ID A0A0D2C3H2_9EURO Unreviewed; 516 AA.
AC A0A0D2C3H2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 22-FEB-2023, entry version 29.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=PV07_08925 {ECO:0000313|EMBL:KIW25773.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW25773.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW25773.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW25773.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN847044; KIW25773.1; -; Genomic_DNA.
DR RefSeq; XP_016245989.1; XM_016396133.1.
DR AlphaFoldDB; A0A0D2C3H2; -.
DR GeneID; 27348119; -.
DR VEuPathDB; FungiDB:PV07_08925; -.
DR OrthoDB; 3714148at2759; -.
DR Proteomes; UP000054466; 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; 3.30.410.40; -; 1.
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; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF152; OXIDASE (CODA), PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04090)-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; 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 Reference proteome {ECO:0000313|Proteomes:UP000054466}.
FT DOMAIN 213..227
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 177
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 516 AA; 57014 MW; 8D6C0B4DBF696941 CRC64;
MDDRVLDLKQ WLSLLGGELD YDYGTTEQPM GNSHIRHSRA KVLGGCSSHN TLISFRPFEY
DCKIWESMGA KGWTFPMFMR VLNKLRNTVQ PVHARHRNQL CKDWVQSCST AMNIPIVHDF
NAHIAGTGAL RECVGFFSVS YNPDDGRRSS ASVAYIHPIL RGEEHRPNLK ILTNAWVSKI
NVRDDTVTGV NITLQSGQKL TLTARTETIL CAGAVDTPRL MLLSGLGPAQ ELSSLSIPVV
KNIPGVGENL LDHPETIIIW ELNRPVPPNQ TTMDSDAGIF LRREAPDAAG TKATPTNPAA
IPDGNIADVM MHCYQIPFCL NTTRLGYDTP VDAFCMTPNI PRPRSRGKLY LTSSDPSVKP
ALDFRYFTDP EGYDAATFVF GLRAARKIAQ QSPFKEWIKR EVAPGPQIQS DEALSEYARK
VAHTVYHPAG TTKMGDVRQD DMAVVDENLK VRGLKGLRIA DAGVFPAMTT INPMLTVLGV
GERCAELVAI EAGWRLTEVE MSGRGWANDT GLRARL
//
