ID A0A443I4A1_BYSSP Unreviewed; 589 AA.
AC A0A443I4A1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Glucose dehydrogenase {ECO:0000313|EMBL:RWQ98910.1};
GN ORFNames=C8Q69DRAFT_511431 {ECO:0000313|EMBL:RWQ98910.1};
OS Byssochlamys spectabilis (Paecilomyces variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=264951 {ECO:0000313|EMBL:RWQ98910.1, ECO:0000313|Proteomes:UP000283841};
RN [1] {ECO:0000313|EMBL:RWQ98910.1, ECO:0000313|Proteomes:UP000283841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101075 {ECO:0000313|EMBL:RWQ98910.1,
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 ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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:RWQ98910.1}.
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DR EMBL; RCNU01000001; RWQ98910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443I4A1; -.
DR STRING; 264951.A0A443I4A1; -.
DR OrthoDB; 858083at2759; -.
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; 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:SF201; 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|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000283841};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..589
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019555041"
FT DOMAIN 102..125
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 297..311
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 526
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 569
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 34..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 108
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 112..115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 589 AA; 63987 MW; 7E972C909EE1CFDB CRC64;
MRSFVGLGLL SLAAALPARP SDSTYDYIVV GGGTSGLVVA NRLSEQKDIN VLVIEAGGSV
YNNPNVTDTS GYGKAFGTEI DWAYSTVDQE YGGGHTTTMR AGKAIGGTST INGMVYLRAQ
TSQVDAWEAI GNKGWNWSTL FPYYKKSEHF QVPSVYSSLR GAGIEYTPSY HGYTGPLKVG
WDSEQLNDGL AQTLNTTYQN LAAPVPYNKD PNGGYMVGYA LYPKTVDSEK NIREDAARAY
YWPYQNRTNL HILPYTNANK LIWKEGEEAT ADGVEVTFAN GTIGVLKASR EVILAAGALK
SPVLLELSGV GNPAILSKYG IETKINLPTV GENLQDQINN GLKYQSKTNY SRQTDYVSYP
SAPELFGNST TAVANDVLRK LPAYAAQVAK ANGNVTKASD LERFFKVQWD LIFKSHIPVA
EVLVEPSGLI YDMEYWASVP FSRGSVHIQS ADPSATARID PKYFMLDFDL HAQAQVARFI
RELFKTEPFA PMAGAETSPG YSSVPSNATD SEWAPYLKAN YRSNYHPIST AAMLPKEAGG
VVDESLKVYG TSNVRVVDAS VLPMQVSGHL SSTVYAVAER AADIIKGNI
//
