYAGAVPATRRKPASRFTEAMTAYLKHEVNGVVSDETLARFSRDSVTNLNWLEKQGATFASTMPGYKTSYPADGMYLYYSGNEVVPAYGNPQLLKKPPPRGHRVVAKGQSGAMFFAALQKSTLAHGARTLTQARVQRLVREKDSGRVLGVEVMVLPEGDPRTERHKKLDELVAKSACIRRRVPRRVAVNVRRSRARSARSATSVPAKVWCCPLAAISSIRNCWSMRRYKPGWLTGAAGCDGSGLR... | Function: Involved in the degradation of steroids having an A:B ring fusion in a trans configuration. Catalyzes the elimination of hydrogens located at positions 4 and 5 and the introduction of double bonds into ring A.
Catalytic Activity: A + a 3-oxo-5alpha-steroid = a 3-oxo-Delta(4)-steroid + AH2
Location Topology: S... |
Q3ZAJ2 | MFDRVEIRIKSGDGGSGKVSFRREKFVPYGGPDGGDGGDGGNVYLEADSGLYSLLNFKHKRVHKAANGENGMGSRCTGHNGADLVIKVPVGTVATIVEENGQKRVLADLAADGDRTLVARGGQGGLGNTHFVSSTNQAPMLAQKGQPGGEYELILELKLIADVAIIGYPNVGKSSLLSLLTAAKPRVANYPFTTLSPVMGVVERTEGTFVMAEVPGLIEDAHLGRGLGHDFLRHISRTRMVIHLLDGTSDNPIDDMIKVNSELYLYDASLSERPQVVAVNKIDDELVQLRREELTETFKEAGLEVFFISALTGEGVEVLL... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
B1I5V8 | MFKDYAKIHVKAGDGGNGCVAFRREKYVPYGGPSGGDGGRGGHVILRADGGLRTLVDFRYRTHYKAGRGTHGQGKNMHGRKGEDLVLRVPVGTEVRRAGDATLMADLTVDGQEYRVARGGRGGRGNARFAAANRRAPSFAEKGEPGEELWLELELKLLADVGLVGFPNAGKSTIISKVSAARPKIADYPFTTLEPHLGVVRVGEGESFVLADIPGLIEGAHRGAGLGHRFLRHVERTRVLIHVVDVSGREGRDPVADFEAINRELAAYDPRLAARPQLVAANKTDLPGARDNARRLAEAAGGRYEVFEISALTGEGLDRL... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
B8J4L3 | MRFVDEARIQVRAGKGGHGCLSFRREKFVPRGGPDGGNGGDGGSVYLRADNRLLSLYDFRLKRLYEAQNGRPGEGSQCDGRKGENLVLNLPVGTLVYAEGPEGEVLVADLSEPDAEVLVASGGRGGKGNEHFKSSTMRAPRFSQPGEPGEEFNLRLELKILADAGLIGLPNAGKSTFISQVSAARPKIAAYPFTTLTPNLGVMIDEVDPDRRMVIADIPGLIEGAHEGQGLGLRFLKHVERTRFLVHILSIEDVGDEDPWAGFSLVNEELRRFDAELGERRQIEVVNKIDLVSPERLEALKERARADGREVYFISARDDL... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
A8ZRY1 | MKFIDEATITVSSGKGGRGCVSFRRERFVPRGGPDGGDGGSGGSLLFRVNPSKRTLYAFRSKKQFAAPNGAPGEGRQKTGKSGDDLVIEVPPGTLIFDADTGAIIRDMVSPEEDFVFLTGGRGGKGNKHFATSTHQTPRFAQPGEPAQTATVRLELKLLADVGLIGLPNAGKSTLLSVISAARPAIGAYPFTTLSPNLGMVTLAGAEPFAVADIPGLIEGAHTGAGLGIRFLKHIERTRLLVHLIDASAIDPADPVAPFRIINAELAMFSPALAERPQVVVLNKMDLTGAEALAQQFINAAGIKKCFLISAATRSGVEEL... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
Q6AK07 | MAFVDEAKFFVKAGDGGNGCVSFRREKFVPKGGPNGGDGGKGGDVIMVASSKVQSLIDFRYRSHFKAERGVHGQGRDMHGRGGKDCYMDIPVGSVVKDSETGRVLADLSEEGEEFVVAQGGSGGMGNPHFSSGSNRTPRVATKGKLGEEKWLLIELKLMADVGLVGLPNAGKSTLLSKLSAANPKVADYPFTTLEPQLGMLHFPMRNSCIIADIPGLVEGAHQGVGLGHKFLRHVERTKILVHVIDASADDPFSDYDIIGNELRSYKEELADRAKILVLNKCDEFDFDKDLLPDFIEARGLEPKNVLFISAITGEGVDKL... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
Q2GDW7 | MKFIDEVKVFLKAGNGGDGCSSFRREKFVEFGGPDGGCGGDGGNVIFITDENLNTLLDYRHRVHLKAENGKPGRKSNKRGESGSDLVCKVPIGTQILTQDRVLLSDLEQPKQSFISAFGGKGGRGNATFKNSLNRAATEFTCGEPGEEKTVILNLKILADIGLIGLPNAGKSTFLSRCSNAKPKIADYPFSTLEPIVGIAKINNHEIVIADIPGIIEGAHKNLGLGVKFLKHIERCKALIYLIDGTEKDIYSVYTLLSNELSLYSKKLEIKEHFILITKSDLLGKDEVQEKCQYIREKTGKLTLHTGIDQELASSLKAAQ... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
Q30XW0 | MRFVDEAVIKAISGNGGHGCVSFRREKFIPRGGPDGGDGGNGGNVVFKASTRLLSLYDFRLKRVYQAENGRPGQGSQMHGRGGKDLVVEMPVGTLVFERGENGAESLIADLSEPDVEVVIAHGGRGGKGNEHFKSSTMQAPRFSQPGEPGEEKSLRLELKILADAGLLGLPNAGKSTFISQVSAAKPKIAAYPFTTLVPNLGVMMDEFDPDRRMVIADIPGLIEGAHEGQGLGHRFLKHVERTRFLVHILSIEDVDMENPWAGFDLINDELQRFDETLGSREQIQVVNKIDLLPPEEVDGLRARAEADGRRIFFISALEG... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
B1ZZ37 | MFVDECVVKLQAGDGGRGCISFRREKYEPWGGPNGGDGGRGGDVILLGDDDTNNLVDYKYQPHWNAERGEHGLGKDQHGKDGAHRVLKMPLGTVVIDEATGKPVAEVVEDGQQIVLCKGGNGGWGNTHFKTATTRAPKRANDGHPGERGTYRLVLKSIADVGLVGFPNAGKSSLTCLITRARPRTAAYPFTTLHPQIGIIDYPPDRHGRRRLRLADVPGLIEGASENRGLGHRFLRHIERCALLLVLIDMAGTDGRDPREDYKHLLRELELYDPALLKKPRLVAANKMDVEAAAANLSKFKRRHRTVDVLPLSCLTSEGI... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
P95722 | MTTFVDRVELHVAAGNGGHGCASVHREKFKPLGGPDGGNGGRGGDVILTVDQSVTTLLDYHHSPHRKATNGKPGEGGNRSGKDGQDLVLPVPDGTVVLDGAGNVLADLVGHGTSYVAAQGGRGGLGNAALASARRKAPGFALLGEPGDLQDIHLELKTVADVALVGYPSAGKSSLISVLSAAKPKIADYPFTTLVPNLGVVTAGETVYTVADVPGLIPGASQGKGLGLEFLRHVERCSVLVHVLDTATLESERDPLSDLDVIETELREYGGLDNRPRIVVLNKIDVPDGKDLAEMVRPDLEARGYRVFEVSAVAHMGLRE... | Function: Plays an unknown essential role and a regulatory role in sporulation. Overexpression suppresses sporulation although cell growth rate was not reduced. Impaired differentiation was eliminated by addition of decoyinine, an inhibitor of GMP synthesis. Overexpression has no effect on undecylprodigiosin production... |
B1VXD8 | MTTFVDRVELHAAAGNGGHGCASVHREKFKPLGGPDGGNGGRGGDVILVVEQSVTTLLDYHHSPHRKATNGQPGAGDNRSGKDGQDLVLPVPDGTVVLDKAGNVLADLVGQGTTFVAGQGGRGGLGNAALASARRKAPGFALLGEPGESRDIVLELKTVADVALVGYPSAGKSSLISVLSAAKPKIADYPFTTLVPNLGVVTAGSTVYTIADVPGLIPGASQGKGLGLEFLRHVERCSVLVHVLDTATLESDRDPVSDLDMIEEELRLYGGLENRPRIVALNKVDIPDGQDLADMIRPDLEARGYRVFEVSAIAHKGLKE... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
B4SP14 | MKLVDEAEIEVFAGNGGNGCIGFRREKFIPLGGPDGGDGGAGGSVYIRADENLNTLVDFRHDRIFKAQRGENGMGRQAYGKGGEDLTITVPVGTVIINVATDEIIGDLTQHGDRLLVAQGGRGGLGNMHFKSSTNRSPRQALPGEPGEERTLKLELKLLADVGLLGFPNAGKSTLIRAVSAATPKVADYPFTTLYPNLGVVKVENYRSFVIADIPGLIEGAADGAGLGAQFLRHLQRTRLLLHLVDISPMEGGVEGISPVEQVRAIERELEKHDPELLQKPRWLVLNKADLMFEDEAKAAAEQIVAELGWKEPWFLVSAL... | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis ... |
Q561T9 | MAGIKALVALSFSGALGLTFLLLGCALEQFGQYWPMFVLIFYILSPIPNLIARRHADDTESSNACRELAYFLTTGIVVSAYGLPVVLARKAVIQWGAAGLVMAGNCVIFLTILGFFLIFGGGDDFSWEQW | Function: Involved in protein trafficking. May be involved in the down-regulation of membrane protein levels (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14130
Sequence Length: 130
Subcellular Location: Golgi apparatus membrane
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O15243 | MAGVKALVALSFSGAIGLTFLMLGCALEDYGVYWPLFVLIFHAISPIPHFIAKRVTYDSDATSSACRELAYFFTTGIVVSAFGFPVILARVAVIKWGACGLVLAGNAVIFLTIQGFFLIFGRGDDFSWEQW | Function: Negatively regulates leptin receptor (LEPR) cell surface expression, and thus decreases response to leptin. Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability.
Location Topology: Multi-pa... |
B9TRX0 | MAGVKALVALSFSGAIGLTFLMLGCALEDYGVYWPLFVLVFHALSPIPHFIAKRATYDSDATSSACRELAYFFTTGIVVSAFGFPVILARVAVIKWGACGLVLAGNAVIFLTIQGFFLVFGRGDDFSWEQW | Function: Negatively regulates leptin receptor (LEPR) cell surface expression, and thus decreases response to leptin/LEP. Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability (By similarity).
Locatio... |
A6WXF0 | MARQEQANDVFALTSFLYGGNADYIEELYAKYEDDPNSVDPQWRDFFAKLGDNADDVKKNAEGASWTRKNWPIAANGELISALDGNWAEVEKHVTDKLKGKAAKGEAKGATGAALTSEEITQAARDSVRAIMMIRAYRMRGHLHANLDPLGLSEKPNDYNELEPENYGFTPADYNRKIFIDNVLGLEYATVPEMLDILKRTYCGTIGVEFMHISDPAEKAWIQERIEGPDKKVAFTPEGKKAILSKLIEAEGFEQFIDVKYKGTKRFGLDGGESLIPALEQIVKRGGAMGVKEIIFGMAHRGRLNVLSQVMGKPHRAIFH... | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + ... |
P57388 | MDKNKIEYWLNSSWLSRENQNYIETIYKSFLTNAQSIDDMWHKAFLEFSEEQKNTYERNNTKNNKYLLIKKIDHMIHAFRSEGYQQSLIDPLKLKKRTKIHDLDLSFYNFTEEETRQTVEINFKNCTNFRTNIISLYKILYKKYCGSIGFEYMYVNNLLEKQWITNHIESFFNENVFTIEEKINFLKELTYAETLEKYIGKKFPGAKRFSLEGAETLIPVLHEVIRFSKKNNISKIVLGMAHRGRLNVLINVLNKSPKVLFDEFSNLNLFQKISGDVKYHMGGTAEIQYEKKIIFHMACNPSHLEIINPVVSGISRSYID... | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + ... |
Q89AJ7 | MYKNEFNSSWMSSFNSSYIDNLYNKFLLDPTSIDNSWYIVFTELSKENYINSTNKYLNNKFQDSKDTIKLTIELLINIFRTLGYKFAHLNPLDTFKNDNSLSLKKFLKSSEAFRIQDSYLVKLSQYVLDDITTKNVYDDYKNIYCKRIGYQFMHIHNSNEMNWIKNYIETKHSNILKKKKKIQILKHLIISEMLEKYFSSKFPSIKRFSIEGAESLIPMLKEVIKYTKKFNLHKIIFGMSHRGRLNVLANILDKPIKTIFNEFCENNSNNFNSGDVKYHMGFCCTKTIGLRKIILDLKSNPSHLEVINPVVVGSSRAYID... | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + ... |
P51056 | MPKITMQQFQKNSYLADNNAGYIETLYENFLKDPHSVNEEWRSYFRTLTNGASTPDISHATIREEFRELARKPRSISPTAITPAAEQAAVDLLIEGYRRFGHLNAKINPLGDNRPVDSRLELGHYNLTESDFNKTFATYGLLNKPKATLKEIYTRLREIYCGSIGVQYSTISDERERNWLRDYVEQRLPSIEFDKETKRNILQQLVTAESLEKYLDTKYVGQVRYSLEGGDSLIPLLDELTKRARHQKIEEIVICMAHRGRVNVLLNIMGQSAAELFQEFEGKKDYGLMSGDVKYHRGYSRDVKTDAGPIHLSLAFNPSH... | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + ... |
Q59106 | MMQQYQSNSYLFGGNAPYVEELYEAYLQNPASVPDNWRAYFDAMQNVPAVDGSNGRDIPHAPIVASFAERAKQGPIRTIVASADSDMGRKRVAATQLIAAYRNIGSHWADLDPLKRQERPPLPDLDPAFYGFSEADLDIVFNASNTYFGKESMSLRELLNNLRETYCGTIGFEFMYVSDQAQKRWWQERLETTRSKPVFTLEKKKHILDRLTAAEGLERFLHTKYVGQKRFSLEGGESFIAAMDELIQHAGSKGVQEIVIGMAHRGRLNVLVNTLGKMPADLFAEFEGKHVDDLPAGDVKYHKGFSSDVSTEGGPVHLSL... | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + ... |
Q54JE4 | MFTLKQVINKSIQTSMKNGVMSSAVKRSFSTVGGINQPKSRKELSESFLDGTSSTYVEDMFANWVKDPKSVHPSWASFFESSERGVPAGEAFMSPPTLGSSVATKATPSTYTSSGSPKQVSDSMRLLLLVRAYQVRGHALANLDPLGLEVKEEPAEFNPAKYGFTEADMDRPIFVGEGFISGFLTNKQPETTLRQVLKRLKETYCGDIGIEYMHIQDREMCDWIRDKFETSQPVEIPDKEKIKILERLSWADQFEGFLGLKYRATRRFGLDGCESLIPGMKAMIDTATEDGVESIVLGMPHRGRLNVLANVVRKPLPAIF... | Function: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Catal... |
P0AFG5 | MQNSALKAWLDSSYLSGANQSWIEQLYEDFLTDPDSVDANWRSTFQQLPGTGVKPDQFHSQTREYFRRLAKDASRYSSTISDPDTNVKQVKVLQLINAYRFRGHQHANLDPLGLWQQDKVADLDPSFHDLTEADFQETFNVGSFASGKETMKLGELLEALKQTYCGPIGAEYMHITSTEEKRWIQQRIESGRATFNSEEKKRFLSELTAAEGLERYLGAKFPGAKRFSLEGGDALIPMLKEMIRHAGNSGTREVVLGMAHRGRLNVLVNVLGKKPQDLFDEFAGKHKEHLGTGDVKYHMGFSSDFQTDGGLVHLALAFNP... | Function: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] + 2-oxoglutarate + ... |
O24457 | MATAFAPTKLTATVPLHGSHENRLLLPIRLAPPSSFLGSTRSLSLRRLNHSNATRRSPVVSVQEVVKEKQSTNNTSLLITKEEGLELYEDMILGRSFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGFIKLLTKSDSVVSTYRDHVHALSKGVSARAVMSELFGKVTGCCRGQGGSMHMFSKEHNMLGGFAFIGEGIPVATGAAFSSKYRREVLKQDCDDVTVAFFGDGTCNNGQFFECLNMAALYKLPIIFVVENNLWAIGMSHLRATSDPEIWKKGPAFGMPGVHVDGMDVLKVREVAKEAVTRARRGEGPTLVECETY... | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Catalytic Activity: (R)-N(6... |
Q7XTJ3 | MAAASSFTAAAKFLAPVSARSAGDYKPPLPLPASASLRPGRKPAPRLRTALAVSSDVLPGNKAAPAAAAHSAVTREEALELYEDMVLGRIFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGFIKLLNQADCVVSTYRDHVHALSKGVPARSVMAELFGKATGCCRGQGGSMHMFSEPHNLLGGFAFIGEGIPVATGAAFAAKYRHEVLKQSSPDGLDVTLAFFGDGTCNNGQFFECLNMAQLWKLPIVFVVENNLWAIGMSHLRATSDPEIYKKGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGEGPTLVECETYRFR... | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Catalytic Activity: (R)-N(6... |
P29803 | MLAAFISRVLRRVAQKSARRVLVASRNSSNDATFEIKKCDLYLLEEGPPVTTVLTRAEGLKYYRMMLTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHGVCYTRGLSVRSILAELTGRRGGCAKGKGGSMHMYTKNFYGGNGIVGAQGPLGAGIALACKYKGNDEICLTLYGDGAANQGQIAEAFNMAALWKLPCVFICENNLYGMGTSTERAAASPDYYKRGNFIPGLKVDGMDVLCVREATKFAANYCRSGKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKRDPIIILQD... | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
PTM: Phosphorylation at Ser-291, Ser-293 and Ser-298 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single ... |
P35487 | MRKMLTAVLSHVFSGMVQKPALRGLLSSLKFSNDATCDIKKCDLYRLEEGPPTSTVLTRAEALKYYRTMQVIRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPTDHVITSYRAHGFCYTRGLSVKSILAELTGRKGGCAKGKGGSMHMYGKNFYGGNGIVGAQVPLGAGVAFACKYLKNGQVCLALYGDGAANQGQVFEAYNMSALWKLPCVFICENNLYGMGTSNERSAASTDYHKKGFIIPGLRVNGMDILCVREATKFAADHCRSGKGPIVMELQTYRYHGHSMSDPGISYRSREEVHNVRSKSDPIML... | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldih... |
P35485 | DQNGKVVNEKMEPKLPKETLLKMYKTAVLGRNADIKALQYQRQGRMLTYAPNMGQEAAQIGMAAAMEPQDWNSPMYRELNTLLYRGDKLENVFLYWYGNERGSIKPEGVKILPTNIIIGSQSNIAAGLAMASKIRKTNEVTAFTIGDGGTAHGEFYEGLNFAASFKAPVVAVIQNNQWAISTPVRKASNSETLAQKGVAFGIPYIQVDGNDMLAMYVASKEAMDRARKGDGPTLIEAFTYRMGPHTTSDDPCSIYRTKEEENEWAKKDQIARFKTYLINKGYWSEEEDKKLEEEVLAEINDTFKKVESYGANVELIEIFE... | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl... |
P21881 | MAAKTKKAIVDSKKQFDAIKKQFETFQILNEKGEVVNEAAMPDLTDDQLKELMRRMVFTRVLDQRSISLNRQGRLGFYAPTAGQEASQIATHFALEKEDFVLPGYRDVPQLIWHGLPLYQAFLFSRGHFRGNQMPDDVNALSPQIIIGAQYIQTAGVALGLKKRGKKAVAITYTGDGGASQGDFYEGINFAGAYKAPAIFVVQNNRYAISTPVEKQSAAETIAQKAVAAGIVGVQVDGMDPLAVYAATAEARERAINGEGPTLIETLTFRYGPHTMAGDDPTKYRTKEIENEWEQKDPLVRFRAFLENKGLWSEEEEAKV... | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl... |
P49823 | XXDATFEIKKXDL | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
PTM: Phosphorylation by PDK family kinases inactivates the enzyme; it is reactivated by dephosphorylation.
Catalytic Activity: (R)-N(6)-... |
Q54C70 | MLSNFLKVNSKALGHIRTFASKSGEIKHNFKKADTYLCDGPSDSTVTNKDELISFFTEMSRFRRLETVCDGLYKKKLIRGFCHLYTGQEAVCAGLESAITKDDHIITAYRDHTYMLSRGATPEEIFAELLMKETGCSKGKGGSMHMFTKNFYGGNGIVGAQCPLGAGIAFAQKYNKTGNVCLAMYGDGAANQGQLFEAFNMASLWKLPVIFICENNKYGMGTSQKRSTAGHDFYTRGHYVAGLKVDGMDVFAVKEAGKYAAEWCRAGNGPIILEMDTYRYVGHSMSDPGITYRTREEVNHVRQTRDPIENIRQIILDNKI... | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Catalytic Activity: (R)-N(6... |
P08559 | MRKMLAAVSRVLSGASQKPASRVLVASRNFANDATFEIKKCDLHRLEEGPPVTTVLTREDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAASTDYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPIMLL... | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
PTM: Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single ... |
O13366 | MLSLKAQSSVVGKSSSLRLVRNFSKNVRALSQVADETKPGDDDLVQIDLPETSFEGYLLDVPELSYQTTKSNLLQMYKDMIIVRRMEMACDALYKAKKIRGFCHSSVGQEAIAVGIENAITKRDTVITSYRCHGFTYMRGAAVQAVLAELMGRRTGVSFGKGGSMHLYAPGFYGGNGIVGAQVPLGAGLAFAHQYKHEDACSFALYGDGASNQGQVFESFNMAKLWNLPAVFCCENNKYGMGTAAARSSAMTEYFKRGQYIPGLKVNGMDILAVYQASKFAKDWTVSGNGPIVLEYETYRYGGHSMSDPGTTYRTRDEIQ... | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl... |
F4IAL1 | MGQERPNDEERPESRDLGVYGCSPPHSPRLGPTRFYVFAGDPNPKQTIKRCKRKRIQACNDQRTAKTAIGVMAILGFFCLVNWFMLSRLHEGRVWLRRGLSENPKHVSAQNEERKKFEKQKMKYNGTYGRMLSLATDALAEGMRDNRYCNGFDFEQNKLETKDLWQEPKEQASAWKPCADQRSLTPDDGKNGYIMVTANGGINQQRVAVCNIVVVARLLNAALVIPKFMLSDVWTDASQFGDIYQEEHFMEYLSPDIRIVKELPKELQSLNLEEIGSVVTDIEVMKEAKPDFYMTHILPILLKNRVIHFVGFGNRLAFDP... | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 67314
Sequence Length: 590
Pathway: Glycan metabolism.
Subcellular Location: Membrane
EC: 2.4.1.-
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Q8WR51 | MHFFPIQLLVLFFAEKIAFAENSDQTVSRVDSNRYSVAAEKKFLLYDVNFGEGFNLRRDVYMRVANTVRSLRDSGENYILVLPPWGRLHHWKRMEVALSWRLFFDLESLNRFIPVIEFEDFLDENRPIDQVIYLQHYAEGWGTEYVRKFEKRSCLPPAESHYKQVEEFKWKGWFYSYEDVYSRNFQCVSIQGDSGTLKDLLKHSNFSESTSIMVDRAETILHEHYGEVDYWKARRSMRYSNDLVDVADAFRKKYLDSDDKRDKTKLVDDWTKEKPRRTAIGGPYLGIHWRRRDFLYARRAQLPTIPGTAKILQDLCKKLD... | Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively . O-fucosylates members of sever... |
Q9W589 | MRGSWPRLGFPALLLLLHLLTGSDAAVRNGTAKREIGDSRGSSGTCVKGFLQEILPLPATCPPEVLGMRGAVYILYDVNISEGFNLRRDVYIRMAVFVRRLQRRRRFRHVRLVLPPWPRLYHWHSQGLQQSGLPWSHFFDLASLRRYAPVLDYEEFLAEQRLFGNPGAPLVHVGHAFRLQHYEVMLEQGIFRDKFERVTDKPCSEGSLSGGPLLQQAELRVGRFHCVRFQGSAGLLEKLLREAIDEDTAGPEDVDDMRTYALLSAETVLHDHWGDEHFWQARRSMRFARRLEQVAADFRRQALDTTDASAGVQRPAMWEL... | Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively. O-fucosylates members of severa... |
Q9Y2G5 | MATLSFVFLLLGAVSWPPASASGQEFWPGQSAADILSGAASRRRYLLYDVNPPEGFNLRRDVYIRIASLLKTLLKTEEWVLVLPPWGRLYHWQSPDIHQVRIPWSEFFDLPSLNKNIPVIEYEQFIAESGGPFIDQVYVLQSYAEGWKEGTWEEKVDERPCIDQLLYSQDKHEYYRGWFWGYEETRGLNVSCLSVQGSASIVAPLLLRNTSARSVMLDRAENLLHDHYGGKEYWDTRRSMVFARHLREVGDEFRSRHLNSTDDADRIPFQEDWMKMKVKLGSALGGPYLGVHLRRKDFIWGHRQDVPSLEGAVRKIRSLM... | Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively . O-fucosylates members of sever... |
W7K6N5 | MKFIIVLLLFFFFKVIDRVICVTPQKLICLKEDVYLGDFFFFLKRKKYIMYDVNIGEGFNLQKEIFYRLSLVIYNLNKKDKINIYYLVLPPWCYVTHWNIRKGNNLRWEFFFNTDIMKKVIPIIEYEEYEKLYGNYSDIMINSKYILDNYKEKSFLILPFEECNINVNRFKQFCKKCEHKYNVLYSGYCTTINTKQSECYSYNMISNYFITSILENLFLYNITSVLIKQSTNILVPFVNELYQSNLEDILLFNNKLLSYGNNYISNILKTNHYISSHLRYTDFKYISRYNVPPIHIALLKLLYIMFINNCRIIFIASDEK... | Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively (By similarity). O-fucosylates s... |
A5K6G1 | MKGRAHIWVALLLACLPPRFRNLDKDVSSPVCRTDDVYTGDAFYPFKKKKYVLYDVHIGEGFNLQKEVLYRVALAVYYLNQEERTHVHYLVLPPWCYVTHWGRERTNARIKWSIFFNLKALQNVIPVMEYAEYEGQFGPHTDYILSYRHIIGEWPKRGDKKSFQVLKLDKCQVKGYKLKKNLRKNCDHKYSVEYSGKCTNVKGKKMECLEFFFITSHFVSSTLLDIFQYDADSVLIKHGSNILVAFMNELVDANLEDVLPYSEDLINEGDQFVEKNFKSSKNYISCHLRYTDFRKISTYDVSPVGISLLKLLYIMFLRKS... | Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively . O-fucosylates sporozoite prote... |
S7WCF5 | MHCQLGGQARALIFLMFESCRNSWHVSPWSSVPFLPSPCLFFSFSALPFLHPLSQLIACRGSSATWLFPVSSGTLVLRYALAASPPRGTMRPSTNPRTAEEGRPWLIHATQTGPQTASVLSLFPAVNAGFFSACRQHRGGRPPCLLNHRRLLLGLVSVLTVFLSCLPFTNATVSPAALQDVCYAFGNISRKLSSFLVPSRVTCPRGATPLSGVEAQDSLEHPEIPDFRFLVYDVKNGEGFHLQKEVIYRVALVISLLNARSAQQGRMTDVHTAEKAREDRGHPQASHMLCASSSFSHACSARSTFPFFPMWVLVLPPWCR... | Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively . O-fucosylates microneme protei... |
Q84WU0 | MVRNSSDEEEDHRNLIPQNDTRDNDLNLRPDARTVNMANGGGRSPRSALQIDEILSRARNRWKISVNKRYVVAAVSLTLFVGLLFLFTDTRTFFSSFKLDPMSSRVKESELQALNLLRQQQLALVSLLNRTNFNSSNAISSSVVIDNVKAALLKQISVNKEIEEVLLSPHRTGNYSITASGSDSFTGSYNADICRKVDQKLLDRKTIEWKPRPDKFLFAICLSGQMSNHLICLEKHMFFAALLDRVLVIPSSKFDYQYDKVIDIERINTCLGRTVVISFDQFKEIDKKNNAHIDRFICYVSSPQPCYVDEDHIKKLKGLG... | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 63622
Sequence Length: 564
Pathway: Glycan metabolism.
Subcellular Location: Membrane
EC: 2.4.1.-
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B7ZWR7 | MRRRRKTVVVAVVIRRVLIWAICVMTLLCFLTVHIYVAPFNRLPKLHLNHHNTRRGYIIDYNKSITEQSLTRNLSRPESNEIPLISNPKTNEIQYQSSISEHINNTELVPPHVSTSPSSSSKLNITSGIPDFDKLWKHPPNRNFVPCVSPNPSYTSPLESRGYLLVHTNGGLNQMRAGICDMVAIARIINATLVVPELDKRSFWQDTSKFSDVFDEDHFINALSKDIRVIKKLPKGIDGLTKVVKHFKSYSGLSYYQNEIASMWDEYKVIRAAKSDSRLANNNLPPDIQKLRCRACYEALRFSTKIRSMGELLVDRMRSY... | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 64514
Sequence Length: 565
Pathway: Glycan metabolism.
Subcellular Location: Membrane
EC: 2.4.1.-
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F4HZX7 | MGKQGSPRSPRPETIDKEEKFGRRSLDSLSGNDLLLGRRIYASEVSKAQGSKHDQSSGSSNKFWKKQHSWLRRNFKSIVLMISVTGFIFCMDSIMVSIFHSDSRAVVQDISRLSNMTLHKNGAVDASPVQMYSRLLNLASDSLAKNEFKPDTPNFREERSSKSSQWKPCADNNKAAVALERSRELSNGYIMVSANGGLNQQRVAICNAVAVAALLNATLVLPRFLYSNVWKDPSQFGDIYQEDHFIEYLKDEVNIVKNLPQHLKSTDNKNLSLVTDTELVKEATPVDYIEHVLPLLKKYGMVHLFGYGNRLGFDPLPFDV... | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 69119
Sequence Length: 611
Pathway: Glycan metabolism.
Subcellular Location: Membrane
EC: 2.4.1.-
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Q8H1E6 | MHGLSRLGNGSSNGRINIPSPSPPSSPRIRHTRGKSLAGGVYKQGLGERLVFLLFSIVFRRKGVLLLAPLLYIAGMLLFMGSFGFTVLDLGHGVEIVYRRGSPGSVYRSPKVFKRLWPVMEADVNGSSHNVLMEAWKPRVKSVWKPCISTNVSAAGSNSNGYFIIEANGGLNQQRLSICDAVAVAGLLNATLVIPIFHLNSVWRDSSKFGDIFDEDFFIYALSKNVNVVKELPKDVLERYNYNISSIVNLRLKAWSSPAYYLQKVLPQLLRLGAVRVAPFSNRLAHAVPAHIQGLRCLANFEALRFAEPIRLLAEKMVDR... | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 63766
Sequence Length: 568
Pathway: Glycan metabolism.
Subcellular Location: Membrane
EC: 2.4.1.-
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O42914 | MSVASKNLFDLLGEETPAATTTEKKTAASRDKKRSDSPPVPRELVAQSTTSRKRDPNQPTPRERTVNKKADQPRRRRQAPQGNEAFAREGKEARANNAAHPVDATGAPSNRRNARARRGREFDRHSQTGRVDTKKATERGWGDLVNSAANPDVAENEGNTPSGAQTPAAEEENVKTLDEYLSERKSAAKPVGRTVEKLENATKVEKSAPEELFASLKKSASQKKSAAKESKPKKVLLDIEQTFTARPARGGRPNRAPRRGPSETASKTQQAPPTLSETDFPALA | Function: Ribosome preservation factor that protect a small pool of nontranslating, vacant ribosomes in cells under nutrient starvation conditions. Under nutrient-limiting conditions, cells reduce ribosome biogenesis and degrade ribosomes via autophagy (ribophagy) or proteasomal degradation. To avoid excessive degradat... |
Q89ZI2 | MKNNKIYLLGACLLCAVTTFAQNVSLQPPPQQLIVQNKTIDLPAVYQLNGGEEANPHAVKVLKELLSGKQSSKKGMLISIGEKGDKSVRKYSRQIPDHKEGYYLSVNEKEIVLAGNDERGTYYALQTFAQLLKDGKLPEVEIKDYPSVRYRGVVEGFYGTPWSHQARLSQLKFYGKNKMNTYIYGPKDDPYHSAPNWRLPYPDKEAAQLQELVAVANENEVDFVWAIHPGQDIKWNKEDRDLLLAKFEKMYQLGVRSFAVFFDDISGEGTNPQKQAELLNYIDEKFAQVKPDINQLVMCPTEYNKSWSNPNGNYLTTLGD... | Function: Can hydrolyze the glycosidic link of O-GlcNAcylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates (in vitro).
Catalytic Activity: 3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H2O = L-seryl-[protein] + N-acetyl-D-glucosamine
Sequence Mass (Da): 84485
Seque... |
Q0TR53 | MKRKMLKRLLTSAFACMFIANGLITTTVRAVGPKTGEENQVLVPNLNPTPENLEVVGDGFKITSSINLVGEEEADENAVNALREFLTANNIEINSENDPNSTTLIIGEVDDDIPELDEALNGTTAENLKEEGYALVSNDGKIAIEGKDGDGTFYGVQTFKQLVKESNIPEVNITDYPTVSARGIVEGFYGTPWTHQDRLDQIKFYGENKLNTYIYAPKDDPYHREKWREPYPESEMQRMQELINASAENKVDFVFGISPGIDIRFDGDAGEEDFNHLITKAESLYDMGVRSFAIYWDDIQDKSAAKHAQVLNRFNEEFVK... | Function: Binds carbohydrates . Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Can bind and deglycosylate O-glycosylated peptides from mammals.
Catalytic Activity: 3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H2O = L-seryl-[protein] + N-acetyl-D-glucosamine
Sequence Mass (Da): 111080
S... |
P9WEQ7 | MVTKCIDPCEQQNQKRPVGHLVWDLIRISRYDKYNSFLALFSGVWSTLLAGALKLRNEPESTSVSFVLSRVVLCSLASYIFSGAGMVWNDWVDRDIDAKVARTKDRPLASGRLHTMEAMAWLIIQVAASTGLLYWMMEGRHVWISLVPPAIGTLLYPYCKRPTAQKFGIYPQYVLGLTAACPAVFGRAAIYNHEDSFQDLINASFPLCLFVFVWTLYFNTAYSYQDVKDDSKMKINSSYVFAGQHIHLFLVLLTGLVLASIPWVLHPLQSGWLWVSWMGVWSVGCAEQLVRFNANDPHTGGLVWRRNILLALWTIFACLV... | Function: Polyprenyl transferase; part of the gene cluster that mediates the biosynthesis of 15-deoxyoxalicine B . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase olcI . Nicotinyl-CoA is then a substrate of polyketide synthase olcA to produce 4-hydrox... |
P9WEQ8 | MDLVSFAFSGPATHADQAPLYIDAKRPSRSLSEAPFRRLVRSLVAGFKAYGVERGDTVLVQLDNLVIHSALLFGIVGAGGVYMGCSPSSPRHELDHFVSLVEPRLILTVASALSVVRDVCTNKGISWSQICLVDDQSVDHLVSFAQNQSYNPQATPPVRDEGVHFDLKDMVSFGESDWMRIYDEATARITPAAMFSTSGTSGLPKAAIRTHHTIISHHQTVHYDVPYPVTRLMALPMSHSFGDFWSNLFPIRYGHPLYVMPRFDLSTFLNVVHRYNITETYLVPAMVHILNQSTLPVRESLGSLFYIGVSGAPIDADSLQ... | Function: Nicotinic acid-CoA ligase; part of the gene cluster that mediates the biosynthesis of 15-deoxyoxalicine B . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase olcI . Nicotinyl-CoA is then a substrate of polyketide synthase olcA to produce 4-hyd... |
P9WEQ9 | MDPNTWSADLFQLASQWQEKGLLTRYNVFMAISITVTALYLIHKGISRARSFRAPLVGRRFSWEPKWLIGLRFSQYGLEHLMEGCKRFNDGIFKVARNDTDILVIPNRYVDELHSKPEEHISAIKAHMKNLLGKYSTIDILQEGNLHTHVLQTKLTPNLGSLMSTIEEELRFAMTEEIPSTHEDWKDVSIYDIILHLVARISARVFVGQPTCRNQEWLDTSIRFTEHAFLTLAILRRLPKFLHPIVAPLLPSYWAVHRDLQTAKRIISPIVKQRTADEASGEPGYKKPTDLLQWMIDVASPRDGQPDKLAHRQLVLSLAA... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of 15-deoxyoxalicine B . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase olcI . Nicotinyl-CoA is then a substrate of polyketide synthase olcA to produce 4... |
P9WEP3 | MTIVSPDKLPSARAVELTAPLDDIYQILNEDGAVIIKNFIPLELVDKINKEVDPYLAQHAAGPNHMSEIYKLTVGSKTKHMGNLTMASKSFRDEVLNHPSMHAISEKLFRANFGDYWLNRAAVLEVDSGEKAQGLHRDDSLYPWKAFLTKDSPELMVNFFIALTEFREENGATRLVLGSHKWEDSTRYPSPEQTIPAEMQAGDAIVYLASLFHGAGQNRSQKTRRGLSITTHPAHFTPMESHIDVPRAIIENMTPLAQKMIGWRTWSTNHGVPVWTVRDGRMEDELKLKSLESPKQIQAAVI | Function: Dioxygenase; part of the gene cluster that mediates the biosynthesis of 15-deoxyoxalicine B . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase olcI . Nicotinyl-CoA is then a substrate of polyketide synthase olcA to produce 4-hydroxy-6-(3-pyri... |
P9WEP4 | MANIGGSNAVSSAQGSQISDSPTTVDDRLDEHKETSTQSIDHSENITQSPTSLQKPPDESNATPVGFGEDGCQSDSQEYPNSWRLAAIMIGVCLAVFSMALDNTILATAIPKITDQFTSLGDVGWYGSVYPLTNCCLTLVFGKLYTFYSTKWVYLSALAVFEIGSLICGATPSSLGLIIGRAIAGLGSSGIYLGSMIILSQSVPLQKRPLFTSLVGGLYGVAGVAGPLLGGAFTDYVSWRWCFYINPLFGAVTALFILLFFDGKEPIKSPGKIKEQISQFDLIGLFFFLPGMISLLLALQWGGQQYNWQSGRIIGLFVCS... | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of 15-deoxyoxalicine B . The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase olcI . Nicotinyl-CoA is then a substrate of polyketide synthase olcA to produce 4-hydroxy-... |
Q17833 | MKGTLIFVVFYSSYGFAHCNTILRSSSLSRNFEDSLRRIPRSTDKDETGFEDSNVQEVIFILLYCLFVALAILICGLIIFYNSRKRELRANRSRGDEYLLEPTSADHKRRNSSNIVPPEPTPYPITSGESDLRQTPSRLSNVECPPELELAPINEKIMYLHYYAEVEINEEDLDISKGRPLGSGEFGIIRKGFLRSKNSKNEEKESRLEVAVKLPLNEYNQIQQELIYDELKVMCAVGKHPNILALVGGITFGERKMIVSEFVENGDLLSFLRDNRIYFTNDQWTLETEQDSLSLVDLLSFAFQIAKGMEYLIHVPCVHR... | Function: Receptor tyrosine kinase which plays a role in promoting longevity and resistance to stresses including UV irradiation and high temperatures, probably downstream of daf-16.
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Location Topology: Single-pass type I membrane... |
P0DV58 | MTIESIRVKNLLSFDDVILRDFRDINCIIGRNNVGKSNLLKVIRYFYAKLENKKVIPLDFHTNYNAVGEITFTFDTTRIKKIVTSRKNNGRFHKHIYNTLFKSSSVKLNFEELIARKNSTNKSFFSLTLTICKDDSVMWSVDDPKVRSLLATLYPFLYIETRHIDLYDWNPIWKLISNLNSFNFDDVDHDELVNFLDEKISSRKGDYKKYIDRVVSVIDTKPYTYKEKVINYIKVAIKGDSFVNAGEELFTQSDGTNSNKFLETLLHLLITLTRTEFISPIVYIDEPEVGLHPKLAESFVSNLNKIYSKFKKTSELSGPG... | Cofactor: Probably binds 2 metal cations.
Function: Probable nuclease member of antiviral defense system retron Eco8, composed of an reverse transcriptase (RT), this nuclease and a non-coding RNA (ncRNA) encoded between them. Expression of retron Eco8 confers protection against bacteriophages T4, T6, T7 and SECphi4, SE... |
E8PLM2 | MLKRLQVKNFRCLEDIDLPLGPLTAIVGPNGAGKTTILRAIDLVLGDVWPSLRSFRIPQDFINFDTTRAIEITVHFDPPYTQGSFNITAFRLTCKGEDADFHVDLEPLDEGGNVPRYPSGNPLRVGTDMRNHARVLFLDHRRNLAQHLPSIRGSILGRLLQPVRREFKLQDNFKQVYEQAMDLLRTEQVKQIEKTIAETAKQMLGFLGKDAMKSMEIGFGFADPANPFNSLRLQYRESDLTLPGDELGLGIQSAIVVGIFEAFRQLGEKIGTVIIEEPEMYLHPQAQRYFYRLLCEMADKDQCQIIYSTHSPIFADVNRF... | Cofactor: Probably binds 2 metal cations. In vitro during a short incubation, Mn(2+) is most efficient on linear or supercoiled dsDNA, nicks but only poorly digests dsDNA with Co(2+), Ni(2+) or Zn(2+). When purified from E.coli Ca(2+) and Mg(2+) are the most abundant metals.
Function: An exodeoxyribonuclease that degra... |
Q84T21 | MADRPQQLQVHPQRGHGHYEGGIKNQRGGGPSAVKVMAVLAALPVGGTLLALAGLTLAGSVIGLLVTSPLFIIFSPVLVPAAIVVGLAVASFLSSGALGLTGLSSLSWVLNYLRCASQSLPREMDQAKRRMQDMAAFVGQKTREVGQEIQSRAQEGRRT | Function: May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth.
Loca... |
Q647G3 | MSDQTRTGYGGGGSYGSSYGGGGTYGSSYGTSYDPSTNQPIRQAIKFMTASTIGVSFLILSGLILTGTVIGLIIATPLLVIFSPILVPAAITLALAAGGFLFSGGCGVAAIAALSWLYSYVTGKHPAGSDRLDYAKGVIADKARDVKDRAKDYAGAGRAQEGTPGY | Function: May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth.
Loca... |
C0HM28 | MADYQHQQQHQRPADAFKGMFPEKGQAQVQGPSASKVIAVVTLLPLGGFLLLLAGLTFAGTLIGLALSTPLFVLCSPVLVPAAIVIGLAVTGFLTSGAFGITGISSLSWILKYLRGTSVPEQMEHAKRRAQDTAGHLGQKARETGQTVTGKGQEAGKTLEGGRGEEKKT | Function: May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth.
Loca... |
Q96543 | MADHHRDRGVLGGGALGERGSHGGYGYTGDHGGYGGDDEQHQQKQPVMMCALKAATAATAGGSMLVLSGLILAGTVIALTVATPVLVIFSPVLVPAAISMALMSAGFVTSGGLGVAAVSVFSWMYKYLAGKHPPGADQLDHAKARLASKARDIKDAAQIRVEQAQGA | Function: May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth (By s... |
Q8EG66 | MKYSRVFINSLAYELAPVVVSSSELESRLAPLYQKFRIPMGQLAALTGITERRWWPKGHQLSDGAINAAHKAIAETGIDVAELGAVVYTGVCRDQHEPATACRIAAALGVSKDTAIYDISNACLGVLSGILDIANRIELGQIKAGMVVSCESARDIVDVTIDNMLADPTMQNFAQSLATLTGGSGAVAVILTDGSLPLTNVRKHQLLGASHLSAPQHHQLCQWGLQEVGHNIYREFMRTDAVTLLKEGVELAKHTWEHFLAQRNWLVEQVDKVICHQVGASNRKQVLSALNIPPEKEFPTYQLLGNMGTVSLPVTAAMAH... | Function: Involved in olefin biosynthesis . Catalyzes a non-decarboxylative head-to-head Claisen condensation of two acyl-CoA molecules, generating an (R)-2-alkyl-3-oxoalkanoate (By similarity). The S.oneidensis oleABCD genes produce 3,6,9,12,15,19,22,25,28-hentriacontanonaene, which may aid the cells in adapting to a ... |
Q8PDX2 | MLFQNVSIAGLAHIDAPHTLTSKEINERLQPTYDRLGIKTDVLGDVAGIHARRLWDQDVQASDAATQAARKALIDANIGIEKIGLLINTSVSRDYLEPSTASIVSGNLGVSDHCMTFDVANACLAFINGMDIAARMLERGEIDYALVVDGETANLVYEKTLERMTSPDVTEEEFRNELAALTLGCGAAAMVMARSELVPDAPRYKGGVTRSATEWNKLCRGNLDRMVTDTRLLLIEGIKLAQKTFVAAKQVLGWAVEELDQFVIHQVSRPHTAAFVKSFGIDPAKVMTIFGEHGNIGPASVPIVLSKLKELGRLKKGDRI... | Function: Involved in olefin biosynthesis . Catalyzes a non-decarboxylative head-to-head Claisen condensation of two acyl-CoA molecules, generating an (R)-2-alkyl-3-oxoalkanoate . Is active with fatty acyl-CoA substrates that ranged from C(8) to C(16) in length, and is the most active with palmitoyl-CoA and myristoyl-C... |
Q8EG65 | MLDTLLPFKRHFLSRNGNKLHYINEGQGEPVVMVHGNPSWSFYYRNLVSALKDTHQCIVPDHIGCGLSDKPDDSGYDYTLKNRIDDLEALLDSLNVKENITLVVHDWGGMIGMGYAARYPERIKRLVILNTGAFHLPDTKPLPLALWICRNTLLGTVLVRGFNAFSSIASYVGVKRQPMSKYIREAYVAPFNSWANRISTLRFVQDIPLKPGDRNYQLVSDIAASLPKFAKVPTLICWGLQDFVFDKHFLVKWREHMPHAQVHEFADCGHYILEDASDEVITHIKHFMTETETLATQVNPADSITEFESASQAPQAER | Function: Involved in olefin biosynthesis . Catalyzes the elimination of carbon dioxide from beta-lactones to form the final olefin product (By similarity). The S.oneidensis oleABCD genes produce 3,6,9,12,15,19,22,25,28-hentriacontanonaene, which may aid the cells in adapting to a sudden drop in temperature .
Catalytic... |
Q8PDW8 | MTYPGYSFTPKRLDVRPGIAMSYLDEGPSDGEVVVMLHGNPSWGYLWRHLVSGLSDRYRCIVPDHIGMGLSDKPDDAPDAQPRYDYTLQSRVDDLDRLLQHLGITGPITLAVHDWGGMIGFGWALSHHAQVKRLVITNTAAFPLPPEKPMPWQIAMGRHWRLGEWFIRTFNAFSSGASWLGVSRRMPAAVRRAYVAPYDNWKNRISTIRFMQDIPLSPADQAWSLLERSAQALPSFADRPAFIAWGLRDICFDKHFLAGFRRALPQAEVMAFDDANHYVLEDKHEVLVPAIRAFLERNPL | Function: Involved in olefin biosynthesis . Catalyzes the elimination of carbon dioxide from beta-lactones to form the final olefin product .
Catalytic Activity: a cis-3-alkyl-4-alkyloxetan-2-one = a cis-alkene + CO2
Sequence Mass (Da): 34080
Sequence Length: 300
Subcellular Location: Cytoplasm
EC: 4.1.1.114
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Q8EG64 | MTKVDDALFEHGASAVAVEQNNGRDNPTKPKDANICRHLKLAAHHIPHHLAVAVQQGKGKSFANLTYQELDFISLNKQSDAIAFALNAYGLTRGMKAVLMVTPSLDFFALTFALFKAGIIPVLVDPGMGIKNLKQCFIEAAPDAFIGIPKAHIARRLLGWGKASVKRLINVDANQSGVTDTLSRLLTGAPSLASMLSFTTKSSSAKLPEQVEYPMALLEHDEMAAILFTSGSTGTPKGVVYSHGMFEAQIQALKQDYGIAHGERDLATFPLFSLFGPALGMTSIVPEMDASKPITANPEFLFAAIEKYQCSNIFVNPALL... | Function: Involved in olefin biosynthesis . Catalyzes the conversion of 2-alkyl-3-hydroxyalkanoic acids to beta-lactones in the presence of ATP (By similarity). The S.oneidensis oleABCD genes produce 3,6,9,12,15,19,22,25,28-hentriacontanonaene, which may aid the cells in adapting to a sudden drop in temperature .
Catal... |
B2FI28 | MNRPCNIAARLPELARERPDQIAIRCPGRRGAGNGMAAYDVTLDYRQLDARSDAMAAGLAGYGIGRGVRTVVMVRPSPEFFLLMFALFKLGAVPVLVDPGIDRRALKQCLDEAQPEAFIGIPLAHVARLVLRWAPSAARLVTVGRRLGWGGTTLAALERAGAKGGPMLAATDGEDMAAILFTSGSTGVPKGVVYRHRHFVGQIQLLGSAFGMEAGGVDLPTFPPFALFDPALGLTSVIPDMDPTRPAQADPVRLHDAIQRFGVTQLFGSPALMRVLAKHGRPLPTVTRVTSAGAPVPPDVVATIRSLLPADAQFWTPYGA... | Function: Involved in olefin biosynthesis . Catalyzes the conversion of beta-hydroxy acid substrates to beta-lactones in the presence of ATP . Can use all four stereoisomers of 2-hexyl-3-hydroxydecanoic acid .
Catalytic Activity: a (2R,3S)-2-alkyl-3-hydroxyalkanoate + ATP = a cis-3-alkyl-4-alkyloxetan-2-one + AMP + dip... |
Q74A86 | MKKGMKVSLSVAAAALLMSAPAAFAFHSGGVAECEGCHTMHNSLGGAVMNSATAQFTTGPMLLQGATQSSSCLNCHQHAGDTGPSSYHISTAEADMPAGTAPLQMTPGGDFGWVKKTYTWNVRGLNTSEGERKGHNIVAGDYNYVADTTLTTAPGGTYPANQLHCSSCHDPHGKYRRFVDGSIATTGLPIKNSGSYQNSNDPTAWGAVGAYRILGGTGYQPKSLSGSYAFANQVPAAVAPSTYNRTEATTQTRVAYGQGMSEWCANCHTDIHNSAYPTNLRHPAGNGAKFGATIAGLYNSYKKSGDLTGTQASAYLSLAP... | Cofactor: Binds 6 low-spin heme groups per subunit.
Function: Plays an important role in extracellular electron transfer. Can transfer electrons to insoluble Fe(3+) oxides as well as other extracellular electron acceptors, including Mn(4+) oxide and humic substances . Essential for direct interspecies electron transfer... |
Q99983 | MGFLSPIYVIFFFFGVKVHCQYETYQWDEDYDQEPDDDYQTGFPFRQNVDYGVPFHQYTLGCVSECFCPTNFPSSMYCDNRKLKTIPNIPMHIQQLYLQFNEIEAVTANSFINATHLKEINLSHNKIKSQKIDYGVFAKLPNLLQLHLEHNNLEEFPFPLPKSLERLLLGYNEISKLQTNAMDGLVNLTMLDLCYNYLHDSLLKDKIFAKMEKLMQLNLCSNRLESMPPGLPSSLMYLSLENNSISSIPEKYFDKLPKLHTLRMSHNKLQDIPYNIFNLPNIVELSVGHNKLKQAFYIPRNLEHLYLQNNEIEKMNLTVM... | Function: May be implicated in biomineralization processes. Has a function in binding of osteoblasts via the alpha(V)beta(3)-integrin.
PTM: Glycosylated; contains keratan sulfate.
Sequence Mass (Da): 49492
Sequence Length: 421
Subcellular Location: Secreted
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O35103 | MGFLSPIYVLFFCFGVRVYCQYEAYRWDDDYDQEPNEDYDPEFQFHQNIEYGVPFYNNILGCAKECFCPTNFPTSMYCDNRKLKTIPIIPMHIQQLNLQFNDIEAVTANSFINATHLKEINLSHNKIKSQKIDYGVFAKLSNLQQLHLEHNNLEEFPFPLPKSLERLLLGYNEISILPTNAMDGLVNVTMLDLCYNHLSDSMLKEKTLSKMEKLMQLNLCNNRLESMPLGLPSSLMYLSLENNSISSIPDNYFDKLPKLHALRISHNKLEDIPYDIFNLSNLIELNVGHNKLKQAFYIPRNLEHLYLQNNEIESINVTMI... | Function: May be implicated in biomineralization processes. Has a function in binding of osteoblasts via the alpha(V)beta(3)-integrin.
PTM: Glycosylated; contains keratan sulfate.
Sequence Mass (Da): 49745
Sequence Length: 423
Subcellular Location: Secreted
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P02931 | MMKRNILAVIVPALLVAGTANAAEIYNKDGNKVDLYGKAVGLHYFSKGNGENSYGGNGDMTYARLGFKGETQINSDLTGYGQWEYNFQGNNSEGADAQTGNKTRLAFAGLKYADVGSFDYGRNYGVVYDALGYTDMLPEFGGDTAYSDDFFVGRVGGVATYRNSNFFGLVDGLNFAVQYLGKNERDTARRSNGDGVGGSISYEYEGFGIVGAYGAADRTNLQEAQPLGNGKKAEQWATGLKYDANNIYLAANYGETRNATPITNKFTNTSGFANKTQDVLLVAQYQFDFGLRPSIAYTKSKAKDVEGIGDVDLVNYFEVG... | Function: Forms pores that allow passive diffusion of small molecules across the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39333
Sequence Length: 362
Subcellular Location: Cell outer membrane
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Q56113 | MMKRKILAAVIPALLAAATANAAEIYNKDGNKLDLYGKAVGRHVWTTTGDSKNADQTYAQIGFKGETQINTDLTGFGQWEYRTKADRAEGEQQNSNLVRLAFAGLKYAEVGSIDYGRNYGIVYDVESYTDMAPYFSGETWGGAYTDNYMTSRAGGLLTYRNSDFFGLVDGLSFGIQYQGKNQDNHSINSQNGDGVGYTMAYEFDGFGVTAAYSNSKRTNDQQDRDGNGDRAESWAVGAKYDANNVYLAAVYAETRNMSIVENTVTDTVEMANKTQNLEVVAQYQFDFGLRPAISYVQSKGKQLNGADGSADLAKYIQAGA... | Function: Forms pores that allow passive diffusion of small molecules across the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40106
Sequence Length: 363
Subcellular Location: Cell outer membrane
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Q8XB59 | MSELLSFALFLASVLIYAWKAGRNTWWFAATLTVLGLFVVLNITLFASDYFTGDGINDAVLYTLTNSLTGAGVSKYILPGIGIVLGLTAVFGALGWILRRRRHHPHHFGYSLLALLLALGSVDASPAFRQITELVKSQSRDGDPDFAAYYKEPSKTIPDPKLNLVYIYGESLERTYFDNEAFPDLTPELGALKNEGLDFSHTQQLPGTDYTIAGMVASQCGIPLFAPFEGNASASVSSFFPQNICLGDILKNSGYQNYFVQGANLRFAGKDVFLKSHGFDHLYGSEELKSVVADPHYRNDWGFYDDTVLDEAWKKFEELS... | Function: Transfers a phosphoglycerol residue from phosphatidylglycerol to the membrane-bound nascent glucan backbones.
Catalytic Activity: phosphatidylglycerol + membrane-derived-oligosaccharide D-glucose = 1,2-diacyl-sn-glycerol + membrane-derived-oligosaccharide 6-(glycerophospho)-D-glucose.
Location Topology: Multi... |
Q8XVC3 | MRLAVGLLALASAQAALAFGLNDVAARAKQLAAKPYQAPPDTLPHELRELRYDQYREIRFKSDQAYWRRDKLPFELGFFHEGSYYDQPVKINEVSPAGAREIRFDPRLFDYGPVKLDPKHLRNLGFAGFRIHYPMNTPKYKDEVIVFLGASYFRGIGKGQVYGLSARGLAIDTALNSGEEFPRFTEFWIERPAANAKELTIYALLNSRRATGAYRFVIKPGTDTEVDVKAQLYMRENVSKLGIAPLTSMFFFGENQPASALDFRPEVHDSDGLSMLSGTGEWIWRPLTNPKRLLVSSFSTTNPGGFGLMQRDRAFSSYQE... | Function: Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).
Sequence Mass (Da): 56761
Sequence Length: 504
Pathway: Glycan metabolism; osmoregulated periplasmic glucan (OPG) biosynthesis.
Subcellular Location: Periplasm
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Q6N5U4 | MNRRQVLTGLAALPLLQAKPDPAAADRSSSIDFDPWMVRKLARELASKPYEAPDSSLPASLNDLSYDAYRSLRFRPERALWRAENLPFQVQFFHRGFLYKNRVTIFEVADGKARHVPYRADDFSFGDVAPPPDSDLGFAGFRIHAPLQRADYYDEVSAFLGAAYFRAVTKGERYGLSARGLSIDTGQSSGEEFPLFKTFWLERPAPGASSMVVHALLDSKSVAGAYRFTIRPGDTTVFDVEMALYPRVDLQHAGLAPMTSMFLFGPNDPADTPDFRAAVHDSDGLAIFNGSGEELWRPLCNPKDLQISSFGDRNPRGFGL... | Function: Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).
Sequence Mass (Da): 56032
Sequence Length: 501
Pathway: Glycan metabolism; osmoregulated periplasmic glucan (OPG) biosynthesis.
Subcellular Location: Periplasm
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P24138 | MLKYIGRRLVYMIITLFVIVTVTFFLMQAAPGGPFSGEKKLPPEIEANLNAHYGLDKPLFVQYVSYLKSVAMWDFGPSFKYKGQSVNDLISSGFPVSFTLGAEAILLALALGVLFGVIAALYHNKWQDYTVAILTIFGISVPSFIMAAVLQYVFSMKLGLFPVAGWDSWAYTFLPSIALASMPMAFIARLSRSSMIEVLNSDYIRTAKAKGLSRPAVTVRHAIRNALLPVVTYMGPMAAQVLTGSFIIETIFGIPGLGAHFVNSITNRDYTVIMGVTVFFSVILLLCVLIVDVLYGIIDPRIKLSKAKKGA | Function: Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane. Also required for sporulation and competence.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34075
Sequence Length: 311
Subcellular Loc... |
P0A4N7 | MWKVIIRRILLMIPQLFILSILVFFFAKLMPGDPFSGLIGPHTDPHEVEALRRAAGLYDPWWEQYLRWLGNAIHGNLGMSYNLKEPVMTVIGHRAINTFWMSLLSVILTYLFAIPMSIVAARNEGKWQDQLWLTYNSITFGIPPYVFYLLIIFIFGYSLNWFPTGGTVSPDAMGIIPVFFSKIYHMILPAFSLAVFGTVGIFTYFRSGILDEQTQDYVRTARAKGVKEKVIFRRHILRNASLPIASNFGFVITGLLGGAIFAETIFGYPGLGQLFITSISGRDYSMITALILLNGFLGLLGALLSDIIMAMVDPRIRIQ | Function: Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35962
Sequence Length: 319
Subcellular Location: Cell membrane
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P75554 | MFIVMTIVFFLVNSTGQTPLSATSSKDLEAVKTQLDAFGFNDPLIVRYGRYWQTLFSGSLGTYYSSPNQTIDQIVFGRVPNTLYVVLISFFIGSLLGIIFGMISGLFRGKLIDAVINVLVVLFVSIPSFVVGLGLLKAAGLFRLPPRFINFDDANFNFGNFLLASIIPILSLVFYTSAAFTYRVRNEVVEVMNQDYIKTARSKGLSTFAVALYHIFRNSIIPSVPLFVFGISGAFSGGFIIESLFGVQGVSRILIDSVQSNETNLVMFNIMFIQGIPLLASVFIELIYVLVDPRIRIASAGGVSLWTKLKFVYLRQAWLR... | Function: Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43538
Sequence Length: 389
Subcellular Location: Cell membrane
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P08005 | MLKFILRRCLEAIPTLFILITISFFMMRLAPGSPFTGERALPPEVLANIEAKYHLNDPIMTQYFSYLKQLAHGDFGPSFKYKDYTVNDLVAASFPVSAKLGAAAFLLAVIIGVSAGVIAALKQNTRWDYTVMGFAMTGVVIPSFVVAPLLVMVFAITLQWLPGGGWNGGALKFMILPMVALSLAYIASIARITRGSMIEVLHSNFIRTARAKGLPMRRIIFRHALKPALLPVLSYMGPAFVGIITGSMVIETIYGLPGIGQLFVNGALNRDYSLVLSLTILVGALTILFNAIVDVLYAVIDPKIRY | Function: Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33420
Sequence Length: 306
Subcellular Location: Cell inner membrane
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P24139 | MQNIPKNMFEPAAANAGDAEKISKKSLSLWKDAMLRFRSNKLAMVGLIIIVLIILMAIFAPMFSRYDYSTTNLLNADKPPSKDHWFGTDDLGRDIFVRTWVGARISIFIGVAAAVLDLLIGVIWGSISGFRGGRTDEIMMRIADILWAVPSLLMVILLMVVLPKGLFTIIIAMTITGWINMARIVRGQVLQLKNQEYVLASQTLGAKTSRLLFKHIVPNAMGSILVTMTLTVPTAIFTEAFLSYLGLGVPAPLASWGTMASDGLPALTYYPWRLFFPAGFICITMFGFNVVGDGLRDALDPKLRK | Function: Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane. Also required for sporulation and competence.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33621
Sequence Length: 305
Subcellular Loc... |
P0AFH7 | MMLSKKNSETLENFSEKLEVEGRSLWQDARRRFMHNRAAVASLIVLVLIALFVILAPMLSQFAYDDTDWAMMSSAPDMESGHYFGTDSSGRDLLVRVAIGGRISLMVGVAAALVAVVVGTLYGSLSGYLGGKVDSVMMRLLEILNSFPFMFFVILLVTFFGQNILLIFVAIGMVSWLDMARIVRGQTLSLKRKEFIEAAQVGGVSTSGIVIRHIVPNVLGVVVVYASLLVPSMILFESFLSFLGLGTQEPLSSWGALLSDGANSMEVSPWLLLFPAGFLVVTLFCFNFIGDGLRDALDPKDR | Function: Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33022
Sequence Length: 302
Subcellular Location: Cell inner membrane
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P0A4N9 | MTEKKHKNSLSLVHSIKEELKKDKLAMISTIFLVAVFLIVYIYSMFLKQSNYVDVNIMDQYLAPLTNGHLLGTDNGGRDIIMMLMISARNSFNIAFAVTLITLVVGNILGVITGYFGGRFDLIFMRFTDFVMILPSMMIIIVFVTIIPRFNSWSLIGIISIFSWIGTTRLIRARTMTEVNRDYVRASKTSGTSDFKIMFREIWPNLSTLVIAEATLVFAGNIGLETGLSFLGFGLPAGTPSLGTMINEATNPETMTDKPWTWVPATVVILIVVLAIIFIGNALRRVADQRQATR | Function: Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32835
Sequence Length: 294
Subcellular Location: Cell membrane
|
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