ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P83798 | MEIDVLGWVALLVVFTWSIAMVVWGRNGL | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3276
Sequence Length: 29
Subcellular Location: Cellular ... |
Q1XDL0 | MDILSLGWAALMAMFTFSIAMVVWGRNGF | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3237
Sequence Length: 29
Subcellular Location: Plastid
|
P33292 | MSLIGGGSDCAAGSNPLAQFTKHTQHDTSLQQSMRNGEFQQGNQRMMRNESTMSPMERQQMDQFMQQQNNPAFNFQPMQHELNVMQQNMNAPQQVANNSWNQEFRMKDPMVANAPSAQVQTPVQSTNWAQDFQQAGPEVQHHAQQHQHPILSVPGVRAGIYGGGRLMGGSMMNRAAQMQQQNPAQAQTSEQSQTQWEDQFKDIESMLNSKTQEPKTKQQEQNTFEQVWDDIQVSYADVELTNDQFQAQWEKDFAQYAEGRLNYGEYKYEEKNQFRNDPDAYEIGMRLMESGAKLSEAGLAFEAAVQQDPKHVDAWLKLGE... | Function: Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) (By similarity). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through... |
O94325 | MSVEAGCSTLSNPLKKLTSTAVVNNSTPSAQYRKHLTKSQSRTYAPLQTLSEDQFTSFKNLQGNNSPLGNVVKNPVSLKTGNHTGTTTRGGSKENWVHSFSSLQQQNSKSAWTSEFSEVFLNSSENDRFRNLNQPLKQSFFGSAGLNLSSNTEIPLQSSLAIDETELAKKFEEASQISNKLEKEKDATGSKSIEELWEEHQKQLKNAGLEPASLEEYQKQWEDFLKSNNISDDPYTSSVNSFANDNLAHNKNIDPQIFQHSDTDNVVENSLQTEDVYSQNQDESSEVVKELNGIDPFVEAMNLIKNGGSISKAAVLLEQS... | Function: Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX14... |
A0A1L8FDW4 | MAMRGLIEAECGGSNPLMKLTNHFTQDKALREEGLQHVSWPPGATVVSKPLGEATEDELVSEFLHTRAPSLQSRAPHTFKMDGLLAEMQEIEQSSFRPEPLRAPGVADLALSEQWSAEFLGVEVDPVEEEDWSREFTEQADPHASPSRWAEEYLQQSEEKLWLGESEGAMAEKWTEEYQPEDDLQREAKSLVSQVTDPKLANTQFLQFVKRIGDGELSFSHAPSTPSQTVSQAEQWSEQFVHEQAEQWVDQFAPLEKDFEKAKAAVESDVDFWDKLQEEWEEMAKRDAEAHPWLSDFQDLSSKSIDKGYMFEDNNPFSEV... | Function: Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) . Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the pex13-pex1... |
Q99144 | MSFMRGGSECSTGRNPLSQFTKHTAEDRSLQHDRVAGPSGGRVGGMRSNTGEMSQQDREMMARFGAAGPEQSSFNYEQMRHELHNMGAQGGQIPQVPSQQGAANGGQWARDFGGQQTAPGAAPQDAKNWNAEFQRGGSPAEAMQQQGPGPMQGGMGMGGMPMYGMARPMYSGMSANMAPQFQPQQANARVVELDEQNWEEQFKQMDSAVGKGKEVEEQTAETATATETVTETETTTEDKPMDIKNMDFENIWKNLQVNVLDNMDEWLEETNSPAWERDFHEYTHNRPEFADYQFEENNQFMEHPDPFKIGVELMETGGRL... | Function: Binds to the C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) and plays an essential role in peroxisomal protein import.
PTM: Ubiquitination at Cys-10 is UBC4-independent but requires the presence of PEX4. Ubiquitination at Lys-22 is UBC4-dependent (By similarity).
Location Topology: Pe... |
P35056 | MDVGSCSVGNNPLAQLHKHTQQNKSLQFNQKNNGRLNESPLQGTNKPGISEAFISNVNAISQENMANMQRFINGEPLIDDKRRMEIGPSSGRLPPFSNVHSLQTSANPTQIKGVNDISHWSQEFQGSNSIQNRNADTGNSEKAWQRGSTTASSRFQYPNTMMNNYAYASMNSLSGSRLQSPAFMNQQQSGRSKEGVNEQEQQPWTDQFEKLEKEVSENLDINDEIEKEENVSEVEQNKPETVEKEEGVYGDQYQSDFQEVWDSIHKDAEEVLPSELVNDDLNLGEDYLKYLGGRVNGNIEYAFQSNNEYFNNPNAYKIGC... | Function: Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) . Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX1... |
Q8RY16 | MVERRNPLVLSSTRSTLRSVLNSSQPSSADGDRVLNKDGDLLRGNARLSAGILRWRKDGENVSDAKLDSLDDSALVGLSTQLLKRLSINSGSLVVVKNIEIGIQRVAQVVVLDPPKTTLEDASLTQVPVSDSLHTMLVFPTYDLMGQQLLDQEVAYLSPMLAFNLSLHISCLKSLVHRGNGVLEKYFEAKCDEEFIGKSAEDGSKIGLDLEPVSQVPGYASHLRVSFVKIPECGTIPSLKVNSSFEAEERQGLIDSALQKYFGTDRQLSRGDIFRIYIDWNCGSSICNPCSQRLCSESDDYIYFKVIAMEPSNERFLRVN... | Function: Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling . Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen thr... |
Q6FW67 | MMITADLIWDENLDNDCEVSKDIWEDDTFIDKSYLKVVLPSYDGVDTPIVYHFKLNDDLKINSIKIPTNSIGNLGKFGRLNTCSLEAVSGEPPVLKEIIIKIDERLYDKLALLPKANEKKQYFQIKYNLVNKQSVIHEGNIWGHVCEVVETKPFSQGVIDFSVTDIVLIRSKILSVENKHDRSLVNLQAFHDLSRIPLKCLHYPVERSLLLPEPPFDDDDSIYVFFPFDLLSKLKISSGSFVRLSNSKNSVLVRAFLLQSPNHYAVDGIYTTPFVLAQFDELPLVEVEPVYNNELAFPTASEVVISKVGNVLHTQKRYQE... | Function: Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen throu... |
Q13608 | MALAVLRVLEPFPTETPPLAVLLPPGGPWPAAELGLVLALRPAGESPAGPALLVAALEGPDAGTEEQGPGPPQLLVSRALLRLLALGSGAWVRARAVRRPPALGWALLGTSLGPGLGPRVGPLLVRRGETLPVPGPRVLETRPALQGLLGPGTRLAVTELRGRARLCPESGDSSRPPPPPVVSSFAVSGTVRRLQGVLGGTGDSLGVSRSCLRGLGLFQGEWVWVAQARESSNTSQPHLARVQVLEPRWDLSDRLGPGSGPLGEPLADGLALVPATLAFNLGCDPLEMGELRIQRYLEGSIAPEDKGSCSLLPGPPFARE... | Function: Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling . Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen thr... |
Q6CPV1 | MVIASLESTHAISTSIVLSSDLWTEFYGTESVSSASPNYVKLTLPSYNKWHHQALISHCDNDDSLPFGSAGLPTNFIKQSQVRPMFSSIEIEPYVQQLPNLDNLVLSLNPDLFNELNQLSKEEQRKFLTLRFNLLFGITVLNVNQVVYPAFCKVTSSSNDFGILTDQTQIVLVPDSNVVEQSRSNDEFTEFDHLFSLHVKIQSLLDPVPVEFLSPPQPDTTDNDLFAFVQPNILLQLGVPSGTFVRVIAEEQEMLVQLFVLFAPNEYECDSLYVSPRVRYVFMNHARVIIQRPNLALNRFSVSNAVTLSRIGCQINAQRR... | Function: Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen throu... |
O34529 | MKRIGVLTSGGDSPGMNAAVRAVVRKAIYHDVEVYGIYNGYAGLISGKIEKLELGSVGDIIHRGGTKLYTARCPEFKTVEGREKGIANLKKLGIEGLVVIGGDGSYMGAKKLTEHGFPCVGVPGTIDNDIPGTDFTIGFDTALNTVIDAIDKIRDTATSHERTYVIEVMGRHAGDIALWAGLAGGAESILIPEADYDMHEIIARLKRGHERGKKHSIIIVAEGVGSGVEFGKRIEEETNLETRVSVLGHIQRGGSPSAADRVLASRLGAYAVELLLEGKGGRCVGIQNNKLVDHDIIEILETKHTVEQNMYQLSKELSI | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 34254
Sequence Length: 319
Pathway: Carbohydrate degra... |
O51669 | MYRIKNENLDFKIDSLGECKQNNPLIDFYASEGSSHFVNEKNKIKFSVYRNEDKGDRYEDVLLEKAGPREKIYFVPRHVKAAITTCGGLCPGFNDVIRSIVRTLWKIYGVRNIYGVKFGYQGLLPESNSPFINLNPDVVDDINKFGGTILGSSRGGIKPVEIVDTLERMNINMIFNIGGDGTQKGSLLIAEEIEKRNLKIAVVGIPKTVDNDFMFVQKSFGFETAVEQAVAAVAGAHFEANSAYNGIGLVKVMGRDSGFIAAHTALSSNDVNFCLIPELDFDIEGPNGFLVHLERRLLEKESLEEIPHAVILIAEGAGQK... | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 49788
Sequence Length: 447
Pathway: Carbohydrate degra... |
C0Z7W7 | MRKLAVLTSGGDSPGMNAAVRAAVRRAHFHEVQMFGVYHGYEGLMRGDIKEMSLGSVGDIIQRGGTILYSARSEAFKTEAGQQRAVEQLRAHEIEGLIVIGGDGSFRGAQKLTEKGFPTIGVPGTIDNDIPCTDFTIGFDTALNTVVEAIDKIRDTATSHERTYIIEVMGRDAGDLALWAGLAAGAESIMIPEASQDMDDIIERLHAGQRRGKKHSIIIVAEGVGSAASYAEAITKETGWETRVTVLGHIQRGGSPTAMDRMLASRMGAAAVDLLLEGKQDRMVGVQNNQIVDVDFQEALAKKHQLDLSIYQLARTLSI | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 34390
Sequence Length: 319
Pathway: Carbohydrate degra... |
Q27543 | GGDGSLTGANRFKGEWSSLVKELLETGKITKEVAEKHSHLNIVGMVGSIDNDFCGTDMTIGTDSALHRIVEVADNIIPTAYSHQRAFVLEVMGRHCGYLALVAGIVTEADFVFAPEWPPEEDWPEKLCKKLELERQSGQRLNIIIVAEGAIDRQGNPITAEGVKKIIVDRLEMDTRTTVLGHIQ | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 20208
Sequence Length: 184
Pathway: Carbohydrate degra... |
Q8R914 | MKTIGILTSGGDAPGMNAAIRAVVRTGIYYGLKVKGIMRGFAGLVEDEVIDLGLSSVGDIIQKGGTILRTARCEEFKQKEVRKKAYETLQKHGIEGLVVIGGDGSFRGAQLLSEEWNVNTICIPGTIDNDIPCTDYTIGFDTACNTVIDAINKIRDTATSHERANIIEVMGRNSGYIALYAGVAGGAEMIILPEVEWSIDELCDKITYGIKRGKLHHIIVLAEGVMSAPELAKMIKERLPKLDLRYTILGHIQRGGAPTVMDRVLASQMGARAVELLLENKTKRVISIRNNQIVDDDIDEALSMKKEFNRKLYELSKILS... | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 35176
Sequence Length: 321
Pathway: Carbohydrate degra... |
A9WCU2 | MASKKQRIGVLTSGGDAPGLNAVIRAVVKSASGLGWEVIGIHDGFEGLLGTKSYRVLTNADVQGLLPRGGTILRTTNKGHFGPRRSDELSEADPYVRAVKAIEEMGLRALITIGGEGTQRIALELHKLGAPVIGVPKTIDNDLAGTDRTFGFDTALQVATDAIDRLHTTAASHNRVMVLEVMGRHTGWIALHAGLAGGADVILIPEIPFSIERVAEKVMARDQQGSSFSIIVVAEGARPRGGSEMYIAEGRLGGIGHWVGEQLEKLTAKEVRVVVLGHLQRGGSPSPYDRLLSTRYGAAAVQAAARGIYGEMVALRGQDI... | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 37703
Sequence Length: 356
Pathway: Carbohydrate degra... |
Q27651 | MSVKRRDHILIPKNPDAPLPSLKIEEVGECTIDNIYASPEPFVNGMTMKLSAVKNHGIERDSGEVELAGPMEKIFYNPETTKVAIVTCGGLCPGLNNVIRGLVLNLYNRYHVNNIFGLRWGYEGLVPELSEVQRLTPEIVSDIHQKGGSILGTSRGAQSPEVMAQFLIDNNFNILFTLGGDGTLRGANAINKELRRRKVPITVVGIPKTIDNDICYTDSTFGFQTAVGLSQEAINAVHSEAKSAKNGIGIVRLMGRDAGFIALYASLANGDANLVLIPEIDIPITQICEFVGKRIMSKGHVVIVVAEGALQNQKPKDLDL... | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 47670
Sequence Length: 436
Pathway: Carbohydrate degra... |
Q8RG98 | MEKKLAILTSGGDAPGMNAAIRATAKIAEYYGFEVYGIRRGYLGMLNDEIFPMTGRFVSGIIDKGGTVLLTARSEEFKEARFREIAANNLKKKGINYLVVIGGDGSYRGANLLYKEHGIKVVGIPGTIDNDICGTDFTLGFDTCLNTILDAMSKIRDTATSHERTILIQVMGRRAGDLALHACIAGGGDGIMIPEMDNPIEMLALQLKERRKNGKLHDIVLVAEGVGNVLDIEEKLKGHINSEIRSVVLGHIQRGGTPSGFDRVLASRMAAKAVEVLNKGEAGVMVGIEKNEMVTHPLEEACSVDKRKSIEKDYELALLL... | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 34931
Sequence Length: 322
Pathway: Carbohydrate degra... |
P00512 | MKRIGVLTSGGDSPGMNAAIRSVVRKAIYHGVEVYGVYHGYAGLIAGNIKKLEVGDVGDIIHRGGTILYTARCPEFKTEEGQKKGIEQLKKHGIEGLVVIGGDGSYQGAKKLTEHGFPCVGVPGTIDNDIPGTDFTIGFDTALNTVIDAIDKIRDTATSHERTYVIEVMGRHAGDIALWSGLAGGAETILIPEADYDMNDVIARLKRGHERGKKHSIIIVAEGVGSGVDFGRQIQEATGFETRVTVLGHVQRGGSPTAFDRVLASRLGARAVELLLEGKGGRCVGIQNNQLVDHDIAEALANKHTIDQRMYALSKELSI | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 34119
Sequence Length: 319
Pathway: Carbohydrate degra... |
Q8CTX6 | MLETNNHTNAWQGFKTGRWNKNIDVREFIQLNYSLYEGDDEFLEGPTKATETLWDQVMQLSKEERERGGMWDMDTKVASTITSHDAGYLDKDLEKVVGVQTEKPFKRSMQPFGGIRMAKAACEAYGYELDPETEKIFTEYRKTHNQGVFDAYSREMLNCRKAGIITGLPDAYGRGRIIGDYRRVALYGVDFLMEQKLKDFNTMSTEMSEDVIRLREELTEQYRSLQDLKELGQKYGFDISRPATNFKEAVQWLYLAYLAAIKEQNGAAMSLGRTSTFLDIYAERDLQNGDITEQEVQEIIDHFIMKLRIVKFARTPEYNE... | Function: Catalyzes the conversion of pyruvate to formate and acetyl-CoA.
Catalytic Activity: acetyl-CoA + formate = CoA + pyruvate
Sequence Mass (Da): 85026
Sequence Length: 748
Pathway: Fermentation; pyruvate fermentation; formate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.54
|
P32675 | MTSSAGQRISCNVVETRRDDVARIFNIQRYSLNDGEGIRTVVFFKGCPHLCPWCANPESISGKIQTVRREAKCLHCAKCLRDADECPSGAFERIGRDISLDALEREVMKDDIFFRTSGGGVTLSGGEVLMQAEFATRFLQRLRLWGVSCAIETAGDAPASKLLPLAKLCDEVLFDLKIMDATQARDVVKMNLPRVLENLRLLVSEGVNVIPRLPLIPGFTLSRENMQQALDVLIPLNIRQIHLLPFHQYGEPKYRLLGKTWSMKEVPAPSSADVATMREMAERAGLQVTVGG | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Activation of pyruvate formate-lyase 2 under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce ... |
P75794 | MIFNIQRYSTHDGPGIRTVVFLKGCSLGCRWCQNPESRARTQDLLYDARLCLEGCELCAKAAPEVIERALNGLLIHREKLTPEHLTALTDCCPTQALTVCGEVKSVEEIMTTVLRDKPFYDRSGGGLTLSGGEPFMQPEMAMALLQASHEAGIHTAVETCLHVPWKYIAPSLPYIDLFLADLKHVADAPFKQWTDGNAARVLDNLKKLAAAGKKIIIRVPLIQGFNADETSVKAITDFAADELHVGEIHFLPYHTLGINKYHLLNLPYDAPEKPLDAPELLDFAQQYACQKGLTATLRG | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Activation of pyruvate formate-lyase 2 under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce ... |
P37836 | GSFPKYGNDDDRVDEIAEWVVSTFSSKLAKQHTYRNSVPTLSVLTITSNVVYGKKTGSTPDGRKKGEPFAPGANPLHGRDAHGALASLNSVAKLPYTMCLDGISNTFSLIPQVLGRGGEHERATNLASILDGYFANGGHHINVNVLNRSMLMDAVEHPEKYPNLTIRVSGYAVHFARLTREQQLEVIARTFHDTM | Catalytic Activity: acetyl-CoA + formate = CoA + pyruvate
Sequence Mass (Da): 21350
Sequence Length: 195
Subcellular Location: Cytoplasm
EC: 2.3.1.54
|
Q46266 | MFKQWEGFQDGEWTNDVNVRDFIQKNYKEYTGDKSFLKGPTEKTKKVWDKAVSLILEELKKGILDVDTETISGINSFKPGYLDKDNEVIVGFQTDAPLKRITNPFGGIRMAEQSLKEYGFKISDEMHNIFTNYRKTHNQGVFDAYSEETRIARSAGVLTGLPDAYGRGRIIGDYRRVALYGIDFLIQEKKKDLSNLKGDMLDELIRLREEVSEQIRALDEIKKMALSYGVDISRPAVNAKEAAQFLYFGYLAGVKENNGAAMSLGRTSTFLDIYIERDLEQGLITEDEAQEVIDQFIIKLRLVRHLRTPEYNELFAGDPT... | Catalytic Activity: acetyl-CoA + formate = CoA + pyruvate
Sequence Mass (Da): 83217
Sequence Length: 740
Pathway: Fermentation; pyruvate fermentation; formate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.54
|
O32797 | MKTEVTENIFEQAWDGFKGTNWRDKASVTRFVQENYKPYDGDESFLAGPTERTLKVKKIIEDTKNHYEEVGFPFDTDRVTSIDKIPAGYIDANDKELELIYGMQNSELFRLNFMPRGGLRVAEKILTEHGLSVDPGLHDVLSQTMTSVNDGIFRAYTSAIRKARHAHTVTGLPDAYSRGRIIGVYARLALYGADYLMKEKAKEWDAITEINEENIRLKEEINMQYQALQEVVNFGALYGLDVSRPAMNVKEAIQWVNIAYMAVCRVINGAATSLGRVPIVLDIFAERDLARGTFTEQEIQEFVDDFVLKLRTMKFARAAA... | Catalytic Activity: acetyl-CoA + formate = CoA + pyruvate
Sequence Mass (Da): 89122
Sequence Length: 787
Pathway: Fermentation; pyruvate fermentation; formate from pyruvate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.54
|
W3XA95 | MVEFVEINGAQLAYRICGPEDAPLVITLHGGRGMGNHQSDFKAFSPLGDSYRILSFDYRGHGQSSRTKPYTFEQIVDDIDGMRARFAGPEKQVIILGGSFGGFLAQQYAIKYASHVSHLILRGTAPSHHHEEGAIKTLEQRLSKVPSFSIEMLKDKVFGAFDSDLEFRMVHLVMSPLYSESFDANAALQSCLNNVYNAESHNDLYSEKEKYFDYTKDLHRITAKTLVVVGDKDWICPPENSKFIAKEIKDAELFLVENANHSVHVEKNDLVVKKIRSHLEK | Function: Proline iminopeptidase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment forming a dark layer in the conidial wall that protects the conidia from UV radiations . The first step of the pathway is the production of the pentaketide 1,3,6,8-tetr... |
W3X9K4 | MSGPALEVAAAKTAEQGQVPVLAAAVRGDTKVSGDSIHAATTAVSDGDNQSSTMSGKTAAGDATSPASGSGSGGWFHWHEPGTSKAEKKLIFKLDWFLLSYSCLCFFIKQLDGNNVTNAYASGMQEQLGFGPGNELSWMNTYFNIGQIIGAPFANMIITVVRPRYWLPACLMTWSAFVLGMYRCETAAQFYVLRFFIGLFEGAAWPGITYTLGCWYRKSEMARRSALFVMSGVLGQMFSGYLQAALYTGMDGKGGLAAWRWLFIFDFILAVPIAIYGLFCFPDTPHKTSAWYLNSWEREKAVERIDSEGRKPIGKLDLSV... | Function: MFS transporter; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment forming a dark layer in the conidial wall that protects the conidia from UV radiations.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58401
Sequence Lengt... |
P24358 | MGTNGVRVFVILYLLAVCGCIEYDVDDNVHICTHTNVSHINHTSWYYNDKVIALATEDKTSGYISSFIKRVNISLTCLNISSLRYEDSGTYKGVSHLKDGVIVTTTMNISVKANIIDLTGRVRYLTRNYCEVKIRCEITSFALNGSTTPPHMILGTVDKWKYLPFPTDDYRYVGELKRYISGNPYPTESLALEISSTFNRFTIVKNLNDDEFSCYLFSQNYSFHKMLNVRNICESEWEALNNNNDNSSSMPASHNNLANDLSSMMSQLQNDNDDNNDYSAPMNVDNLIMIVLITMLSIILVIIVVIAAISMYKRSKYRHI... | Function: Plays a role in the spread of virus to neighboring cells ex vivo.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 36600
Sequence Length: 322
Subcellular Location: Host cell membrane
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P16713 | MIVLPNKVRIFINDRMKKDIYLGISNFGFENDIDEILGIAHLLEHLLISFDSTNFLANASTSRSYMSFWCKSINSATESDAIRTLVSWFFSNGKLKDNFSLSSIRFHIKELENEYYFRNEVFHCMDILTFLSGGDLYNGGRIDMIDNLNIVRDMLVNRMQRISGSNIVIFVKRLGPGTLDFFKQTFGSLPACPEIIPSSIPVSTNGKIVMTPSPFYTVMVKINPTLDNILGILYLYETYHLIDYETIGNQLYLTVSFIDETEYESFLRGEAILQISQCQRINMNYSDDYMMNIYLNFPWLSHDLYDYITRINDDSKSILI... | Cofactor: Binds 1 zinc ion.
Function: Probably involved in maturation of some viral proteins by processing them preferentially at Ala-Gly-|-Ser/Thr/Lys motifs. Does not seem to be responsible for the cleavage of major core proteins.
PTM: Undergoes proteolytic processing during the course of infection. May be cleaved in... |
Q9J5D2 | MTLFLVIFFILFLLLCYFFSFKRTNKMEIGINPIKKIPWSDNEHIFVSSLFTNKDKYLTGPMRLTYRPDSKTAVLDFKGTNYTYYLDNFDDVRKLVPTLLLSK | Function: Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation.
PTM: Unglycosylated be... |
P0DOM3 | MASLLYFILFLLFVCISYYFTYYPTNKLQAAVMETDRENAIIIQRNDEIPTRTLDTAIFTDASTVASAQIYLYYNSNIGKIIMSLNGKKHTFNLYDDNDIRTLLPILLLSK | Function: Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation.
PTM: Unglycosylated be... |
Q80HX0 | MGIKNLKSLLLENKSLTILDDNLYKVYNGIFVDTMSIYIAVANCVRNLEELTTVFIKYVNGWVKKGGHVTLFIDRGSIKIKQDVRDKRRKYSKLTKDRKMLELEKCTSEIQNVTGFMEEEIKAEMQLKIDKLTFQIYLSDSDNIKISLNEILTHFNNNENVTLFYCDERDAEFVMCLEAKTHFSTTGEWPLIISTDQDTMLFASADNHPKMIKNLTQLFKYVPSAEDNYLAKLTALVNGCDFFPGLYGASITPNNLNKIQLFSDFTIDNIVTSLAIKNYYRKTNSTVDVRNIVTFINDYANLDDVYSYIPPCQCTVQEFI... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme.
Function: Putative nuclease that seems to be required for double-strand break repair, homologous recombination, and production of full-length viral genomic DNA.
Sequence Mass (Da): 49847
Sequence Length: 434... |
P0DON1 | MMTPENDEEQTSVFSATVYGDKIQGKNKRKRVIGICIRISMVISLLSMITMSAFLIVRLNQCMSANEAAITDATAVAAALSTHRKVASSTTQYKHQESCNGLYYQGSCYIFHSDYQLFSDAKANCATESSTLPNKSDVLTTWLIDYVEDTWGSDGNPITKTTTDYQDSDVSQEVRKYFCVKTMN | Function: Forms a complex with OPG162 and OPG190 to coordinate the incorporation of OPG164 into wrapped enveloped virion (EV) membranes and, subsequently, the production of actin tails. Therefore plays an essential role in efficient cell-to-cell spread of viral particles.
Location Topology: Single-pass type II membrane... |
P24761 | MKSLNRQTVSRFKKLSVPAAIMMILSTIISGIGTFLHYKEELMPSACANGWIQYDKHCYLDTNIKMSTDNAVYQCRKLRARLPRPDTRHLRVLFSIFYKDYWVSLKKTNDKWLDINNDKDIDISKLTNFKQLNSTTDAEACYIYKSGKLVKTVCKSTQSVLCVKKFYK | Function: Forms a complex with OPG162 and OPG190 to coordinate the incorporation of OPG164 into wrapped enveloped virion (EV) membranes and, subsequently, the production of actin tails . Therefore plays an essential role in efficient cell-to-cell spread of viral particles.
Location Topology: Single-pass type II membran... |
Q5RFB8 | MAAYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYEFDICFTSVQKRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYDVPPPPMEPDHPFYSNISKDRRYADLTEDQLPSCESLKDTIARALPFWNEEIVPQIKEGKRVLIAAHGNSLRGIVKHLEGLSEEAIMELNLPTGIPIVYELDKNSKPIKPMQFLGDEETVRKAMEAVAAQGKAKK | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglyceratea crucial step in glycolysis, by using 2,3-bisphosphoglycerate. Also catalyzes the interconversion of (2R)-2,3-bisphosphoglycerate and (2R)-3-phospho-glyceroyl phosphate.
PTM: Acetylated at Lys-253, Lys-253 and Lys-254 under high glucos... |
P15259 | MATHRLVMVRHGESTWNQENRFCGWFDAELSEKGTEEAKRGAKAIKDAKMEFDICYTSVLKRAIRTLWAILDGTDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEEQVKIWRRSFDIPPPPMDEKHPYYNSISKERRYAGLKPGELPTCESLKDTIARALPFWNEEIVPQIKAGKRVLIAAHGNSLRGIVKHLEGMSDQAIMELNLPTGIPIVYELNKELKPTKPMQFLGDEETVRKAMEAVAAQGKAK | Function: Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase), but with a reduced activity.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 28766
Sequence Length: 253
EC... |
Q61CA3 | MVSKILMYGLPSAAVAVGTALLNEDNRNTIFRKAFAFTQNHTPKSFDEHFPRGEWDKNWDFRDPTSLVDKSKWEKADEVGKKKLLEECKATASRNIFLIRHGQYHLDREQKHLTELGREQAELLGKRLANSDIKFTNMTMSTMTRATETANIILKHLPGDLPKSSSSLIEEGPPYPPVPDHKTWRPLDPEFYTEAARIESAFRKLIHRAPPSQKEDSYELIVCHANVIRYFICRALQFPPEGWLRMSLGNCSITWLVIRPKGHVSIRSVGDIGHLTPNKISFT | Function: Displays phosphatase activity for serine/threonine residues. Has apparently no phosphoglycerate mutase activity.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 32352
Sequence Length: 283
Subcellular Loca... |
Q09422 | MVSKIIKLGVPTATLAVGTLLLGDDEKRSAFFRTASAFTQNHGHKTFDEHFPRGEWDKNWDFRDPISLVDKGKWEKADEEGKKKLIEEKKATATRNIFLIRHGQYHLDHEVKMLTPLGREQAELLGKRLANSDIKFTNMTMSTMVRATETANIILKHLPDDLTRTSSPFIEEGPPYPPVPDHKTWRPLDPEFYTEAARIESAYRKIFHRASPSQKEDSFELIVCHANVIRYFICRALQFPPEGWLRMSLGNCSLTWITIRPKGHVSVRSIGDIGHLPPNKISFT | Function: Displays phosphatase activity for serine/threonine residues. Has apparently no phosphoglycerate mutase activity.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 32490
Sequence Length: 284
Subcellular Loca... |
Q502L2 | MSFRRALSLACGFAGGSAVLVCAAVVADKNGYFGEGRRVTETLAAVNAAHPPAWPTANGWDYNWDKREPSSMVNGKRKESTGENGSQDAENNKPRATRHIFLIRHSQYNLKGDGDKERFLTPLGREQAEFTGQRLASFGLKYDTLIHSSMTRATETANIISKYLPGVELVSCDLLREGAPIEPVPPVTHWKPEAVQYHEDGARIEAAFRRYIHRADAKQKEDSYEIIVCHANVIRYFVCRALQFPPEGWLRLGLNNGSITWLTVRPSGRVSLRALGDSGFMPPDKLTRT | Function: Displays phosphatase activity for serine/threonine residues. Has apparently no phosphoglycerate mutase activity. May be regulator of mitochondrial dynamics (By similarity). May be a central mediator for programmed necrosis (By similarity).
PTM: Phosphorylated by the RIPK1/RIPK3 complex under necrotic conditio... |
O46084 | MRKLTSFVCGTGAGLAAYYLQRLRDPQTVVQNSWTHSDKPVDPWALWDTNWDCREPRALVRPLRNSQPEEENRYNAELEKAKAKKARHIILVRHGEYLDVGDSDDTHHLTERGRKQAEFTGKRLCELGIKWDKVVASTMVRAQETSDIILKQIDFEKEKVVNCAFLREGAPIPPQPPVGHWKPEASQFLRDGSRIEAGFRRYFHRAYPDQEKESYTLIVGHGNVIRYFVCRALQFPAEGWLRININHASITWLTISPSGNVSIKYLGDSGFMPAELLTNRIPRDVKNVV | Function: Displays phosphatase activity for serine/threonine residues, and dephosphorylates and activates Pk92B kinase. Has apparently no phosphoglycerate mutase activity.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Location Topology: Single-pass membrane protein
Sequence Mass ... |
Q29HG0 | MRKFTAFACGTGAGLLTFYLTKLNEPKAAVHNSWTRSEKPVDPCALWDHNWDLRDPKSLVKPVKNDLSQEQNRYNSELEKVVPKHARHIILIRHGEYLDVGDTDETHHLTERGREQAKYTGKRLCELGIKWDKVIASTMVRAQETADIILNEIDYEKAKVKNCAFLREGAPIPPQPPVGHWKPEASQFFRDGARIEAAFRRYFYRAYPDQTKDSYTLLVGHGNVIRYFVCRALQFPPEAWLRISINHASITWLTISPSGNVSIKYLGDTGFMPVNHLTNRIPRAAKNVV | Function: Displays phosphatase activity for serine/threonine residues, and dephosphorylates and activates Pk92B kinase. Has apparently no phosphoglycerate mutase activity (By similarity).
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Location Topology: Single-pass membrane protei... |
Q8TK32 | MLRVMTSRNFLTIDDFDIRGKTILLRVDMNSPMDTQGHILDDMRIKSHIATLKDLESAKVVLLAHQSRPGKKDFTTMKPHAHLLSRYLGKQVTYVDDIFGTFAKTHIASMEDGDVIMLENVRFYSEESLERTPAEQANTYMVKKLAPFVDIFLNDAFAVAHRSHLSVVGFTEVLPSGAGRVMEKELVSLDRGVKGGERPSIFVLGGAKVDDSLRVTENVLTSGGADRVLLTGVVANVALAASGVNIGKVNMDFIKSQGYENQIEKARGLLAKFKDRIGLPKDVALNDNRERVEVHISELNSDSLPINDIGLETIVDYTNE... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 45499
Sequence Length: 416
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
Q49156 | MILVEGKVAGKKYREPFSKGVLARSLTRSGMDPTDAYLLAAEVESYLKKEKKKIVTIDELVKIVYNKLKEKDEKIAEKYIRWRKIREYKEPLILLIAGASGVGTSSIAFEVANRLGIRNMISTDMIREVMRKMISKELIPSLHESTFTAYKSLRTPAPVEFDEVLVGFRDHVNVVTVGIEAVIERALTEGISIVIEGAHLVPGFIREELINKNNVAMFVLTVPDEKMHRSRFYSRCRQKWARRPLERYLKYFWAIRRIHDYIEMQARKHNIPIIENIDVVTTIDSIVKSLTEDLVHKDVGKYKG | Function: Catalyzes the phosphorylation of 2-phosphoglycerate to 2,3-diphosphoglycerate. Involved in the biosynthesis of cyclic 2,3-bisphosphoglycerate, a thermoprotectant.
Catalytic Activity: (2R)-2-phosphoglycerate + ATP = (2R)-2,3-bisphosphoglycerate + ADP + H(+)
Sequence Mass (Da): 35036
Sequence Length: 304
Pathwa... |
Q58877 | MDLQNDIIVRGKSYEMPFSKGILARSLTAAGLKPSIAYRIAWDIYEMLKKENIRVIDKADLRRRVYYYLISKNYDEVAKKYLLWRMVLGRRPIVILIGGASGVGTSTIAFEIASRLGIPSVIGTDSIREVMRKVISRDLIPTLYESSYTAWKVLRDDEGNKYIKGFERHSEAVLTGVEGVIDRCLVEGQSVIIEGTHLVPTLLKDKYLENSHVVFIMLTIYNEELHKMRFYARGRVSSRPTERYLKYFKIIRMINDYMVETAKKKGIPVVENIKISETVDKCLNIITERLKTMIELEGLSEEDMLEEGL | Function: Catalyzes the phosphorylation of 2-phosphoglycerate to 2,3-diphosphoglycerate. Involved in the biosynthesis of cyclic 2,3-bisphosphoglycerate, a thermoprotectant.
Catalytic Activity: (2R)-2-phosphoglycerate + ATP = (2R)-2,3-bisphosphoglycerate + ADP + H(+)
Sequence Mass (Da): 35545
Sequence Length: 309
Pathwa... |
Q8TGY9 | MSEKSSRKERDEKTEKETARQGKHRRIRVKSRHYEMPFSRGVLARSLTAIGVEPHKAYEIALKIKEELQDEGIEEISTDELADIIRTKLEEIDETLAERYELWRRIKKREEPIIVLIGGASGVGTSTIASEVGHRLGITNVIGTDAIREVMRRVLAEELYPTLYESSYTAWKRLRYEPAEDPVITGFLDHSEPVVVGIEGVVNRSINEGIHVIVEGVHIVPRLIKKEILNYPNVFVFMLAVEDEEAHKWRFYARSRDTKLSRPAERYLKYFEEIRRIHDFLVEDAEEHDIPVINNEHIDETVDQIVSYISSKLLKGEREL... | Function: Catalyzes the phosphorylation of 2-phosphoglycerate to 2,3-diphosphoglycerate. Involved in the biosynthesis of cyclic 2,3-bisphosphoglycerate, a thermoprotectant.
Catalytic Activity: (2R)-2-phosphoglycerate + ATP = (2R)-2,3-bisphosphoglycerate + ADP + H(+)
Sequence Mass (Da): 37960
Sequence Length: 327
Pathwa... |
P09041 | MALSAKLTLDKVDLKGKRVIMRVDFNVPMKNNQITNNQRIKAAIPSIKHCLDNGAKSVVLMSHLGRPDGIPMPDKYSLEPVADELKSLLNKDVIFLKDCVGPEVEQACANPDNGSIILLENLRFHVEEEGKGKDSSGKKISADPAKVEAFQASLSKLGDVYVNDAFGTAHRAHSSTVGVNLPQKASGFLMKKELDYFSKALEKPERPFLAILGGAKVKDKIQLIKNMLDKVNFMIIGGGMAYTFLKELKNMQIGASLFDEEGATIVKEIMEKAEKNGVKIVFPVDFVTGDKFDENAKVGQATIESGIPSGWMGLDCGPES... | Function: Essential for sperm motility and male fertility but is not required for the completion of spermatogenesis .
Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 44853
Sequence Length: 417
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D... |
P29406 | MSLSNKLSIRDLDLKNKRVLIRVDFNVPMKDGAITNNNRIVQALPTVKYALDNGASAVILMSHLGRPNGEAVAKYSLKPVAAEVEKLLGKPVEFLNDCVGPDVEKACQSATGGKVILLENLRFHIEEEGSAKVRWSKVKADAEAVKKFRASLTALADIYVNDAFGTAHRAHSSMVGVDLSQRAAGFLMQKELEYFAKALENPARPFLAILGGAKVSDKIQLIENMLDKVNALIVCGGMAFTFKKTLDNVKQIGKSLFDEAGSKLVRNLVKKAAEKNVKLVFPVDFVTADKFAPDANTGYATDADGIPDEWEGLDCGKKSS... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 44656
Sequence Length: 417
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
Q5JDW9 | MIIVTDSERKIRLPFSRGILTRSITLAGIDVGIAYAIATEVQKELEWKGKKSVTTEEIRELTYQKLLEKGLREEAKRYLFWRELRRRKVRLTVLLGGATGVGKSTIATELAFRLGIRSIIGTDTIREVMRKIIAKELLPDIHVSSFLAERVVKAPKNSDPLIYGFETQVKHVSVGIKAVLERARREGLNTLIEGIHVVPGFVEPREDEFMYVIAVPKKDYLIAHFYERARYSQRDAEKYVKHVDRIMRIQDYLVERAREHGIPVIENVELESTVSTILADMMKKLEEMGV | Function: Catalyzes the phosphorylation of 2-phosphoglycerate to 2,3-diphosphoglycerate. Involved in the biosynthesis of cyclic 2,3-bisphosphoglycerate, a thermoprotectant.
Catalytic Activity: (2R)-2-phosphoglycerate + ATP = (2R)-2,3-bisphosphoglycerate + ADP + H(+)
Sequence Mass (Da): 33291
Sequence Length: 290
Pathwa... |
A7HCN7 | MALKTIDALDLAGKRVFIRVDFNVPLDEQRRVTDDARIRAALPTIKHAIQARAKVILGSHLGRPKGKPDDREKFSLEPAAQRLSELLKQDVILADDCIGDGVKKLVRDLKEGQVLLLENLRFHPQEEKNDEGFARELATLCDVWVNDAFGTAHRAHASTAGMAAFVKEKAAGFLIQKEVEYLGKALGSPERPFVALIGGAKVSDKIKVLENLIAKADAICIGGAMAYTFLKAQGVAVGKSLVEEDKLELARQILERAQARKVDLLLPVDHVCGAEPKDTAERVVVNDRAIPDGLMGLDIGPKTLDRYRQRIVDAKTVFWN... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 42732
Sequence Length: 396
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
O66519 | MLRKKTLRDVDVKGKRVLVRVDYNVPLDEQGNIVDDTRIRASLPTVEYLLDANAKVILMSHLGRPKNRDPKYSLAPVAKRLSRYINKEVKLAPDCVGEEVKRIVNSMKEGDVVLLENLRFHKEETECDENFARELASLGEVYVADAFGTCHRKHASVYLVPKFLKPAVMGFLLEKEITYFEKAMVAPQRPVVAILGGAKVSSKLEVIKNLIRRVDKLFIGGAMAFTFLKAMGYKVGNSLVEDDLQDVARDLIDVAKKLEIKLYLPVDFVIGQEVSENTPTKVVPWQEIPDGWMGLDIGPVSVELVKEIISDAQTIVWNGP... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 43956
Sequence Length: 397
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
O29119 | MMIDGLPTLDDIPYRGKHVLLRVDINAPIVNSTILDTSRFESHIPTIEALEDSKLVLLAHQSRPGKKDFTSLESHASTLSKLLGKRVEYIDEIFSKGVLRRIKEMENGEVILLENVRFYSEEQLNRSAEEHAECHMVRKLSTAFDLFVNDAFSASHRSHASLVGFVPVLPSVVGRLVENEVTALSKPLKGEGRKIFVLGGAKIKDSVKVLKNVLENNIAEKVVLTGVVANYFLMLKGYDIGEVNRKVVEDNKEDVSDEEMINILKKYSDKIILPIDLGIEKDGVRVDIPLEKFDGKYRIMDIGLETVNQLSEIIPKYDYV... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 45278
Sequence Length: 407
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
Q5P7K8 | MNVKKLADLDVAGKRVFIRADLNVPQDEAGNIVEDTRIRASLPSIRYCLERSATVMVTSHLGRPTEGECRAEDTLAPIAVRLGELLGKPVRLIRDWVEGGFEVRAGEVVLLENCRCNKGEKKDNEELAKKMAALCDIYVNDAFGTAHRAEATTHGIARFAPVACAGMLMGAEIDALTKATENPARPLVAIVGGAKVSTKLTILKTLAEKVDQLIVGGGIANTFLLASGKRIGESLAEPELVKEAQAIMDMMKARGAEVPLPVDVVVADEVSALARANRIPVDEVGPHDRILDVGPKSSAKLAEIIAHAGTIVWNGPVGVF... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 41688
Sequence Length: 394
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
B5Y8I0 | MKLRSIRDAEVRNKRVIVRVDFNVPLDAEGNVVDDFRIRAALPTIEYLVENGAKVILISHLGRPKGKRDKKYSLVGVAKRLAELLHKEILFAPDVVGEEVELAVNGLRSGDILLCENVRFHEEEEKNDAEFAKNIASLGEIFVNDAFSASHRAHATVEGITKFLPSYAGFLMEKEVNYLSMLTENPQRPYYLVLGGAKVSDKVALLQNLLPKVDGMVIGGAMVFTFWKAQGKEIGKSIVEDDLVGFAKELLEQATTQNKEIVLAKDFVVADENKEHVEIKAISDFGPADIGYDIGPESIKEFKNALVKARTVFWNGPLGL... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 42974
Sequence Length: 393
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
C4LIR6 | MAVKKLADLLKEGVEGRHVLVRADLNVPLKDKVITDPGRIDASLPTIKALTEAGARVIVAAHLGRPKSPQDTQFSLAPVAEALSQRLDQYVALASDVSGEDAHERANGLNDGDVLLLENVRFDPREKSKNDAEREELASELAALTGDNGAFVSDGFGVVHRKQASVYDVAKKLPAYVGYLVEKELEQLSKCTDDPQHPYAVCLGGSKVSDKLGVIKALAPKVDTLIIGGGMCYTFLKAKGYGVGDSLLEESMIDECKNLLSEYSDKIVLPSDIVVGKEFDANTEHKTVSADGIEDGWMGLDTGAESIKTFGERLNGAKTI... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 42648
Sequence Length: 403
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
Q83AU6 | MSNLNLHNKRVMIREDLNVPMKNGKITNDERIVRALPTIQKAIEQKARVMILSHLGRPEEGKFEKEFSLAPVARLLSKKLNQKVPLINDWLKGVAVEPGQAILCENVRFNKGENENNTELAKRMAELCDIFVMDAFATAHRAQASTAGVAAYAKLACAGPLLISEVEALSRALENPQKPLVAVVGGSKVSTKIHLLENLLDKVDQLIVGGGIANTFLKAQGYSIGKSLCENEWLDAAQQFWEKAAEKNVSLPLPVDVIVADELSEDAKATVKNIDAVTSNESIFDVGPNTSATYAKLMAQAGTIVWNGPIGVFEIEAFSQ... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 42363
Sequence Length: 391
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
B8HXQ5 | MSKKTVANLSAADLAGKRVLVRVDFNVPLDDQGKITDDTRIRAALPTIQDLTSKGAKVILSSHFGRPKGETFAERVKDKFRLTPVAARLSELLGKPVPKPNDCIGEEVKAQVAAMQNGDVLLLENVRFHPGEEANTPEFAQELASVADLYVNDAFGTAHRAHASTEGVTRYLRPSVAGYLIEKELQYLQSAIENPQRPLAAIVGGSKVSSKIGVIETLLEKVDKLLLGGGMIFTFYKARGLNVGKSLVEEDKLELARTLEAKAKERGVALLLPTDVVVADAFAADANAQTVSVESIPDGWMGLDIGPDAVKTFQEALSDC... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 42955
Sequence Length: 406
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
Q9RUP2 | MTGLCPLHQPSPLDHPHSGGTPMQNLSQLDVKGKRVLVRVDYNVPVGDGVVQDDTRITASVPTIKKLLDGGASVVLMSHFGRPKNGPEDKYSLKPVAEAVSRALGQDVKFIPSLPGSDETLQAVQALRPGEVALLENVRFEAGEEKNDAALNDKLAKLGDAFVLDAFGSAHRAHSSVSGVAGKLPHAAGGLLQSEVDALGKLLHAPEHPYVVIIGGAKVSDKIKVIENLLPKVDRMLIGGGMMFTFIKARGGQIGNSLVEDDQLDLAKGLLEKYGDKLLLPTDAVAADKFAADAQSKVVPADQIPDGWMGLDIGPDTQRA... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 42899
Sequence Length: 411
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
Q98QW4 | MKKLITDLNLNDKKVLIRLDLNVPLKGKKITSLKRIEESIPTIKYVQERGGKIILLSHLGRVKTKEDKEKKSLSIVVEALASLLNSPVKFVDQTRGKKLESAIEKLKPGDVLLIENTRFEDLNNNAESNNDPELGKYWASLGDVFINDAFGTAHRAHASNVGIASNIKESALGILVQKEVNALWKLMEQQEKPFVAILGGSKVSDKINVLEKIIDKVDRLIIGGAMAYTFLKAQGIGIGDSIYEQDKIEFATEFLKKYNHKIILPIDHALAKKFKNAKPIFNNENPLEIPQTFIGMDVGPKTIELIHKYIKGDTKLGISP... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 86689
Sequence Length: 771
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
A0QWW3 | MSVKTLDDLLAEGVQGRGVLVRSDLNVPLDDDGNITDPGRVIASVPTLQALAEAGAKVIVTAHLGRPKGEPDPKLSLAPVAAALGEKLGRHVQLAGDVVGTDALARAEGLTDGDVLLLENIRFDARETSKDDSERLSLAKALAALVEGPDGSPGVFVSDGFGVVHRKQASVYDVATLLPHYAGTLVAAEVKVLQQLTSSTDRPYAVVLGGSKVSDKLAVIENLATKADSLIIGGGMCFTFLAAQGFSVGSSLLQEEMVDTCRRLLDEYADVIHLPVDIVVADKFAADAEAETVAADRIPDGKMGLDIGPGSVERFTALLS... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 42095
Sequence Length: 408
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
Q3INZ6 | MIRTLDDLEADGTALGVRIDINSPLSSDGLADDARLRAHVDTVEELCRRDARVALLAHQGRPGGDEFSDLERHAERLDELLDAPVEYCDSTFSAEARTRIDELDPGRAVLLENTRFYSEEYMSFEPSAAAETYLVSRLAPALDAYVNDAFATAHRSQPSVVGFPERLPAYAGRVMERELDVLGNIESSPEPRVYVLGGAKVDDSIAVARSVLERGLADSVLTAGIVGNAFLLADGVSLGAASAAVVNERSHEAVKQAGDLLDDFSHRIYMPRDVAVENDAGERVEHDLEDLPASTPAMDIGARTVAAYANILDDAGTAIL... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 42316
Sequence Length: 396
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
B2FSF3 | MSIVRMTDLDLSGKRVLIRQDLNVPIENGRITSEQRITASLPTLKRALEQGAAVMVTSHLGRPKEGVWSEADSLAPVAQRLSELLGREVPLVRDWVDGVEVQPGQLVLLENCRMNVGEGKDDEALSKKYAALCDVFVMDAFGTAHRAQASTHGVIRFAPVAAGGPLLMAELDALAQALDAPAKPLLAIVAGSKVSTKLELLANLVGKVDQLIVGGGIANTFIAAAGYNVGKSLYEPDLLDTAKKIVADAKARGADIPLPVDVVTAKQFMPDAVAEVKAVDAVAEDDLILDIGPQTAAQYAQLIDKAGTVVWNGPVGVFEF... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 40921
Sequence Length: 391
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
Q04LZ5 | MAKLTVKDVDLKGKKVLVRVDFNVPLKDGVITNDNRITAALPTIKYIIEQGGRAILFSHLGRVKEESDKAGKSLAPVAADLAAKLGQDVVFPGVTRGAELEAAINALEDGQVLLVENTRYEDVDGKKESKNDPELGKYWASLGDGIFVNDAFGTAHRAHASNVGISANVEKAVAGFLLENEIAYIQEAVETPERPFVAILGGSKVSDKIGVIENLLEKADKVLIGGGMTYTFYKAQGIEIGNSLVEEDKLDVAKALLEKANGKLILPVDSKEANAFAGYTEVRDTEGEAVSEGFLGLDIGPKSIAKFDEALTGAKTVVWN... | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 41939
Sequence Length: 398
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
Q00293 | MRLTHVLSHTLGLLALGATAEAFSRSREAACGPKKPFRPLPTSQSRDKTCHVRSHGDGTDDSDYILSALNQCNHGGKVVFDEDKEYIIGTALNMTFLKNIDLEVLGTILFTNDTDYWQANSFKQGFQNATTFFQLGGEDVNMYGGGTINGNGQVWYDLYAEDDLILRPILMGIIGLNGGTIGPLKLRYSPQYYHFVANSSNVLFDGIDISGYSKSDNEAKNTDGWDTYRSNNIVIQNSVINNGDDCVSFKPNSTNILVQNLHCNGSHGISVGSLGQYKDEVDIVENVYVYNISMFNASDMARIKVWPGTPSALSADLQGG... | Function: Specific in hydrolyzing the terminal glycosidic bond of polygalacturonic acid and oligogalacturonates.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl](n) + H2O = [(1->4)-alpha-D-galacturonosyl](n-1) + alpha-D-galacturonate
Sequence Mass (Da): 47296
Sequence Length: 435
Subcellular Location: Secreted
EC: 3... |
P35336 | MALQRRFFQFVIITLLIPSFILGYTSAVHEDPPHDYHLEEYGYDFKAYPSYITTIGDNDFGSSMSHENGIFGLRKVDYGMDRVLDASKTVNVDDFGAKGDGRDDTKAFEKAWKAACSSTSSAVLLVPKKNYLVRPISFSGPCKSGLTMQIYGTIEASDDRSDYRKDGRHWLVFDSVQNLRVEGGGTINGNGKIWWQNSCKTNKALPCKDAPTALTFYKSKHVIVKNLKIENAQQIHVSFDNCVNVQASNLMVTAPENSPNTDGIHVTGTQNIHISSCVIGTGDDCISIVNGSRKVRVNDITCGPGHGISIGSLGYGNSEA... | Function: Acts in concert with the pectinesterase, in the ripening process. Is involved in cell wall metabolism, specifically in polyuronide degradation.
Catalytic Activity: (1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.
Sequence Mass (Da): 50776
Sequence Length: ... |
P35337 | MGSYLGIYTILVLCLLGYSANAEVFTAGGPPNSDITAAVLKAFTSACQAPAPSQVLIPKGDFKLGETVMTGPCKSPIEFTLQGNVKTDGGSTQGKDRWVVFEKINGFKLNGGGTFDGEGNAAWKANNCHKTFECKKLPISVRFDFVDNAEIKDVTSLDAKNFHFNVISGKNMTFDNIKIIAPAESPNTDGIHLGRCEGVKILNTKIATGDDCISVGDGMKNLLIEKVVCGPGHGISVGSLGRYGWEQDVTDITVKNCTLEGTSNGLRIKTWPSAACTTTAAGIHFEDIILNKVSNPILIDQEYCPWNQCNKNKPSTIKLV... | Function: May function in depolymerizing pectin during pollen development, germination, and tube growth.
Catalytic Activity: (1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.
Sequence Mass (Da): 42447
Sequence Length: 397
Subcellular Location: Secreted
EC: 3.2.1.15
|
C0HKB1 | DVAIVFNVEHTLSAVFLVPANKKVDGIIAAYPDPVKIWMHFARTVCNDKGRPTAIKIDFSKSELTLMNSPEFHLVFGECDGVKIQGIKIKRFEIEKDLTCGPGHGMSIGSLGKGNSRSEVSFVHLDGAKFIDTQNGLRSAVKIEDVTFKNANGYYTNPLNPPCK | Catalytic Activity: (1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.
Sequence Mass (Da): 17996
Sequence Length: 164
Subcellular Location: Secreted
EC: 3.2.1.15
|
Q07181 | MVRNIVSRLCSQLFALPSSSLQERDPCSVTEYSGLATAVSSCKNIVLNGFQVPTGKQLDLSSLQNDSTVTFKGTTTFATTADNDFNPIVISGSNITITGASGHVIDGNGQAYWDGKGSNSNSNQKPDHFIVVQKTTGNSKITNLNIQNWPVHCFDITGSSQLTISGLILDNRAGDKPNAKSGSLPAAHNTDGFDISSSDHVTLDNNHVYNQDDCVAVTSGTNIVVSNMYCSGGHGLSIGSVGGKSDNVVDGVQFLSSQVVNSQNGCRIKSNSGATGTINNVTYQNIALTNISTYGVDVQQDYLNGGPTGKPTNGVKISNI... | Function: Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.
Catalytic Activity: (1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.
Sequence Mass (Da)... |
Q39786 | MAPHLNIVPSMFVLLLLFISASKVQSDAFDVVAKFGAKADGKTDLSKPFLDAWKEACASVTPSTVVIPKGTYLLSKVNLEGPCKAPIEINVQGTIQAPADPSAFKDPNWVRFYSVENFKMFGGGIFDGQGSIAYEKNTCENREFRSKLPVNIRFDFLTNALIQDITSKDSKLFHINVFACKNITLERLKIEAPDESPNTDGIHMGKSEGVNIIASDIKTGDDCISIGDGTKNMVIKEITCGPGHGISIGSLGKFQNEEPVEGIKISNCTITNTSNGARIKTWPGEHGGAVSEIHFEDITMNNVSSPILIDQQYCPWNKCK... | Function: May function in the depolymerization of the pectin in its walls during pollen tube elongation, or in that of the pistil during pollination.
Catalytic Activity: (1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.
Sequence Mass (Da): 43921
Sequence Length: 407
... |
Q40312 | MKFSTAIIVSFLFIADFCAAQSGVLDISKFGGKPNSDIGQALTSAWNEACASTTAAKIVIPAGTYQLNGIELKGPCKAPIELQVDGTIQAPADPSVIKGTEQWFKFLYMDHLTLSGKGVFDGQGATVYKKAAPASAWSGKNSNSKVFMNFGFNFVNNSIVRGVTSKDSKNFHVMVFGCKNITFDGFTITAPGDSPNTDGIHMGKSTDVKILNTNIGTGDDCVSIGDGSKQITVQGVNCGPGHGLSVGSLGKFTTEENVEGITVKNCTLTATDNGVRIKTWPDAPGTITVSDIHFEDITMTNVKNPVIIDQEYYPWNQCSK... | Function: May function in the depolymerization of the pectin in its walls during pollen tube elongation, or in that of the pistil during pollination.
Catalytic Activity: (1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.
Sequence Mass (Da): 43953
Sequence Length: 421
... |
P24548 | DSTQALTTAWKEACASASPSTILVPKGNFAVGLITLEGPCKSSIGLQLQGTLKAPADPSKIKGLGWINLNKIDLLTIFGGGVFDGQGKSAWVQNDCHKNGPICKTLSMNLRLYAVTNSILRDVTTLDSKNFHVNVIGCKNLTFERFKISAAETSINTDGIHIGRSDGVNIINTEIKTGDDCISLGDGSKNINITNITCGPGHGISVGSLGRYKNEESVVGIYVKNCTITGSQNGVRIKTWPKSEPGEASEMHFQDITMNSVGTPILIDQGYCPYNQCTAEVPSSVKLSKISFKNIKGTSTTKEAVKLVCSKSFPCNGVEL... | Function: May function in depolymerizing pectin during pollen development, germination, and tube growth. Acts as an exo-polygalacturonase.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl](n) + H2O = [(1->4)-alpha-D-galacturonosyl](n-1) + alpha-D-galacturonate
Sequence Mass (Da): 38207
Sequence Length: 362
Subcellula... |
Q9LXR9 | MQTPSMAASTTSYYPIPKSFLLSPPRHKRNPNLISCSTKPICSPPPPSSSSSSPLQTTTTHRSQKQNLRLPTFEDSFLLYQFSSPTEDPGFSNRIPEQFDGEPRELVLPRVEDNNKGLAISSNMWWADLKAALGQRINIEGIVSSVSVVVKDRQFVLPHVSVKDLRYIDWEVLKRKGFKGVVFDKDNTLTAPYSLAIWPPLRPSIERCKAVFGHDIAVFSNSAGLTEYDHDDSKAKALEAEIGIRVLRHRVKKPAGTAEEVEKHFGCTSSELIMVGDRPFTDIVYGNRNGFLTVLTEPLSRAEEPFIVRQVRRLELALLK... | Function: Phosphatidylglycerophosphate (PGP) phosphatase involved in the biosynthesis of phosphatidylglycerol (PG), a phosphoglycerolipid predominantly present in chloroplastic thylakoid membranes and which has important photosynthetic function; seems to use PGP 34:3, PGP 34:2 and PGP 34:1 as substrates . Required for ... |
A0A2K3DU55 | MRSVPGPSPPCTRSLAHSCRAAARGPCGSARPRARSVSARAHSSEASDMARVQQNFNSAGVGLFFSLFGGNQSLALPHLAAPDIRHVDWRALKAAGFKGLVFDKDNTLSLPFALEVEPRLQPALAGCLEAFGGRAVLYSNSAGLQQYDPEGKEAAALEAALGIPVLRHADKKPGGGCAELEAHFGCPAPQLIMVGDRYLTDIAFGNRHGMLTVHVQPLTTSGEPFGVVMARRIEEFWVARWTSFGVHPPAHSLAPHDTLAAYVKDQPIA | Function: Phosphatidylglycerophosphate phosphatase involved in the biosynthesis of phosphatidylglycerol (PG), a phosphoglycerolipid predominantly present in chloroplastic thylakoid membranes and which has important photosynthetic function . Required for thylakoid membranes development and chloroplast function (By simil... |
O80952 | MLRSGLASLIVDVNLRRTLRPSPTFSFPAHLSRCIITSRYSSRTSLRFPIQISRHQHRLSYFSSSSSSEQSRPTSSSRNSFSGHGQLDSDDNSSPPPSQSSSKVLTLPTVLTLGRVAAVPLLVATFYVDSWWGTTATTSIFIAAAITDWLDGYLARKMRLGSAFGAFLDPVADKLMVAATLILLCTKPIQVAELGPLPWLLTVPSIAIIGREITMSAVREWAASQNGKLLEAVAVNNLGKWKTATQMTALTILLASRDSNVGWLVASGAGLLYVSAGLSVWSLAVYMRKIWKVLMK | Function: Catalyzes the committed step to the synthesis of the acidic phospholipids. Transfers specifically a phosphatidyl group from CDP-diacylglycerol to glycerol-3-phosphate to form phosphatidylglycerophosphate. Cannot catalyze the phosphatidyl group transfer to inositol, serine, choline or phosphatidylglycerol. Pos... |
Q2KJ28 | MAAAAAAAAGPVFWRRLLGLLPGRPGLAALLGRLSDRLGRNPDRRRRRSPWLLLAPLLSPAVPVVTSPPCCLCAEGVHRFQWIRNLVPEFGVSSSHVRVLSSPAEFFELMKGQIKVAKRRVVMASLYLGIGPLEQELVDCLESTLEKSLQAKFPSGLRVSILLDFTRGSRGRKNSRTMLLPLLQRFPEQVRVSLFHTPNLRGLLRLLIPERFNETIGLQHIKVYLFDNNVILSGANLSDSYFTNRQDRYVFLQDCPEIADFFTELVDAVGDVSLQLQGDDTVQMVEGMVHPYKGDRAAYCRAANKRVMDVINSARMRQQM... | Function: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
Sequence Mass (Da): 62732
Sequence Length: 556
Pathway: Phosph... |
Q5ZHN9 | MAAAGGAALWRRLAAWLPRGPPGLAALLGRLSDRLSRGRDRRSRRSSWLLLAPLLTPPVPVITAMPCSLCPEGAHRFQWIRNLVPEFGISSSHVKVLSSPAEFYELLKVQIKTAKQRVVMASLYLGTGLLEQELVNCLEETLEKSLQANESPNLRVSILLDYTRGSRGRKNSRTMLIPLLQRFPEQVRVSLFHTPNLRGLLKLLIPERFNETIGLQHIKVYLFDDNVILSGANLSDLYFTNRQDRYVLLQDSPEIADFFTELVDAIGDVSLQLQQDDTVQMMEGMVHPYQGDKVRYCEIANQRVMEVIDSARTRQELLHA... | Function: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
Sequence Mass (Da): 63067
Sequence Length: 557
Pathway: Phosph... |
Q9Z2Z7 | MAAPAAGPVFWRRLLGLLPGRPGLAALLGRLSDRLGRSRERRRRRSPWLLLAPLLSPTVPQVTSPPCCLCPEGVHRFQWIRNLVPEFGVSSSHVRVLSSPAEFFELLKGQIKMAKRRVVMASLYLGTGPLEQELVDCLESSLEKSLQSKFPSDLKVSILLDFTRGSRGRKNSRTMLLPLLQRFPEHVRVSLFHTPNLRGLLRLLIPERFNETIGLQHIKVYLFDNNVVLSGANLSDSYFTNRQDRYVFLQDCAEIADFFTELVDAVGDVSLQLQGDDTVDVVDGMVHPYKGDRAAYCRAANKRVMDVIHSARTRQQLLHA... | Function: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
Sequence Mass (Da): 62369
Sequence Length: 553
Pathway: Phosph... |
Q7KWX2 | MIKRALAPIVQPQRLFAALMVIGGGGRSATTTTTTTTKACGNGSSQSPPSTPLLSSKSSTITSNKKSAIPSSHLYIPKKSTLDSRQIGNYSREYSTSSSSSSKKSIFNDTYLNDLFWQLSSQGPAFEVNPNNIDFIQEPIDFYNHLIDGVKRSKKRITMASLYLGTSKQEIELVKEMKLAMERNKELKIHILLDGLRGTRIGLDKESSATILGELLSLYSDRVTISMYHTPDLNGILKKVLPPRINETIGVQHIKTYIFDDDLLLSGANLSKDYFTNRQDRYVLIRSTSTVSNYFNEIVEIIGSLSLHVDKDNRNQLLLS... | Function: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
Sequence Mass (Da): 65509
Sequence Length: 581
Pathway: Phosph... |
Q32NB8 | MAVAAAAAAGPVFWRRLLGLLPGRPGLAALLGRLSDRLGRNRDRQRRRSPWLLLAPLLSPAVPQVTSPPCCLCPEGVHRFQWIRNLVPEFGVSSSHVRVLSSPAEFFELMKGQIRVAKRRVVMASLYLGTGPLEQELVDCLESTLEKSLQAKFPSNLKVSILLDFTRGSRGRKNSRTMLLPLLRRFPEQVRVSLFHTPHLRGLLRLLIPERFNETIGLQHIKVYLFDNSVILSGANLSDSYFTNRQDRYVFLQDCAEIADFFTELVDAVGDVSLQLQGDDTVQVVDGMVHPYKGDRAEYCKAANKRVMDVINSARTRQQM... | Function: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
Sequence Mass (Da): 62730
Sequence Length: 556
Pathway: Phosph... |
Q5N9A1 | MAFLKTLNPLLRRSPTPIPNPRSLLSLDAFLAASSPTAASHATAPAPFAAAAHHHVPIRSGGPLFLSSPPWMLSQSATPLTAAAAALRARLRRARALAGGGAQAVADAVGWEPRRISRDESEVAEAVTGGRERFLNLPNLVSIGRMASGPVIGWMIVNEWYLPAFGTLALSGASDWLDGFLARKMGINSVFGSYLDPLADKVLIGCVAIAMVEKDLLHPGLVGLVVVRDLLLVGGAVYKRASSLGWKWNSWSDFVNLDAIHREKVKPLFISKVNTVFQLMLVAAALLQPEFGTEETQNYITVLSWLVASTTIASTVGYGI... | Function: Catalyzes the committed step to the synthesis of the acidic phospholipids. Transfers specifically a phosphatidyl group from CDP-diacylglycerol to glycerol-3-phosphate to form phosphatidylglycerophosphate (By similarity).
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-s... |
Q9HDW1 | MDEGIEKNIFVNLESQIDGVCPKFYVNVDDIDIIHEPPEFYQRLKKLIKKAQKRIFLSTLYIGKEERELINCLSNALSNNPSLHVHILADQLRCTRESPGCCSASLLMQLKKKFPDRCEIKLYHTPNLRGLRKQLVPHRFNEGWGLQHMKIYGADDNLIISGANLSRDYFTNRKDRYYLFSDKGLADFFFKTHFLFSQLSFECIPHLSDSSIQLSSTSPVIPFTLKWNNSCPNPLTNPQEFRVAASAKIQQLLQGNREKFLSRNPSKPLSSVYGSELINQAGDDNNKPFHKYEESAIVYPLFQCVPILTSDVHSTEEKVL... | Function: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
Sequence Mass (Da): 57676
Sequence Length: 502
Pathway: Phosph... |
P25578 | MTTRLLQLTRPHYRLLSLPLQKPFNIKRQMSAANPSPFGNYLNTITKSLQQNLQTCFHFQAKEIDIIESPSQFYDLLKTKILNSQNRIFIASLYLGKSETELVDCISQALTKNPKLKVSFLLDGLRGTRELPSACSATLLSSLVAKYGSERVDCRLYKTPAYHGWKKVLVPKRFNEGLGLQHMKIYGFDNEVILSGANLSNDYFTNRQDRYYLFKSRNFSNYYFKLHQLISSFSYQIIKPMVDGSINIIWPDSNPTVEPTKNKRLFLREASQLLDGFLKSSKQSLPITAVGQFSTLVYPISQFTPLFPKYNDKSTEKRTI... | Function: Essential for the viability of mitochondrial petite mutant. Catalyzes the committed step to the synthesis of the acidic phospholipids.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
Sequence Mass (Da): 5937... |
Q9M2W3 | MGEEDTATVDQNSFGGGKDSLLRNRHSSPLPSPTQLSSKVITLPTVLTLGRVAAVPILVATFYVDCWWGRTATTSIFIAAAITDWLDGYIARKMRLGSEFGAFLDPVADKLMVAATLILLCTKPMVAVVLGPVPWLVTVPSIAIIGREITMSAVREWAASQNGKLSEAVAVNSLGKWKTATQMIALTILLASRDSSFERLLPSGIGLLYVSAGLSIWSLVVYMRKIWRVLLKK | Function: This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 2522... |
Q9VYX7 | MQPVRFGSPWIMAIGLVLLLLAFVSAGKSRQRSPANCPTIKLKRQWGGKPSLGLHYQVRPIRYVVIHHTVTGECSGLLKCAEILQNMQAYHQNELDFNDISYNFLIGNDGIVYEGTGWGLRGAHTYGYNAIGTGIAFIGNFVDKLPSDAALQAAKDLLACGVQQGELSEDYALIAGSQVISTQSPGLTLYNEIQEWPHWLSNP | Function: Peptidoglycan-recognition protein that plays a key role in innate immunity by binding to peptidoglycans (PGN) of Gram-positive bacteria and activating the Toll pathway upstream of spz activating enzyme SPE . Has no activity against Gram-negative bacteria and fungi . Shows some partial redundancy with PRPGP-SD... |
Q9YE03 | MQGLAGSVRVAALDIDGTLTERRGAARLDGCSIAVARLLNDLGVTSILMTGNSLPVARGVAVYLGLEGPVVAENGCVAVVGGERVHICSGRPPEGLVKRIMELGFKPSWQNEYRYHEYSLIPVKAAPGIVERASAIAEEEGYRAIWSGYALHIQPPGGGKARGVGEVLARIGAGWSEVLAIGDGENDVEVLARAGYSGAPGDAAEQAKRAAKIVARSPGARGTLEIIQRVLGGARAPAC | Function: Catalyzes the dephosphorylation of 2-phosphoglycolate.
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 24758
Sequence Length: 239
EC: 3.1.3.18
|
O29805 | MFKPKAIAVDIDGTLTDRKRALNCRAVEALRKVKIPVILATGNISCFARAAAKLIGVSDVVICENGGVVRFEYDGEDIVLGDKEKCVEAVRVLEKHYEVELLDFEYRKSEVCMRRSFDINEARKLIEGMGVKLVDSGFAYHIMDADVSKGKALKFVAERLGISSAEFAVIGDSENDIDMFRVAGFGIAVANADERLKEYADLVTPSPDGEGVVEALQFLGLLR | Function: Catalyzes the dephosphorylation of 2-phosphoglycolate.
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 24481
Sequence Length: 223
EC: 3.1.3.18
|
P06184 | MLNDECSILLIDDDVDVLDAYTQMLEQAGYRVRGFTHPFEAKEWVKADWEGIVLSDVCMPGCSGIDLMTLFHQDDDQLPILLITGHGDVPMAVDAVKKGAWDFLQKPVDPGKLLILIEDALRQRRSVIARRQYCQQTLQVELIGRSEWMNQFRQRLQQLAETDIAVWFYGEHGTGRMTGARYLHQLGRNAKGPFVRYELTPENAGQLETFIDQAQGGTLVLSHPEYLTREQQHHLARLQSLEHRPFRLVGVGSASLVEQAAANQIAAELYYCFAMTQIACQSLSQRPDDIEPLFRHYLRKACLRLNHPVPEIAGELLKGI... | Function: Member of the two-component regulatory system PgtB/PgtA that regulates the inducible phosphoglycerate transport system. When activated by PgtB it acts in conjunction with sigma-54 as a transcriptional activator.
PTM: Phosphorylated by PgtB.
Sequence Mass (Da): 47526
Sequence Length: 415
Subcellular Location: ... |
O94412 | MHGILRVKLSEEQRKLKAEKERAKIEEYRGLVSRFQEARKRKDYSEGNLKLTTELLDWNPETYSVWNYRREILLNDVFPKISLNEKQDLLDNELKYVLSKMKVFPKVYWIFNHRRWCLENAPYPNWNYEMMITEKLLSADARNFHGWHYRRYVVSQIERAGNCSLAKKEMEYTTSAIATNFSNFSALHNRTKLIETILNLEADPNSQKALAKQILEQELDMIHQAVFTDPDDSSVWIYHRWLMGHCNPNSMTPLISMITIEERIQYLQKEIELIQELHEMEPENRWCCESLVNYEALCKTLEKQKPTEADIKRWTLLVDK... | Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to proteins having the C-terminal-XCC or -XCXC, where both cysteines may become modified.
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence... |
Q00618 | MHGIKRKQWTKELLRQKRVQDEKKIYDYRSLTENVLNMRDEKIYSIEALKKTSELLEKNPEFNAIWNYRRDIIASLASELEIPFWDKELVFVMMLLKDYPKVYWIWNHRLWVLKHYPTSSPKVWQTELAVVNKLLEQDARNYHGWHYRRIVVGNIESITNKSLDKEEFEYTTIKINNNISNYSAWHQRVQIISRMFQKGEVGNQKEYIRTEISYIINAMFTDAEDQSVWFYIKWFIKNDIVCKTLDEQEYLKMLKDLRENILLINNDEIEFSGKQNIWCLKILLVLEDILEEKEALTERSSEQYLVQLIDADPLRKNRYL... | Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to proteins having the C-terminal -XCC or -XCXC, where both cysteines may become modified. Acts on YPT1 and SEC4.
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cyst... |
O80642 | MSETAVSIDSDRSKSEEEDEEEYSPPVQSSPSANFEKDRHLMYLEMMYELLPYHYQSQEINRLTLAHFIISGLHFLGARDRVDKDVVAKWVLSFQAFPTNRVSLKDGEFYGFFGSRSSQFPIDENGDLKHNGSHLASTYCALAILKVIGHDLSTIDSKSLLISMINLQQDDGSFMPIHIGGETDLRFVYCAAAICYMLDSWSGMDKESAKNYILNCQSYDGGFGLIPGSESHGGATYCAIASLRLMGYIGVDLLSNDSSSSIIDPSLLLNWCLQRQANDGGFQGRTNKPSDTCYAFWIGAVLKLIGGDALIDKMALRKFL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X (CaaX). Seems to exclusively prenylate CaaX substrates wit... |
Q55DA3 | MGSCINEEKLAKFFQRSLNALPAPYTSGLPNHLSLIFFVVSGLDLLNKTDILEKEKQDIINWVYSRQILPSKDNPEINLENCGFRGYNFLGQEFCCDKSVHTSENGPLEYDLPSTPNTYCALLILRILGDDFSGVNKKAIIDSLRKRQRESDGAISGSPNVGDYDLRHLFSACAISFILDDWSAINKESAIDYIKSCLSYEFAFGQTPQQEAHGGPTYCAIASLSLLGRLDVLEPFKEQLTFWLVKKQITGFCGRTNKDPDTCYAFWIGASLMMIDRYDLIDFASINAFIGSAQHEAIGGVAKEPGQLPDVMHSYLSLVG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X.
Catalytic Activity: geranylgeranyl diphosphate + L-cystei... |
P53609 | MAATEDERLAGSGEGERLDFLRDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDMLDSLDVVNKDDIIEWIYSLQVLPTEDRSNLNRCGFRGSSYLGIPFNPSKAPGTAHPYDSGHIAMTYTGLSCLVILGDDLSRVNKEACLAGLRALQLEDGSFCAVPEGSENDMRFVYCASCICYMLNNWSGMDMKKAITYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVFSEKELNRIKRWCIMRQQNGYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDAL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. Known substrates include RAC1, RAC2, RAP1A and RAP1B.
Cat... |
P53610 | MAATEDDRLAGSGEGERLDFLRDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDMLDSLDVVNKDDIIEWIYSLQVLPTEDRSNLDRCGFRGSSYLGIPFNPSKNPGTAHPYDSGHIAMTYTGLSCLIILGDDLSRVDKEACLAGLRALQLEDGSFCAVPEGSENDMRFVYCASCICYMLNNWSGMDMKKAISYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVFSEKELNRIKRWCIMRQQNGYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDAL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of proteins with the C-terminal sequence Cys-aliphatic-aliphatic-X. Known substrates include RAC1, RAC2, RAP1A and RAP1B.
Catalytic... |
P32434 | MELTRAKHIAFFKRHLILFPTPYEEHDCERTVLAFFCLLGLDLLNALNTIDDDDKKSWIEWIYKNYVTKESKGIKYSGFQAYRTGIQPISFEQEPQLAGTVFSICCLLFLGDNLSRIDRDLIKNFVELCKTSQGHFRSIAVPSCSDQDMRQLYMATTIASLLDFSLSDPLCSIQYIKSCQRYEGGFSLLPYGEAHAGATFCALASWSLILKMIPNSSLNTSNQSYNLMDCVPKVERLIRWLASRQLSSGGLNGRTNKDVDTCYAYWVLSSLKLLDALPFIDGGELEKYLLLHAQHALGGFSKTPGEFPDVLHSALGLYAM... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to proteins having the C-terminal C-A-A-L where A is an aliphatic amino acid . In particular it modifies the GTP-binding component of the 1,3-beta-D-glucan synthase .
Catalytic Activit... |
P18898 | MCQATNGPSRVVTKKHRKFFERHLQLLPSSHQGHDVNRMAIIFYSISGLSIFDVNVSAKYGDHLGWMRKHYIKTVLDDTENTVISGFVGSLVMNIPHATTINLPNTLFALLSMIMLRDYEYFETILDKRSLARFVSKCQRPDRGSFVSCLDYKTNCGSSVDSDDLRFCYIAVAILYICGCRSKEDFDEYIDTEKLLGYIMSQQCYNGAFGAHNEPHSGYTSCALSTLALLSSLEKLSDKFKEDTITWLLHRQVSSHGCMKFESELNASYDQSDDGGFQGRENKFADTCYAFWCLNSLHLLTKDWKMLCQTELVTNYLLDR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl diphosphate to proteins having the C-terminal sequence Cys-Ile-Ile-Leu or Cys-Val-Leu-Leu. Acts, among other substrates, on Rho1 and Rho2 and CDC42 proteins. Participates in a RAS-like C-terminal mo... |
Q9LHL5 | MADKLVAGKHLRYILNLMAEKKKESFESVVMDHLRMNGAYWGLTTLALLDKLGSVSEDEVVSWVMTCQHESGGFAGNTGHDPHVLYTLSAVQILALFDKLNILDVEKVSNYIAGLQNEDGSFSGDIWGEVDTRFSYIAICCLSILKCLDKINVKKAVDYIVSCKNLDGGFGCSPGAESHAGQIFCCVGALAITGNLHRVDKDLLGWWLCERQDYESGGLNGRPEKLPDVCYSWWVLSSLIMIDRVHWIEKAKLVKFILDSQDMDNGGISDRPSYTVDIFHTYFGVAGLSLLEYPGVKTIDPAYALPVHVINRILFTK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -CCXX, CXXX, -XCCX and -XCXC, such as RABA1A, RABA2A, RABF2A and RABG2 . In vitro, can prenylate PGGTI targets with the C-ter... |
Q5E9B3 | MGTPQKDVIIKSDAPDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGIYWGLTVMDLMGQLHRMNREEILTFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYDSINVIDINKVVEYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVSPVFCMPEEVL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A.
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[... |
O93830 | MSNLPPDEKVILFDKSKHVQYIVEQESHRSFEYWLSEHLRMNGLYWGVTALITMNELSALAQQDVIDYIMLCWDDKTGAFGSFPKHDGHILSTLSALQVLKIYDQELTVLNDNNESSNGNKRERLIKFITGLQLPDGSFQGDKYGEVDTRFVYTAVSSLSLLNALTDSIADTASAFIMQCFNFDGGFGLIPGSESHAAQVFTCVGALAIMNKLDLLDVENKKVKLIDWLTERQVLPSGGFNGRPEKLPDVCYSWWVLSSLSILKRKNWVDLKILENFILTCQDLENGGFSDRPGNQTDVYHTCFAIAGLSLIDYKKYGFK... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to proteins having the C-terminal -XCC or -XCXC, where both cysteines may become modified. Acts on YPT1 and SEC4 (By similarity).
Catalytic Activity: geranylgeranyl diphosphate + L-cys... |
P53611 | MGTPQKDVIIKSDAPDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGIYWGLTVMDLMGQLHRMNREEILAFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYDSINVIDVNKVVEYVKGLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRNFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVNPVFCMPEEVL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A.
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[... |
P53612 | MGSLLFSWKGTQQKDVTIKSDAPDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQLHRMNREEILVFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYDSVHVINVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVSPV... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A.
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[... |
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