ID S3D5M3_GLAL2 Unreviewed; 607 AA.
AC S3D5M3;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=FAD/NAD(P)-binding protein {ECO:0000313|EMBL:EPE33752.1};
GN ORFNames=GLAREA_06765 {ECO:0000313|EMBL:EPE33752.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE33752.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE33752.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
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}.
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DR EMBL; KE145357; EPE33752.1; -; Genomic_DNA.
DR RefSeq; XP_008078904.1; XM_008080713.1.
DR AlphaFoldDB; S3D5M3; -.
DR GeneID; 19465818; -.
DR KEGG; glz:GLAREA_06765; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_5_1_1; -.
DR OMA; IMRRTKM; -.
DR OrthoDB; 2392848at2759; -.
DR Proteomes; UP000016922; 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:SF78; 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|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000016922}.
FT DOMAIN 283..297
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 140..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 234
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 539..540
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 607 AA; 66479 MW; DD4205CA8CA7DEBE CRC64;
MSTYNDSVGE VDIVFAGGGT AACVAAGRLA KANPDLKILL VEGGKNNFND PTVTNPAVYL
SHLAPDSKTA LFYKSKQSKH LNNREAIVPM GGILGGGSSI NFMMYTRAQG ADFDAWNTPG
WSAKEMLPHL NRLETYHPTG KDIDQSRHGH DGPINVGDGG YRGKSENQFM DTVKSMGYKD
ITDLQDLDAI GGFSRWHRYV GPDGKRQDAA HRYVHPLLQS GDYPNLHILT ETKVIRVLFD
ESSPPKAIGI EYKPNADHQP ELALSKPVHK TIKASKLVVV SAGALGSPQI LERSGVGNPE
ILKKLDIPVV SELPGVGEEY QDHHLLLYPY KTNLDEGETL DGILSGRKDF AKALEAKDPM
LGWNGIDICA KLRPTDAEIN SLGANFQEDW DRDFKPFPTR PLMLCGVVNA FLADPSLVEP
GQYMTMGTYT AYPYSRGSIH ITSKEDVING YDFDAGFLNH PSDIKKQLWA YKMSREITRR
LPYYKGELEL GHPKFKDGSA AAISESASAV DINAPNIEYS KEDDEAIMDW VRDNLNTTWH
SLGTCAMRER EKGGVLDGDL NVYGTQGLKV ADLSMVPENV GANTNNTALV VGEKAATIIG
RELGIEV
//
