A0A1B7YCC9 · DPCHA_COLHI
- ProteinNon-reducing polyketide synthase dpchA
- GenedpchA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids2224 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the diterpenoid pyrones higginsianins A and B (PubMed:32286350).
The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpchA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpchD through the action of the prenyltransferase dpchC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpchE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpchB (Probable). The short chain dehydrogenase/reductase dpchG then oxidizes the 8S hydroxy group to a ketone and the short chain dehydrogenase/reductase dpchH reduces the ketone to the 8R hydroxy group to yield higginsianin B (PubMed:32286350).
Finally, the FAD-dependent oxidoreductase dpchF converts higginsianin B into higginsianin A (PubMed:32286350).
The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpchA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpchD through the action of the prenyltransferase dpchC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpchE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpchB (Probable). The short chain dehydrogenase/reductase dpchG then oxidizes the 8S hydroxy group to a ketone and the short chain dehydrogenase/reductase dpchH reduces the ketone to the 8R hydroxy group to yield higginsianin B (PubMed:32286350).
Finally, the FAD-dependent oxidoreductase dpchF converts higginsianin B into higginsianin A (PubMed:32286350).
Biotechnology
Diterpenoid pyrones display various biological activities and higginsianin A shows anti-HIV activity.
Pathway
Secondary metabolite biosynthesis; terpenoid biosynthesis.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 567 | For beta-ketoacyl synthase activity | ||||
Sequence: C | ||||||
Active site | 703 | For beta-ketoacyl synthase activity | ||||
Sequence: H | ||||||
Active site | 745 | For beta-ketoacyl synthase activity | ||||
Sequence: H | ||||||
Active site | 1027 | For acyl/malonyl transferase activity | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 3-oxoacyl-[acyl-carrier-protein] synthase activity | |
Molecular Function | methyltransferase activity | |
Biological Process | fatty acid biosynthetic process | |
Biological Process | methylation | |
Biological Process | secondary metabolite biosynthetic process | |
Biological Process | terpenoid biosynthetic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNon-reducing polyketide synthase dpchA
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Glomerellales > Glomerellaceae > Colletotrichum > Colletotrichum destructivum species complex
Accessions
- Primary accessionA0A1B7YCC9
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000451523 | 1-2224 | Non-reducing polyketide synthase dpchA | |||
Sequence: MSAETPSLLVCGPLISDPDATHLARIRSALVHTPQLAELRQAVTELPGVWSLLAGGEPSLERVHAAPLLQAFAEWINKGNSSGLLAAGQSSRNTRLAVLTVLSHLAEYVTFLRGLDAGAEEDLAGELDEHTKTLGGLRDGGVQGLCVGMLSASALACARNTSEVAELGAVAVRLAMCSAAFVDLDQIQSSDPTVCVSARLPRNAGEGDEQDRQPFQEALESYPEVRIQHSQSSQSWVQKEKAWLTCALRRQAYIGVRMDVAGTTITATKSITGPLTRHLEGQGAMTKEIDLKGRFHYPGHEDALQKLVRLCESTPMLQFPQNRYPLVPLRQTITGDVVTDETPLHETVLRCILTETADWHTTMTRAVSALAGSPETKSSPAGNRTRLLVQLGIAECIPRSVLAGIPSIRVLQPTTGKPARPGHYPDDAIAVIGMSCRFPDAETPEHFWEIIQSGAKAGSVFPDVGSFDCGLFRKSPREAEYMDPQHRLALHLAYEALEAAGHFSPSSSSTDDVGCYVGMSSCDYEDHVNARPPTAFSFTGTARAFASGRISHFFGLTGPSVVVDTACSSSGVAIHTACRAVLSGECAVALAGGVNLMTDEGQAHQNLAGASFLSPTGQCRPFDAAADGYRRGQGGGFVLLKRLSAAVADNDRVLGVIAASAVNNSKGNRSITLPSSESQSRLYRQVLGSANVHPSHVSYVEAHGTGTQKGDPVECQSIRSVFGGSSRAGSSSPIRLGSVKGNLGHGEAASGIASLVKVLLMLQHGVITPQANFSMLNPAIPPLEGDNMEIVVSPASWRGPFRTALVNNYGASGANAAMVVCQAPSTHLSQIASTRTAAMTTTHRYPFVITANTASSLHRSCLALLRFIETLPAGLNNDSLPSLAFHLAQRQNHALVHRIVFSARSVAELKAHLLAQVEGGNIPSDTSSQAQKTGTKPVVLLFSGQTGRRAHLNRDAYTSFHLLRHHLDRCDRTLQTLGLRSLFPRIFDADPLEDLVDLHCMQFALQYSVAASWTDSGLEIKALVGHSLGQLTALCVSGALSLADSLRMVSGRALLIQTAWKQERGCMLSVDADAATVETLAQSVSAEDKVEIACYNAALHQVVAGTEAAVAAFENAAGSSGISTKRLAVTHAFHSKLLDDILPEYHRLLRSLEFRPAKIPIEPCSEFGGGWDSVTPDIVGRQSREPVYFAAAMARVEQRLGSCVWLEVGSGSAAITMARRALESQKPSSQAMVSHSFYAAQLHSPEPVSSVADSTVGLWNEGVRVQFWLYHASQRQSFVPMDLPSYQFDKTQYWLPFIERNKGSDSNDQSASSQAAPDLVTLVGSLGSAEPQAYEFSINQESDEYALFVKGRTVFGHFLAPGSVYAESAARAFALLPTDNTPQPPASVELGQMKLHAPFGLDLQRRLRLVLRQQTASSWEFVVESCPLHDDKEISPKPQASGTVRLQGQGRSPFGTSQSILRRLFDRCGELREDRGASVVQGAYVKKIMSRVASYDDRYFGIRFVASRGLEAVGDVDALPIVSECRAGTALSPPVFDNFLLVAEMHAGSLGDLADDHLYICGGFEAIVPGDQTSQTDGPWTVLSTLERENDKTLVSDILVFHAGSKKLALSILGARLTQIPARSLQKTLDDMNAARPAKVSNSEDVLTPPLPAVESPPTDLSNGQIHCDLRSALSPLIRSTTSLSQLTSSDDTKDSLGLSSRPSITPASSATSENDQDTTALYNLLAEHLDCSNGIPPDMPLGNIGLDSLISIQLQSDLEKLFGKSPALKLIDENTTFLELCGMVLQQDLSSQLKSRLSPVDSANARTTLNEPLQAYGGYGHAMSVVAPAPVSPQDTPPFLPLAVEAFKRVKKDTGAFAQKTGFAGFYPDVQQKQTSLVLSYILEAFATLGCDLGTLQLKDRLPGIPHPAKYQRLMGRLHDILEEAGIISPPDAQLFRYRTDAPLPPPTPSEDLYRQILDECPLYRPDHQLLGVTASRLADCISGRADPLQLLFQDQASLKLLEDVYVSSPMFSTGNSMLGEMLRGLFSQARFQREGGSEKLRILEIGAGTGATTRRVLDQLIQSGVDFSYTFTDISLALVNGSKRKFTASYGRQRVDSDMEFTVLDIERPPPASMLQAFHLVISSNCIHATRDLRTSCGNIEKLVRRGDGMLCLLELTRPLAWLDCVFGLLDGWWRFEDGRKYALAHEDEWRARLESAGFQNVDWTGDGSRESEHFRLITAWH | ||||||
Modified residue | 1749 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S |
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 74-183 | N-terminal acylcarrier protein transacylase domain (SAT) | ||||
Sequence: EWINKGNSSGLLAAGQSSRNTRLAVLTVLSHLAEYVTFLRGLDAGAEEDLAGELDEHTKTLGGLRDGGVQGLCVGMLSASALACARNTSEVAELGAVAVRLAMCSAAFVD | ||||||
Domain | 426-822 | Ketosynthase family 3 (KS3) | ||||
Sequence: DDAIAVIGMSCRFPDAETPEHFWEIIQSGAKAGSVFPDVGSFDCGLFRKSPREAEYMDPQHRLALHLAYEALEAAGHFSPSSSSTDDVGCYVGMSSCDYEDHVNARPPTAFSFTGTARAFASGRISHFFGLTGPSVVVDTACSSSGVAIHTACRAVLSGECAVALAGGVNLMTDEGQAHQNLAGASFLSPTGQCRPFDAAADGYRRGQGGGFVLLKRLSAAVADNDRVLGVIAASAVNNSKGNRSITLPSSESQSRLYRQVLGSANVHPSHVSYVEAHGTGTQKGDPVECQSIRSVFGGSSRAGSSSPIRLGSVKGNLGHGEAASGIASLVKVLLMLQHGVITPQANFSMLNPAIPPLEGDNMEIVVSPASWRGPFRTALVNNYGASGANAAMVVCQ | ||||||
Region | 941-1245 | Malonyl-CoA:ACP transacylase (MAT) domain | ||||
Sequence: LFSGQTGRRAHLNRDAYTSFHLLRHHLDRCDRTLQTLGLRSLFPRIFDADPLEDLVDLHCMQFALQYSVAASWTDSGLEIKALVGHSLGQLTALCVSGALSLADSLRMVSGRALLIQTAWKQERGCMLSVDADAATVETLAQSVSAEDKVEIACYNAALHQVVAGTEAAVAAFENAAGSSGISTKRLAVTHAFHSKLLDDILPEYHRLLRSLEFRPAKIPIEPCSEFGGGWDSVTPDIVGRQSREPVYFAAAMARVEQRLGSCVWLEVGSGSAAITMARRALESQKPSSQAMVSHSFYAAQLHSP | ||||||
Region | 1317-1451 | N-terminal hotdog fold | ||||
Sequence: PDLVTLVGSLGSAEPQAYEFSINQESDEYALFVKGRTVFGHFLAPGSVYAESAARAFALLPTDNTPQPPASVELGQMKLHAPFGLDLQRRLRLVLRQQTASSWEFVVESCPLHDDKEISPKPQASGTVRLQGQGR | ||||||
Domain | 1317-1626 | PKS/mFAS DH | ||||
Sequence: PDLVTLVGSLGSAEPQAYEFSINQESDEYALFVKGRTVFGHFLAPGSVYAESAARAFALLPTDNTPQPPASVELGQMKLHAPFGLDLQRRLRLVLRQQTASSWEFVVESCPLHDDKEISPKPQASGTVRLQGQGRSPFGTSQSILRRLFDRCGELREDRGASVVQGAYVKKIMSRVASYDDRYFGIRFVASRGLEAVGDVDALPIVSECRAGTALSPPVFDNFLLVAEMHAGSLGDLADDHLYICGGFEAIVPGDQTSQTDGPWTVLSTLERENDKTLVSDILVFHAGSKKLALSILGARLTQIPARSLQ | ||||||
Region | 1327-1620 | Product template (PT) domain | ||||
Sequence: GSAEPQAYEFSINQESDEYALFVKGRTVFGHFLAPGSVYAESAARAFALLPTDNTPQPPASVELGQMKLHAPFGLDLQRRLRLVLRQQTASSWEFVVESCPLHDDKEISPKPQASGTVRLQGQGRSPFGTSQSILRRLFDRCGELREDRGASVVQGAYVKKIMSRVASYDDRYFGIRFVASRGLEAVGDVDALPIVSECRAGTALSPPVFDNFLLVAEMHAGSLGDLADDHLYICGGFEAIVPGDQTSQTDGPWTVLSTLERENDKTLVSDILVFHAGSKKLALSILGARLTQI | ||||||
Region | 1476-1626 | C-terminal hotdog fold | ||||
Sequence: GASVVQGAYVKKIMSRVASYDDRYFGIRFVASRGLEAVGDVDALPIVSECRAGTALSPPVFDNFLLVAEMHAGSLGDLADDHLYICGGFEAIVPGDQTSQTDGPWTVLSTLERENDKTLVSDILVFHAGSKKLALSILGARLTQIPARSLQ | ||||||
Region | 1635-1664 | Disordered | ||||
Sequence: ARPAKVSNSEDVLTPPLPAVESPPTDLSNG | ||||||
Region | 1684-1717 | Disordered | ||||
Sequence: LSQLTSSDDTKDSLGLSSRPSITPASSATSENDQ | ||||||
Domain | 1713-1789 | Carrier | ||||
Sequence: SENDQDTTALYNLLAEHLDCSNGIPPDMPLGNIGLDSLISIQLQSDLEKLFGKSPALKLIDENTTFLELCGMVLQQD | ||||||
Region | 2022-2207 | Methyltransferase (CMeT) domain | ||||
Sequence: EMLRGLFSQARFQREGGSEKLRILEIGAGTGATTRRVLDQLIQSGVDFSYTFTDISLALVNGSKRKFTASYGRQRVDSDMEFTVLDIERPPPASMLQAFHLVISSNCIHATRDLRTSCGNIEKLVRRGDGMLCLLELTRPLAWLDCVFGLLDGWWRFEDGRKYALAHEDEWRARLESAGFQNVDWT |
Domain
Multidomain protein; including a starter unit:ACP transacylase (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a product template (PT) domain that controls the immediate cyclization regioselectivity of the reactive polyketide backbone; a methyltransferase (CMeT) domain responsible for methylations; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,224
- Mass (Da)240,092
- Last updated2016-11-02 v1
- Checksum24ACD0E52A7883C3
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM004458 EMBL· GenBank· DDBJ | OBR09781.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CACQ02004382 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |