ID   SORD_PENRW              Reviewed;         471 AA.
AC   B6HNK6;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=FAD-linked oxidoreductase sorD {ECO:0000303|PubMed:28618182};
DE            EC=1.1.1.- {ECO:0000305|PubMed:28618182};
DE   AltName: Full=Sorbicillinoid biosynthetic cluster protein D {ECO:0000303|PubMed:28618182};
DE   Flags: Precursor;
GN   Name=sorD {ECO:0000303|PubMed:28618182}; ORFNames=Pc21g05110;
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-linked oxidoreductase; 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:G0R6T3, 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   -!- DISRUPTION PHENOTYPE: Leads to the accumulation of sorbicillinol and
CC       impairs the production of oxosorbicillinol (PubMed:28618182).
CC       {ECO:0000269|PubMed:28618182}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AM920436; CAP95408.1; -; Genomic_DNA.
DR   RefSeq; XP_002567557.1; XM_002567511.1.
DR   AlphaFoldDB; B6HNK6; -.
DR   SMR; B6HNK6; -.
DR   STRING; 500485.B6HNK6; -.
DR   EnsemblFungi; CAP95408; CAP95408; PCH_Pc21g05110.
DR   GeneID; 8313808; -.
DR   KEGG; pcs:Pc21g05110; -.
DR   VEuPathDB; FungiDB:PCH_Pc21g05110; -.
DR   eggNOG; ENOG502QVGN; Eukaryota.
DR   HOGENOM; CLU_018354_10_1_1; -.
DR   OMA; NLFNIHY; -.
DR   OrthoDB; 1049549at2759; -.
DR   BioCyc; PCHR:PC21G05110-MON; -.
DR   Proteomes; UP000000724; Contig Pc00c21.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW   Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..471
FT                   /note="FAD-linked oxidoreductase sorD"
FT                   /id="PRO_5002843712"
FT   DOMAIN          41..212
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   CARBOHYD        18
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   471 AA;  50365 MW;  5DE2BAB4437B8D72 CRC64;
     MQAASAFATC LLASVGGNSS AVAFPNQANY STLVAPYNFD LLTTPSAIVW PQDTQQVAAA
     VKCAVDSDIK VQPKSGGHNY GNYGSTTGEL SVNLDNLQHF SMDETSWTAR LGPGNRLGRV
     TELMYNNGGR HVPHGTTFTV GLGGHATVGG AGAASRMHGL LLDYVEEVEV VLANSSIVRA
     SKSHNEDLFF AVRGAASSVG IVTDFSIRTE PVPVSSVTYS YIWEGTDPAA RAEVFLTWQS
     LLAGGSLPQH MAYDLVATAN SMILGGAYFG SQEDFEAFNL SSHFKVAPDV AHIKTYTNFF
     DFSAAASAQT KAAGIASPSH FYAKSLVFNQ QTLIPDDAAE EVFKYLATTK NGTDLYAVTF
     AALGGAVRDV SASETAFYHR DASYFMFSFG RTSGDLTDTT VQFLDGLSEV LTSGQPDAYY
     GQYVGNVDPR QSTDKALTGY YGKNLHRLQQ IKSAVDPNDV FHNQQSIPPL S