ID W6Q6W5_PENRF Unreviewed; 544 AA.
AC W6Q6W5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:CDM32095.1};
GN ORFNames=PROQFM164_S02g002246 {ECO:0000313|EMBL:CDM32095.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM32095.1};
RN [1] {ECO:0000313|EMBL:CDM32095.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM32095.1};
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; HG792016; CDM32095.1; -; Genomic_DNA.
DR AlphaFoldDB; W6Q6W5; -.
DR STRING; 1365484.W6Q6W5; -.
DR OMA; LDVWNQY; -.
DR OrthoDB; 52047at2759; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR47190:SF5; PX DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..544
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004881838"
FT DOMAIN 278..292
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 113
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 121..124
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 240
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 544 AA; 57914 MW; 4EF9F9162911DE52 CRC64;
MRIFQAGSLA ISLSVFTTAA TASVFQNHTY DYIVVGGGPS GIISAEKFAQ AGKKVLLLER
GVGPTVATGN NETLTWDHSL TPIDLPGLSA DIGSLDVWNQ YVCTDTAGTA ACVLGGGVTV
NYMVFVHPPA RDFDDKWPKG WKWKDVQSAA DRLYKRNPGT ILPSADGKRY DQALYGVLSK
FLGGLGWKSV DMIAQPNEKH QVYSYPAWNV KNQMRAGPVR TYLPDATKLD NFHLALQTKV
IRLVRSGSQV TGVEVQTASG GSEIITIAPH GRVVLASGAL STPRLLWNSG IGGQAQIETA
KKSGVTVPPK AQWIDLPVGV GLKDHPIFSI VFNTNASFGL VDYDGVLNGT DSSDISLYRN
HSGVLTQGKH RMIFFTSEEI DGHTQYYQGS CAPTSEGVVT ITTYMTHGLT SSGVLGLDAS
GNTVIVKSPY LQTAADQKAA RTFIQKMVNS ITAPSTGFEL ETYTNVSAIL GSQTAGIHYT
STAKMGTDDG RKGGTSVVDT NTKVYGVDNL FIVDASIHPD LPTGNIQAAV MVVAEAAAAR
ILSC
//
