ID A0A136IZ99_9PEZI Unreviewed; 610 AA.
AC A0A136IZ99;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=GMC oxidoreductase-domain-containing protein {ECO:0000313|EMBL:KXJ90310.1};
GN ORFNames=Micbo1qcDRAFT_189331 {ECO:0000313|EMBL:KXJ90310.1};
OS Microdochium bolleyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ90310.1, 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}.
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DR EMBL; KQ964253; KXJ90310.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136IZ99; -.
DR STRING; 196109.A0A136IZ99; -.
DR InParanoid; A0A136IZ99; -.
DR OrthoDB; 2392848at2759; -.
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; 3.50.50.60; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 285..299
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 236
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 540..541
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 610 AA; 67324 MW; BDD5ED1F13ECD7DD CRC64;
MPLYQKDLPD GLDEFDVIIA GGGSAGCVVA GRVAAADPSL SVLLIESGRN NYMNPAVMIP
AMYASHLLPN SESTIFYSTN KSKHLAGREV IVPAGNILGG GSSTNFMMYT RAQRSDYDSW
QTPGWSTDEL LPYLKKLETY HGPGDASVHG SDGPIVISDG TYRSKKTEDD WLQAAAKVGY
PEIRDLQDLS SNNGFQRWLR YVNPQGIRSD AAHGYVHPLL NDGKHPNFYV LVEAKVVRVL
FDKGDEKRAC GVEYEPNVKF HPLTGEVPHV KNVVKARKQV VISCGSCSTP TVLERSGLGD
AEILKAAGVP LVEHLPGVGA DYQDHNLILY AYSTNLDAMD TLDGVLQQRI PPEELAGHPH
LGWNSCDIAS KVRPTDEDVD ALGPEFRAAW DRDFRDRPDR PIMLIAVLNG FYDERPVPPG
QYITLAMYTA YPYSRGHVHI TGRETTDRVD FELGFLNDEH DIDLKKHVWA YKKGREIMRR
TKMHAGEVDL VQPKFAPGSK VAAVLNRDKE HDDVSRNLEY SADDDAAIEQ YIRENVGTTW
HSLGTARMCP RDRLGVVDER CSVYGVKGLK IADLSIVPLN IGANTNNTAL LIGEKVADFV
IQDLGLKDSA
//
