ID   E9DR06_METAQ            Unreviewed;       618 AA.
AC   E9DR06;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Glucose dehydrogenase, putative {ECO:0000313|EMBL:EFY93684.1};
GN   ORFNames=MAC_00175 {ECO:0000313|EMBL:EFY93684.1};
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN   [1] {ECO:0000313|EMBL:EFY93684.1, ECO:0000313|Proteomes:UP000002499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY93684.1,
RC   ECO:0000313|Proteomes:UP000002499};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
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}.
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DR   EMBL; GL698470; EFY93684.1; -; Genomic_DNA.
DR   RefSeq; XP_007806515.1; XM_007808324.1.
DR   AlphaFoldDB; E9DR06; -.
DR   STRING; 655827.E9DR06; -.
DR   GeneID; 19244486; -.
DR   KEGG; maw:MAC_00175; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_002865_7_2_1; -.
DR   InParanoid; E9DR06; -.
DR   OMA; NAMMYHH; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000002499; 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, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002499}.
FT   DOMAIN          38..346
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          455..607
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   ACT_SITE        552
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        595
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         262
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   618 AA;  67205 MW;  6ECBBCF8D66F21F2 CRC64;
     MGRRHANPLH NPLHYAALQP HSGPPVTAAA AERALPSYDY VIVGAGAAGC VLANKLSEDD
     NVSVLVLEAG GDNTKVLETK VPAMFSKLFH SKHDWDYYTV EQEALASRRL YWPRGRIVGG
     CSSMNAMIYH HCSASDFDEW VAVHGCHGWG YQDLAPHFRS LEKFTPNPAR PAIDAANRGD
     AGKWQTGYSW LSQIVEDGFL PACDDAGIPP NSDINTKDGS LGVTRLQTFI DAKGQRSSLA
     TAFLTPDVLR RPNLYVACGA QVTRVLFDRI NSTKPTAIGV EFQVSQGGER YQVHAKREVI
     LCAGAVNTPQ TLMLSGIGPE EELKKHSISR VFANDNVGKQ LKDHLVSNGV FCKSKKGSTL
     DYLADDIKAI PALVQWLLFG TGPLTSNIGE AAAFVRTFEH EFPASAGVLP KDYSSGDKAP
     DLEIIGAPIA FIHHGEERPL DDANVFSLVP IGLRPQSSGT ISLKSADVFD HPIIDPKYLT
     DEEGNDKKVL IAGLRLCLEI MRSPAFQKYL DPVPTNDDPS SYWWPYSCSD PDAVTDEQLG
     RYLVERAFTL YHPVGSARMG PSPSNSVVDA ECRVHGTHGL RVVDASIFPE QISGHPTAPI
     AAIAHRASEM IKQGHKTA
//