ID A0A0M9VR88_9BASI Unreviewed; 600 AA.
AC A0A0M9VR88;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Gmc oxidoreductase {ECO:0000313|EMBL:KOS16335.1};
GN ORFNames=Malapachy_2962 {ECO:0000313|EMBL:KOS16335.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS16335.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS16335.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS16335.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOS16335.1}.
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DR EMBL; LGAV01000001; KOS16335.1; -; Genomic_DNA.
DR RefSeq; XP_017993967.1; XM_018137445.1.
DR AlphaFoldDB; A0A0M9VR88; -.
DR STRING; 77020.A0A0M9VR88; -.
DR GeneID; 28729321; -.
DR VEuPathDB; FungiDB:Malapachy_2962; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000037751; 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 GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 4.10.450.10; Glucose Oxidase, domain 2; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027424; Glucose_Oxidase_domain_2.
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:SF218; GMC_OXRDTASE_N 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; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000037751}.
FT DOMAIN 303..317
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 538
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 581
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 108
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 261
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 600 AA; 65291 MW; 1F4E69786F6A6F39 CRC64;
MAFVNVTSFD RRSLTANGWD LDGKSFDYVI VGGGTAGLVL ANRLSADGSN SVAVIEAGNS
GYDDNDKFTT PDATLYDSSV NTQYDWQYKT TSQKNMNGRR ASWPRGKVLG GSSAINGLYY
VRHSRVEQEV WADLAGGNAN DHWNWDNMLS HMKKSEHNKS PLKSVRDQAH IQYNPDSHGH
NGPVDTTWPA VMYRPIGAFM EAANSVASPY TSDAYGGENH GTYMANSAIN KDNWHRSFSR
NAYLDPVLDR GNLHVLTGHQ VTEIMFDQSN RDNVEATGVH YSSGKGQDVH TVHANKEVIL
CGGAINSPAL LQLSGIGDAG HLQSLGIDVV VDLPGVGENL QDHLSAGMSF SAKHSQDRGP
TSVTGNARKD SYVNSAVSYV SMDSLFNNKD SIISQIQDRA NSIVNNHNVA DSVKKGQRKA
YKAIANRIYT SNVSPVEILG NVMFGSISIQ AALQHPLSRG SVRINSKNAF DYPTINPHYL
AEDLDLKILR EGFKLARLIS QQSPLKELIG QENVPGDKVQ SNSEWEDWIR RSAGTEYHPS
STCAMMPRGD GGVVGTDLKV HGTRNLRVVD ASVTPLAMST HLMAVVYGIA EIAAEIILGN
//
