SORC_PENRW
ID SORC_PENRW Reviewed; 445 AA.
AC B6HN76;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=FAD-dependent monooxygenase sorC {ECO:0000303|PubMed:25580210};
DE EC=1.-.-.- {ECO:0000305|PubMed:25580210};
DE AltName: Full=Sorbicillinoid biosynthetic cluster protein C {ECO:0000303|PubMed:25580210};
GN Name=sorC {ECO:0000303|PubMed:25580210}; ORFNames=Pc21g05060;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
RN [2]
RP FUNCTION.
RX PubMed=25580210; DOI=10.1039/c3sc52911h;
RA Fahad A.A., Abood A., Fisch K.M., Osipow A., Davison J., Avramovic M.,
RA Butts C.P., Piel J., Simpson T.J., Cox R.J.;
RT "Oxidative dearomatisation: the key step of sorbicillinoid biosynthesis.";
RL Chem. Sci. 5:523-527(2014).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28618182; DOI=10.1111/1751-7915.12736;
RA Guzman-Chavez F., Salo O., Nygaard Y., Lankhorst P.P., Bovenberg R.A.L.,
RA Driessen A.J.M.;
RT "Mechanism and regulation of sorbicillin biosynthesis by Penicillium
RT chrysogenum.";
RL Microb. Biotechnol. 10:958-968(2017).
CC -!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of sorbicillinoids, a diverse group of yellow
CC secondary metabolites that restrict growth of competing pathogenic
CC fungi but not of bacteria (PubMed:25580210, PubMed:28618182).
CC Sorbicillinoids biosynthesis requires the action of two PKSs
CC (PubMed:25580210). SorA iteratively combines three acetyl units and the
CC growing chain is modified by the ketoacyl reductase subunit, and
CC optional by the enoyl reductase subunit in the second cycle
CC (PubMed:25580210). The polyketide is then handed over to the PKS SorB,
CC which adds three more acetyl units, and two methyl groups
CC (PubMed:25580210). SorB releases an aldehyde, which undergoes
CC spontaneous cyclization resulting in the formation of sorbicillin or
CC 2',3'-dihydrosorbicillin (PubMed:25580210). The monooxygenase sorC
CC oxidizes sorbicillin and 2',3'-dihydrosorbicillin to 2',3'-
CC dihydrosorbicillinol and sorbicillinol, respectively (PubMed:28618182).
CC The oxidoreductase sorD further converts sorbicillinol into
CC oxosorbicillinol (PubMed:28618182). Sorbicillinol is the building block
CC for the other sorbicillinoids such as disorbicillinol, bisvertinolon,
CC and dihydrobisvertinolone (By similarity).
CC {ECO:0000250|UniProtKB:G0R6T0, ECO:0000269|PubMed:25580210,
CC ECO:0000269|PubMed:28618182}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:28618182}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Leads to the accumulation of dihydrosorbicillinol
CC (PubMed:28618182). {ECO:0000269|PubMed:28618182}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AM920436; CAP95403.1; -; Genomic_DNA.
DR RefSeq; XP_002567552.1; XM_002567506.1.
DR AlphaFoldDB; B6HN76; -.
DR SMR; B6HN76; -.
DR STRING; 1108849.XP_002567552.1; -.
DR EnsemblFungi; CAP95403; CAP95403; PCH_Pc21g05060.
DR GeneID; 8313803; -.
DR KEGG; pcs:Pc21g05060; -.
DR VEuPathDB; FungiDB:PCH_Pc21g05060; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_6_3_1; -.
DR OMA; TRFMYNG; -.
DR OrthoDB; 521070at2759; -.
DR BioCyc; PCHR:PC21G05060-MON; -.
DR Proteomes; UP000000724; Contig Pc00c21.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Glycoprotein; Membrane; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..445
FT /note="FAD-dependent monooxygenase sorC"
FT /id="PRO_0000443845"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 38..39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 242..244
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 323
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 333..337
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 445 AA; 48160 MW; DD325C358870F6F2 CRC64;
MTRSANSPFE VAIVGGGITG LALAVGLLKR NVSFTIYERA ENFGELGVGI TFTPNAQRAM
EALDPCVLQS FTNVASAPSG GTINFVDGVR EQGSEDPRTS TAALLFQLHV KGGYKACRRC
DFVDQIVQHI PKDCVQYRKW LDSIETDHES GRAVLKFRDG EIAHADVVIG CDGIRSQVRA
SMFGTDELCP RAQYSHQLGY RGMVPLAQAT AVLGPEKTSS AVLHTGPGAF VLTIPLAEVH
AMHIEAFIMD KEEWPEVQTS SDSKRYVLPA TRNEATKAFA EFGPTVRSAV SMFPEKLEKW
AVFDMLEAPV PTFAKGRVCL AGDAAHASTP NQGGGAGFGI EDALVLAEVL AVLAEAPNVS
GIVASEALAV YSEVRYERSQ WLVRSSRRTG ELCTWKDRDW GLAAEELSRD IISRSHQLWD
HDTAGMVSDA LAILGERVRG ADTAF
