ID A0A179UEJ1_BLAGS Unreviewed; 565 AA.
AC A0A179UEJ1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:OAT06163.1};
GN ORFNames=BDBG_02434 {ECO:0000313|EMBL:OAT06163.1};
OS Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT06163.1, ECO:0000313|Proteomes:UP000002038};
RN [1] {ECO:0000313|Proteomes:UP000002038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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; GG657450; OAT06163.1; -; Genomic_DNA.
DR RefSeq; XP_002627763.1; XM_002627717.1.
DR AlphaFoldDB; A0A179UEJ1; -.
DR GeneID; 8506428; -.
DR KEGG; bgh:BDBG_02434; -.
DR VEuPathDB; FungiDB:BDBG_02434; -.
DR OrthoDB; 3073733at2759; -.
DR Proteomes; UP000002038; 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:SF134; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN; 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:UP000002038}.
FT DOMAIN 83..106
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 262..276
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 498
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 542
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 93..96
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 231
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 497..498
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 565 AA; 62256 MW; 0A5FC5801CC6D721 CRC64;
MASVFDFIVV GSGPAGSAVA SGLAGAPANP KVLLLEAGED IEDRNLRVDG QRWLTFQNKN
MNWGYKTVPQ EYCNNRELDY SRGRGVGGSS TINFGVYSVG ARDDYNEWAR IVGDDSFNWE
HIQSRFKKLE TFHSEIPAGI DSKYASPNAA DHGTSGPLHV GFAAEWERDI VPTLDIFEQA
GFPLNPDHNS GNPIGMSVLI NSAHKGLRST AKDLLLRPSA VNLTIIANSP VQHVILEGKK
AVGVVANGTR YLASKEVILS AGALDTPKIL MHSGIGPKEQ LEKFNIPVVL DALAVGQGLR
DHYFVPLINT VAGTNNDRRA FYGDKKVMDD ALEQWKRDGT GPWSKFACEC GVGWFKIDGL
TQTKEFQDLP TTEKEYLQKE TVPHYEILTH FPIHWFVPDF PDSALDYTCL LVFLYNAQAR
GEVTLQSSDP NEPLRMDPKF LSHPFDRRAA IDSLRDALRV AEHPAYIKDK LAELAAPKSD
SDEDLLEYWK QNISSSWHMK CTVKMGKAGD ADAVVDCNYR LMGIDGLRVA DMSVIPVLVS
GHIQAAAYVT GATCAEKLIK EYNLA
//
