| IED ID | IndEnz0005000097 |
| Enzyme Type ID | lipase000097 |
| Protein Name |
Non-reducing polyketide synthase pkbA NR-PKS pkbA EC 2.3.1.- Cichorine biosynthesis cluster protein pkbA |
| Gene Name | pkbA ANIA_06448 |
| Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Enzyme Sequence | MAPAPSALVFGSQTTLPSVEAASRLRAALLLDPRLYRMRTSIESLPEIWPALAISDPALERVAGPAEKSLRQLCRWLSHSEFPDATEISELPATFVTPFTVILHTVLYMHYTDENGSRGHADVLRAVRNNGGVQGFCTGFLTAVSVATSPDLEALSRQASVALRLAVAIGAYIDLDLLDSDVSSVAVRSRAGKKGLEETLAQFPGAYISVITDELNATVTAPRASLDALSQSLASNGLSAKRFDLRGRFHHPAHQKALEGLYNLVASNPVFQFSHSELLAPVYSNIDGQLLSSDSIIDTLLQSILVQRCDWYASISTALHKRSNGEKTSVVQFSLVECIPPSVLRQARLSVQRITDVPVQNSPATVPAPLNAVRARIQTSEPIAIIGMGCKFPGADTLDEYWQLLAQGTSMCRTMPEERFKTSSLRRSPGEKLKFWGNFVNDVDAFDHRFFKKSSREAASMDPQQRLVLQVAYQTLESAEYSGLSGIKASRDVGCYLGLCASDYTDNVASHPPNAFSSLGTLRAFLSGKISHFFGWTGPSITYDTACSSSAVAIQAACRALQTGECSMALAGGVSLYTSPNFYQNLSAASFLSPTGPTKPFDAKGDGYCRGEGVGLVFLKPLSSALADHDNIMGVIAAAAVNQNQNSTAITVPHSESQIELYRKVVSEAGLHPHDVSFVEAHGTGTPVGDPIEFTSIRTVFGGSNRANPLAIASVKGNIGHTEGAAACINNYGAAGSNAAMIVTEAPTGARSEKQGTLPKCPIYVSANTVSSLKEYCKELLRSLRGRSPDCLASLAFQLANSQNRGFPHALITSVTSKAELEDQLSAVVENRNNSLHTVAPTERPVVLAFGGQVARSVGLSRQVYDSSAVLRTHLSNCDDILTSAGLNSIFPAIFRKEPIADVVLLHSALFSAQYACAMTWIEAGVIPAALIGHSFGQLTALSVGRVLSLKDGLGLITERAKLMRDAWGPEHGSMVSVQADVQTVARLMKAAETKDPKDALEIACFNGPTSHVVVGSADAADRLEAALTQESIRYKRLAVSHGFHSKFTEPLLLGLEQCAERLTFRTPKYAIETCSSGSSWSEFNASMIVQHTRTPVYYTEALARIEAKLGACTWLEVGTGGSVAGMIRGALNVPSDHLIQAVNLAGETGTAALADATVNLWKSSHKLQFWAFHRSERECYQPLELPPYQFEKTRHWLDWKDTMTEQATVTQSTREETSVEEFLTFVKYKDSTKQQAEFRISTEHEKYSFFVKGHAVLAEPLCPAPLYIDLACKAGQMVYSDTSETLIIPSVEDLEIQAPLGVGDRVIILRLQQSPFLKTAWTFCFCSRPVMGNSAEEQLHASGTVVLRENDTKTAAEFSRFGRLVSSKRVQEMKSDPDCHILQGPVVYQLFSRVVSYADYYKGVQSVYASGAEVTGRIRLPPTVKDADTRRPLLVDNFIQTAGIHVNCLTDVGAKEVYVCTKVDRVQSAAAFTEDLANVDASWIVHSSYHPTSEKEVVNDIFVFNAATGELAMFILGAHFTRVQISSLGRVLSRANTADAAPIKVAVPVQSPALRAQPKRVLLPPLTKRSITRPTLEISEKLKKTLSRVVEVPVADIHDGGILADLGVDSLLGTEVLTEINQVFNVSIPADEFALLTDVASISKCLASYLGVHDSGSQPEDLADADSVESDSDMPTGAVTSGITTPDDAVSRLADLLAENLEYDGTIEASNNLADLGLDSILSIELANDIKKIFNCDVDMSQLNMESTFADLIALVPALNIEQSLSSVPASLTTQGSDFEMAQHAFEQIRFDYDIYTKETGFYDFWKRVYPAQSRLVLAYTVEAFAQLGCDLALMHPGDRLPKIGYLPAHEKLVQQLYNILRDGMLVATSDSGFVRSDKPVDPTSSTRLLEEINTIAPQHASEHSLLHITGSKLADCLTGTADPLNLLFRSKANRDLLAEVYLNGPMYAAISRLLCSFLGNAFSDRQSSGTFQILELGGGTGGTTGHVLDYLVRSGIPFTYTFSDVSGSFVAAARKKFAGRPYMEYQVIDIEKEPADSLTGKFHAVISTNCIHATTNLEISTGNIHRMLRPDGFVALVEFTRNMYWFDLVFGLLEGWWLFEDGRQHVIASESFWNTSMRKAGFQHVSWTDGDSFEARTLRIIAGFRAPAVNEIYTPRLDSRDTETAVESVMYKQADGIPLFADIYYPPSVSNEPRPIALMIHGGGHIMLSRKDIRPKQTAHLHTLGFLPVSIDYRLCPETTLTEGPMRDVSDAMAWARSTLCSLPLLCPGLTLDPSRVVVVGWSTGGHLAMTTAFTSIERGLSPPDAILAFYCPTDYEDRVWTQPNYPENTDVDGLSLMKYNLLEGVQDRPITAYNIPLTSRSNSKAGGTPAGGWMAPDDPRSRIVLHMNWKGQCLPVLLRGLPPSNSLSPGDAEKLISQPQPEIEEIQRVSPYAQIRRGVYRTPTFVIHGTDDDLIPYEQSVRTVQALKDMGVRAEVSVPQGKAHLFDMFKDADGSSWEVVKRGYDFLKEEVSGK |
| Enzyme Length | 2517 |
| Uniprot Accession Number | Q5AZ32 |
| Absorption | |
| Active Site | ACT_SITE 547; /note=For beta-ketoacyl synthase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10022; ACT_SITE 935; /note=For acyl/malonyl transferase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10022 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + 3 malonyl-CoA + S-adenosyl-L-methionine = 3-methylorsellinate + 3 CO2 + 4 CoA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:64500, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:146372; Evidence={ECO:0000269|PubMed:22510154};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64501; Evidence={ECO:0000269|PubMed:22510154}; |
| DNA Binding | |
| EC Number | 2.3.1.- |
| Enzyme Function | FUNCTION: Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of cichorine, a phytotoxin active against knapweed, corn, and soybeans (PubMed:22510154, PubMed:24244835, PubMed:30708999). The first step in the pathway is performed by the non-reducing polyketide synthase pkbA that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units (PubMed:22510154). PkbA also catalyzes one methylation step to produce 3-methylorsellinate (PubMed:22510154). The nonribosomal peptide synthase-like protein cicB, the cytochrome P450 monooxygenase cicH and the O-methyltransferase cicE are involved in the conversion of 3-methylorsellinate into nidulol (PubMed:24244835). CicB converts 3-methylorsellinate to a yet unidentified intermediate, cicH may play a ring-closing role for cichorine and cicE is plausibly responsible for the methylation of one of the phenol groups (Probable). The oxidoreductase cicC acts downstream with still unidentified enzymes to further convert nidulol into cichorin (PubMed:24244835). {ECO:0000269|PubMed:22510154, ECO:0000269|PubMed:24244835, ECO:0000269|PubMed:30708999, ECO:0000305|PubMed:24244835}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Phytotoxin biosynthesis. {ECO:0000269|PubMed:22510154, ECO:0000269|PubMed:24244835, ECO:0000269|PubMed:30708999}. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (2); Modified residue (2); Region (7) |
| Keywords | Acyltransferase;Methyltransferase;Multifunctional enzyme;Phosphopantetheine;Phosphoprotein;Reference proteome;Repeat;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 1611; /note=O-(pantetheine 4'-phosphoryl)serine; /evidence=ECO:0000255|PROSITE-ProRule:PRU00258; MOD_RES 1721; /note=O-(pantetheine 4'-phosphoryl)serine; /evidence=ECO:0000255|PROSITE-ProRule:PRU00258 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 274,132 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:64500; RHEA:64501 |
| Cross Reference Brenda |