ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9XYN1 | MFDVFGSVKGLLKLDSVCIDNNLFRLHYKATVIILIAFSLLVTSRQYIGDPIDCIVDEIPLAVMDTYCWIYSTFTIPNRLNGKIGLEVAHPGVGAHVAGKDEVKYHKYYQWVCFVLFFQAILFYIPRYLWKTWEGGRIKMLVLDLNSPVVNEQSKADRKKLLVDYFATNLHTQNFYAYRFFICEALNFVNVVGQIYFMDLFLDGEFTTYGSDVVRFTEMEPEERSDPMSRVFPKVTKCTFHKYGPSGSVQTFDGLCVLPLNIVNEKIYVFLWFWFVILSVLTGIGLVYRLATAMGPQMRMYLLRARSRLAPQDQIETISN... | Function: Structural components of the gap junctions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41446
Sequence Length: 359
Subcellular Location: Cell membrane
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Q19746 | MLGVPFIDRWLSETFKPKTFDDAVDRLSYVTTATLLAFFSIMVSCKQYVGSAIQCWMPMEFKGGWEQYAEDYCFIQNTFFIPERSEIPGDVEDRQKAEIGYYQWVPIVLAIQAFMFYLPSWIWSSLYKQCGLDFPSVISEAEALRSQDSETRTKGVNKLVDFIGDILDTRSKNEYGRFYCYRFGKGLGSMTSMLYICIKLMYLANVFVQFIILNKFLGNETFLWGFHTFADLYAGREWQDSGVFPRVTLCDFSVRKLANVHRYTVQCVLMINMFNEKIYLFIWFWFVFVLITTFINTLCTIYRLSFDSSRHNYIRSLLSG... | Function: Structural component of gap junctions . Plays a role in maintaining gap junction activity to promote phayngeal muscle contraction .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48917
Sequence Length: 420
Subcellular Location: Cell membrane
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Q9VAS7 | MAVFGMVSAVSGFIKIRYLLDKAVIDNMVFRCHYRITTAILFTCCIIVTANNLIGDPISCINDGAIPMHVINTFCWITYTYTIPGQQHRQIGTDVAGPGLGNEYGQEKRYHSYYQWVPFVLFFQGLMFYVPHWVWKNMEDGKIRMITDGLRGMVSVPDDYRRDRQDRILKYFVNSLNTHNGYSFAYFFCELLNFINVIVNIFMVDKFLGGAFMSYGTDVLKFSNMDQDKRFDPMIEIFPRLTKCTFHKFGPSGSVQKHDTLCVLALNILNEKIYIFLWFWFIILATISGVAVLYSLVVIMMPTTRETIIKRSYRSAQRKE... | Function: Structural components of the gap junctions. Essential for proper epithelial development of the epidermis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45357
Sequence Length: 395
Subcellular Location: Cell membrane
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Q9VRX6 | MYAAVKPLSKYLQFKSVHIYDAIFTLHSKVTVALLLACTFLLSSKQYFGDPIQCFGDKDMDYVHAFCWIYGAYVSDNVTVTPLRNGAAQCRPDAVSKVVPPENRNYITYYQWVVLVLLLESFVFYMPAFLWKIWEGGRLKHLCDDFHKMAVCKDKSRTHLRVLVNYFSSDYKETHFRYFVSYVFCEILNLSISILNFLLLDVFFGGFWGRYRNALLSLYNGDYNQWNIITMAVFPKCAKCEMYKGGPSGSSNIYDYLCLLPLNILNEKIFAFLWIWFILVAMLISLKFLYRLATVLYPGMRLQLLRARARFMPKKHLQVA... | Function: Structural component of the gap junctions in germline cells. Required for differentiation and survival of germline cysts in females and of spermatogonia in males; gap junctional communication between spermatogonia and somatic cyst cells may be required for normal differentiation and survival of spermatogonia.... |
Q23027 | MIGVLLPYVRKFQRSAESNDIADRFSYQYTSTLLGFSAIMMAASQYVGRPIQCWVPAQFTRTWEKYAETYCFIKGTYFLPGAFASEGEMSVTSPDDAVTATPQVGYYQWIPIVLVLQAFLFYLPSIIWRTFNESCELKIKELAAVSEASRKIKSNMSDDQVKATKFGRYFFKKLNFRNESPVFKETGSVVASGKFLPALYLLVKILYLANIVLQFWILTYFLETKSWMWGWQTFQDLMAGREWETTGIFPRVTMCDFSIMDLTSVHDHSIQCVIVINMLAEKVYVFFWFWLLFVGLLTVCSLAYWAVIYMLQSVGRNFIY... | Function: Structural component of the gap junctions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51147
Sequence Length: 447
Subcellular Location: Cell membrane
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Q9VWL5 | MFSAVKPLSKYLQFKSIRIYDSVFTIHSRCTVVILLTCSLLLSARQYFGDPIQCISEEKNIEYIQSYCWTMGTYILKLDDFGDQEQALVSPNQEVSYNSAFFSSATTNAPQSSSRVRTRPHFRSSLRRIGEYNEAYARSLSIAEGVGPEIRGQTERQYLRYYQWVIILLLFQSFVFYFPSCLWKVWEGRRLKQLCSEVGDALLSEETYNTRLRMLVKYFTTDYEDMHFCYMAKYVFCEVLNFLISVVNIIVLEVFLNGFWSKYLRALATIPFYDWDRWNRVSSSVFPKIAKCEVLKFGGSGTANVMDNLCILPLNILNEK... | Function: Structural component of the gap junctions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48978
Sequence Length: 419
Subcellular Location: Cell membrane
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Q9U3N4 | MASQVGAINSVNALISRVFVQPKGDLADRLNSRVTVVILAVSSALLLSSHFIGDPITCWTPAQFNAQWVNFVNQYCFVHGTYFVPLDQQLAFEEEERTKVSIQYYQWVPYVFALQAFLFYIPRFIWKAMIAYSGYDLAAAVKYVDRFWSENRDKDDKFKTRLAAFEGRPSVYIWDGIRLARKKRSRNMALFYTLSTVWQAVNAWIQFYILTQLLDSSIYTLWGPSILGDLLQGNDWQTTGHFPRIVHCDFNRRRPASVQLDTVLCVLTLNIYYEKLFIFLWFWLVFVAVVSTVNCFKWIYYLCNKTKAQKTIKNYLSTAP... | Function: Structural component of the gap junctions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45132
Sequence Length: 389
Subcellular Location: Cell membrane
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Q9VR82 | MYAAVKPLSNYLRLKTVRIYDPIFTLHSKCTIVILLTCTFLLSAKQYFGEPILCLSSERQADYVQSYCWTMGTYILPAEVDRDGGSSWEYALYAPTSTAAETFNVSSLRALVAQNEQYARFISIAEGVGPETRGVTKRMYLRYYQWVFMILLFQSLLFYFPSFLWKVWEGQRMEQLCCEVGDALIVEATYRTRLQMLTRYFRAQFAPIHWCYSIKYAFCELLNVFISILNFWLMDVVFNGFWYKYIHALAAIPVYDWNLWNLMTSRVFPKVAKCEMFVYGPSGTPNIMDILCVLPLNILNEKIFAVLYVWFLFIALLAIM... | Function: Structural components of the gap junctions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55661
Sequence Length: 481
Subcellular Location: Cell membrane
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Q21123 | MFVFRVLNTVPYTNRTGAKDLVASIHSFLTSNLLVGLAVLISWKQFGGTPIECMVPLDFTSAWVQYSNNYCWAQPTYFIPFTEELVEQVVDPADVVADGITIGNGGNRPRFVKKGGEKISYYQWMSFFLLFEAACFRLPCFIWKYFASQSGMQVGEILRVASDENNAVPLVKKANIDALCIHLRGVLRFQKRLKLKKIVPHKILRFLNIKYSAYYVTFIYFVAKVAFLLNVILQSKLLNKYMLPHDRQQNFGFDMWKTIFYGSTNGNETWRENGVFPRVTLCDFETRDMGNVQMHTVQCVLLLNLFTEKIFVFLWAWYIL... | Function: Structural component of the gap junctions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63797
Sequence Length: 556
Subcellular Location: Cell membrane
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Q9V3W6 | MLNTFSSVRQYLKFDLTRVVIDNIVFKLHYRWTFVILLVATLLITSRQYIGEHIQCLSDGVVSPVINTFCFFTPTFTVVRDQNQTAYRPGSEPPGIGAFDPEKDTIKRHAYYQWVPFVLFFQALCFYIPHALWKSWEGGRIKALVFGLRMVGLTRYLKNDSLRIGKLNIPSMAEAEERVKDIRRTMIDRMRLNQSWGAHLVFAEVLNLINLLLQITWTNRFLGGQFLTLGPHALKNRWSDELSVLDLVFPKITKCKFHKFGDSGSIQMHDALCVMALNIMNEKIYIILWFWYAFLLIVTVLGLLWRILTLCFYRNVTFTR... | Function: Structural components of the gap junctions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50669
Sequence Length: 438
Subcellular Location: Cell membrane
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Q23593 | MFSVPFLTSLTSHLGITAIDDASDTLSCLITAFLFITAAILTSAKTYVGSAMECWLPQTYSGDWGEFAENYCFLKDTYFYPRQQSMTDIPMYHKERHRLTYYQWSSMYLAVAGIAFMIPKFLWRLSQSTTDMPVVYFCDTANEIKNETEDKRSAKIKEMARFMRTKITSVHTPSLFSFIRMYMVYSVIKILYLVNAIAQFVIIAIFLGQKRNLFWGWTLFMNLLNGITWETTGLFPRVTFCDFQVREMAGNNRDETVECVIGINEFNEKIFLFFWFWLVFLVFSTLIAHFYNAAQIVKPYFIHSLLFAIRDHDIVDQKEL... | Function: Structural component of the gap junctions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44541
Sequence Length: 382
Subcellular Location: Cell membrane
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Q6AC27 | MTTTPDLRVGVGGAGQMGADHIQRITRVISGATVSAIVEPDAGRAAAAAAAPGSRAFASLDDALDASALEAVVIATPGQFHELVLVPALAAGLPVLCEKPLTPDSAEALRVLELEQTLDRPHIQLGFMRRFDDEYRALRELVVSGDAGELLFLRGVHRNPSVPESYTQSMLITDSVVHEFDVMPWLAGSPVASVEVKYPRRNDRAPERLREPILVLIELRNGVLVDVEMNVSVRFGYQVATEAVFQTGTARIGQPAGLQRWSDARFSIAEHTSFTTRFARAYDAQVQAWVDAVRDGSLVAGPNAWDGYLVALACEAGVRA... | Function: Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose).
Catalytic Activity: myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose
Sequence Mass (Da): 36423
Sequence Length: 339
EC: 1.1.1.18
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Q1AV95 | MRGDSERIAVGVVGTGGMGGMHAENLHFRVPGARLVAVADLDTRRAGGVAERSGAEVFEDGFDLIRSDRVEAVVIASPDPTHAPLVLECLKNEKPVLCEKPLADSADAARKVVEAEVELGRKLVQVGFMRRYDPQHVAVKEAVASGAVGAPVLFRGWHRNADIEPGITSEWVVINATIHDIDSARWFIEEEIEEVYVRGMNTAPKLGANVWDLQLIQFTTAGGRLGSIETNVVSGYGYEVGVEIVGERGTVQVPPLSGAIVRRGFAASQRIEDGWLARFHAAYVIEMQGWVGALLRGEAPAGPDAWDGYASLVVADACIA... | Function: Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose).
Catalytic Activity: myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose
Sequence Mass (Da): 37298
Sequence Length: 347
EC: 1.1.1.18
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C3MH72 | MTLRVGVIGTGMIGQDHIRRLTQVLSAVEVVAVSDIDGARAAAVAPQGADVYAAAGDLIRSETVEAVVICSWGPAHEEQLLDCIAAGKPVFCEKPLVTTAAAALRVMEAEVAFGRRLVQVGFMRRFDADYRRLKATLDAGVLGAPLMFHSTHRNASVPEGLYTSDMPLNDTLVHDAYISRWLLNDEVTGVEVRVPRRSRRGGELRDPVVVLLHMGSGALVDVEISVNIAYGYDIRGEVSCEEGTASLPLRPATVIRDIHGVRQPVPADWRERFIEAYDQEFREWIVAAAQGTATGPSTWDGYAATLVADAALRAAESGAL... | Function: Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose).
Catalytic Activity: myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose
Sequence Mass (Da): 36744
Sequence Length: 340
EC: 1.1.1.18
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W8JIS5 | MATITFDSLNPVTVAISAGFLLLLIIFVKSRTGSSKRKPPGPPGWPIFGNMFDLGDLPHQTLYKLKSKYGPIVWLQLGSINTMVVQNAVSAAELFKKHDVPFCDRKVPDTLTAFNFNQGSLGMNTYGGHWRVLRRLCSMEFLVNKRMNETTDLRRRIEDNMVRWIEEDSLASKAQGGTGAVQLSRFLFLMAFNLVGNLMLSRDLMDNKDPEGREFFDCMNEILELAGTPNIADFLPLLKKLDPLGMKKRMVDNMSRTMKISSKFVQERLDNRKAGKINEKKDFLDVMLEYQGDGKDGPDKFTEQHVNIVIMEMFFAGSET... | Function: Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. vincristine, quinine, and strychnine) biosynthesis pathway. Catalyzes the conversion of cis-trans-nepetalactol (iridodial) into 7-deoxyloganetic acid. Converts also iridotrial into 7-deoxyloganetic acid.
Catalytic Activit... |
Q6FV07 | MENKATLARNIGEKRVSPRSKVNGTGKSWRISYSPQRMDGVSSGRNVSKIPSPVRERLFLKNQERKPLGVSPLSNLSPNSLGRNSLEKSTYNNKLSLKDFEVGRKLGKGKFGKVYCVRHKKSGFICALKAIEKNEILQFNLLKQLKREVDIQLGMDHPNIIKLYAHFHDEKRVYLLMEHSINGELYKSLKNNGPFNDVLASHYIYQIADALHYMHKKRIIHRDVKPENVLIGFDNVVKLADFGWSILNPEGSKRKTLCGTIDYLSPEMITPREYDEQVDVWALGVLAYELVVGVPPFEENSKELTYKRILKCDLNFPESI... | Function: Required for high-fidelity chromosome segregation during the later part of each cell cycle. Acts in opposition to the phosphatase PP1. Has a role in attaching the kinetochores to the microtubules and ensuring that sister kinetochores connect to opposite poles. The promotion of bi-orientation is achieved by se... |
Q6BVA0 | MYCRVFTHFSLYRLYTLSDNININKTNHNKSIGLHQHRVNYMPRSMTASSSQLKRIETRIESLSESLSKSNARKPLGKFQLNTFDNNKITKLQNEKVRPSKSSHIPVKSPIRKKGHSPAQVLQNERMDTKLLLQKLPSASRHMTLDDFEIGKVLGKGKLGKVYCVKHKTSGYIAALKVMAKKDLIDLKLEKNFRREIEIQSNLIHPKISRLYGFFYDHKNVYLILEYSIHGELYHHLKVQRRFNDATASHYIYQVALALDYLHTKHIIHRDIKPENILLSTDNCIKLSDFGWSVKSSPSSSTKRLTICGTLDYLPPEMIE... | Function: Required for high-fidelity chromosome segregation during the later part of each cell cycle. Acts in opposition to the phosphatase PP1. Has a role in attaching the kinetochores to the microtubules and ensuring that sister kinetochores connect to opposite poles. The promotion of bi-orientation is achieved by se... |
Q8SRL5 | MVEYWTLDRFEIGRLLGRGKFGQVWLAREREKGFIVALKIIPIKEIQTVETARQIRREIEIHSNLKHPNILRMYGHFHDKDNIYLILEYAGKGEFFKFLSDRGGKFGEKETSLYIRQVMLALTYMKECNVIHRDIKPENLLLGSDNQLKIADFGWAVYNADKRRMTFCGTMEYLAPEMVNNDIHDSGIDLWCLGILTYEFLMGKTPFESKNRNMREAYKKINSLKYTIPETISSNASDFISRLLVLSPGDRMELTEALNHPFIVKHHGRSSD | Function: Required for high-fidelity chromosome segregation during the later part of each cell cycle. Has a role in attaching the kinetochores to the microtubules and ensuring that sister kinetochores connect to opposite poles. The promotion of bi-orientation is achieved by selectively detaching kinetochore-microtubule... |
Q6C3J2 | MSMKQLETSMSSVSLQEKKPTRIKIALHPQSKSEQNETDRASKIPTGRISTTQPQTYYRPTNLTKTPASQVSRRSSYTTDPPSPLTGITGFRNYSLDDFEIGKALGKGKFGKVYLVKDKKTGFVSALKCMEKKELVEGNVEKQFRREVEIQSNLRHTNVLRLFGHFHDKDRVYLILEYVVHGELYKLLRNQKRFTESTASSYIYQMSEALLYLHGKNIIHRDIKPENILLHFNDTIKISDFGWSVHAPSNRRSTLCGTMDYLPPEIVQSRPYDKNVDVWSLGILMYEFLCGAPPFEEPGGAQATYRRIVKLDLRIPPYVS... | Function: Required for high-fidelity chromosome segregation during the later part of each cell cycle. Acts in opposition to the phosphatase PP1. Has a role in attaching the kinetochores to the microtubules and ensuring that sister kinetochores connect to opposite poles. The promotion of bi-orientation is achieved by se... |
P38991 | MQRNSLVNIKLNANSPSKKTTTRPNTSRINKPWRISHSPQQRNPNSKIPSPVREKLNRLPVNNKKFLDMESSKIPSPIRKATSSKMIHENKKLPKFKSLSLDDFELGKKLGKGKFGKVYCVRHRSTGYICALKVMEKEEIIKYNLQKQFRREVEIQTSLNHPNLTKSYGYFHDEKRVYLLMEYLVNGEMYKLLRLHGPFNDILASDYIYQIANALDYMHKKNIIHRDIKPENILIGFNNVIKLTDFGWSIINPPENRRKTVCGTIDYLSPEMVESREYDHTIDAWALGVLAFELLTGAPPFEEEMKDTTYKRIAALDIKM... | Function: Required for high-fidelity chromosome segregation during the later part of each cell cycle. Acts in opposition to the phosphatase PP1. Has a role in attaching the kinetochores to the microtubules and ensuring that sister kinetochores connect to opposite poles. The promotion of bi-orientation is achieved by se... |
P86799 | SEPQXGRDAGGAL | Function: Has insecticidal activity when consumed by D.melanogaster larvae. Has low chitinase and chitosanase activity.
PTM: Glycosylated; contains galactose.
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Mass (Da): 1269
Sequence L... |
P86800 | SEQQXGRDVGGAL | Function: Has insecticidal activity when consumed by D.melanogaster larvae. Has low chitinase and chitosanase activity.
PTM: Glycosylated; contains galactose.
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Mass (Da): 1328
Sequence L... |
Q9LY23 | MQLKVPEHQVAGHIAKDGKPGPLVDDKGRFFKPLQGDSRGEIEVKFYESFSSNTEVPEHIHRYFPVYHGTQAVEGSDGAAMMVLENLLAEYTKPSVMDVKMGSRTWYPDASEEYIQKCLKKDTGTTTVSSGFRISGFEVYDHKESSFWKPERKLLRGLDVDGARLTLRKFVSSNSLSDTGSKPDSAFASSVYGGSHGILTQLLELKTWFENQTLYHFNSCSILMVYENESILKGNDDDARPQVKLVDFAHVLDGNGVIDHNFLGGLCSFINFIREILQSPDESADS | Function: Inositol phosphate kinase with a broad substrate specificity. Phosphorylates inositol 1,4,5-trisphosphate (Ins(1,4,5)P3), inositol 1,4,5,6-tetrakisphosphate (Ins(1,4,5,6)P4), inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4), inositol 1,3,4,6-tetrakisphosphate (Ins(1,3,4,6)P4) and inositol 1,2,3,4,6-pentaki... |
Q9FLT2 | MLKVPEHQVAGHIASDGKLGPLVDDQGRFFKPLQGDSRGEHEAKFYESFTSNMKVPDHIHRYFPVYHGTQLVEASDGSGKLPHLVLDDVVSGYANPSVMDVKIGSRTWYPDVSEEYFKKCIKKDRQTTTVSLGFRVSGFKIFDHQESSFWRAEKKLVLGYNADGARLALRKFVSSNSPADSNLTPNCAFASEVYGGCNGILAQLLELKDWFETQTLYHFNSCSILMIYENESILMQGGDDAPAPRAQVKLVDFAHVLDGNGVIDHNFLGGLCSFIKFIKDILQSVEKHDETDTSLLENGR | Function: Inositol phosphate kinase with a broad substrate specificity. Phosphorylates inositol 1,4,5-trisphosphate (Ins(1,4,5)P3), inositol 1,4,5,6-tetrakisphosphate (Ins(1,4,5,6)P4), inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4), inositol 1,3,4,6-tetrakisphosphate (Ins(1,3,4,6)P4) and inositol 1,2,3,4,6-pentaki... |
Q8NFU5 | MATEPPSPLRVEAPGPPEMRTSPAIESTPEGTPQPAGGRLRFLNGCVPLSHQVAGHMYGKDKVGILQHPDGTVLKQLQPPPRGPRELEFYNMVYAADCFDGVLLELRKYLPKYYGIWSPPTAPNDLYLKLEDVTHKFNKPCIMDVKIGQKSYDPFASSEKIQQQVSKYPLMEEIGFLVLGMRVYHVHSDSYETENQHYGRSLTKETIKDGVSRFFHNGYCLRKDAVAASIQKIEKILQWFENQKQLNFYASSLLFVYEGSSQPTTTKLNDRTLAEKFLSKGQLSDTEVLEYNNNFHVLSSTANGKIESSVGKSLSKMYAR... | Cofactor: Binds two Mg(2+), but the interaction with the protein is mostly indirect.
Function: Inositol phosphate kinase with a broad substrate specificity . Phosphorylates inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) first to inositol 1,3,4,5-tetrakisphosphate and then to inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4... |
Q9US14 | MKLKLFPFQAAGHGQVLVSEDDKILIKPCIKSEVDFYKTCNDNITLYNWIPKNFGEWMPSSRDIEGINPIAESVAFSLTGKAIILENILYQMETPCVMDIKLGKQLWADDAPLEKRKRLDAVSRSTTSGSLGFRITGILSWDRTNNTYIKRSTAWGKTLTDSDVVEGLNDFFVSCSLSQKARLVESFLNLLKLFEVDLSESYIELKSSSILFVYDYSSLNPTYHCESNVVLKLIDLAHSRWTKNTIDHNTLIGVKNLIHCFAMLLKNE | Function: Inositol phosphate kinase with both monophosphoinositol and diphosphoinositol polyphosphate synthase activities. Able to phosphorylate inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) on both the carbon-3 and carbon-6 positions to synthesize inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4) and inositol 1,4,5,6-... |
P07250 | MDTVNNYRVLEHKAAGHDGTLTDGDGLLIFKPAFPQELEFYKAIQVRDVSRRKSSADGDAPLCSWMPTYLGVLNEGAKIEQSGDAALLKIDERLSDSTDNLDSIPVKSEKSKQYLVLENLLYGFSKPNILDIKLGKTLYDSKASLEKRERMKRVSETTTSGSLGFRICGMKIQKNPSVLNQLSLEYYEEEADSDYIFINKLYGRSRTDQNVSDAIELYFNNPHLSDARKHQLKKTFLKRLQLFYNTMLEEEVRMISSSLLFIYEGDPERWELLNDVDKLMRDDFIDDDDDDDDNDDDDDDDAEGSSEGPKDKKTTGSLSS... | Function: Inositol phosphate kinase with both monophosphoinositol and diphosphoinositol polyphosphate synthase activities. Able to phosphorylate inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) on both the carbon-3 and carbon-6 positions to synthesize inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4) and inositol 1,4,5,6-... |
P05189 | MGSVPVPVANVPRIDVSPLFGDDKEKKLEVARAIDAASRDTGFFYAVNHGVDLPWLSRETNKFHMSITDEEKWQLAIRAYNKEHESQIRAGYYLPIPGKKAVESFCYLNPSFSPDHPRIKEPTPMHEVNVWPDEAKHPGFRAFAEKYYWDVFGLSSAVLRGYALALGRDEDFFTRHSRRDTTLSSVVLIRYPYLDPYPEPAIKTADDGTKLSFEWHEDVSLITVLYQSDVQNLQVKTPQGWQDIQADDTGFLINCGSYMAHITDDYYPAPIHRVKWVNEERQSLPFFVNLGWEDTIQPWDPATAKDGAKDAAKDKPAISY... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Isopenicillin N synthase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic . IpnA catalyzes the cyclization of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) to form ... |
A0A1S4GYH6 | MFKRIVLAVINLVFLIVSTTAFASLHYPESFNQQLIRYKGRDSSNGYFELASEAYYTGTYDLVEELNETATCLRADCREQSNSSPVVRDRRRVDPTFYGHPKTREQIWERNFAHVIEDNRQTLSLVTLLNKIILKYLHSCIPIVLFDTYVATTENYMLEALFSDFPITYITGRIGPNYTLDNPGILEPTGPQCRSYIIFLADVMMTRKVIGPQMNSYVVLIPRSSQWKLQEFLAAKQSRDIINLLVIGESYSVDKRINNEQPYVLYTHELYIDGLGANRPQVLTSWIGNKFSRNNVNLFPRKLRKGFSGHRFTVKAAHQP... | Function: Integral part of a neural sensory system in the antenna that provides the neural basis for the response to environmental changes in temperature (thermosensation) . Specifically, required for thermosensing by the cooling cell . Plays a role in heat seeking and heat-stimulated blood feeding behavior .
Location ... |
Q9VPI2 | MSYYWVALVLFTAQAFSIEGDRSASYQEKCISRRLINHYQLNKEIFGVGMCDGNNENEFRQKRRIVPTFQGNPRPRGELLASKFHVNSYNFEQTNSLVGLVNKIAQEYLNKCPPVIYYDSFVEKSDGLILENLFKTIPITFYHGEINADYEAKNKRFTSHIDCNCKSYILFLSDPLMTRKILGPQTESRVVLVSRSTQWRLRDFLSSELSSNIVNLLVIGESLMADPMRERPYVLYTHKLYADGLGSNTPVVLTSWIKGALSRPHINLFPSKFQFGFAGHRFQISAANQPPFIFRIRTLDSSGMGQLRWDGVEFRLLTMI... | Function: Integral part of a neural sensory system in the antenna that provides the neural basis for the response to environmental changes in temperature (thermosensation) . Together with Ir25a and Ir93a, mediates the response of the dorsal organ cool cells, a trio of cool-responsive neurons, to cooling and is required... |
Q59XW9 | MKLSTIFTAFAATIATVAGYETTGSKQTVDILIDYIIKETPELSQNDVANWENGDTVTLQYVVNNNEESEITVVGVTGQFKNPINNEIVTNLTTGKVGPIAVPPGEAIKFDQKINVDLIPANYELIPHVFIAQDSLIKVIPCRGQLATIVDAAVSFFDPRLIFLELVLLITFAGLIYVGYEIWGKQYFKGVAPVKAKKVSAAKASSPVATGPSTTSATGYDTNWIPESHLKQKKTKKVN | Function: Is probably involved in a pathway contributing to genomic integrity.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 25964
Sequence Length: 239
Subcellular Location: Endoplasmic reticulum membrane
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C5M501 | MKFSAILTALTATIATVAGYETSGKPHTVDILIDYSIKETPEISQTDVANWVNGQKYTLEYVVNNNEETEIAVVGVTGQFKNPVTNQIVTNLTTGQVGPIAVAPGESIKFEQIVDVDLIPDNYELIPHVFVAHDDLIKVIPCRGQLASIVDAAVSFFDPRLIFLELVLLATFGGIAYFVYEIWGKQYLRGTAPVKVPVKKSGSPVAVKEASPVGSASGFDESWIPEAHLKKNKKKA | Function: Is probably involved in a pathway contributing to genomic integrity.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 25618
Sequence Length: 236
Subcellular Location: Endoplasmic reticulum membrane
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E9NA96 | MILMNPKTSKILWLLGFLSLLSSFSLEIAAQTTQNINVLFINEVDNEPAAKAVEVVLTYLKKNIRYGLSVQLDSIEANKSDAKVLLEAICNKYATSIEKKQTPHLILDTTKSGIASETVKSFTQALGLPTISASYGQQGDLRQWRDLDEAKQKYLLQVMPPADIIPEAIRSIVIHMNITNAAILYDDSFVMDHKYKSLLQNIQTRHVITAIAKDGKREREEQIEKLRNLDINNFFILGTLQSIRMVLESVKPAYFERNFAWHAITQNEGEISSQRDNATIMFMKPMAYTQYRDRLGLLRTTYNLNEEPQLSSAFYFDLAL... | Function: Integral part of various neural sensory systems in the antenna that provide the neural basis for the response to environmental changes in temperature (thermosensation), humidity (hygrosensation) and odor detection . Required for odor-evoked electrophysiological responses in multiple neuron classes in the ante... |
Q4VBI2 | MAFTLYALIQTAILFTNAIAVLHEERFLSKIGWGAEQGVGGFGDDPGIKAQLLNLIRSVRTVMRVPLIAVNSVCIVLLLLFG | Function: Regulator of endoplasmic reticulum secretion that acts as a key determinant of brain size. Required for secretion of extracellular matrix proteins. Required for correct brain development by depositing sufficient extracellular matrix proteins for tissue integrity and the proliferation of neural progenitors (By... |
Q9Y5U9 | MAFTLYSLLQAALLCVNAIAVLHEERFLKNIGWGTDQGIGGFGEEPGIKSQLMNLIRSVRTVMRVPLIIVNSIAIVLLLLFG | Function: Regulator of endoplasmic reticulum secretion that acts as a key determinant of brain size . Required for secretion of extracellular matrix proteins . Required for correct brain development by depositing sufficient extracellular matrix proteins for tissue integrity and the proliferation of neural progenitors .... |
Q9CR20 | MAFTLYSLMQAALLCVNAIAVLHEERFLKNIGWGTDQGIGGFGEEPGIKSQLMNLIRSVRTVMRVPLIIVNSITIVLLLLFG | Function: Regulator of endoplasmic reticulum secretion that acts as a key determinant of brain size. Required for secretion of extracellular matrix proteins. Required for correct brain development by depositing sufficient extracellular matrix proteins for tissue integrity and the proliferation of neural progenitors (By... |
Q08630 | MGLYRPSKFFHPPIPHIPFTINPDFFSFHIQRLKAKANPENFLICFPPPDIYKGFVFCCQLDLVHLFSYVFFLFLLKICVDVLQYVIYPKHFTHKKPGFENYSI | Function: May be involved in a pathway contributing to genomic integrity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12390
Sequence Length: 104
Subcellular Location: Membrane
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P47056 | MKVQMIERIFLIQLCLLTVVLASSRAVVEFESTGTKLVNSLRVLAAYSQSSVCVDEKISGIERQIEEVKDMYGNHSFILKGLNGILNNKVNMLTREIQMETVGNNTFETETGKLTKGLNRAVNISPFKYIKKFKTVSTKKFESLLNKYDLVAKKGGELTEEQKKKKEVLSRISRVVAATTIEAGLAQGVVDLCITVTTSLCLVSASIGGVGFLIWLTIIYQALT | Function: Involved in spore wall assembly.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24746
Sequence Length: 224
Subcellular Location: Membrane
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P59823 | MKAPIPHLILLYATFTQSLKVVTKRGSADGCTDWSVDIKKYQVLVGEPVRIKCALFYGYIRTNYSLAQSAGLSLMWYKSSGPGDFEEPIAFDGSRMSKEEDSIWFRPTLLQDSGLYACVIRNSTYCMKVSISLTVGENDTGLCYNSKMKYFEKAELSKSKEISCRDIEDFLLPTREPEILWYKECRTKAWRPSIVFKRDTLLIKEVKEDDIGNYTCELKYGGFVVRRTTELTVTAPLTDKPPKLLYPMESKLTVQETQLGGSANLTCRAFFGYSGDVSPLIYWMKGEKFIEDLDENRVWESDIRILKEHLGEQEVSISLI... | Function: May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK (By similarity). Plays a role in neurite outgrowth (By similarity). During dendritic spine formation can bidirectionally induce pre- and post-synap... |
Q9NP60 | MKPPFLLALVVCSVVSTNLKMVSKRNSVDGCIDWSVDLKTYMALAGEPVRVKCALFYSYIRTNYSTAQSTGLRLMWYKNKGDLEEPIIFSEVRMSKEEDSIWFHSAEAQDSGFYTCVLRNSTYCMKVSMSLTVAENESGLCYNSRIRYLEKSEVTKRKEISCPDMDDFKKSDQEPDVVWYKECKPKMWRSIIIQKGNALLIQEVQEEDGGNYTCELKYEGKLVRRTTELKVTALLTDKPPKPLFPMENQPSVIDVQLGKPLNIPCKAFFGFSGESGPMIYWMKGEKFIEELAGHIREGEIRLLKEHLGEKEVELALIFDS... | Catalytic Activity: H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 78670
Sequence Length: 686
Domain: The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.
Subcellular Loc... |
C1CZ84 | MTDPAPPPTALAAAKARMRELAASYGAGLPGRDTHSLMHGLDGITLTFMPMGQRDGAYDPEHHVILINSQVRPERQRFTLAHEISHALLLGDDDLLSDLHDEYEGDRLEQVIETLCNVGAAALLMPAELIDDLLTRFGPTGRALAELARRADVSATSALYALAERTAPPVIYAVCALSRQEDEGEGGGAKELTVRASSASAGVKYSLSAGTPVPDDHPAALALDTRLPLAQDSYVPFRSGRRMPAYVDAFPERQRVLVSFALPAGRSEPDADKPEAPGDQS | Function: Plays a central regulatory role in DNA repair and protection pathways in response to radiation stress. Acts as a site-specific metalloprotease that cleaves and inactivates the repressor proteins DdrOC and DdrOP3, resulting in induced expression of genes required for DNA repair and cell survival after exposure... |
O54055 | MEKRFIYADNAATTAVSEEVLSAMLPYFRTAYGNASSIYKLGRDAQRDVELAREKVAKALGAEPREIYFTSCGSESDNWAIKGTAELMAKKGKKHIVTSVFEHHAVLHTCEYLEKHGYEVTYVPVNDKGLIDPEDVRKAVREDTALVTIMYANNEIGTIQPIEEIAAVCREKGVLFHTDAVQAVGHVDIDVHKQGIDMLSLSGHKIHAQKGIGAIYIRKGIVLPNLVHGGGQERGKRAGTENVPAIVGLGVAIEAAVRNTAEKAAIIIPRRNRIIDELLKIPYTRLNGDREKRLPGNINISFEGIEGESLLLMLDLNGIC... | Function: Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine.
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-... |
Q2RTS1 | MAKVAALIVAAGRGKRFGGDLPKQYQTLGGRPILRHTLARFAAHPDVALVRAIIHPEDRDLYGAAAHGLATLLDAVEGGAERQDSVRLGLESLTDVAPDYVLIHDGARPLVDGALIDRVIAALADHPGAIPALAVADTLKRGAGGMIGQTVDRAGLWRAQTPQGFRYDAILAAHRAQAGTMLTDDAAVLEAAGGAVALVDGAEDNAKITTFADLERAERLFRGEGEQRIGSGFDVHRLGPGDFVTLNGIRIPHSHGLVGHSDADAPMHALTDALLGCLNAGDIGRHFPPSDMRWKGADSAIFLRHAAALITALGGRILNV... | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CP... |
Q5LRN5 | MTTAAIIVAAGRGTRAGGGVPKQWRPLAGRRVADWTLDRFALRQITHVVLVLHPEDHDAWDEFATTPLILAPGGSDRAGSVRNGLAALDGLGITKVLIHDVARPCVSAATIGAVLDALDAHPGAAPGLAVTDALWTGAEGLVTGTRERDGLFAAQTPQGFRYDAIVAAHAAHPGGAADDVEVARAAELTVAIVPGDPDNLKITRAEDFARAERILRQDMDVRLGNGYDVHRFGPGDHVILCGIKVPHDRGLQGHSDADVGMHAVTDALYGALVEGDIGRHFPPSDPQWKGAASEIFLRHAVDLVRARGFAVSNIDCTLVC... | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CP... |
Q1GGW9 | MTLAVLIVAAGKGTRAGGGLAKQWRPLAGRLVIDWTIEAFQRAGCGTIMVVRDPDNEHAIEALAPYPELLLADGGPSRSESVRNGLIALQEIGVERVLIHDAARPCVCPQVIQQVLDALDDTPAAAPGLAVTDALWTGADGHVTGTQDRSALFAAQTPQGFHFDAILAAHMRHDGTAADDVEVARQAGLAVRITPGDVNNIKITRPEDFSRAEHILRSTMDNIPDIRLGNGYDVHRFGPGDHVMLCGVQVPHERGLQGHSDADVGMHAVTDALYGAMAEGDIGRHFPPSDPQWKGAASDIFLRHAVELARSKGFTINNVD... | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CP... |
C4XSW4 | MSLWTVLLAAGSGTRLAQASGGVKKQFLSVGGRPLYWKALTAFAKSPDVAGVVVVFAPEDLAEATRELAGFLDANHPGLPVLTAAGGARRQDSVKNGLDALPREARLVLIHDAARPFVDAGLIARVADALAAGRKAVIPTLPVTDTVKQVDGDRVTATLPRHELAAVQTPQGFDLTLLRQAYAHARPDFDVTDDASLVEHYGQPVFTVPGAPRNMKITHPEDLASLAEAAAPPVPVTGYGYDVHRYADPRNPGKQPPRPMKLGGFPILGAPEVLAHSDGDVLLHALTDAVLGCVAGGDIGRLFPDSNPDFDNMASGVFLS... | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CP... |
Q1GTN0 | MTESAAPSPRCVAAILLAGGRGLRAGFGRPKQLEWLCGKPVLRWSLDVLAGYPGLSGGVLVANHDVMAATYPLPEGWMAADPGVERQQSVANALSALTDWPDDAVVLVHDAARPGVDSAVVDRLLAALDGADAAIPVLPVPDTLVEAADGAAGAVVARDRLARVQTPQAFRLGTLRRAHAEASGAAATDDAQLVRSLGVSVATVEGDARLHKLTYAADMAILAGLLGTKDMMRTAVGMGYDVHRLVEGKPLWIGGIEIAHSHGLEGHSDADVGLHALTDAILGALGDGDIGDHFPPSDPQWRGAASHHFLSFAGERVAAN... | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CP... |
Q30QG7 | MYNFVTLSILGAYLHTITLILLAAGSSSRFELDIKKQWLRVGDRPLWHFVADRCEKTGYFDKIIITSSLDDIEFMKNYADYTFVEGGQTRQQSLKNSLLHVDTEYVLVSDVARSCIDEAFLKKIISHVGKSDAVVPYLNITDTIVYDDKTIDRERVKRVQTPQLSLTTALKSALLREEEFTDESSAIVANGGSREFILGQESAHKITHIEDLKKLSCLSAPSSDTLSGVGFDVHAFDDKGEMFLGGIKIDSEYGFLAHSDGDVAIHALIDALLGAAGMGDIGMMFPDNDVKYKGADSKELLGTLVTKLRHFGFVIVNVDI... | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CP... |
O83525 | MRRGGACVQKKEYLPLTSRQPGVCLLSEILVRALEARSFFLVVVTVPAGEVAYAESQVACDSRLSAFPSRTRPVILYVPGAHTRSASVRAGLDAMATHAPDVVLVHDGARPFVSVALIHSVLEATCRYGAAVPVIEATDTPKGVAADGSIETHLIRSRVRLAQTPQGFCYASLCAAHHRAATDGEQYTDDSELYARYGGTVHVCAGERSNVKITYPEDLEQRASEPALTRGISVLPCTEEGALRVGLGTDMHALCAGRPLILAGIHIPSKKGAQGHSDADVLAHASIDALLGAAGLGDIGTFFPSCDGRWKDAHSCALLR... | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CP... |
Q83NK3 | MAVGLLLLAAGVGSRLSSSLPKAFVSVGGLDLIQWCLKNLGQLRTALEVVVTVPKGFVELCERNVLQSLGTLEKIKIVTGGATRQDSVGLGIRYFSARITKLLVHDVARAFTPPEIYLSVIKQLETSKAVIPVIAIVDSIKKVNMQDAYREVARGPGEPFHTKSVLHLDRREFFSAQTPQGFDRALLEAAHERSVASNEQFADDSVMVAQIEKDITLINGHEASFKVTNPCDLQRAEFAASSLLSKSNVSPVNISQPPISALSMPLPLIGVGIDFHKFILDESPLFLACLEWKNYRRLQGHSDGDVVAHACTTALLSAAN... | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CP... |
Q7MQW9 | MSQVSLVVMGAGESSRFRQGLSIKKQWLRLGETPLWKHVALHLSKQACFDQVIITASPKEVKYMQKQVDFEVIEGGGTRQESLQNALASVKTPWVLVSDVARFDVPSEVISRVIGRLGEAECVAPAIGVSDTVSYQGEYLSRSEVKLIQTPQLSHVESLLLAFRQGDFTDESSAIAKSGGRVLLVEGSERLKKLTHPHELTLLQGFEPPFGGCYGGSGFDVHAFMEGEGLRLAGVNIPAPVTFKAHSDGDVAIHALIDALLGAAGAGDIGEWFPDSDLAYKGVDSTLLLQEVIKFIRGIGFELINADLTIMAQAPKLSPY... | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CP... |
Q5GSM7 | MTLADKPVLSHAVKKLLTNQYIDYVRVIINRNHEDFYRETIDSLHNYYLSEAVHSFQYVTLKSRKKEEWIPVSSTGMKGRVDTKLLSPVYGGKSRQNSVKLGLESLQKINPDFVVIHDACRPFVSNTLINNLARSMINNQHTGVVPAIEVEDTISLVNDDLIESTIPRERLRAIQTPQIFNFKELLSYHRSNKEFTDDSSLMVEHKKRVVVTRGEKINFKLTTKEDINMAKLLLDEPKYRVGTGYDIHRFIKAQGKAKSFIKICGVEIEYDMKIEAHSDGDVAIHAVVDAILGALGCGDIGAHFPPSFPEWKDRNSSHFL... | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CP... |
Q9RNZ1 | MKRTDNIALIVAAGQGKRAGEGLPKQYRQIAGKAILAHAIDNLLAHPEIDTVQVVIADGHQTLYQEAVGDRDLPQPVIGGVFRRDSVINGLKAAHDRGYKRVLIHDAARPFLPKTVIDRLLDALKSSKAAIPVLPVVDTLVNQEVEAVDRNLFHRVQTPQAFDLETVIAAHQAWTGSDEPTDDAQVVRAFGKKIALVTGDRLLEKLTYPADFSVAEAQMTEKMISVCGSGFDVHCFEAGDHIMLGGIKIPHDHGLAGHSDADVALHALTDALLGAIADGDIGTHFPPSDPQWKGANSTQFLEYAVALAKKAGAIIDHADV... | Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CP... |
Q6MEE8 | MEHQLIPFTVVLLAGGMGTRMKNLIPKQYLTIQEKPIALHSFEKLASMPEIEQMIVVCEPQYEQLFTVYKLNKPLIFARPGLRRQDSLWNGIKLIAGNPLVCIHDSARPFIEIDRIRQTVAEAEKWGAAVLGVRVKATIKICEEKQFIVNTPNRAFLWEMQTPQIVRLKLLYDGFSVAQKNELTVSDDVSLVELIDKPVKVVEGSYLNIKITTPEDLLIAQSILKNHALL | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 26101
Sequence Length: 230
Pathway: Isoprenoid bi... |
P57953 | MTTPIAKSTRRIVAVVPAAGIGSRMQMDKPKQYLHIHGKTILEHTLSVLLGYPLIEKIILAVAANDPYISTCPLLTHPKIQLVEGGSSRADSVLNGLNAVKSAVQNSEDFWVMVHDAARPCLTHQDLDKLVQVEDQNGAILAIPATDTIKRALHNQQIHYTEDRSQLWLAQTPQFFPIATLAQALEQALAQGLQVTDEASAMEFAGFRPHLVAGRSDNIKVTRPEDFALAEFYLSRTK | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 26195
Sequence Length: 238
Pathway: Isoprenoid bi... |
A5D5L4 | MDKVAAVVAAAGRGSRMGTETRKQYLSLAGLPVVGHVLRAMEASSAVKSVVTVVAPGEENYFRLTVVERLGIRKVAAIVPGGEERQDSVYNGLLALAPDTGIVVVHDGARPLLSPGDINAVVQAAAAYGAATLAVPVKDTVKMAGRDGFVLRTLSREHLWLVQTPQAFRYDIIMNAHRQARQKKYAATDDAGLVELLGRPVKIVAGSYENIKITTPEDLTVAEAVIKARQGRLAEAGG | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 25218
Sequence Length: 238
Pathway: Isoprenoid bi... |
A9BHR2 | MVYAIIVAAGEGKRAGFEIPKQFVKLNNKTILRMSAEKFQNSASIDKFLVVSHRNYVDLTEKEVKIFSKFENVVIGGSNRQESVYNALMYLGKKENKPDFVCIHDAVRPFVDTNKIDESIYKAKEIGGAVLAEMAENTISQVNNGRIVKTLERSQIYLHHTPQTFDFNKLLKAYQKAEKILSSFTDDASIFIHAGYETAIVEDYKNNIKLTKKEDFELAKCIFELNS | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 25818
Sequence Length: 227
Pathway: Isoprenoid bi... |
B2RJ15 | MKQKRYALIVAGGHGLRMGADRPKQFLLLAGLPVLMHTLNRFAPHVDAIVLVLPTDHHAYWQELCRKYDFSVSHRVVAGGNTRFASVRNGLQVVPDGVLVAVHDGVRPLVSAETIDACFDLAELKGAVAPCRPMTESLRYYATDGNYAVDRSRYVTVQTPQTFRSEWLREAYRQPYEEYFTDDCSVYEHHFGRPVALIVGNIENIKLTTPLDLSLAKLLLTS | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 24928
Sequence Length: 222
Pathway: Isoprenoid bi... |
A2BVB5 | MHVLIPAAGSGRRMEAGKNKLLIDLEGESLIYWTLKSVFSASLVSWVGIIGQPNDKKKLLNSVKKFSNEIEWINGGNTRQESVFNGLNSLPSNAEKVLIHDGARCLINPDLINKCALELEENDAVILATKVTDTIKIVDNEGYIQQTPNRQNLWAAQTPQGFLVKKLREAHEMAIEKNWKVTDDASLFEMLNWQVRIIEGNSSNIKITSPLDLQIAKLFLKDY | Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Mass (Da): 25030
Sequence Length: 223
Pathway: Isoprenoid bi... |
Q7VUH0 | MTLYDVPAPAKLNLFLHVVGRRADGYHLLQTAFRFIDLADTLHFEARADGAIGRAYELPGVAESDDLVMRAARSLQRATGTRQGAQIGLHKRIPQGGGLGGGSSDAATTLIALNRLWGTGLSRSQLMQLALPLGADVPVFVFGQSAFAQGVGEDLTAVALSPAAYLVVQPDAGVPTAVIFSDPDLTRDCASVTIADFLALPTSCFGRNDLEPVVLRRYPEVSGAVRWLFEHGLRVRMSGSGACLFAEFPTLPEAVLAQEEITATMRVAGKTTSHTHPGFRLVQASTGLTEHPLRNWIAS | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 31887
Sequence Length: 299
Pathway: Isoprenoid biosynthesis; isopente... |
Q89S79 | MSPMPALIEEGRAKVNLSLRVVGRRADGYHDLESVVAFADCADRLTLEPGGELKLATTGPLAAACGDTADNLVFKAAKLLAEAVPNLKLGAFALDKVLPVAAGIGGGSADAAAALRLLARLNNLSLDDPRLQKVALATGADVPVCLYSRACDMTGVGEQLLPLALPSMPCVMVNPRVPVATKDVFQALGLRNGELLVGATSVIGAPAWPEEGASIADWVEVLETVANDLEAPAMRIEPVIGEVLEALRDSAGVKLARMSGSGATCFAIYGAPAEAHAAAEKIRRDHPGWWVHAGTLS | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 30754
Sequence Length: 297
Pathway: Isoprenoid biosynthesis; isopente... |
Q8YFI3 | MTAFQNAGPSITRLAPAKINLALHVTGRRDDGYHLLDMLVVFADQGDRIHIEKAGSDSFTVSGPFASGIPAGRGNLVLKARDALRQHGGPDLSPVAIHLEKNLPIASGIGGGSSDAAATLLALNTLWQLDLDFEMLAAIGLSLGADLPMCLHGAAHGTPLIARGIGEELNDVSGIAALPMLLVNDGTALATPDVFRALTRRENAPLPPPACEGTDALCAYLRETRNDLLPAAISLAPQIEPKLALLRAKGALYARMSGSGATCFAIFSDKSALTRAAKEIADENPGWFAVPSHSFPSRA | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 31207
Sequence Length: 299
Pathway: Isoprenoid biosynthesis; isopente... |
P57267 | MIYTCLSPAKINLFLYVTGRRKDGYHNIQTLFQFLDYGDQFKIIANKTGNIELFTEKKIFMNVQNSIIIAAKLLKKTALLQGKLQNSSYGAKIFLKKNIPMGSGLGGGSSNAATTLVVLNKLWNTQYTLKELSLLGLRIGADVPGFVMGNTAVIEGIGDILYPIVQKEKWYLVVYPCINISTRYMFSSPFLMSNTAKKSLQVLLKTPFKNDFENIAKKQFVPIKKLIRMLSSYAPSRMTGTGSCVFSEFDNKKSAQKIFSVLPKNVQGFIAKSVNISPLHKTLYKR | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 32040
Sequence Length: 286
Pathway: Isoprenoid biosynthesis; isopente... |
Q2GG78 | MLKFLVKAPAKVNLFLHITGKRSDQHHYLESLFVFVNVYDILEVDVGGSKRGVYFSNLRISKYNNTVYKAIELLLKHSAVCPNVSVSIIKNILVSAGLAGGSADAAAIMRLLGNMWNIDYTLLQDLALKIGSDVPACLESKTLFAKGVGEDILLLPDLLLPKYIILVAPRGKTLSTAKVFNNYQSATYSPSICDKLPVKQDDWMELICNAKNDLLEVALKFVPEIEEILFVLKQLKNSVIARMTGSGATCFALFNELSHAEDAARKLQMTRPDWIIFNAKIL | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 31277
Sequence Length: 282
Pathway: Isoprenoid biosynthesis; isopente... |
Q839U9 | MEIIERAPAKINLGLDVLHKRVDGYHEVESIFASVDLADHLTFENLEEDIIRIETDSSFLPVDRRNHVYQAVDLLKRTYNIHKGIKIYIEKRIPVAAGLAGGSSDCAAALRGLNKLWNLGLTMDELCEIGSQIGMDVPYCLRGGTAFANGRGEKIEALPTMPQCWIVLVKPRISVSTSTVFNDLAVDELHHPDIAGLRIAIENGDYTGMTQTVGNALESVTIARHPIVQQIKDRMLKYGADAALMSGSGPTVFALCEKKTRAQRIYNGLKGFCEEVYLVRTLK | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 31281
Sequence Length: 283
Pathway: Isoprenoid biosynthesis; isopente... |
A7HNL5 | MGESYRIVLRTYAKLNLCLDVLGKRQDGYHEINSLFQNISLFDEMDITLSDGKGKLLINSNVNIGNNILNSVWELVNCDNKNVYVNLQKNIPMGGGLGGGSSNAAGFIIALEKVGIISKEQSLKIAQKVGSDVPFFLFGGTAIVKGRGEVILPVEPLTNFGKFKVDLHLPNFSISTKEAYSKLKAEWFGKAPITPEELYDFYKTRNFEMIKKGTYNIFERVIPMDLLEKIESLRRDFPAALTGSGSTYFALKEDGKYSFVPKGVEINAFEKS | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 30259
Sequence Length: 272
Pathway: Isoprenoid biosynthesis; isopente... |
B0S057 | MMKINSYAKINLSLDVLDLREDGYHNIDTIMNLIDLHDVIEINRNNTNELKLSSNNSNFPTDKTNLIYKIFENLKKFRKINCSYDVFVDKQIPISAGLAGGSSNACEFLMYVNDDLSLNLSNQEIKEICRLTGADTFYFTSKKCVRATGIGNEFVRLSDFSNKNIIIVNNGMSISSKDVYDNLKESNGGLGKITVAIDSRDYETFYRKAFNTMESVSERLVEEISDIKEQLNNLGCDLSLMSGSGPTVFGIFENYNDYENCYSKLKDKYKYVFKTKTL | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 31631
Sequence Length: 278
Pathway: Isoprenoid biosynthesis; isopente... |
B0TVZ0 | MANIKLKNYQSYAKINLFLHILNKRDDGYHNLQTWFTFLDLKDHISFRFNNSNKIEITSNIQIASKEDNLIYKAVKEFQEAYNIESIGVDIDIIKNIPMGAGLGGGSSNAATTLIALRDYYLPELSNEQMIPLATKLGADVPIFVYGRSAWAEGIGDVLYSKDFEQQYVVLVKPNIHISTKEFFESENLVKTKNMLPRDLSFDTSVMHNDFENVFFAKYPEFKSQLDEIDQDFRMTGTGSCFYLLSKDLNKLQQLARKVDKSLDKWVVKTLNYAY | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 31625
Sequence Length: 275
Pathway: Isoprenoid biosynthesis; isopente... |
C4XHQ9 | MASFPCPIEETLLPVPCKVNLRLAVGARRPNGYHDIDTFFLPLPEPADVLRLRRFDGPGDIDLQCSDPELETDDNLVVRAYRAYAAATGYAPRLEVHLAKHIPHGAGLGGGSSDAAVMLRYLNDRADEAALSPVDLAALALTLGADIPFFLLGVPAVATGVGETLIPADPGLAGWCAVVVCPEARVKTAWAYAALDASRALPQKPGANLLTTAFDANKRAFCVTGAPMRNDFESVVFAAHPELGRVKERLLALGAAGALLSGTGSAVFGLFRKRQTATLALAMLTGSGPRAYLAPL | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 31109
Sequence Length: 296
Pathway: Isoprenoid biosynthesis; isopente... |
Q01QR0 | MSTTRHAHLRALAKINLDLRVLGKRPDGFHELRTIFQTISLADTLEISFTPARKTTIELTDVLNIADNLVVRAARMVMDAMRATGRIEMRLTKRIPMGAGLGGGSSDAAAVLLALPVLAGRVLPLPKLSHIGEQLGSDVPFFLLGGAATGIGRGSELFPLPDVPAQSGVVVAPGIHVNTAQAYRDLSRRLSGSLTTELQQNKIFSFQSLTWDTGRLAEARNDFEAVVFEQHPKLAAIKRRLVRAGASAAMMSGSGSALYGLFRDRNAIFRAIELLGEDTTYRISLVSRKRYRALWRRAMSEHTRSNVWPLQSRYNP | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 34667
Sequence Length: 316
Pathway: Isoprenoid biosynthesis; isopente... |
Q1GTW9 | MSATMRETGWAKINLALHVRARRADGYHDIETLFAFVDGGDTIEAALAATDTLVIDGEFAEGLSSGADNLVLRVLALLRARYGADRVPPLAVRLTKRLPLAAGIGGGSADAAAMARLVRTHFLPELGDATLARIVGPLGADIAACVASTTCMGSGTGEDLHAVAGLRIAGVPVLLVNPRQPVATGPVFAAWDGIDRGPLYIGTDYRAQLIGARNDLQRPALAACPAISDILLELGALRPWLARMSGSGATCFALFDAAADRDAAKAVLAARHPGWWLMAGALR | Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Mass (Da): 29450
Sequence Length: 283
Pathway: Isoprenoid biosynthesis; isopente... |
Q18CD3 | MRIGLGYDVHKLTEDRKLIIGGVEIPHDKGLLGHSDADVLIHAIMDSILGALALGDIGKHFPDTDEEYKGADSMKLLEHVYNLITSKGYKIGNIDSTIIAQSPKMAPYIESMRSNISKVLNTDIDNINIKATTEEGLGFTGAKQGIASQSICLLLLTSQNN | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-meth... |
Q4JXJ6 | MNTPHIIPRVGIATDAHQVQPGKDCWMACLLWEDQDGCEGHSDGDVVAHAVVDALLSAAGLGDLGSFVGVGRQEYDNVSGERLLRECRELLESKGFVIGNAAVQMVGNRPKMGTRREEAEKVMGELIGAPVSVSATTTDHMGFTGRGEGVAAVATAVVWQAQN | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-meth... |
Q165P5 | MDIRLGNGFDVHAFGPGDHVTLCGVKIPHGQGLVGHSDADVAMHTVTDAIYGALAMGDIGQHFPPSDPQWKGAASDIFLKHAVAQASEQGFEINNVDCTLICEFPKIGPHAQAMREAMARIMGMALSRISVKATTSERLGFTGRGEGIACIATAALVRA | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-meth... |
Q1AU09 | MGGYRVGLGVDVHAFADPAEGRQLVLGGVRIPSERGLRGHSDADVLAHAVTDALLGAAGLEDIGHYFPDTDERFRDADSIWLLREARRIVGGGWEVVNVDAVVICERPRIREHREKMRENLAAALGVEASRVSVRGTTSERLGFTGRGEGIAAQAVCLLERAVGT | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-meth... |
Q8RA30 | MIKMRKLTREIKIGNKKIGGNNPILVQSMTNTDTHDVEKTVEQIKRLEEEGCDIIRVAVPDEKAAYSIKEIKKHINIPLVADIHFDYRLAIKSIENGADKIRINPGNIGREENIKKVVEAAKERGIPIRIGVNAGSLEKEILNKYGGITPEAVVESALKSVRLLEKLGFYDIVISLKTSNVPLTIEAYKLASSKVDYPLHLGITEAGTLESGTIKSAIGIGTLLYMGIGDTIRVSLTGDPVHEVRVGRQILRALGLLKEGVEVISCPTCGRTKIDVIKLATEVERRTSHIKKPLKVAVMGCVVNGPGEAKEADIGIAGGD... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Catalytic Activity: (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + H2O + oxidized [flavodoxin] = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + ... |
Q9PPM1 | MEYKRFKTRQIKVGNVLIGGDAPISVQSMLFTKTRDIEGSLEQINRLYFAGANIVRLACLDMADARALKEIKAKSPLPLIVDIHFNHNLAVYCAEFIDGVRINPGNIGSKENIKEVVKACKERGIPIRIGVNHGSIEKQFSDKFGYGVDAMLESAMYNIKLLEDLDFFDIKISMKTSDAQKTIEAYERLRPLCDYPFHLGVTEAGTKFHSTVKSSIALGNLLLKGIGDTMRVSMTGELEEEIRVARAILQDSGVQKSGVNIISCPTCGRIQSDLLSAIKIVEEKTKHIKEPLNISVMGCVVNALGEAKGADVAIAFGKNQ... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Catalytic Activity: (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + H2O + oxidized [flavodoxin] = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + ... |
Q9A9W0 | MAADHTHVRPWRMITRRQSRKIRVGSVEVGGDAPISVQSMTNTLTSDAAATLEQIRQLEEAGADIVRVSCPDVESTAAFKTIAREAKVPLVADIHFHYKRGIEAAQAGAACLRINPGNIGSPDRVRDVIQAARDHGCSMRIGVNAGSLERELLEKYGEPCPDAMVESALNHARILQDHDFHEFKISVKASDPFMTVAAYYQLAEAIDCPLHLGVTEAGATRTGTVKSAIGIGAMLWAGIGDTIRVSLAADPVEEIKVGFDILKSLGLRHRGVNIIACPSCARQGFNVIKTVEALEERLAHISTPMSLSIIGCVVNGPGEA... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Catalytic Activity: (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + H2O + oxidized [flavodoxin] = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + ... |
A6L089 | MDLFNYSRRESSEVNIGATPLGGNNPIRIQSMTNTVTMDTEACVEQAKRIIDAGGEYVRLTTQGVREAENLKNINIGLRSQGYDTPLVADVHFNPKVADVAAQYAEKVRINPGNYVDPGRTFQKLEYTDEEYAQEIEKIRARFIPFLNICKENHTAIRIGVNHGSLSDRIMSHYGDTPEGMVESCMEFLRICVAEHFNDVVISIKASNTVVMVRTVRLLVKEMEKEGMAFPLHLGVTEAGDGEDGRIKSALGIGALLADGLGDTIRVSLSEAPENEIPVARKLVDYILTREGHPFIPGKEAPQFNYLSPGRRKTKAVRNI... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Catalytic Activity: (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + H2O + oxidized [flavodoxin] = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + ... |
Q7MVT7 | MLDLFGYKRRKTSVAQIGDTPLGGDFPIRIQSMANVSTMDTQASVDQAARIIDAGADYVRFTAQGVREAVNLQHIHAGLCRLGYHIPLVADIHFSPKAAEEALLHVEKVRINPGNFVEMKSGGNLTEEEAFDLGHKAVRERFGSFVEDAKRLGRAIRIGVNHGSLSERMLTRYGDTAEGMVQSCMEYLDVCHEHEFDDVVISMKASNTLVMTAAVRLLVERMDAADMHYPLHIGVTEAGDGEDGRIKSAVGIGSLLADGIGDTIRVSLSEDPEHEIPVARKLLAYIEKRNGHPSVAVPQPDRYDRDKLRRQETYAVGDFI... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Catalytic Activity: (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + H2O + oxidized [flavodoxin] = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + ... |
Q7V215 | MSLTQSKEVNSLSRRYSTYIERRITRTVMVGDIAIGSDYPVRVQSMINEDTMDVDNSYLAIKRLHEVGCEIVRLTVPSLAHAKAVGDIKEKLIKNNIDTPLVADVHHNGMKIAMEVAKHVDKVRINPGLFVFEKSDPTRTEYTDTEFETIKKTILKRFTPLVEVLKSENKALRIGVNHGSLSERMLFTYGDTPLGMTESAMEFVKICDELDFHNIIISMKASRAPVMLAAYRMIADRLDAEGYNYPLHLGVTEAGDGDYGRIKSTAGIGTLLAEGLGDTIRVSLTEAPEKEIPVCYSILQSLGLRKTMVEYISCPSCGRT... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Catalytic Activity: (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate ... |
P72241 | MHNESPIKRRKSTRIYVGNVPIGDGAPIAVQSMTNTRTTDVEATVRQIQSLERVGVDIVRVSVPTMDAAEAFKLIKQRVNVPLVADIHFDYRIAMKVAEYGVDCLRINPGNIGSEERIRQVVDSARHHNIPIRIGVNGGSLEKDIQEKYGEPTPEALVESAMRHVDILDRLNFDQFKVSVKASDVFLAVGSYRLLAQKIDQPLHLGITEAGGARSGSVKSAIGLGMLLAEGIGDTLRISLAADPVEEVKVGFDILKSLRIRSRGINFIACPTCSRQEFDVIGTVNALEQRLEDIITPMDVSIIGCVVNGPGEAEVSTLGV... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (By similarity). Involved in density-dependent regulation of 2'-N-acetyltransferase .
Catalytic Activity: (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + H2O... |
Q8A625 | MIKVEIDEGSGFCFGVVTAIHKAEEELAKGETLYCLGDIVHNSREVERLKAMGLITINRDEFRQLRNAKVLLRAHGEPPETYQIAHKNNIEIIDATCPVVLRLQKRIKQEFRKEDFEEKQIVIYGKNGHAEVLGLVGQTGGQAIVIESAEEAKKLDFTKSIRLFSQTTKSLDEFQEIVEYIKLHISPDATFEYYDTICRQVANRMPNLREFAATHDLIFFVSGKKSSNGKMLFEECLKVNANSHLIDNEKEIDPTLLRNVKSIGVCGATSTPKWLMEKIHDHIQLLIKD | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Cat... |
B1ZXD4 | MKVLRAKSAGFCWGVERAIEITRDYAHQGRKPVYTDGPLIHNRQMMEKLSEEGIREVGDYQSRANIAVNPAAPGENPVMVVRAHGISPERRNYLKSLGMDFKDATCPDVGIIAGKIRLHAKKGYATIIFGDKNHPEAIGLLGYTEGRGYCITSKADIDALPALERVCMVSQSTMFMHEFAELSEYARQKFKEVLVFDTICQATKDRQTDVVALARQGAQAIVVIGGHHSANTVKLASLARLQNLPTYHIETAAELSPEEMKKFTVIGVTAGASTPEFLISEVCAKLEAL | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Cat... |
Q6AVG6 | MATITTQLRSALLSPAASPSRRARRAPSSVRCDSSAASSLSASASLDADFDKKQFRHNLTRSDNYNRKGFGHKKETLELMSQEYTSDVIKTLKENGNQHTWGPVTVKLAEAYGFCWGVERAVQIAYEARKQFPDDRIWLTNEIIHNPTVNKRLEDMGVQNIPVDAGIKDFDVVEQGDVVVLPAFGAAVEEMYTLNEKKVQIVDTTCPWVSKVWNMVEKHKKGDYTSIIHGKYSHEETVATASFAGTYIIVKNIAEASYVCDYILGGQLDGSSSTKEEFLEKFKNAVSPGFDPDVDLVKVGIANQTTMLKGETEEIGKLVE... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is essential for chloroplast development.
Catalytic Ac... |
A1B842 | MDKKPPLTLYLAAPRGFCAGVDRAIKIVEMALQKWGAPVYVRHEIVHNKFVVDSLRDKGAVFVEELDDVPSDRPVIFSAHGVPKAVPAEARRREMVFVDATCPLVSKVHVEAERHHAEGLQMVMIGHAGHPEVLGTMGQLPEGEVLLVETVEDVARIEPRDPGRLAFITQTTLSVDDTAAIVAALQARFPGIRGPAKEDICYATTNRQASVKAIAGRIDALLVIGAPNSSNSRRLVEVGSAAGCAYSQLVMRADQIDWRAIAGARAVGVTAGASAPEVLVDEVVAAFHARYDLTVEMVETARENVEFKVPRVLREA | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Cat... |
Q6MC97 | MKLLLSKPRGFCAGVERAIETVEKALLLWGSPIYVKHEIVHNRHVVQGLKTKGAIFIEDVEDVPVGARLIYSAHGVSPAVREQAKKRQLIEIDATCGLVTRVHSAVKRYALQGYQIILIGHHNHVEIIGTAGEAPDVTTIVESVEDVKNLNFSSQDKLFYITQTTLSLDDVKEITQALIVKYPHVETLPSSSICYATTNRQMALREITDLTDLVLVVGDPQSSNSNRLREAASTRGIESYLINDEKEIHPEWLLGKQVIGLTAGASTPEEIVQKCIQCLIELGVNEVEDIVYTHEDVVFQLPKPIVNARFSVD | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Cat... |
Q6D0C6 | MQILLANPRGFCAGVDRAISIVERALELFGTPIYVRHEVVHNRYVVNGLRERGAIFIEQIEDVPDGAILIFSAHGVSQAVRNEAKNRDLTVFDATCPLVTKVHMEVARASKKGVEAILIGHAGHPEVEGTMGQYSNADGGMYLVESPDDVWQLQVKDEKNLCFMTQTTLSVDDTYAVIDALRERFPRIIGPRKDDICYATTNRQEAVRHLSDKADVVFVVGSKNSSNSNRLAELAQRAGKAAYLIDSADDIQESWLTGASYVGVTAGASAPDILVQQVIQRLKELGGKVAVEMQGREENIVFEVPKELRVEVKQID | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Cat... |
A1ANP9 | MRVILAKRAGFCFGVKRATQMAFEAAGMDKKTYTLGPIIHSPQVVKKLEEMGVRALKDLDSMDSGTIIIRSHGVASHEIAEAMQKKLEIVDATCPFVKKAQEHVKSLSETGYGVVVVGDADHPEVQGIVSYGGDKVFVVGSGEEVRKLPIMNKIGVVAQTTQSFENLKNVVSECLQRGGEIRVFNTICDATAVRQEEAKELARQVDCMLVVGGFNSANTRRLAEVCAELQPRTHHIETAAEIDPAWFEGVATVGVTAGASTPKWIIDEVMGRIGEINKKN | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Cat... |
A9BGS3 | MEINVAKRTGFCSGVQKTYNEVKNSLVDKNKIYIYGELVHNRKVIEELNSAGAITITGMDDIPDDSIDETLIIRAHGISKAEKDLLKKRFSKVIDMTCPIVTNLVKYVEKKQKDGFFVVVYGKPDHPEILGLKGNVDESKLLITLSPVTIPQKKVLIVSQTTMGEEEYKNFITSILTINSFTEVLIRDTICSETILREKETLELSQKSTLMLVLGGKNSSNTQKLYRISKKYCKRTYHIESGEELKEITISPQDKIGIVTGSSTPTSELNKVLEYLSQEKEDFS | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Cat... |
Q8I295 | MSVTTFCSLKKTDKCNIYISKRAFSVFLFYLFFFLFFHFYFLCSSSFAVIIHESEKRKNIMRRKRSILQIFENSIKSKEGKCNFTKRYITHYYNIPLKIKKHDLPSVIKYFSHKPNGKHNYVTNMITQKNRKSFLFFFFLYNKYFFGKQEQIRKMNYHEEMNKINIKNDGNRKIYMYPKNDIHEEDGDHKNDVEINQKRNEQNCKSFNDEKNENARDPNKILYLINPRGFCKGVSRAIETVEECLKLFKPPIYVKHKIVHNDIVCKKLEKEGAIFIEDLNDVPDGHILIYSAHGISPQIREIAKKKKLIEIDATCPLVNK... | Cofactor: Was shown to bind 1 [3Fe-4S] cluster . However, it initially contains a [4Fe-4S] cluster which easily degrades into a [3Fe-4S] form in the presence of oxygen (Probable).
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP)... |
Q97I62 | MLNFIRSDKDKGKGNDNDINFSNIPKHIAIIMDGNGRWAKKRNLPRTMGHKAGGEALKRIVRECSDIGVKYLTVYGFSTENWIRPKEEVNAIMRLIVEFLKREFNELNKNNVIINPIGNILGLPEACITALNDAKNKTKNNTGLMLNLALNYGGRDEILNAVKNIFASYEENKISKDEIFNLSDEEFSSYLYTGCIPDPDIIIRPSGEKRLSNFLLWQCAYSEFWYSNINWPDFSIEDLHTAIKDYQNRDRRFGGVK | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 29507
Sequence Length: 257
EC: 2.5.1.-
|
Q8XJQ9 | MLDFFSKKGNEDSEEIVLIEDKMPKHIAIIMDGNGRWAKKRGLPRTMGHRAGVKTIKTIVKECDKLGVKYLTLYAFSTENWKRPEDEVNALMKLVVEFIKNEIDELHQNGVRVQTIGDLSRFPEEPKKAILWAMEKTKDNTGVVLSLALNYGGRNEIVRGIKSVIEDVKAGKISIDDINEDMFNDYLYTKGMPDPDLIIRPSGEQRLSNFLLWQCAYSEFWYSQINWPDFNGEDLRKAIFDYQNRDRRFGGIK | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 29259
Sequence Length: 253
EC: 2.5.1.-
|
Q895K8 | MWNIFKNKSGQSHKVKDKFQLDLDNIPKHIAIIMDGNGRWAKERKLPRSLGHKAGVETIRDIVKECNNIGVRYLTLYAFSTENWKRPKEEINALMELLVNYLRKEVAELHQNNVVVNTIGDVSKLPKACEDELMKAYNKTKNNTGLVLNLALNYGGRDEIIRAIKLMYKDIEKKGLDIENVNEDLLKNYLYTKGMPDPDLIIRPSGEQRISNFLLWQCAYSEFWYSNIKWPDFKKHHLHKAIKDYQNRNRRFGGV | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 29820
Sequence Length: 255
EC: 2.5.1.-
|
Q9RRP1 | MASLNSALRTAQHVRTATRGALLWGYEQKLAREVKANGKLPRHLGLILDGNRRFARAAGLQREMGHSFGADKAHEVLQWCLELGIPSATIWVLSTDNGSREPAELAHILSLLEREARQLAVDPRIHANRVRVRAIGQHDNFPPQVLAALNNLEESTAGYEGMRLNIAVGYGGREEIVDAVQSYLRTQAAQGATLEQAAENLTPDAIGAHLYAADQPDPDFIIRTSGEIRLSGFMLWQSVYSEYYFCDVYWPGFRRVDFLRALRDFQGRDRRFGK | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 30699
Sequence Length: 274
EC: 2.5.1.-
|
Q8RE08 | MEKNIPKHIAIIMDGNGRWAKKRGLARSFGHMEGAKTLRKALEYLTEIGVKYLTVYAFSTENWNRPQDEVSTLMKLFLKYIKNERKNMMKNKIRFFVSGRKNNVPEKLQKEIEKLEEETKNNDKITLNIAFNYGSRAEIVDAVNRIIKDGKENITEEDFSKYLYNDFPDPDLVIRTSGEMRISNFLLWQIAYSELYITDVLWPDFDEKEIDKAIESYNQRERRFGGVKNV | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 27108
Sequence Length: 230
EC: 2.5.1.-
|
P60482 | MHGLIPDKLPRHLAIIMDGNGRWAQERMLTRIIGHQKGVETVRIIVEECSRLGIGYLTLFAFSAENWLRPKTEVKALMALLKKYIASEAARMDANNIRFNVIGNRDELPPDVNKAVQGAIDRTSGNTGMILTLALSYGARQEIMTAATRIASDIASGVLKADDLSETAFASYLFTSGLPDPDFLIRTSGEMRISNFLLWQLAYTEFYFSSVNWPEFTPEELYRALSDYQARERRFGRTSAQINTRS | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 27689
Sequence Length: 246
EC: 2.5.1.-
|
Q7VH74 | MKPSYPQHIAVIMDGNGRWAKKQGKKRTQGHKEGAKIVRDITQWCAEKGIPYLTLYAFSTENWKRPKIEVDFLMKLLEKYLHDEKPVYMKNHIRFRVIGDISVFNTRLKNAILELEHATQNHTKLTQILALNYGSRDEIARTFIKLAHTLTPHTLASLSSQDIISMINANLDTATLPDVDMLIRTGGEKRISNFMLWQASYAELFFTPTLFPSFGKNELNAMLEEFLQRQRRFGGVE | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 27370
Sequence Length: 237
EC: 2.5.1.-
|
P55984 | MDNTLKHLAIIMDGNGRWAKLKNKARAYGHKKGVKTLKDITIWCANHKLECLTLYAFSTENWKRPKSEVDFLMKMLKKYLKDERSTYLNNNIRFRAIGDLEGFSKELRDTILQLENDTRHFKDFTQVLALNYGSKNELSRAFKSLLESPPSHINLLESLENEISNRLDTHDLPEVDLLLRTGGEMRLSNFLLWQSSYAELFFTPILWPDFTPKDLENIISDFYKRVRKFGELKC | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 27455
Sequence Length: 234
EC: 2.5.1.-
|
Q9CDT1 | MFNNLKNKEQEELLPEHIGIIMDGNGRWAKQKGKPRIFGHKAGMDSLKDVAVHGARRGIKVMTVYAFSTENWTRPVDEVKFIMSLPIDFYSKYVPVLKEENIQIRMIGEREGLPKATLDSIDRAAQETSENDGMILNFAMNYGGRRDIILAIQELAKSGQDLSLLTEEELSKHLQTAVLSENLRDPDLIIRTSGEQRMSNFLTWQSAYSELYFAQTAWPDFDDKELDKAISAFQKRDRRYGGVK | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 27906
Sequence Length: 244
EC: 2.5.1.-
|
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