ID A0A136IMN9_9PEZI Unreviewed; 556 AA.
AC A0A136IMN9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:KXJ86216.1};
GN ORFNames=Micbo1qcDRAFT_168831 {ECO:0000313|EMBL:KXJ86216.1};
OS Microdochium bolleyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ86216.1, ECO:0000313|Proteomes:UP000070501};
RN [1] {ECO:0000313|Proteomes:UP000070501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG DOE Joint Genome Institute;
RA David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA Barry K., Grigoriev I.V.;
RT "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT beachgrass.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ964270; KXJ86216.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136IMN9; -.
DR STRING; 196109.A0A136IMN9; -.
DR InParanoid; A0A136IMN9; -.
DR OrthoDB; 3714148at2759; -.
DR Proteomes; UP000070501; 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; 3.30.410.40; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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:SF152; OXIDASE (CODA), PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04090)-RELATED; 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:UP000070501}.
FT DOMAIN 265..279
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 94
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 229
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 556 AA; 61529 MW; 67F8BBCE2A455314 CRC64;
MASVTQLDAS AAGQFDYVVV GGGTAGCVIA SRLAEYLPHK KTLLIEAGPS DFMDDRVLNL
REWLALLGGE LDYDYGTTEQ PMGNSYIRHS RAKVLGGCSS HNTLISFRPF EYDFKLWQSL
GAKGWDFDTF MRLMDKLRNT VQPVHGRHRN KLCKDWVKAC SSALDIPVLH DFNHHITEQG
ALKQGVGFFS ISYNPDDGRR SSASVAYIHP IFRGTEKRPN LTVLTNAWVS KINVQGDDVK
GVSVTLQDGA KLDITPKTET IICAGAVDTP RLMLLSGLGP KEQLSQLGIP VVKNIPGVGE
NLQDHPESII MWELNQQVPP NQTTMDSDAG IFLRREPPNA AKNHRHKLQN PQGIPDGDIA
DVMMHCYQIP FTLNTTRLGY PIVPDGYAFC MTPNIPRPRS RGRLYLTSAD PSVKPALDFR
YFTDEEGYDA ATLVYGMRAA RKVAQQSPFK DWIKAEIAPG PKIQSDEELS EYARKAAHTV
YHPAGTTRMG DVANDELAVV SEKLQVRGLK RLRIADAGVF PTIPTINPML TVLGVAERCA
EFIVEEANAE QEKARL
//
