| IED ID | IndEnz0015000123 |
| Enzyme Type ID | laccase000123 |
| Protein Name |
Non-reducing polyketide synthase PKS12 EC 2.3.1.- Aurofusarin biosynthesis cluster protein PKS12 |
| Gene Name | PKS12 AUR1 FG12040 FGRAMPH1_01T05593 |
| Organism | Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Nectriaceae Fusarium Fusarium sambucinum species complex Gibberella zeae (Wheat head blight fungus) (Fusarium graminearum) Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) (Wheat head blight fungus) (Fusarium graminearum) |
| Enzyme Sequence | MEVFVFGDQSTRFAPPLKDLLLKGNSPYLTHFVKQVHALLRREISSLPAVQQKLFPNFADIQELVSKSDWGSGNPALTSALACFYHLCSFIHFYDGQGRTFPSENSRIIGLCVGSLAAAAVSCSTSLSELVSAGVDAVRVALHVGLRVWRTTSLFDVPDRPSATWSIIVPEAVLPRESAQDRLDSFIIEMGLARSSVPYISSVAHHNMTISGPPSVLEKFIHSISTSPKDSLPVPIYAPYHASHLYSMDDVDEVLSLSAPSFASESIIPLISSSSGDELQPLKYADLLRCCVSDMLIQPLDLTKVSQAVAQLLEVSSSTRAIIKPIATSVSNSLVSALEPTLAERCAVDNSMGPKASTSHSSAETQTESSSKNSKIAIVAMSGRFPDAADLGEFWDLLYKGRDVHRQIPEDRFNAELHYDATGRRKNTSKVMNGCFIKEPGLFDARFFNMSPKEAEQSDPGQRMALETAYEALEMAGIVPDRTPSTQRDRVGVFYGMTSDDWREVNSGQNVDTYFIPGGNRAFTPGRLNYFFKFSGPSASVDTACSSSLAALHLACNSLWRNDCDTAIAGGTNVMTNPDNFAGLDRGHFLSRTGNCNTFDDGADGYCRADGVGTIILKRLEDAEADNDPILGVILGAYTNHSAEAVSITRPHAGAQEYIFSKLLRESGTDPYNVSYIEMHGTGTQAGDATEMTSVLKTFAPTSGFGGRLPHQNLHLGSVKANVGHGESASGIIALIKTLLMMEKNMIPPHCGIKTKINHHFPTDLTQRNVHIAKVPTSWTRSGQANPRIAFVNNFSAAGGNSAVLLQDAPRPSVVSDVTDPRSSHVVTMSARSADSLRKNLANLKELVEGQGDSEVDFLSKLSYTTTARRMHHQFRASVTAQTREQLLKGLDSAIERQDVKRIPAAAPSVGFVFSGQGAQYRGMGKEYFTSFTAFRSEIMSYDSIAQAQGFPSILPLIRGEVEADSLSPVEIQLGLTCLQMALAKLWKSFGVEPGFVLGHSLGHYAALHVAGVLSANDTIYLTGIRAQLLVDKCQAGTHSMLAVRASLLQIQQFLDANIHEVACVNGPREVVISGRVADIDQLVGLLSADNIKATRVKVPFAFHSAQVDPILSDLDTAASRVTFHSPQIPVLCALDSSVISPGNHGVIGPLHLQRHCRETVNFEGALHAAEREKIINKTSTLWIEIGPHVVCSTFLKSSLGPSTPTIASLRRNDDCWKVLADGLSSLYSSGLTIDWNEYHRDFKASHQVLRLPCYSWEHKNYWIQYKYDWSLTKGDPPIAPNSSVEAVSALSTPSVQKILQETSLDQVLTIVAETDLASPLLSEVAQGHRVNGVKVCTSSVYADVGLTLGKYILDNYRTDLEGYAVDVHGIEVHKPLLLKEDMNGTPQATPFRIEVRYPIQSTTALMSISTTGPNGQHIKHANCELRLEHPSQWEAEWDRQAYLINRSVNYLLQRSAQGLDSMLATGMVYKVFSSLVDYADGYKGLQEVVLHSQELEGTAKVRFQTPSGGFVCNPMWIDSCGQTTGFMMNCHQTTPNDYVYVNHGWKSMRLAKAFREDGTYRTYIRMRPIDSTKFAGDLYILDEDDTVVGVYGDITFQGLPRRVLNTVLPSANAVPVDAPMGRRDVPPSRMDVPPVRSGEGPPTSAPTQQAIALPFAADTSMDSRLRPLLRILSEEIGLGLDVLSDDELDFADHGVDSLLSLTITGRMREELGLDVESTAFMNCPTLGSFKLFLGLVDQDNKSSSGSDGSGRSSPAPGIESGATTPPMSEEDQDKIVSSHSLHQFQASSTLLQGSPSKARSTLFLLPDGSGSATSYASLPPISPDGDVAVYGLNCPWLKDASYLVEFGLKGLTELYVNEILRRKPQGPYNLGGWSAGGICAYEAALILTRAGHQVDRLILIDSPNPVGLEKLPPRLYDFLNSQNVFGSDNPHSTAGTSVKAPEWLLAHFLAFIDALDAYVAVPWDSGLVGLASPLPAPPQTYMLWAEDGVCKDSDSARPEYRDDDPREMRWLLENRTNFGPNGWEALLGGKEGLFMDRIAEANHFSMLKRGRNAEYVSAFLARALDN |
| Enzyme Length | 2067 |
| Uniprot Accession Number | I1RF58 |
| Absorption | |
| Active Site | ACT_SITE 545; /note=For beta-ketoacyl synthase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10022; ACT_SITE 1001; /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 + 6 H(+) + 6 malonyl-CoA = 6 CO2 + 7 CoA + H2O + YWA1; Xref=Rhea:RHEA:62652, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:133763; Evidence={ECO:0000269|PubMed:23557488};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62653; Evidence={ECO:0000269|PubMed:23557488}; |
| DNA Binding | |
| EC Number | 2.3.1.- |
| Enzyme Function | FUNCTION: Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of aurofusarin, a red mycelium pigment which is acting as a mycotoxin (PubMed:15811992, PubMed:16278459, PubMed:15809006, PubMed:15780665, PubMed:16879655). The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide and yellow pigment YWA1 (PubMed:21296881, PubMed:23557488). The C2 hydroxyl group in the pyrone ring of YWA1 is probably formed during ring closure by an aldol-type cyclization reaction (PubMed:21296881). The dehydratase aurZ then acts as the first tailoring enzyme in the aurofusarin biosynthetic pathway by converting YWA1 to nor-rubrofusarin (PubMed:21296881, PubMed:23557488). Nor-rubrofusarin is then methylated to rubrofusarin by the O-methyltransferase aurJ (PubMed:21296881, PubMed:23557488). Rubrofusarin is then transported across the plasma membrane by the rubrofusarin-specific pump aurT for further enzymatic processing by the extracellular complex composed of GIP1, aurF, aurO and aurS to yield aurofusarin (PubMed:21296881). {ECO:0000269|PubMed:15780665, ECO:0000269|PubMed:15809006, ECO:0000269|PubMed:15811992, ECO:0000269|PubMed:16278459, ECO:0000269|PubMed:16879655, ECO:0000269|PubMed:21296881, ECO:0000269|PubMed:23557488}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:15809006, ECO:0000269|PubMed:16879655, ECO:0000269|PubMed:23557488}. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (2); Domain (1); Modified residue (1); Region (8) |
| Keywords | Multifunctional enzyme;Phosphopantetheine;Phosphoprotein;Reference proteome;Transferase |
| Interact With | |
| Induction | INDUCTION: Expression is regulated by the aurofusarin biosynthesis cluster-specific transcription factor aurR1/GIP2 (PubMed:16879655, PubMed:16461721). Expression is negatively regulated by the MAPK-mediated osmotic stress-signaling pathway (PubMed:17897620). Expression is also regulated by the CID1 cyclin C-like protein (PubMed:19909822). {ECO:0000269|PubMed:16461721, ECO:0000269|PubMed:16879655, ECO:0000269|PubMed:17897620, ECO:0000269|PubMed:19909822}. |
| Subcellular Location | |
| Modified Residue | MOD_RES 1698; /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 | 225,115 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62652; RHEA:62653 |
| Cross Reference Brenda |