ID A0A443HX18_BYSSP Unreviewed; 593 AA.
AC A0A443HX18;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=Glucose-methanol-choline (Gmc) oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=C8Q69DRAFT_465022 {ECO:0000313|EMBL:RWQ96382.1};
OS Byssochlamys spectabilis (Paecilomyces variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=264951 {ECO:0000313|EMBL:RWQ96382.1, ECO:0000313|Proteomes:UP000283841};
RN [1] {ECO:0000313|EMBL:RWQ96382.1, ECO:0000313|Proteomes:UP000283841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101075 {ECO:0000313|EMBL:RWQ96382.1,
RC ECO:0000313|Proteomes:UP000283841};
RX PubMed=30619145; DOI=10.3389/fmicb.2018.03058;
RA Urquhart A.S., Mondo S.J., Makela M.R., Hane J.K., Wiebenga A., He G.,
RA Mihaltcheva S., Pangilinan J., Lipzen A., Barry K., de Vries R.P.,
RA Grigoriev I.V., Idnurm A.;
RT "Genomic and genetic insights into a cosmopolitan fungus, Paecilomyces
RT variotii (Eurotiales).";
RL Front. Microbiol. 9:3058-3058(2018).
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}.
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:RWQ96382.1}.
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DR EMBL; RCNU01000004; RWQ96382.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443HX18; -.
DR STRING; 264951.A0A443HX18; -.
DR OrthoDB; 3382025at2759; -.
DR Proteomes; UP000283841; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000283841}.
FT DOMAIN 10..312
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 430..568
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 593 AA; 65839 MW; 8B481FE33D3FAF7F CRC64;
MATVSNGSSY DFIVVGGGTA GNAVAGRLAE NPEVRVLVVE AGIPNPDQFE EITTPSKAFN
LRGSKHDWAY KSTMVKRDDY ERIEKPNTRG KMLGGSSGAN YFTWIPGSKP TFDDWEEFGG
PEWNWDHCVD YLRKCATYHD DEKLYPADLK KIGTGGPINI AHADLVPEMA PFRDALTQAW
VSKGQPLTED IYSGEMKGLT HCVDTIYGGQ RQGSYLYLKN KPNVTILYGV HSKRLIIDPQ
TRVCQGVTVI SEAHNTEISV YATREVILSQ GVFETPKLLL LSGVGPAAEL AKHNIPQILE
SPHVGQHLLD HPIVPFVLQV KDGYGLDDHI LRPGPKNEVA IKAYAKDKTG AISSGLLELV
GFPRIDERLE KYPEYRQAKA ANGGLDPFGP AGQPHFELDF VGMFSTAFQW HYPVPESGSY
MTVIVDLLRP LSEGEVTLNS SNPLVQPNIN LNFFANDLDI LAMREGIRWT YDVLTTGAGF
KDIVVKEYPF KMPLHSDEDM KRAVLDRSQT GYHPCGTARL SKNIQQGVVD SKLRVHGIRN
LRIADASIMP VIPDCRIQNS VYMIGEKAAD IIKADYKDIY EGKNIPYFLQ SRL
//
