ID W6PYR3_PENRF Unreviewed; 358 AA.
AC W6PYR3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Isopenicillin N synthase {ECO:0000313|EMBL:CDM28871.1};
GN ORFNames=PROQFM164_S01g002682 {ECO:0000313|EMBL:CDM28871.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM28871.1};
RN [1] {ECO:0000313|EMBL:CDM28871.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM28871.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
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DR EMBL; HG792015; CDM28871.1; -; Genomic_DNA.
DR AlphaFoldDB; W6PYR3; -.
DR STRING; 1365484.W6PYR3; -.
DR OMA; PISCGKW; -.
DR OrthoDB; 2908779at2759; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR47990:SF62; IRON_ASCORBATE OXIDOREDUCTASE DDB_G0283291-RELATED; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PRINTS; PR00682; IPNSYNTHASE.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|RuleBase:RU003682};
KW Metal-binding {ECO:0000256|RuleBase:RU003682};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003682}.
FT DOMAIN 203..314
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 111..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 40160 MW; CCF2DF989B7DC57F CRC64;
MTTLLEYTQV ELLTLSGPEF RRVSTAPPRP PTEDEIPIID LASIDKDLEA RKTIASKVRV
AAESTGFFYI KNHGISEELI ENALSQAKAF FDQPIEKKQL ASSKIQNNTD GWHGLGTTQI
NKTETRDHKE SFSLRYNPKN DPTVSDPDAL SIEDAFAWDT TSHLPGFHET TIEFYQRRLM
LARKIIRIFA LALDMPEDYF DAVTTSPGAD GLYIHYPPAP ANTLEENNAN VDVGIGSHTD
IQCVTLLWQD MSGGLQVLSA SDEWLDARPI PGTLVVNIGD FLQRLSNNRF KSTVHRVYNR
QPTSRYSMPF FLGFNPDTVC KVVPSCIDET HPALYEPISC GKWHRNRIEL AHGKPISA
//
