ID C5FJ01_ARTOC Unreviewed; 580 AA.
AC C5FJ01;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:EEQ29331.1};
GN ORFNames=MCYG_02150 {ECO:0000313|EMBL:EEQ29331.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ29331.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; DS995702; EEQ29331.1; -; Genomic_DNA.
DR RefSeq; XP_002849216.1; XM_002849170.1.
DR AlphaFoldDB; C5FJ01; -.
DR STRING; 554155.C5FJ01; -.
DR GeneID; 9229271; -.
DR VEuPathDB; FungiDB:MCYG_02150; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_3_1; -.
DR OMA; YGQPHFE; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000002035; 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:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 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.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000002035}.
FT DOMAIN 89..112
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
SQ SEQUENCE 580 AA; 63969 MW; 7B2A741928251F9E CRC64;
MSVQDGARYD FIVVGGGTAG NIVAARLADS PNTHILVVEA GIGDSIDNED IRTPALAMDL
RGSKYDWAYK TTMVKRDDYE RIEKPNTRGK ALGGSSSLNY FSWVPGSKGT FDMWEEYGGK
EWTWDPLVPY LRKSVTYHDD AGLFPPELKS IGAGGPIPIA HADLIPEMKP FRDLLVQGWK
STGEPVTENI FDGKMHGLTH SVNTIYKGRR SGSFLAVAGK PNITILPGVF SKCLIIDAAD
RSAKGVTVIT GSGQELSFYA TREVIVSQGV FETPKLLMLS GIGPAAELAR HNIPLIVDSR
HVGQHLLDHP GVPFALRLKD SFSLDNHILR KGPLQTQVLD AYSKGHAGPM GSPFLEMIGF
PRIDKYLEKS PEYRAAKAAN GGLDPFCPYG QPHFELDFIP LFGSAFQWHF PHPNRGSYMT
VMVDLVRPAS EGGEVTLNSA DPLEQANINL NYFNNDLDII AIREGIRFAY DVLKNGEGFK
DVVEDEYPWD MPLDDDEAMK RTVLDRSQTS FHPCGTARLS KDIQQGVVDP NLKVHGIKNL
RVIDASVIPV IPDCRIQNSV YMIAEKGADA IKRDHADFYH
//
