ids
stringlengths 6
10
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stringlengths 11
1.02k
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stringlengths 108
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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 thylakoid membrane
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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
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P33292 | MSLIGGGSDCAAGSNPLAQFTKHTQHDTSLQQSMRNGEFQQGNQRMMRNESTMSPMERQQMDQFMQQQNNPAFNFQPMQHELNVMQQNMNAPQQVANNSWNQEFRMKDPMVANAPSAQVQTPVQSTNWAQDFQQAGPEVQHHAQQHQHPILSVPGVRAGIYGGGRLMGGSMMNRAAQMQQQNPAQAQTSEQSQTQWEDQFKDIESMLNSKTQEPKTKQQEQNTFEQVWDDIQVSYADVELTNDQFQAQWEKDFAQYAEGRLNYGEYKYEEKNQFRNDPDAYEIGMRLMESGAKLSEAGLAFEAAVQQDPKHVDAWLKLGEVQTQNEKESDGIAALEKCLELDPTNLAALMTLAISYINDGYDNAAYATLERWIETKYPDIASRARSSNPDLDGGDRIEQNKRVTELFMKAAQLSPDVASMDADVQTGLGVLFYSMEEFDKTIDCFKAAIEVEPDKALNWNRLGAALANYNKPEEAVEAYSRALQLNPNFVRARYNLGVSFINMGRYKEAVEHLLTGISLHEVEGVDASEMSSNQGLQNNALVETLKRAFLGMNRRDLVDKVYPGMGLAQFRKMFDF | 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 the PEX13-PEX14 docking complex along with cargo proteins (By similarity). PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle (By similarity). Required for PEX7 ubiquitination .
PTM: Monoubiquitinated at Cys-10 by PEX2 during PEX5 passage through the retrotranslocation channel: monoubiquitination acts as a signal for PEX5 extraction and is required for proper export from peroxisomes and recycling. When PEX5 recycling is compromised, polyubiquitinated at Lys-22 by PEX10 during its passage through the retrotranslocation channel, leading to its degradation.
Sequence Mass (Da): 65083
Sequence Length: 576
Domain: The TPR repeats mediate interaction with proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type).
Subcellular Location: Cytoplasm
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O94325 | MSVEAGCSTLSNPLKKLTSTAVVNNSTPSAQYRKHLTKSQSRTYAPLQTLSEDQFTSFKNLQGNNSPLGNVVKNPVSLKTGNHTGTTTRGGSKENWVHSFSSLQQQNSKSAWTSEFSEVFLNSSENDRFRNLNQPLKQSFFGSAGLNLSSNTEIPLQSSLAIDETELAKKFEEASQISNKLEKEKDATGSKSIEELWEEHQKQLKNAGLEPASLEEYQKQWEDFLKSNNISDDPYTSSVNSFANDNLAHNKNIDPQIFQHSDTDNVVENSLQTEDVYSQNQDESSEVVKELNGIDPFVEAMNLIKNGGSISKAAVLLEQSVKENPQHFEAWKWLGRIHTLLGNESRVVEALLEAVKLDSTNLDLMMDLAVSYVNQSLNVQALVCLEDWIVNSFPQYRNRFAKINERFEEKDSANDLLKMQMYFLDVAYELSLAKKRSSKVQAGLGIIMYMLKEYERSADCFRQALQDEPSNEILWNKLGAALTNAEKNTEAVSSYNRAVSLQPQYVRVRSNMAVSNINLGYFEDAAKHLLAAIDIIQNSSTSMESCESNEELWEMLRKVFLIGFQSTDLASQSYPGANTSYIRAQLSDLQGWPGVELE | 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 docking complex along with cargo proteins. PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle.
PTM: Monoubiquitinated at Cys-7 by PEX2 during PEX5 passage through the retrotranslocation channel: monoubiquitination acts as a signal for PEX5 extraction and is required for proper export from peroxisomes and recycling. When PEX5 recycling is compromised, polyubiquitinated by PEX10 during its passage through the retrotranslocation channel, leading to its degradation.
Sequence Mass (Da): 67104
Sequence Length: 598
Domain: The TPR repeats mediate interaction with proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type).
Subcellular Location: Cytoplasm
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A0A1L8FDW4 | MAMRGLIEAECGGSNPLMKLTNHFTQDKALREEGLQHVSWPPGATVVSKPLGEATEDELVSEFLHTRAPSLQSRAPHTFKMDGLLAEMQEIEQSSFRPEPLRAPGVADLALSEQWSAEFLGVEVDPVEEEDWSREFTEQADPHASPSRWAEEYLQQSEEKLWLGESEGAMAEKWTEEYQPEDDLQREAKSLVSQVTDPKLANTQFLQFVKRIGDGELSFSHAPSTPSQTVSQAEQWSEQFVHEQAEQWVDQFAPLEKDFEKAKAAVESDVDFWDKLQEEWEEMAKRDAEAHPWLSDFQDLSSKSIDKGYMFEDNNPFSEVSLPFEEGLKHLREGDLPSAVRLFEVAVKRDPQHMEAWQYLGTTQAENEQELAAISALRRCIDLKPDNLSALMALAVSYTNECLQQQACHTLREWLRHNPKYSHLVKEESSSNASRARSFGTLLSDSVFSDVRELFLSAVNSDPSQVDPDVQCGLGVLFNLSGEYQKAVDCFTAALGQRPDDYLLWNKLGATLANGNDSEAAVEAYRRALQLQPGFIRSRYNLGIACINLGAHREAIEHFLEALSMQQQSGGCESAMSDNIWSTLRMALSMIGQSDLYSSADARDLATLQAAFPPHSAAQ | 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 docking complex along with cargo proteins . Pex5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle .
PTM: Monoubiquitinated at Cys-11 by pex2 during pex5 passage through the retrotranslocation channel (By similarity). Cys-11 monoubiquitination acts as a recognition signal for the pex1-pex6 complex and is required for pex5 extraction and export from peroxisomes . When pex5 recycling is compromised, polyubiquitinated by pex10 during its passage through the retrotranslocation channel, leading to its degradation .
Sequence Mass (Da): 69403
Sequence Length: 619
Domain: The TPR repeats mediate interaction with proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type).
Subcellular Location: Cytoplasm
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Q99144 | MSFMRGGSECSTGRNPLSQFTKHTAEDRSLQHDRVAGPSGGRVGGMRSNTGEMSQQDREMMARFGAAGPEQSSFNYEQMRHELHNMGAQGGQIPQVPSQQGAANGGQWARDFGGQQTAPGAAPQDAKNWNAEFQRGGSPAEAMQQQGPGPMQGGMGMGGMPMYGMARPMYSGMSANMAPQFQPQQANARVVELDEQNWEEQFKQMDSAVGKGKEVEEQTAETATATETVTETETTTEDKPMDIKNMDFENIWKNLQVNVLDNMDEWLEETNSPAWERDFHEYTHNRPEFADYQFEENNQFMEHPDPFKIGVELMETGGRLSEAALAFEAAVQKNTEHAEAWGRLGACQAQNEKEDPAIRALERCIKLEPGNLSALMNLSVSYTNEGYENAAYATLERWLATKYPEVVDQARNQEPRLGNEDKFQLHSRVTELFIRAAQLSPDGANIDADVQVGLGVLFYGNEEYDKAIDCFNAAIAVRPDDALLWNRLGATLANSHRSEEAIDAYYKALELRPSFVRARYNLGVSCINIGCYKEAAQYLLGALSMHKVEGVQDDVLANQSTNLYDTLKRVFLGMDRRDLVAKVGNGMDVNQFRNEFEF | 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: Peripheral membrane protein
Sequence Mass (Da): 66601
Sequence Length: 598
Subcellular Location: Cytoplasm
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P35056 | MDVGSCSVGNNPLAQLHKHTQQNKSLQFNQKNNGRLNESPLQGTNKPGISEAFISNVNAISQENMANMQRFINGEPLIDDKRRMEIGPSSGRLPPFSNVHSLQTSANPTQIKGVNDISHWSQEFQGSNSIQNRNADTGNSEKAWQRGSTTASSRFQYPNTMMNNYAYASMNSLSGSRLQSPAFMNQQQSGRSKEGVNEQEQQPWTDQFEKLEKEVSENLDINDEIEKEENVSEVEQNKPETVEKEEGVYGDQYQSDFQEVWDSIHKDAEEVLPSELVNDDLNLGEDYLKYLGGRVNGNIEYAFQSNNEYFNNPNAYKIGCLLMENGAKLSEAALAFEAAVKEKPDHVDAWLRLGLVQTQNEKELNGISALEECLKLDPKNLEAMKTLAISYINEGYDMSAFTMLDKWAETKYPEIWSRIKQQDDKFQKEKGFTHIDMNAHITKQFLQLANNLSTIDPEIQLCLGLLFYTKDDFDKTIDCFESALRVNPNDELMWNRLGASLANSNRSEEAIQAYHRALQLKPSFVRARYNLAVSSMNIGCFKEAAGYLLSVLSMHEVNTNNKKGDVGSLLNTYNDTVIETLKRVFIAMNRDDLLQEVKPGMDLKRFKGEFSF | 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 docking complex along with cargo proteins . PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle .
PTM: Monoubiquitinated at Cys-6 by PEX2 during PEX5 passage through the retrotranslocation channel: monoubiquitination acts as a signal for PEX5 extraction and is required for proper export from peroxisomes and recycling . Ubiquitination at Cys-6 is UBC4-independent but requires the presence of PEX4 . When PEX5 recycling is compromised, polyubiquitinated at Lys-18 and Lys-24 by PEX10 during its passage through the retrotranslocation channel, leading to its degradation . Ubiquitination at Lys-18 and Lys-24 are UBC4-dependent . Monoubiquitination at Cys-6 and polyubiquitination at Lys-18 and Lys-24 are removed by UBP15 in the cytosol, resetting PEX5 for a subsequent import cycle .
Sequence Mass (Da): 69324
Sequence Length: 612
Domain: The TPR repeats mediate interaction with proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type).
Subcellular Location: Cytoplasm
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Q8RY16 | MVERRNPLVLSSTRSTLRSVLNSSQPSSADGDRVLNKDGDLLRGNARLSAGILRWRKDGENVSDAKLDSLDDSALVGLSTQLLKRLSINSGSLVVVKNIEIGIQRVAQVVVLDPPKTTLEDASLTQVPVSDSLHTMLVFPTYDLMGQQLLDQEVAYLSPMLAFNLSLHISCLKSLVHRGNGVLEKYFEAKCDEEFIGKSAEDGSKIGLDLEPVSQVPGYASHLRVSFVKIPECGTIPSLKVNSSFEAEERQGLIDSALQKYFGTDRQLSRGDIFRIYIDWNCGSSICNPCSQRLCSESDDYIYFKVIAMEPSNERFLRVNHSQTALVLGGTVSSGLPPDLLVYRSKVPMPLQEETVNILASVLSPPLCPSALASKLRVAVLLHGIPGCGKRTVVKYVARRLGLHVVEFSCHSLLASSERKTSTALAQTFNMARRYSPTILLLRHFDVFKNLGSQDGSLGDRVGVSFEIASVIRELTEPVSNGDSSMEEKSNSNFSENEVGKFRGHQVLLIASAESTEGISPTIRRCFSHEIRMGSLNDEQRSEMLSQSLQGVSQFLNISSDEFMKGLVGQTSGFLPRDLQALVADAGANLYISQESETKKINSLSDDLHGVDIHQASQIDNSTEKLTAKEDFTKALDRSKKRNASALGAPKVPNVKWDDVGGLEDVKTSILDTVQLPLLHKDLFSSGLRKRSGVLLYGPPGTGKTLLAKAVATECSLNFLSVKGPELINMYIGESEKNVRDIFEKARSARPCVIFFDELDSLAPARGASGDSGGVMDRVVSQMLAEIDGLSDSSQDLFIIGASNRPDLIDPALLRPGRFDKLLYVGVNADASYRERVLKALTRKFKLSEDVSLYSVAKKCPSTFTGADMYALCADAWFQAAKRKVSKSDSGDMPTEEDDPDSVVVEYVDFIKAMDQLSPSLSITELKKYEMLRDQFQGRSS | 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 through the PEX2-PEX10-PEX12 retrotranslocation channel (By similarity). Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5 (By similarity). Required for jasmonate biosynthesis . Necessary for the developmental elimination of obsolete peroxisome matix proteins .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 103045
Sequence Length: 941
Subcellular Location: Cytoplasm
EC: 3.6.4.-
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Q6FW67 | MMITADLIWDENLDNDCEVSKDIWEDDTFIDKSYLKVVLPSYDGVDTPIVYHFKLNDDLKINSIKIPTNSIGNLGKFGRLNTCSLEAVSGEPPVLKEIIIKIDERLYDKLALLPKANEKKQYFQIKYNLVNKQSVIHEGNIWGHVCEVVETKPFSQGVIDFSVTDIVLIRSKILSVENKHDRSLVNLQAFHDLSRIPLKCLHYPVERSLLLPEPPFDDDDSIYVFFPFDLLSKLKISSGSFVRLSNSKNSVLVRAFLLQSPNHYAVDGIYTTPFVLAQFDELPLVEVEPVYNNELAFPTASEVVISKVGNVLHTQKRYQELILQKLRYYFLTARRILSNGSLIPITIDSSFDEIILEDIDLDVNTIKSDDDCIVWFVVSNRKFENISNYDPKAEFFVDPKHTKLITSAMENRSLSSNTFNSALKYYGLPGVFHYRPDIFPVVNDIKNVINTHAEANKKVPNLPMILNLSSNVPKVGKASILRSIAIDLSYQFVDIDTLSVVFSSGSSDIATTFLGYLKGKLENLLPFTGNTIILIKHIDHILKKVDQNQDIQQSRQVKALEGDLISFIKSYSRIYPGVVFAFTSASIDNLPEGFRSEIKFDYVVHPPNEKQRRSIIDELLSTSDLFQKYGNRKLRIQCSNEIEISTLSLHSAGLSPYDIQYIISLAVADSLRKCNNYLLWRQNKIKVDMISIQNALEKVRSDYSASIGAPSIPNVTWDDVGGLSSVKDAIMETIDLPLKHPELFGSGLKKRSGILFYGPPGTGKTLLAKAIATNFSLNFFSVKGPELLNMYIGESEANVRRVFQKARDAKPCVIFFDEVDSVAPKRGNQGDSGGVMDRIVSQLLAELDGMSSDGDGVFIIGATNRPDLLDEALLRPGRFDKLIYLGIADTREKQANIMRALTRKFKVSSDINFDELVSDFPFSYTGADFYALCSDAMLKAMTRISKEIDEKVDKYNQDNGTSISIRYWFDHVCSDEDTDVIVKKEDFLNANKELIPSVSQQELEHYKQIRANFEDSK | 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 through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 114807
Sequence Length: 1017
Subcellular Location: Cytoplasm
EC: 3.6.4.-
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Q13608 | MALAVLRVLEPFPTETPPLAVLLPPGGPWPAAELGLVLALRPAGESPAGPALLVAALEGPDAGTEEQGPGPPQLLVSRALLRLLALGSGAWVRARAVRRPPALGWALLGTSLGPGLGPRVGPLLVRRGETLPVPGPRVLETRPALQGLLGPGTRLAVTELRGRARLCPESGDSSRPPPPPVVSSFAVSGTVRRLQGVLGGTGDSLGVSRSCLRGLGLFQGEWVWVAQARESSNTSQPHLARVQVLEPRWDLSDRLGPGSGPLGEPLADGLALVPATLAFNLGCDPLEMGELRIQRYLEGSIAPEDKGSCSLLPGPPFARELHIEIVSSPHYSTNGNYDGVLYRHFQIPRVVQEGDVLCVPTIGQVEILEGSPEKLPRWREMFFKVKKTVGEAPDGPASAYLADTTHTSLYMVGSTLSPVPWLPSEESTLWSSLSPPGLEALVSELCAVLKPRLQPGGALLTGTSSVLLRGPPGCGKTTVVAAACSHLGLHLLKVPCSSLCAESSGAVETKLQAIFSRARRCRPAVLLLTAVDLLGRDRDGLGEDARVMAVLRHLLLNEDPLNSCPPLMVVATTSRAQDLPADVQTAFPHELEVPALSEGQRLSILRALTAHLPLGQEVNLAQLARRCAGFVVGDLYALLTHSSRAACTRIKNSGLAGGLTEEDEGELCAAGFPLLAEDFGQALEQLQTAHSQAVGAPKIPSVSWHDVGGLQEVKKEILETIQLPLEHPELLSLGLRRSGLLLHGPPGTGKTLLAKAVATECSLTFLSVKGPELINMYVGQSEENVREVFARARAAAPCIIFFDELDSLAPSRGRSGDSGGVMDRVVSQLLAELDGLHSTQDVFVIGATNRPDLLDPALLRPGRFDKLVFVGANEDRASQLRVLSAITRKFKLEPSVSLVNVLDCCPPQLTGADLYSLCSDAMTAALKRRVHDLEEGLEPGSSALMLTMEDLLQAAARLQPSVSEQELLRYKRIQRKFAAC | 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 through the PEX2-PEX10-PEX12 retrotranslocation channel . Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5 .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 104061
Sequence Length: 980
Subcellular Location: Cytoplasm
EC: 3.6.4.-
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Q6CPV1 | MVIASLESTHAISTSIVLSSDLWTEFYGTESVSSASPNYVKLTLPSYNKWHHQALISHCDNDDSLPFGSAGLPTNFIKQSQVRPMFSSIEIEPYVQQLPNLDNLVLSLNPDLFNELNQLSKEEQRKFLTLRFNLLFGITVLNVNQVVYPAFCKVTSSSNDFGILTDQTQIVLVPDSNVVEQSRSNDEFTEFDHLFSLHVKIQSLLDPVPVEFLSPPQPDTTDNDLFAFVQPNILLQLGVPSGTFVRVIAEEQEMLVQLFVLFAPNEYECDSLYVSPRVRYVFMNHARVIIQRPNLALNRFSVSNAVTLSRIGCQINAQRRYQDIISHHLALYFSEKQRIVKVGDLIPITFDSNYASMFTDDIRSGQHDTLVWFKVEEIESDSNEEYHIIDSSITRLSTVKITSRELMPKSICDYDRFYNLSPLFHYDEDAFPFAKRLKDILNTAIKCSARNVNVGTSIMLHSSSPNVGKTMLTRSVCAELGFHLIHVDCLSLTSNSNTSDATNKTIGYIRAKIETIISYVEKVVIFLSHLETILEDEQNQQDNTSSKMARQMNVEMADLIEEYTTKYKGTVFVGSTNDIDNIPAIVRSRIKFEIDVPVPTEKQRLQMFRWYFDPYVLNSQTPKLRSLISHNVPLQTVSVQSAGLTPMDIRSIVKAVKYKCYQRLKQNDLLIDMTDITAVINIARDRFSDSIGAPKIPNVTWDDIGGMDVVKGEIMDTIDMPLKHPELFSSGMKKRSGILFYGPPGTGKTLLAKAIASNFSLNFFSVKGPELLNMYIGESEANVRRVFQKARDAKPCVIFFDELDSVAPKRGNQGDSGGVMDRIVSQLLAELDGMSSGGDGVFVIGATNRPDLLDEALLRPGRFDKMLYLGISDTDKKQANIIKALTRKFTLESGIDILDIAKKCPFNYTGADFYALCSDALLNAMTRVAGEVDEKWEKYNMENKKNISLRYWFDNVANENDLKVVVKLQDFELAQQNLIPSVSEDELRHYLRLKSSFESQ | 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 through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 112961
Sequence Length: 1000
Subcellular Location: Cytoplasm
EC: 3.6.4.-
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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 degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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O51669 | MYRIKNENLDFKIDSLGECKQNNPLIDFYASEGSSHFVNEKNKIKFSVYRNEDKGDRYEDVLLEKAGPREKIYFVPRHVKAAITTCGGLCPGFNDVIRSIVRTLWKIYGVRNIYGVKFGYQGLLPESNSPFINLNPDVVDDINKFGGTILGSSRGGIKPVEIVDTLERMNINMIFNIGGDGTQKGSLLIAEEIEKRNLKIAVVGIPKTVDNDFMFVQKSFGFETAVEQAVAAVAGAHFEANSAYNGIGLVKVMGRDSGFIAAHTALSSNDVNFCLIPELDFDIEGPNGFLVHLERRLLEKESLEEIPHAVILIAEGAGQKYFDHFPKKKDDSGNLLYEDIGLYIKDKITEYFKAKNIQFTLKYIDPSYIIRSSPANASDSLYCARLGSNAVHAAMAGKTKMLISLWSTKFVHIPIKMAVIDRNKVNPNGSFWRDVLSSTGQPISMKN | 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 degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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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 degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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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 degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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Q8R914 | MKTIGILTSGGDAPGMNAAIRAVVRTGIYYGLKVKGIMRGFAGLVEDEVIDLGLSSVGDIIQKGGTILRTARCEEFKQKEVRKKAYETLQKHGIEGLVVIGGDGSFRGAQLLSEEWNVNTICIPGTIDNDIPCTDYTIGFDTACNTVIDAINKIRDTATSHERANIIEVMGRNSGYIALYAGVAGGAEMIILPEVEWSIDELCDKITYGIKRGKLHHIIVLAEGVMSAPELAKMIKERLPKLDLRYTILGHIQRGGAPTVMDRVLASQMGARAVELLLENKTKRVISIRNNQIVDDDIDEALSMKKEFNRKLYELSKILSI | 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 degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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A9WCU2 | MASKKQRIGVLTSGGDAPGLNAVIRAVVKSASGLGWEVIGIHDGFEGLLGTKSYRVLTNADVQGLLPRGGTILRTTNKGHFGPRRSDELSEADPYVRAVKAIEEMGLRALITIGGEGTQRIALELHKLGAPVIGVPKTIDNDLAGTDRTFGFDTALQVATDAIDRLHTTAASHNRVMVLEVMGRHTGWIALHAGLAGGADVILIPEIPFSIERVAEKVMARDQQGSSFSIIVVAEGARPRGGSEMYIAEGRLGGIGHWVGEQLEKLTAKEVRVVVLGHLQRGGSPSPYDRLLSTRYGAAAVQAAARGIYGEMVALRGQDIVTVPLAEACGHLNRVRPHSDLVLCARSLGIAFGDEL | 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 degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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Q27651 | MSVKRRDHILIPKNPDAPLPSLKIEEVGECTIDNIYASPEPFVNGMTMKLSAVKNHGIERDSGEVELAGPMEKIFYNPETTKVAIVTCGGLCPGLNNVIRGLVLNLYNRYHVNNIFGLRWGYEGLVPELSEVQRLTPEIVSDIHQKGGSILGTSRGAQSPEVMAQFLIDNNFNILFTLGGDGTLRGANAINKELRRRKVPITVVGIPKTIDNDICYTDSTFGFQTAVGLSQEAINAVHSEAKSAKNGIGIVRLMGRDAGFIALYASLANGDANLVLIPEIDIPITQICEFVGKRIMSKGHVVIVVAEGALQNQKPKDLDLGTDKSGNILHWDSINYLRDSITKYLKSIGIEEHTIKFVDPSYMIRSAPCSAADAHFCMCLANAAVHVAMAGKTGLVICHHHNNFVSVPIDRTSYYIKRVNTDGPLYTMMTAIEKPK | 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 degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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Q8RG98 | MEKKLAILTSGGDAPGMNAAIRATAKIAEYYGFEVYGIRRGYLGMLNDEIFPMTGRFVSGIIDKGGTVLLTARSEEFKEARFREIAANNLKKKGINYLVVIGGDGSYRGANLLYKEHGIKVVGIPGTIDNDICGTDFTLGFDTCLNTILDAMSKIRDTATSHERTILIQVMGRRAGDLALHACIAGGGDGIMIPEMDNPIEMLALQLKERRKNGKLHDIVLVAEGVGNVLDIEEKLKGHINSEIRSVVLGHIQRGGTPSGFDRVLASRMAAKAVEVLNKGEAGVMVGIEKNEMVTHPLEEACSVDKRKSIEKDYELALLLSK | 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 degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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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 degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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Q8CTX6 | MLETNNHTNAWQGFKTGRWNKNIDVREFIQLNYSLYEGDDEFLEGPTKATETLWDQVMQLSKEERERGGMWDMDTKVASTITSHDAGYLDKDLEKVVGVQTEKPFKRSMQPFGGIRMAKAACEAYGYELDPETEKIFTEYRKTHNQGVFDAYSREMLNCRKAGIITGLPDAYGRGRIIGDYRRVALYGVDFLMEQKLKDFNTMSTEMSEDVIRLREELTEQYRSLQDLKELGQKYGFDISRPATNFKEAVQWLYLAYLAAIKEQNGAAMSLGRTSTFLDIYAERDLQNGDITEQEVQEIIDHFIMKLRIVKFARTPEYNELFSGDPTWVTESIGGVGIDGRPMVTKNSFRFLHSLDNLGPAPEPNLTVLWSTRLPENFKIYCAKMSIKTSSIQYENDDLMRESYGDDYGIACCVSAMKIGKQMQFFGARANLAKALLYAINGGKDEKSGKQVGPSYEGIKSDVLDYDEVFERYEKMMDWLAGVYINSLNIIHYMHDKYSYERLEMALHDTEIIRTMATGIAGLSVAADSLSAIKYAQVKPIRNEEGLVTDFEIEGDFPKYGNNDSRVDEIAVDLVERFMTKLRSHKTYRNSEHTMSVLTITSNVVYGKKTGNTPDGRKAGEPFAPGANPMHGRDQKGALSSLSSVAKIPYDCCKDGISNTFSIVPKSLGKEEADQNKNLTSMLDGYAMQHGHHLNINVFNRETLIDAMEHPEEYPQLTIRVSGYAVNFIKLTREQQLDVISRTFHESM | 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
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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 5'-deoxy-adenosine.
Catalytic Activity: glycyl-[formate C-acetyltransferase] + reduced [flavodoxin] + S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical-[formate C-acetyltransferase] + H(+) + L-methionine + semiquinone [flavodoxin]
Sequence Mass (Da): 32430
Sequence Length: 292
Subcellular Location: Cytoplasm
EC: 1.97.1.4
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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 5'-deoxy-adenosine.
Catalytic Activity: glycyl-[formate C-acetyltransferase] + reduced [flavodoxin] + S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical-[formate C-acetyltransferase] + H(+) + L-methionine + semiquinone [flavodoxin]
Sequence Mass (Da): 33038
Sequence Length: 299
Subcellular Location: Cytoplasm
EC: 1.97.1.4
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P37836 | GSFPKYGNDDDRVDEIAEWVVSTFSSKLAKQHTYRNSVPTLSVLTITSNVVYGKKTGSTPDGRKKGEPFAPGANPLHGRDAHGALASLNSVAKLPYTMCLDGISNTFSLIPQVLGRGGEHERATNLASILDGYFANGGHHINVNVLNRSMLMDAVEHPEKYPNLTIRVSGYAVHFARLTREQQLEVIARTFHDTM | Catalytic Activity: acetyl-CoA + formate = CoA + pyruvate
Sequence Mass (Da): 21350
Sequence Length: 195
Subcellular Location: Cytoplasm
EC: 2.3.1.54
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Q46266 | MFKQWEGFQDGEWTNDVNVRDFIQKNYKEYTGDKSFLKGPTEKTKKVWDKAVSLILEELKKGILDVDTETISGINSFKPGYLDKDNEVIVGFQTDAPLKRITNPFGGIRMAEQSLKEYGFKISDEMHNIFTNYRKTHNQGVFDAYSEETRIARSAGVLTGLPDAYGRGRIIGDYRRVALYGIDFLIQEKKKDLSNLKGDMLDELIRLREEVSEQIRALDEIKKMALSYGVDISRPAVNAKEAAQFLYFGYLAGVKENNGAAMSLGRTSTFLDIYIERDLEQGLITEDEAQEVIDQFIIKLRLVRHLRTPEYNELFAGDPTWVTESIAGVGIDGRSLVTKNSFRYLHTLINLGSAPEPNMTVLWSENLPESFKKFCAEMSILTDSIQYENDDIMRPIYGDDYAIACCVSAMRVGKDMQFFGARCNLAKCLLLAINGGVDEKKGIKVVPDIEPITDEVLDYEKVKENYFKVLEYMAGLYVNTMNIIHFMHDKYAYEASQMALHDTKVGRLMAFGIAGFSVAADSLSAIRYAKVKPIRENGITVDFVKEGDFPKYGNDDDRVDSIAVEIVEKFSDELKKHPTYRNAKHTLSVLTITSNVMYGKKTGTTPDGRKVGEPLAPGANPMHGRDMEGALASLNSVAKVPYVCCEDGVSNTFSIVPDALGNDHDVRINNLVSIMGGYFGQGAHHLNVNVLNRETLIDAMNNPDKYPTLTIRVSGYAVNFNRLSKDHQKEVISRTFHEKL | 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
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O32797 | MKTEVTENIFEQAWDGFKGTNWRDKASVTRFVQENYKPYDGDESFLAGPTERTLKVKKIIEDTKNHYEEVGFPFDTDRVTSIDKIPAGYIDANDKELELIYGMQNSELFRLNFMPRGGLRVAEKILTEHGLSVDPGLHDVLSQTMTSVNDGIFRAYTSAIRKARHAHTVTGLPDAYSRGRIIGVYARLALYGADYLMKEKAKEWDAITEINEENIRLKEEINMQYQALQEVVNFGALYGLDVSRPAMNVKEAIQWVNIAYMAVCRVINGAATSLGRVPIVLDIFAERDLARGTFTEQEIQEFVDDFVLKLRTMKFARAAAYDELYSGDPTFITTSMAGMGNDGRHRVTKMDYRFLNTLDTIGNAPEPNLTVLWDSKLPYSFKRYSMSMSHKHSSIQYEGVETMAKDGYGEMSCISCCVSPLDPENEEGRHNLQYFGARVNVLKAMLTGLNGGYDDVHKDYKVFDIEPVRDEILDYDTVMENFDKSLDWLTDTYVDAMNIIHYMTDKYNYEAVQMAFLPTKVRANMGFGICGFANTVDSLSAIKYAKVKTLRDENGYIYDYEVEGDFPRYGEDDDRADDIAKLVMKMYHEKLASHKLYKNAEATVSLLTITSNVAYSKQTGNSPVHKGVFLNEDGTVNKSKLEFFSPGANPSNKAKGGWLQNLRSLAKLEFKDANDGISLTTQVSPRALGKTRDEQVDNLVQILDGYFTPGALINGTEFAGQHVNLNVMDLKDVYDKIMRGEDVIVRISGYCVNTKYLTPEQKQELTERVFHEVLSNDDEEVMHTSNI | 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
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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-tetrahydroxynaphthalene (1,3,6,8-THN or T4HN) by the polyketide synthase PfmaE though condensation of acetyl-CoA with malonyl-CoA. T4HN is not stable and easily oxidizes into the stable form flaviolin . T4HN is also substrate of the hydroxynaphthalene reductase PfmaG to yield scytalone . The scytalone dehydratase PfmaJ then reduces scytalone to 1,3,8-THN . 1,3,8-THN is then substrate of the hydroxynaphthalene reductase PfmaI to yield vermelone (Probable). Vermelone is further converted by the multicopper oxidase PfmaD to 1,8-DHN (Probable). Finally the laccase PFICI_06862 transforms 1,8-DHN to DHN-melanin (Probable). The roles of the 5-oxoprolinase PfmaA and the proline iminopeptidase PfmaB within the cluster have not been elucidated yet (Probable).
Catalytic Activity: Release of N-terminal proline from a peptide.
Sequence Mass (Da): 31682
Sequence Length: 281
EC: 3.4.11.5
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W3X9K4 | MSGPALEVAAAKTAEQGQVPVLAAAVRGDTKVSGDSIHAATTAVSDGDNQSSTMSGKTAAGDATSPASGSGSGGWFHWHEPGTSKAEKKLIFKLDWFLLSYSCLCFFIKQLDGNNVTNAYASGMQEQLGFGPGNELSWMNTYFNIGQIIGAPFANMIITVVRPRYWLPACLMTWSAFVLGMYRCETAAQFYVLRFFIGLFEGAAWPGITYTLGCWYRKSEMARRSALFVMSGVLGQMFSGYLQAALYTGMDGKGGLAAWRWLFIFDFILAVPIAIYGLFCFPDTPHKTSAWYLNSWEREKAVERIDSEGRKPIGKLDLSVFKRIFTSWQVYAFTLGYALWSLTVGSYVMQYFTLYLKATKEYTIPQINNIPTALGAVNFVTMLTTGFVSDKIGRRGPVCLAVGCVLIFTYSIFTAWNVPHRLLMAVFILNGVYGCYTPLLAGWVNECCGGDQQKRAFILGLMTSVGGAVVIPFQQLQFPSSQAPQFKQTHGWPSALAFVIALTCWTGLGIPLLQRRMEKQAKRNEAEHEA | 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 Length: 530
Subcellular Location: Cell membrane
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P24358 | MGTNGVRVFVILYLLAVCGCIEYDVDDNVHICTHTNVSHINHTSWYYNDKVIALATEDKTSGYISSFIKRVNISLTCLNISSLRYEDSGTYKGVSHLKDGVIVTTTMNISVKANIIDLTGRVRYLTRNYCEVKIRCEITSFALNGSTTPPHMILGTVDKWKYLPFPTDDYRYVGELKRYISGNPYPTESLALEISSTFNRFTIVKNLNDDEFSCYLFSQNYSFHKMLNVRNICESEWEALNNNNDNSSSMPASHNNLANDLSSMMSQLQNDNDDNNDYSAPMNVDNLIMIVLITMLSIILVIIVVIAAISMYKRSKYRHIDN | 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 | MIVLPNKVRIFINDRMKKDIYLGISNFGFENDIDEILGIAHLLEHLLISFDSTNFLANASTSRSYMSFWCKSINSATESDAIRTLVSWFFSNGKLKDNFSLSSIRFHIKELENEYYFRNEVFHCMDILTFLSGGDLYNGGRIDMIDNLNIVRDMLVNRMQRISGSNIVIFVKRLGPGTLDFFKQTFGSLPACPEIIPSSIPVSTNGKIVMTPSPFYTVMVKINPTLDNILGILYLYETYHLIDYETIGNQLYLTVSFIDETEYESFLRGEAILQISQCQRINMNYSDDYMMNIYLNFPWLSHDLYDYITRINDDSKSILISLTNEIYASIINRDIIVIYPNFSKAMCNTRDTQQHPIVVLDATNDGLIKKPYRSIPLMKRLTSNEIFIRYGDASLMDMITLSLSKQDISLKRNAEGIRVKHSFSADDIQAIMESDSFLKYSRSKPAAMYQYIFLSFFASGNSIDDILANRDSTLEFSKRTKSKILFGRNTRYDVTAKSSFVCGIVRGKSLDKTSLVEMMWDLKKKGLIYSMEFTNLLSKNTFYLFTFTIYTDEVYDYLNTNKLFFAKCLVVSTKGDVENFSSLKKDVVIRV | 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 into 46 kDa and 22 kDa products (Potential).
Sequence Mass (Da): 68040
Sequence Length: 591
Subcellular Location: Virion
EC: 3.4.24.-
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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 because produced in viral factories instead of the classic ER -Golgi route.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12236
Sequence Length: 103
Subcellular Location: Virion membrane
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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 because produced in viral factories instead of the classic ER -Golgi route.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12820
Sequence Length: 111
Subcellular Location: Virion membrane
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Q80HX0 | MGIKNLKSLLLENKSLTILDDNLYKVYNGIFVDTMSIYIAVANCVRNLEELTTVFIKYVNGWVKKGGHVTLFIDRGSIKIKQDVRDKRRKYSKLTKDRKMLELEKCTSEIQNVTGFMEEEIKAEMQLKIDKLTFQIYLSDSDNIKISLNEILTHFNNNENVTLFYCDERDAEFVMCLEAKTHFSTTGEWPLIISTDQDTMLFASADNHPKMIKNLTQLFKYVPSAEDNYLAKLTALVNGCDFFPGLYGASITPNNLNKIQLFSDFTIDNIVTSLAIKNYYRKTNSTVDVRNIVTFINDYANLDDVYSYIPPCQCTVQEFIFSALDEKWNEFKSSYLESVPLPCQLMYALEPRKEIDVSEVKTLSSYIDFENTKSDIDVIKSISSIFGYSNENCNTIVFGIYKDNLLLSINSSFYFNDSLLITNTKSDNIINIGY | 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
Subcellular Location: Virion
EC: 3.1.-.-
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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 protein
Sequence Mass (Da): 20512
Sequence Length: 184
Subcellular Location: Virion membrane
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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 membrane protein
Sequence Mass (Da): 19555
Sequence Length: 168
Subcellular Location: Virion membrane
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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 glucose condition. Acetylation increases catalytic activity. Under glucose restriction SIRT1 levels dramatically increase and it deacetylates the enzyme (By similarity).
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 28778
Sequence Length: 254
EC: 5.4.2.11
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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: 5.4.2.11
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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 Location: Mitochondrion outer membrane
EC: 3.1.3.16
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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 Location: Mitochondrion outer membrane
EC: 3.1.3.16
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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 conditions. This phosphorylation increases PGAM5 phosphatase activity (By similarity).
Location Topology: Single-pass membrane protein
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 32173
Sequence Length: 289
Domain: The N-terminal 35 amino acids, including the potential transmembrane alpha-helix, function as a non-cleaved mitochondrial targeting sequence that targets the protein to the cytosolic side of the outer mitochondrial membrane.
Subcellular Location: Mitochondrion outer membrane
EC: 3.1.3.16
|
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 (Da): 33166
Sequence Length: 289
Subcellular Location: Mitochondrion outer membrane
EC: 3.1.3.16
|
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 protein
Sequence Mass (Da): 33069
Sequence Length: 289
Subcellular Location: Mitochondrion outer membrane
EC: 3.1.3.16
|
Q8TK32 | MLRVMTSRNFLTIDDFDIRGKTILLRVDMNSPMDTQGHILDDMRIKSHIATLKDLESAKVVLLAHQSRPGKKDFTTMKPHAHLLSRYLGKQVTYVDDIFGTFAKTHIASMEDGDVIMLENVRFYSEESLERTPAEQANTYMVKKLAPFVDIFLNDAFAVAHRSHLSVVGFTEVLPSGAGRVMEKELVSLDRGVKGGERPSIFVLGGAKVDDSLRVTENVLTSGGADRVLLTGVVANVALAASGVNIGKVNMDFIKSQGYENQIEKARGLLAKFKDRIGLPKDVALNDNRERVEVHISELNSDSLPINDIGLETIVDYTNEIQNSKTVVLNGPAGVSEIEDFALGTHEIIKAAIKSDFSIIGGGHISVEVAHLGLEHRFSHISTGGGACIDYLAGEKLPGVESLKAAYIKYQEAKKL | 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
Pathway: Thermoadapter biosynthesis; cyclic 2,3-diphosphoglycerate biosynthesis; cyclic 2,3-diphosphoglycerate from 2-phospho-D-glycerate: step 1/2.
EC: 2.7.2.16
|
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
Pathway: Thermoadapter biosynthesis; cyclic 2,3-diphosphoglycerate biosynthesis; cyclic 2,3-diphosphoglycerate from 2-phospho-D-glycerate: step 1/2.
EC: 2.7.2.16
|
Q8TGY9 | MSEKSSRKERDEKTEKETARQGKHRRIRVKSRHYEMPFSRGVLARSLTAIGVEPHKAYEIALKIKEELQDEGIEEISTDELADIIRTKLEEIDETLAERYELWRRIKKREEPIIVLIGGASGVGTSTIASEVGHRLGITNVIGTDAIREVMRRVLAEELYPTLYESSYTAWKRLRYEPAEDPVITGFLDHSEPVVVGIEGVVNRSINEGIHVIVEGVHIVPRLIKKEILNYPNVFVFMLAVEDEEAHKWRFYARSRDTKLSRPAERYLKYFEEIRRIHDFLVEDAEEHDIPVINNEHIDETVDQIVSYISSKLLKGERELSKSVSWW | 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
Pathway: Thermoadapter biosynthesis; cyclic 2,3-diphosphoglycerate biosynthesis; cyclic 2,3-diphosphoglycerate from 2-phospho-D-glycerate: step 1/2.
EC: 2.7.2.16
|
P09041 | MALSAKLTLDKVDLKGKRVIMRVDFNVPMKNNQITNNQRIKAAIPSIKHCLDNGAKSVVLMSHLGRPDGIPMPDKYSLEPVADELKSLLNKDVIFLKDCVGPEVEQACANPDNGSIILLENLRFHVEEEGKGKDSSGKKISADPAKVEAFQASLSKLGDVYVNDAFGTAHRAHSSTVGVNLPQKASGFLMKKELDYFSKALEKPERPFLAILGGAKVKDKIQLIKNMLDKVNFMIIGGGMAYTFLKELKNMQIGASLFDEEGATIVKEIMEKAEKNGVKIVFPVDFVTGDKFDENAKVGQATIESGIPSGWMGLDCGPESIKINAQIVAQAKLIVWNGPIGVFEWDAFAKGTKALMDEVVKATSNGCVTIIGGGDTATCCAKWGTEDKVSHVSTGGGASLELLEGKILPGVEALSNM | 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-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
|
P29406 | MSLSNKLSIRDLDLKNKRVLIRVDFNVPMKDGAITNNNRIVQALPTVKYALDNGASAVILMSHLGRPNGEAVAKYSLKPVAAEVEKLLGKPVEFLNDCVGPDVEKACQSATGGKVILLENLRFHIEEEGSAKVRWSKVKADAEAVKKFRASLTALADIYVNDAFGTAHRAHSSMVGVDLSQRAAGFLMQKELEYFAKALENPARPFLAILGGAKVSDKIQLIENMLDKVNALIVCGGMAFTFKKTLDNVKQIGKSLFDEAGSKLVRNLVKKAAEKNVKLVFPVDFVTADKFAPDANTGYATDADGIPDEWEGLDCGKKSSELFREEILKSKTIVWNGPSGVFEFDAFANGTKSVLNAVIEATKEGATTIIGGGDTATAALKWGAEGKVSHISTGGGASLELLEGKELPGVTALSSKN | 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
Pathway: Thermoadapter biosynthesis; cyclic 2,3-diphosphoglycerate biosynthesis; cyclic 2,3-diphosphoglycerate from 2-phospho-D-glycerate: step 1/2.
EC: 2.7.2.16
|
A7HCN7 | MALKTIDALDLAGKRVFIRVDFNVPLDEQRRVTDDARIRAALPTIKHAIQARAKVILGSHLGRPKGKPDDREKFSLEPAAQRLSELLKQDVILADDCIGDGVKKLVRDLKEGQVLLLENLRFHPQEEKNDEGFARELATLCDVWVNDAFGTAHRAHASTAGMAAFVKEKAAGFLIQKEVEYLGKALGSPERPFVALIGGAKVSDKIKVLENLIAKADAICIGGAMAYTFLKAQGVAVGKSLVEEDKLELARQILERAQARKVDLLLPVDHVCGAEPKDTAERVVVNDRAIPDGLMGLDIGPKTLDRYRQRIVDAKTVFWNGPMGLFEQKPWAEGTFGVAQAMAQSPAVTVVGGGDSAAAVEEAGLVSKMKHVSTGGGASLEFIEGRVLPGIQVLEG | 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 | MLRKKTLRDVDVKGKRVLVRVDYNVPLDEQGNIVDDTRIRASLPTVEYLLDANAKVILMSHLGRPKNRDPKYSLAPVAKRLSRYINKEVKLAPDCVGEEVKRIVNSMKEGDVVLLENLRFHKEETECDENFARELASLGEVYVADAFGTCHRKHASVYLVPKFLKPAVMGFLLEKEITYFEKAMVAPQRPVVAILGGAKVSSKLEVIKNLIRRVDKLFIGGAMAFTFLKAMGYKVGNSLVEDDLQDVARDLIDVAKKLEIKLYLPVDFVIGQEVSENTPTKVVPWQEIPDGWMGLDIGPVSVELVKEIISDAQTIVWNGPMGVFEIDKFKHGTIEVAKLLAQSSALTIAGGGDTDHAIHKAGVYHAFDFVSTGGGAFLELLAGKELPCLVNLDDKEA | 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 | MMIDGLPTLDDIPYRGKHVLLRVDINAPIVNSTILDTSRFESHIPTIEALEDSKLVLLAHQSRPGKKDFTSLESHASTLSKLLGKRVEYIDEIFSKGVLRRIKEMENGEVILLENVRFYSEEQLNRSAEEHAECHMVRKLSTAFDLFVNDAFSASHRSHASLVGFVPVLPSVVGRLVENEVTALSKPLKGEGRKIFVLGGAKIKDSVKVLKNVLENNIAEKVVLTGVVANYFLMLKGYDIGEVNRKVVEDNKEDVSDEEMINILKKYSDKIILPIDLGIEKDGVRVDIPLEKFDGKYRIMDIGLETVNQLSEIIPKYDYVVLNGPAGVFEDERFSLGTYEILRAATRAGYSVVGGGHIASAARLFGLSDKFSHISTAGGACIRFLSGEKLVALEVIKEYWAKKWGKS | 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 | MNVKKLADLDVAGKRVFIRADLNVPQDEAGNIVEDTRIRASLPSIRYCLERSATVMVTSHLGRPTEGECRAEDTLAPIAVRLGELLGKPVRLIRDWVEGGFEVRAGEVVLLENCRCNKGEKKDNEELAKKMAALCDIYVNDAFGTAHRAEATTHGIARFAPVACAGMLMGAEIDALTKATENPARPLVAIVGGAKVSTKLTILKTLAEKVDQLIVGGGIANTFLLASGKRIGESLAEPELVKEAQAIMDMMKARGAEVPLPVDVVVADEVSALARANRIPVDEVGPHDRILDVGPKSSAKLAEIIAHAGTIVWNGPVGVFEHNQFAGGTKMMASAIAHSEAFCIAGGGDTLAAIAKFHIAQDIGYISTGGGAFLEFLEGKKLPAIAALEARFAD | 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 | MKLRSIRDAEVRNKRVIVRVDFNVPLDAEGNVVDDFRIRAALPTIEYLVENGAKVILISHLGRPKGKRDKKYSLVGVAKRLAELLHKEILFAPDVVGEEVELAVNGLRSGDILLCENVRFHEEEEKNDAEFAKNIASLGEIFVNDAFSASHRAHATVEGITKFLPSYAGFLMEKEVNYLSMLTENPQRPYYLVLGGAKVSDKVALLQNLLPKVDGMVIGGAMVFTFWKAQGKEIGKSIVEDDLVGFAKELLEQATTQNKEIVLAKDFVVADENKEHVEIKAISDFGPADIGYDIGPESIKEFKNALVKARTVFWNGPLGLFEDAKFAEGTKQVGAFLADFPGTVVVGGGDTANAVREMELFEKFAHVSTGGGASLEFLEGKVLPGIAPLVVEG | 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 | MAVKKLADLLKEGVEGRHVLVRADLNVPLKDKVITDPGRIDASLPTIKALTEAGARVIVAAHLGRPKSPQDTQFSLAPVAEALSQRLDQYVALASDVSGEDAHERANGLNDGDVLLLENVRFDPREKSKNDAEREELASELAALTGDNGAFVSDGFGVVHRKQASVYDVAKKLPAYVGYLVEKELEQLSKCTDDPQHPYAVCLGGSKVSDKLGVIKALAPKVDTLIIGGGMCYTFLKAKGYGVGDSLLEESMIDECKNLLSEYSDKIVLPSDIVVGKEFDANTEHKTVSADGIEDGWMGLDTGAESIKTFGERLNGAKTIFWNGPVGVFEFEAFANGTKGLAEAIAEATKNGAFSVIGGGDSASAVRNLGFADEAFSHISTGGGASLELIEGKTLPGVAVLDR | 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 | MSNLNLHNKRVMIREDLNVPMKNGKITNDERIVRALPTIQKAIEQKARVMILSHLGRPEEGKFEKEFSLAPVARLLSKKLNQKVPLINDWLKGVAVEPGQAILCENVRFNKGENENNTELAKRMAELCDIFVMDAFATAHRAQASTAGVAAYAKLACAGPLLISEVEALSRALENPQKPLVAVVGGSKVSTKIHLLENLLDKVDQLIVGGGIANTFLKAQGYSIGKSLCENEWLDAAQQFWEKAAEKNVSLPLPVDVIVADELSEDAKATVKNIDAVTSNESIFDVGPNTSATYAKLMAQAGTIVWNGPIGVFEIEAFSQGTRALAQAVAKSTAYSIVGGGDTLAALDKFNLTDQMSYVSTAGGAFLEFLEGKILPAIKILTQRAKEYEQK | 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 | MSKKTVANLSAADLAGKRVLVRVDFNVPLDDQGKITDDTRIRAALPTIQDLTSKGAKVILSSHFGRPKGETFAERVKDKFRLTPVAARLSELLGKPVPKPNDCIGEEVKAQVAAMQNGDVLLLENVRFHPGEEANTPEFAQELASVADLYVNDAFGTAHRAHASTEGVTRYLRPSVAGYLIEKELQYLQSAIENPQRPLAAIVGGSKVSSKIGVIETLLEKVDKLLLGGGMIFTFYKARGLNVGKSLVEEDKLELARTLEAKAKERGVALLLPTDVVVADAFAADANAQTVSVESIPDGWMGLDIGPDAVKTFQEALSDCKTVIWNGPMGVFEFDKFAVGTEAIAHSLAGLTGKGASTIIGGGDSVAAVEKVGVAEQMSHISTGGGASLELLEGKELPGIVALDDA | 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 | MTGLCPLHQPSPLDHPHSGGTPMQNLSQLDVKGKRVLVRVDYNVPVGDGVVQDDTRITASVPTIKKLLDGGASVVLMSHFGRPKNGPEDKYSLKPVAEAVSRALGQDVKFIPSLPGSDETLQAVQALRPGEVALLENVRFEAGEEKNDAALNDKLAKLGDAFVLDAFGSAHRAHSSVSGVAGKLPHAAGGLLQSEVDALGKLLHAPEHPYVVIIGGAKVSDKIKVIENLLPKVDRMLIGGGMMFTFIKARGGQIGNSLVEDDQLDLAKGLLEKYGDKLLLPTDAVAADKFAADAQSKVVPADQIPDGWMGLDIGPDTQRAYADALQGAKTVFWNGPMGVFEFDQFAAGTNAVAAAVGSLKDQAYTVVGGGDSVSAINKSGKADQIDHISTGGGASLELLEGKELPGVVAMA | 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 | MKKLITDLNLNDKKVLIRLDLNVPLKGKKITSLKRIEESIPTIKYVQERGGKIILLSHLGRVKTKEDKEKKSLSIVVEALASLLNSPVKFVDQTRGKKLESAIEKLKPGDVLLIENTRFEDLNNNAESNNDPELGKYWASLGDVFINDAFGTAHRAHASNVGIASNIKESALGILVQKEVNALWKLMEQQEKPFVAILGGSKVSDKINVLEKIIDKVDRLIIGGAMAYTFLKAQGIGIGDSIYEQDKIEFATEFLKKYNHKIILPIDHALAKKFKNAKPIFNNENPLEIPQTFIGMDVGPKTIELIHKYIKGDTKLGISPAKTIFWNGPMGVTEFEEFQSGSLAVVEAISQLVGAYSVVGGGDSIAIIEKLNAQMLFSHISTGGGASLEFIESKVLPGIDAIQNYEQTYEQYDSQVQSQDFSQNFDSPLVEETFSQSTSENFSDFASSTQEHFATSENQNTLINNYENPGFDSQDMFKTEEQNDSTSSFLTSTNPFSSEFSNEFKTSDFQDLKQTQETETQETLIPHTFEYTTDDLRHTLEQYVRETSFQTRESTFPTEEASFETLEETSFQTLEESFPTQSFEQVEQTSEKNMEVSTENFENASSQTNSFTVSDIPKTTSTFEDLETPETQNTTLEEVALETSNFEAQNLETPNLQTSNFETSNLETSNFETSNFETSTFESFNTGNFSTPSSTFEDLDLQSATFQTNDESERSTQENFEPTEVIESDLLAMKTTELEQEITNNTSRDILSEDEVAAPHKKRFWFFGRKR | 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 | MSVKTLDDLLAEGVQGRGVLVRSDLNVPLDDDGNITDPGRVIASVPTLQALAEAGAKVIVTAHLGRPKGEPDPKLSLAPVAAALGEKLGRHVQLAGDVVGTDALARAEGLTDGDVLLLENIRFDARETSKDDSERLSLAKALAALVEGPDGSPGVFVSDGFGVVHRKQASVYDVATLLPHYAGTLVAAEVKVLQQLTSSTDRPYAVVLGGSKVSDKLAVIENLATKADSLIIGGGMCFTFLAAQGFSVGSSLLQEEMVDTCRRLLDEYADVIHLPVDIVVADKFAADAEAETVAADRIPDGKMGLDIGPGSVERFTALLSNAKTVFWNGPMGVFEFPAFAAGTKGVAEAIIGATGKGAFSVVGGGDSAAAVRRLGLPEDGFSHISTGGGASLEYLEGKELPGIQVLES | 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 | MIRTLDDLEADGTALGVRIDINSPLSSDGLADDARLRAHVDTVEELCRRDARVALLAHQGRPGGDEFSDLERHAERLDELLDAPVEYCDSTFSAEARTRIDELDPGRAVLLENTRFYSEEYMSFEPSAAAETYLVSRLAPALDAYVNDAFATAHRSQPSVVGFPERLPAYAGRVMERELDVLGNIESSPEPRVYVLGGAKVDDSIAVARSVLERGLADSVLTAGIVGNAFLLADGVSLGAASAAVVNERSHEAVKQAGDLLDDFSHRIYMPRDVAVENDAGERVEHDLEDLPASTPAMDIGARTVAAYANILDDAGTAILNGPAGVFEDDRFETGTLELYKSATRAEQSIVGGGDTASALRKLGILEDFDHVSTGGGAALNMLTGETLVGVEALRE | 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 | MSIVRMTDLDLSGKRVLIRQDLNVPIENGRITSEQRITASLPTLKRALEQGAAVMVTSHLGRPKEGVWSEADSLAPVAQRLSELLGREVPLVRDWVDGVEVQPGQLVLLENCRMNVGEGKDDEALSKKYAALCDVFVMDAFGTAHRAQASTHGVIRFAPVAAGGPLLMAELDALAQALDAPAKPLLAIVAGSKVSTKLELLANLVGKVDQLIVGGGIANTFIAAAGYNVGKSLYEPDLLDTAKKIVADAKARGADIPLPVDVVTAKQFMPDAVAEVKAVDAVAEDDLILDIGPQTAAQYAQLIDKAGTVVWNGPVGVFEFEAFSKGTEALARAIASSRAFSIAGGGDTLAAVDKFDIAQQVSYISTGGGAFLEFLEGKTLPAVAALDARGA | 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 | MAKLTVKDVDLKGKKVLVRVDFNVPLKDGVITNDNRITAALPTIKYIIEQGGRAILFSHLGRVKEESDKAGKSLAPVAADLAAKLGQDVVFPGVTRGAELEAAINALEDGQVLLVENTRYEDVDGKKESKNDPELGKYWASLGDGIFVNDAFGTAHRAHASNVGISANVEKAVAGFLLENEIAYIQEAVETPERPFVAILGGSKVSDKIGVIENLLEKADKVLIGGGMTYTFYKAQGIEIGNSLVEEDKLDVAKALLEKANGKLILPVDSKEANAFAGYTEVRDTEGEAVSEGFLGLDIGPKSIAKFDEALTGAKTVVWNGPMGVFENPDFQAGTIGVMDAIVKQPGVKSIIGGGDSAAAAINLGRADKFSWISTGGGASMELLEGKVLPGLAALTEK | 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 | MRLTHVLSHTLGLLALGATAEAFSRSREAACGPKKPFRPLPTSQSRDKTCHVRSHGDGTDDSDYILSALNQCNHGGKVVFDEDKEYIIGTALNMTFLKNIDLEVLGTILFTNDTDYWQANSFKQGFQNATTFFQLGGEDVNMYGGGTINGNGQVWYDLYAEDDLILRPILMGIIGLNGGTIGPLKLRYSPQYYHFVANSSNVLFDGIDISGYSKSDNEAKNTDGWDTYRSNNIVIQNSVINNGDDCVSFKPNSTNILVQNLHCNGSHGISVGSLGQYKDEVDIVENVYVYNISMFNASDMARIKVWPGTPSALSADLQGGGGSGSVKNITYDTALIDNVDWAIEITQCYGQKNTTLCNEYPSSLTISDVHIKNFRGTTSGSEDPYVGTIVCSSPDTCSDIYTSNINVTSPDGTNDFVCDNVDESLLSVNCTATSD | 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: 3.2.1.67
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P35336 | MALQRRFFQFVIITLLIPSFILGYTSAVHEDPPHDYHLEEYGYDFKAYPSYITTIGDNDFGSSMSHENGIFGLRKVDYGMDRVLDASKTVNVDDFGAKGDGRDDTKAFEKAWKAACSSTSSAVLLVPKKNYLVRPISFSGPCKSGLTMQIYGTIEASDDRSDYRKDGRHWLVFDSVQNLRVEGGGTINGNGKIWWQNSCKTNKALPCKDAPTALTFYKSKHVIVKNLKIENAQQIHVSFDNCVNVQASNLMVTAPENSPNTDGIHVTGTQNIHISSCVIGTGDDCISIVNGSRKVRVNDITCGPGHGISIGSLGYGNSEAHVSDVVVNGAKLCGTTNGVRIKTWQGGSGSASNIKFQNVEMHNVENPIIIDQNYCDQDKPCQEQSSAVQVKNVVYQNIKGTCASNVAITFDCSKRFPCQGIVLEDVDLEIEGGAAAKALCNNVELSETGVVSPHCQEEGGEEEEEAS | 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: 467
Subcellular Location: Secreted
EC: 3.2.1.15
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P35337 | MGSYLGIYTILVLCLLGYSANAEVFTAGGPPNSDITAAVLKAFTSACQAPAPSQVLIPKGDFKLGETVMTGPCKSPIEFTLQGNVKTDGGSTQGKDRWVVFEKINGFKLNGGGTFDGEGNAAWKANNCHKTFECKKLPISVRFDFVDNAEIKDVTSLDAKNFHFNVISGKNMTFDNIKIIAPAESPNTDGIHLGRCEGVKILNTKIATGDDCISVGDGMKNLLIEKVVCGPGHGISVGSLGRYGWEQDVTDITVKNCTLEGTSNGLRIKTWPSAACTTTAAGIHFEDIILNKVSNPILIDQEYCPWNQCNKNKPSTIKLVDITFRNIRGTSENKDAVKLLCSKGHPCENVEIGDINIEYTGPDGPPTFECTNVTPKLVGAQNPKACVGPVVKAPGKE | 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
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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
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Q07181 | MVRNIVSRLCSQLFALPSSSLQERDPCSVTEYSGLATAVSSCKNIVLNGFQVPTGKQLDLSSLQNDSTVTFKGTTTFATTADNDFNPIVISGSNITITGASGHVIDGNGQAYWDGKGSNSNSNQKPDHFIVVQKTTGNSKITNLNIQNWPVHCFDITGSSQLTISGLILDNRAGDKPNAKSGSLPAAHNTDGFDISSSDHVTLDNNHVYNQDDCVAVTSGTNIVVSNMYCSGGHGLSIGSVGGKSDNVVDGVQFLSSQVVNSQNGCRIKSNSGATGTINNVTYQNIALTNISTYGVDVQQDYLNGGPTGKPTNGVKISNIKFIKVTGTVASSAQDWFILCGDGSCSGFTFSGNAITGGGKTSSCNYPTNTCPS | 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): 38915
Sequence Length: 373
Subcellular Location: Secreted
EC: 3.2.1.15
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Q39786 | MAPHLNIVPSMFVLLLLFISASKVQSDAFDVVAKFGAKADGKTDLSKPFLDAWKEACASVTPSTVVIPKGTYLLSKVNLEGPCKAPIEINVQGTIQAPADPSAFKDPNWVRFYSVENFKMFGGGIFDGQGSIAYEKNTCENREFRSKLPVNIRFDFLTNALIQDITSKDSKLFHINVFACKNITLERLKIEAPDESPNTDGIHMGKSEGVNIIASDIKTGDDCISIGDGTKNMVIKEITCGPGHGISIGSLGKFQNEEPVEGIKISNCTITNTSNGARIKTWPGEHGGAVSEIHFEDITMNNVSSPILIDQQYCPWNKCKKNEESKVKLSNISFKNIRGTSALPEAIKFICSGSSPCQNVELADIDIKHNGAEPATSQCLNVKPITSGKLNPIPCSGPVPKTPSATA | 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
Subcellular Location: Secreted
EC: 3.2.1.15
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Q40312 | MKFSTAIIVSFLFIADFCAAQSGVLDISKFGGKPNSDIGQALTSAWNEACASTTAAKIVIPAGTYQLNGIELKGPCKAPIELQVDGTIQAPADPSVIKGTEQWFKFLYMDHLTLSGKGVFDGQGATVYKKAAPASAWSGKNSNSKVFMNFGFNFVNNSIVRGVTSKDSKNFHVMVFGCKNITFDGFTITAPGDSPNTDGIHMGKSTDVKILNTNIGTGDDCVSIGDGSKQITVQGVNCGPGHGLSVGSLGKFTTEENVEGITVKNCTLTATDNGVRIKTWPDAPGTITVSDIHFEDITMTNVKNPVIIDQEYYPWNQCSKKNPSKIKLSKISFKNVKGTSGTAEGVVLICSSAVPCDGVELNNVDLKFNGAPTTAKCTNVKPLVTGTAPVCQAPGAPAASTTATPAASKTATPAAGKSPAK | 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
Subcellular Location: Secreted
EC: 3.2.1.15
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P24548 | DSTQALTTAWKEACASASPSTILVPKGNFAVGLITLEGPCKSSIGLQLQGTLKAPADPSKIKGLGWINLNKIDLLTIFGGGVFDGQGKSAWVQNDCHKNGPICKTLSMNLRLYAVTNSILRDVTTLDSKNFHVNVIGCKNLTFERFKISAAETSINTDGIHIGRSDGVNIINTEIKTGDDCISLGDGSKNINITNITCGPGHGISVGSLGRYKNEESVVGIYVKNCTITGSQNGVRIKTWPKSEPGEASEMHFQDITMNSVGTPILIDQGYCPYNQCTAEVPSSVKLSKISFKNIKGTSTTKEAVKLVCSKSFPCNGVELADIDLTYSGKGGPATSVCENIKPTIKGKQIPAICSGSAAKAA | 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
Subcellular Location: Secreted
EC: 3.2.1.67
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Q9LXR9 | MQTPSMAASTTSYYPIPKSFLLSPPRHKRNPNLISCSTKPICSPPPPSSSSSSPLQTTTTHRSQKQNLRLPTFEDSFLLYQFSSPTEDPGFSNRIPEQFDGEPRELVLPRVEDNNKGLAISSNMWWADLKAALGQRINIEGIVSSVSVVVKDRQFVLPHVSVKDLRYIDWEVLKRKGFKGVVFDKDNTLTAPYSLAIWPPLRPSIERCKAVFGHDIAVFSNSAGLTEYDHDDSKAKALEAEIGIRVLRHRVKKPAGTAEEVEKHFGCTSSELIMVGDRPFTDIVYGNRNGFLTVLTEPLSRAEEPFIVRQVRRLELALLKRWLRKGLKPVDHSLVSDITQFVKVPSDL | 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 thylakoid membranes development and chloroplast function . Necessary for normal cell growth . Required for root growth and columella cells organization .
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate
Sequence Mass (Da): 39094
Sequence Length: 348
Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
Subcellular Location: Plastid
EC: 3.1.3.27
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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 similarity).
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate
Sequence Mass (Da): 28620
Sequence Length: 269
Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
Subcellular Location: Plastid
EC: 3.1.3.27
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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. Possesses high activity with CDP-dipalmitoylglycerol and low activity with CDP-dioleoylglycerol.
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): 32158
Sequence Length: 296
Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Subcellular Location: Plastid
EC: 2.7.8.5
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Q2KJ28 | MAAAAAAAAGPVFWRRLLGLLPGRPGLAALLGRLSDRLGRNPDRRRRRSPWLLLAPLLSPAVPVVTSPPCCLCAEGVHRFQWIRNLVPEFGVSSSHVRVLSSPAEFFELMKGQIKVAKRRVVMASLYLGIGPLEQELVDCLESTLEKSLQAKFPSGLRVSILLDFTRGSRGRKNSRTMLLPLLQRFPEQVRVSLFHTPNLRGLLRLLIPERFNETIGLQHIKVYLFDNNVILSGANLSDSYFTNRQDRYVFLQDCPEIADFFTELVDAVGDVSLQLQGDDTVQMVEGMVHPYKGDRAAYCRAANKRVMDVINSARMRQQMLHAQTFHSDPLLTQEDAAAAGDRRPAPDTWIYPLIQMKPFEIQIDEIVTETLLTEAERGAKVYLTTGYFNLTQAYMDLVLGTRAEYQILLASPEVNGFFGAKGVAGAIPAAYVHIERQFYSEVCSLGQQERVQLQEYWRRDWTFHAKGLWLYLAGSSLPCLTLIGSPNFGYRSVHRDLEAQIAIVTESRALQQQLHQEQEQLYRRAGVVSSATFEQPSRQVKLWVKMVTPLIKNFF | 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: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Subcellular Location: Mitochondrion
EC: 2.7.8.5
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Q5ZHN9 | MAAAGGAALWRRLAAWLPRGPPGLAALLGRLSDRLSRGRDRRSRRSSWLLLAPLLTPPVPVITAMPCSLCPEGAHRFQWIRNLVPEFGISSSHVKVLSSPAEFYELLKVQIKTAKQRVVMASLYLGTGLLEQELVNCLEETLEKSLQANESPNLRVSILLDYTRGSRGRKNSRTMLIPLLQRFPEQVRVSLFHTPNLRGLLKLLIPERFNETIGLQHIKVYLFDDNVILSGANLSDLYFTNRQDRYVLLQDSPEIADFFTELVDAIGDVSLQLQQDDTVQMMEGMVHPYQGDKVRYCEIANQRVMEVIDSARTRQELLHAKTFHSSQQGSSMLPQHDSEASEGLKPEPDTWIYPLIQMKPFGIQIDEMVTETLLTEAERDAKIYLTTGYFNLTQAYMDLILGTRAEYRILLASPEVNGFFGAKGVAGAIPSAYVYIEHQFYNEVCCLHQQERVQLQEYSRAGWTFHAKGLWLYLAGSSLPCLTLIGSPNFGYRSVHRDLEAQVAIVTENKALQQQLHQEQEQLYLCSGVVSSSTFEQPSRHVKLWVKLVTPLIKNFF | 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: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Subcellular Location: Mitochondrion
EC: 2.7.8.5
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Q9Z2Z7 | MAAPAAGPVFWRRLLGLLPGRPGLAALLGRLSDRLGRSRERRRRRSPWLLLAPLLSPTVPQVTSPPCCLCPEGVHRFQWIRNLVPEFGVSSSHVRVLSSPAEFFELLKGQIKMAKRRVVMASLYLGTGPLEQELVDCLESSLEKSLQSKFPSDLKVSILLDFTRGSRGRKNSRTMLLPLLQRFPEHVRVSLFHTPNLRGLLRLLIPERFNETIGLQHIKVYLFDNNVVLSGANLSDSYFTNRQDRYVFLQDCAEIADFFTELVDAVGDVSLQLQGDDTVDVVDGMVHPYKGDRAAYCRAANKRVMDVIHSARTRQQLLHAQTFHSDSLLSQEEAAAAGDRRPAPDTWIYPLIQMKPFEIQIDEIVTETLLTEAERGAKVFLTTGYFNLTQAYMDLVLGTRAEYQILLASPEVNGFFGAKGVAGAIPAAYVHIERQFYGEVCGLGQQDRVQLQEYWRTGWTFHAKGLWLYLAGSSLPCLTLIGSPNFGYRSVHRDLEAQIAIVTESRALQQQLHQEQEQLYLRSSVVTSATFEQPGRQVKLWVKMVTPLIKNFF | 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: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Subcellular Location: Mitochondrion
EC: 2.7.8.5
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Q7KWX2 | MIKRALAPIVQPQRLFAALMVIGGGGRSATTTTTTTTKACGNGSSQSPPSTPLLSSKSSTITSNKKSAIPSSHLYIPKKSTLDSRQIGNYSREYSTSSSSSSKKSIFNDTYLNDLFWQLSSQGPAFEVNPNNIDFIQEPIDFYNHLIDGVKRSKKRITMASLYLGTSKQEIELVKEMKLAMERNKELKIHILLDGLRGTRIGLDKESSATILGELLSLYSDRVTISMYHTPDLNGILKKVLPPRINETIGVQHIKTYIFDDDLLLSGANLSKDYFTNRQDRYVLIRSTSTVSNYFNEIVEIIGSLSLHVDKDNRNQLLLSSGSIDPVTQSNEFKNLAYTKLSTLLKSHSYYPSNSNSNSSVDSPFDCNNINNGETTWIFPTIQMGPFNIRQDEVVTSHIFESVPNDSKFFITSPYFNLTENYLNLILTGKPKLDIITCSPQANGFYGSKGLSSAVPDCYAIIEKRFLQRVQDTDNGDRISVQEYIRDKWTYHAKGLWIQVKNQQHPSITLIGSPNFGSRSVEKDLEAQIILITQNKQLQQKMENEKNYLWTDTQNANLELFEKRKVSLMVRFLVYIFGNYL | 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: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
EC: 2.7.8.5
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Q32NB8 | MAVAAAAAAGPVFWRRLLGLLPGRPGLAALLGRLSDRLGRNRDRQRRRSPWLLLAPLLSPAVPQVTSPPCCLCPEGVHRFQWIRNLVPEFGVSSSHVRVLSSPAEFFELMKGQIRVAKRRVVMASLYLGTGPLEQELVDCLESTLEKSLQAKFPSNLKVSILLDFTRGSRGRKNSRTMLLPLLRRFPEQVRVSLFHTPHLRGLLRLLIPERFNETIGLQHIKVYLFDNSVILSGANLSDSYFTNRQDRYVFLQDCAEIADFFTELVDAVGDVSLQLQGDDTVQVVDGMVHPYKGDRAEYCKAANKRVMDVINSARTRQQMLHAQTFHSNSLLTQEDAAAAGDRRPAPDTWIYPLIQMKPFEIQIDEIVTETLLTEAERGAKVYLTTGYFNLTQAYMDLVLGTRAEYQILLASPEVNGFFGAKGVAGAIPAAYVHIERQFFSEVCSLGQQERVQLQEYWRRGWTFHAKGLWLYLAGSSLPCLTLIGSPNFGYRSVHRDLEAQIAIVTENQALQQQLHQEQEQLYLRSGVVSSATFEQPSRQVKLWVKMVTPLIKNFF | 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: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Subcellular Location: Mitochondrion
EC: 2.7.8.5
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Q5N9A1 | MAFLKTLNPLLRRSPTPIPNPRSLLSLDAFLAASSPTAASHATAPAPFAAAAHHHVPIRSGGPLFLSSPPWMLSQSATPLTAAAAALRARLRRARALAGGGAQAVADAVGWEPRRISRDESEVAEAVTGGRERFLNLPNLVSIGRMASGPVIGWMIVNEWYLPAFGTLALSGASDWLDGFLARKMGINSVFGSYLDPLADKVLIGCVAIAMVEKDLLHPGLVGLVVVRDLLLVGGAVYKRASSLGWKWNSWSDFVNLDAIHREKVKPLFISKVNTVFQLMLVAAALLQPEFGTEETQNYITVLSWLVASTTIASTVGYGIKYRQIRPRR | 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-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35410
Sequence Length: 329
Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Subcellular Location: Plastid
EC: 2.7.8.5
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Q9HDW1 | MDEGIEKNIFVNLESQIDGVCPKFYVNVDDIDIIHEPPEFYQRLKKLIKKAQKRIFLSTLYIGKEERELINCLSNALSNNPSLHVHILADQLRCTRESPGCCSASLLMQLKKKFPDRCEIKLYHTPNLRGLRKQLVPHRFNEGWGLQHMKIYGADDNLIISGANLSRDYFTNRKDRYYLFSDKGLADFFFKTHFLFSQLSFECIPHLSDSSIQLSSTSPVIPFTLKWNNSCPNPLTNPQEFRVAASAKIQQLLQGNREKFLSRNPSKPLSSVYGSELINQAGDDNNKPFHKYEESAIVYPLFQCVPILTSDVHSTEEKVLSIIGTLLSRKEVNWTLTAGYFNVYPALRKQLLKSEGIGEVIVASQQANGFYRSPGPSKLIPPAYQYIAEQFLKDSRKKKRNIDVLQWQNKGNTYHAKGFWLSTQHHKHPFLTTIGSSNYTSRSQQLDLESTLVVMTQNEKLKRKFSTEIELIKQHTKPMNTCQLEKVPMYVKALTSLMKKKL | 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: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Subcellular Location: Mitochondrion
EC: 2.7.8.5
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P25578 | MTTRLLQLTRPHYRLLSLPLQKPFNIKRQMSAANPSPFGNYLNTITKSLQQNLQTCFHFQAKEIDIIESPSQFYDLLKTKILNSQNRIFIASLYLGKSETELVDCISQALTKNPKLKVSFLLDGLRGTRELPSACSATLLSSLVAKYGSERVDCRLYKTPAYHGWKKVLVPKRFNEGLGLQHMKIYGFDNEVILSGANLSNDYFTNRQDRYYLFKSRNFSNYYFKLHQLISSFSYQIIKPMVDGSINIIWPDSNPTVEPTKNKRLFLREASQLLDGFLKSSKQSLPITAVGQFSTLVYPISQFTPLFPKYNDKSTEKRTILSLLSTITSNAISWTFTAGYFNILPDIKAKLLATPVAEANVITASPFANGFYQSKGVSSNLPGAYLYLSKKFLQDVCRYRQDHAITLREWQRGVVNKPNGWSYHAKGIWLSARDKNDANNWKPFITVIGSSNYTRRAYSLDLESNALIITRDEELRKKMKAELDNLLQYTKPVTLEDFQSDPERHVGTGVKIATSILGKKL | 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): 59370
Sequence Length: 521
Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Subcellular Location: Mitochondrion
EC: 2.7.8.5
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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): 25220
Sequence Length: 233
Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Subcellular Location: Microsome membrane
EC: 2.7.8.5
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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 in Gram-positive bacteria recognition . May act by forming a complex with GNBP1 that activates the proteolytic cleavage of Spatzle and the subsequent activation of Toll pathway . Binds to diaminopimelic acid-type tetrapeptide PGN (DAP-type PGN) and lysine-type PGN (Lys-type PGN) . Has some L,D-carboxypeptidase activity for DAP-type PGN, which are specific to prokaryotes, but not for Lys-type PGN .
Catalytic Activity: H2O + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl-D-alanine = D-alanine + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl
Sequence Mass (Da): 22260
Sequence Length: 203
Subcellular Location: Secreted
EC: 3.4.17.13
|
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 | MLNDECSILLIDDDVDVLDAYTQMLEQAGYRVRGFTHPFEAKEWVKADWEGIVLSDVCMPGCSGIDLMTLFHQDDDQLPILLITGHGDVPMAVDAVKKGAWDFLQKPVDPGKLLILIEDALRQRRSVIARRQYCQQTLQVELIGRSEWMNQFRQRLQQLAETDIAVWFYGEHGTGRMTGARYLHQLGRNAKGPFVRYELTPENAGQLETFIDQAQGGTLVLSHPEYLTREQQHHLARLQSLEHRPFRLVGVGSASLVEQAAANQIAAELYYCFAMTQIACQSLSQRPDDIEPLFRHYLRKACLRLNHPVPEIAGELLKGIMRRAWPSNVRELANAAELFAVGVLPLAETVNPQLLLQEPTPLDRRVEEYERQIITEALNIHQGRINEVAEYLQIPRKKLYLRMKKYGLSKEHYKF | 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: Cytoplasm
|
O94412 | MHGILRVKLSEEQRKLKAEKERAKIEEYRGLVSRFQEARKRKDYSEGNLKLTTELLDWNPETYSVWNYRREILLNDVFPKISLNEKQDLLDNELKYVLSKMKVFPKVYWIFNHRRWCLENAPYPNWNYEMMITEKLLSADARNFHGWHYRRYVVSQIERAGNCSLAKKEMEYTTSAIATNFSNFSALHNRTKLIETILNLEADPNSQKALAKQILEQELDMIHQAVFTDPDDSSVWIYHRWLMGHCNPNSMTPLISMITIEERIQYLQKEIELIQELHEMEPENRWCCESLVNYEALCKTLEKQKPTEADIKRWTLLVDKMIKVDPQRRGRYRTLQEKINNLNK | 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 Mass (Da): 41194
Sequence Length: 344
EC: 2.5.1.60
|
Q00618 | MHGIKRKQWTKELLRQKRVQDEKKIYDYRSLTENVLNMRDEKIYSIEALKKTSELLEKNPEFNAIWNYRRDIIASLASELEIPFWDKELVFVMMLLKDYPKVYWIWNHRLWVLKHYPTSSPKVWQTELAVVNKLLEQDARNYHGWHYRRIVVGNIESITNKSLDKEEFEYTTIKINNNISNYSAWHQRVQIISRMFQKGEVGNQKEYIRTEISYIINAMFTDAEDQSVWFYIKWFIKNDIVCKTLDEQEYLKMLKDLRENILLINNDEIEFSGKQNIWCLKILLVLEDILEEKEALTERSSEQYLVQLIDADPLRKNRYLHLLEQHK | 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-cysteinyl-[protein]
Sequence Mass (Da): 39675
Sequence Length: 327
EC: 2.5.1.60
|
O80642 | MSETAVSIDSDRSKSEEEDEEEYSPPVQSSPSANFEKDRHLMYLEMMYELLPYHYQSQEINRLTLAHFIISGLHFLGARDRVDKDVVAKWVLSFQAFPTNRVSLKDGEFYGFFGSRSSQFPIDENGDLKHNGSHLASTYCALAILKVIGHDLSTIDSKSLLISMINLQQDDGSFMPIHIGGETDLRFVYCAAAICYMLDSWSGMDKESAKNYILNCQSYDGGFGLIPGSESHGGATYCAIASLRLMGYIGVDLLSNDSSSSIIDPSLLLNWCLQRQANDGGFQGRTNKPSDTCYAFWIGAVLKLIGGDALIDKMALRKFLMSCQSKYGGFSKFPGQLPDLYHSYYGYTAFSLLEEQGLSPLCPELGLPLLAAPGI | 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 with leucine in the terminal position. The beta subunit is responsible for peptide-binding. May negatively regulate abscisic acid (ABA) signaling in guard cells and auxin-induced lateral root initiation.
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Mass (Da): 41472
Sequence Length: 375
EC: 2.5.1.59
|
Q55DA3 | MGSCINEEKLAKFFQRSLNALPAPYTSGLPNHLSLIFFVVSGLDLLNKTDILEKEKQDIINWVYSRQILPSKDNPEINLENCGFRGYNFLGQEFCCDKSVHTSENGPLEYDLPSTPNTYCALLILRILGDDFSGVNKKAIIDSLRKRQRESDGAISGSPNVGDYDLRHLFSACAISFILDDWSAINKESAIDYIKSCLSYEFAFGQTPQQEAHGGPTYCAIASLSLLGRLDVLEPFKEQLTFWLVKKQITGFCGRTNKDPDTCYAFWIGASLMMIDRYDLIDFASINAFIGSAQHEAIGGVAKEPGQLPDVMHSYLSLVGLSFGNIPSIQQVIPCLNLSKRAAGKDWFEKLI | 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-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Mass (Da): 39168
Sequence Length: 352
EC: 2.5.1.59
|
P53609 | MAATEDERLAGSGEGERLDFLRDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDMLDSLDVVNKDDIIEWIYSLQVLPTEDRSNLNRCGFRGSSYLGIPFNPSKAPGTAHPYDSGHIAMTYTGLSCLVILGDDLSRVNKEACLAGLRALQLEDGSFCAVPEGSENDMRFVYCASCICYMLNNWSGMDMKKAITYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVFSEKELNRIKRWCIMRQQNGYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHAYFGICGLSLMEESGICKVHPALNVSTRTSERLLDLHQSWKTKDSKQCSENVHIST | 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.
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Mass (Da): 42368
Sequence Length: 377
EC: 2.5.1.59
|
P53610 | MAATEDDRLAGSGEGERLDFLRDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDMLDSLDVVNKDDIIEWIYSLQVLPTEDRSNLDRCGFRGSSYLGIPFNPSKNPGTAHPYDSGHIAMTYTGLSCLIILGDDLSRVDKEACLAGLRALQLEDGSFCAVPEGSENDMRFVYCASCICYMLNNWSGMDMKKAISYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVFSEKELNRIKRWCIMRQQNGYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHAYFGICGLSLMEESGICKVHPALNVSTRTSERLRDLHQSWKTKDSKQCSDNVHISS | 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 Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Mass (Da): 42414
Sequence Length: 377
EC: 2.5.1.59
|
P32434 | MELTRAKHIAFFKRHLILFPTPYEEHDCERTVLAFFCLLGLDLLNALNTIDDDDKKSWIEWIYKNYVTKESKGIKYSGFQAYRTGIQPISFEQEPQLAGTVFSICCLLFLGDNLSRIDRDLIKNFVELCKTSQGHFRSIAVPSCSDQDMRQLYMATTIASLLDFSLSDPLCSIQYIKSCQRYEGGFSLLPYGEAHAGATFCALASWSLILKMIPNSSLNTSNQSYNLMDCVPKVERLIRWLASRQLSSGGLNGRTNKDVDTCYAYWVLSSLKLLDALPFIDGGELEKYLLLHAQHALGGFSKTPGEFPDVLHSALGLYAMAYQDDKSFPKVNADIHMTSKYINICRDCIQAAKGK | 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 Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Mass (Da): 40023
Sequence Length: 355
EC: 2.5.1.59
|
P18898 | MCQATNGPSRVVTKKHRKFFERHLQLLPSSHQGHDVNRMAIIFYSISGLSIFDVNVSAKYGDHLGWMRKHYIKTVLDDTENTVISGFVGSLVMNIPHATTINLPNTLFALLSMIMLRDYEYFETILDKRSLARFVSKCQRPDRGSFVSCLDYKTNCGSSVDSDDLRFCYIAVAILYICGCRSKEDFDEYIDTEKLLGYIMSQQCYNGAFGAHNEPHSGYTSCALSTLALLSSLEKLSDKFKEDTITWLLHRQVSSHGCMKFESELNASYDQSDDGGFQGRENKFADTCYAFWCLNSLHLLTKDWKMLCQTELVTNYLLDRTQKTLTGGFSKNDEEDADLYHSCLGSAALALIEGKFNGELCIPQEIFNDFSKRCCF | 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 modification of proteins involved in nuclear division and bud growth. It is involved in bud positioning and cell polarity . The beta subunit is responsible for isoprenoid and peptide-binding .
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Mass (Da): 42690
Sequence Length: 376
Subcellular Location: Cytoplasm
EC: 2.5.1.59
|
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-terminal sequence Cys-aliphatic-aliphatic-X (CaaX) with leucine in the terminal position. Substrates with the C-terminal sequence -CSIL such as ARAC11/ROP1 or GG2/AGG2 are prenylated independently of REP and when the beta subunit is associated with the alpha subunit RGTA1 .
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Mass (Da): 35193
Sequence Length: 317
EC: 2.5.1.60
|
Q5E9B3 | MGTPQKDVIIKSDAPDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGIYWGLTVMDLMGQLHRMNREEILTFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYDSINVIDINKVVEYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVSPVFCMPEEVLRRVNVQPELVS | 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-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Mass (Da): 36972
Sequence Length: 331
EC: 2.5.1.60
|
O93830 | MSNLPPDEKVILFDKSKHVQYIVEQESHRSFEYWLSEHLRMNGLYWGVTALITMNELSALAQQDVIDYIMLCWDDKTGAFGSFPKHDGHILSTLSALQVLKIYDQELTVLNDNNESSNGNKRERLIKFITGLQLPDGSFQGDKYGEVDTRFVYTAVSSLSLLNALTDSIADTASAFIMQCFNFDGGFGLIPGSESHAAQVFTCVGALAIMNKLDLLDVENKKVKLIDWLTERQVLPSGGFNGRPEKLPDVCYSWWVLSSLSILKRKNWVDLKILENFILTCQDLENGGFSDRPGNQTDVYHTCFAIAGLSLIDYKKYGFKEIDPVYCMPVEVTSKFVRRSA | 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-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Mass (Da): 38460
Sequence Length: 341
EC: 2.5.1.60
|
P53611 | MGTPQKDVIIKSDAPDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGIYWGLTVMDLMGQLHRMNREEILAFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYDSINVIDVNKVVEYVKGLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRNFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVNPVFCMPEEVLQRVNVQPELVS | 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-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Mass (Da): 36924
Sequence Length: 331
EC: 2.5.1.60
|
P53612 | MGSLLFSWKGTQQKDVTIKSDAPDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQLHRMNREEILVFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYDSVHVINVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVSPVFCMPEEVLQRVNVQPELVS | 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-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Mass (Da): 37803
Sequence Length: 339
EC: 2.5.1.60
|
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