ID A0A0D2ETG9_9EURO Unreviewed; 637 AA.
AC A0A0D2ETG9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV05_02572 {ECO:0000313|EMBL:KIW58020.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW58020.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW58020.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW58020.1,
RC ECO:0000313|Proteomes:UP000054342};
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 Exophiala xenobiotica CBS118157.";
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}.
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DR EMBL; KN847318; KIW58020.1; -; Genomic_DNA.
DR RefSeq; XP_013318604.1; XM_013463150.1.
DR AlphaFoldDB; A0A0D2ETG9; -.
DR STRING; 348802.A0A0D2ETG9; -.
DR GeneID; 25324480; -.
DR HOGENOM; CLU_002865_6_1_1; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000054342; 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:SF115; DEHYDROGENASE XPTC-RELATED; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 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.
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:UP000054342};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..637
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002241442"
FT DOMAIN 48..355
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 481..627
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT ACT_SITE 572
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 615
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 276
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 637 AA; 68360 MW; C4F25A34D2BC10F4 CRC64;
MSPSFRGHFS STCAALLAFG SLAKGLPQDS STSSNDTFST LGSSAKQFDY VIVGGGLSGL
VVANRLSEDS RASVLVLEFG PFDRSNTTLW PGNAVLLNSA DMFNITSAPE PGMSGNAYSV
LAGSVPGGGS TVNGMELDRA SAADYDSWEQ LGNPGWGWSG LFPYFKKANI ISPAHWTSAD
RIFRYNYTWD TSAYGNGPLQ ACYPEFQYPD NYPFFTAFEE CGVPFIREHA LGNAVGVFWT
PASEDPKKKT RSSSLNAYYD PVSYRSNLKM LTEYQVTQVL FDRSLTAQGV EAIDRTTGKV
YQFKANKEVI LAAGGVHTPQ VLQLSGIGPK DVLKAAGVPV KLNFPAVGSN FQDHPTAYLN
WNLNATFPYP GILLANATYN AEAVSLYLNK LTGPYTKAQG SSAGFLSLNM ITNKASSMIS
SLLAQNAASY LPPIYSSSKA LLAGFAAQRT ILASQIKSGK VAVLEVPFQG SGSVPNAMQK
PLSRGTVYLN ASNPHGEPVV TYYAFSNPFD KTQLGIMVNF TRELMATDAL AHLAPVETVP
GPQYKTEDEI FNQLLVSKSP FGSSALSPTF AHPSCSCPMM PQQLGGVVSS DLLVYGTRKL
SIVDCSILPI IPAAHLQATM YAVAEKAADL IKKRNRN
//
