ID A0A0U1M6P2_TALIS Unreviewed; 545 AA.
AC A0A0U1M6P2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:CRG91197.1};
GN ORFNames=PISL3812_08245 {ECO:0000313|EMBL:CRG91197.1};
OS Talaromyces islandicus (Penicillium islandicum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Islandici.
OX NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG91197.1, ECO:0000313|Proteomes:UP000054383};
RN [1] {ECO:0000313|EMBL:CRG91197.1, ECO:0000313|Proteomes:UP000054383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG91197.1};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; CVMT01000009; CRG91197.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U1M6P2; -.
DR STRING; 28573.A0A0U1M6P2; -.
DR OMA; SDHMIFF; -.
DR OrthoDB; 3714148at2759; -.
DR Proteomes; UP000054383; Unassembled WGS sequence.
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 Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 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; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF123; GMC OXIDOREDUCTASE (AFU_ORTHOLOGUE AFUA_2G01770)-RELATED; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000054383}.
FT DOMAIN 84..107
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 256..270
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 487
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 525
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 220
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 545 AA; 59647 MW; AEAB4ED072857667 CRC64;
MTSDSYDYVI VGGGTAGSVV ATRLKEGHPS LSILIIEAGP DVSGRADVLD GTQWARLLRG
DLDWGDLTVP QTHLHGRVLP NFSGKSLGGS SAINAGGWTR GEKENYDIWA QLVKDSRWSY
EGLLPYFRKT ETYWDPNGDS TVHGFDGPIK MEAAVNRQYP LREKVKDAWA AVGALYKRDM
NDGNPIGLGE LIENRVNGVR HIASSAYGLK DVEVLTETLV KRVIVTEKDG SKVATAVELV
DGRILAARRE IIVSAGTYRS PQILMLSGLG PQKELQQHGI EAILDLPDVG RHLQDHFSVN
QWWKLKEPEK GLSVGSPVFN NPAHFKGLPL DFIATQSVPK EGLLKALSTD KEANPELHPV
ALQRGHIEVY ILYLARNQED PVIIPDGTHI TTSTMCMLPT SRGSIQLKDA NPETMPLIDP
NYLATETDRY VLREGLRKTH QVLRETEAGQ QFVISEAVGE GGQQVSADST DEELNDLIRR
RLGTMFHPAG SVSMGKVVDS ELRVKGVDRL RVVDASVIPV PIAGHIQNCV YALAEQAANM
IIGSP
//