ID K2S169_MACPH Unreviewed; 631 AA.
AC K2S169;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 22-FEB-2023, entry version 29.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:EKG20738.1};
GN ORFNames=MPH_01905 {ECO:0000313|EMBL:EKG20738.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG20738.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG20738.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG20738.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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 -!- 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:EKG20738.1}.
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DR EMBL; AHHD01000079; EKG20738.1; -; Genomic_DNA.
DR AlphaFoldDB; K2S169; -.
DR STRING; 1126212.K2S169; -.
DR VEuPathDB; FungiDB:MPH_01905; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_1_1; -.
DR InParanoid; K2S169; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000007129; 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:SF115; DEHYDROGENASE XPTC-RELATED; 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.
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:UP000007129};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..631
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003864462"
FT DOMAIN 303..317
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 558
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 601
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 46..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 265
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 631 AA; 68083 MW; 420D4BF163A40A55 CRC64;
MCLWDFAFIL TLVIGVQAKL GRLAQVVGRD VSLQDSYDFV VAGGGTSGLT VADRLTEDPN
ITVLVIEYGP LDKHEDSVLV PGLLDLDTTP YWFNLTSAPQ EGLNNKTFRV PAAAVVGGGT
VINGMFFDRG TAADYDLWEQ LGNPGWGWDG LLPYFRKSEN FTPPAESFAA EWNISWDLSA
HGREGPVQSS FPVFQFGSTK NFLRACLSLG LAKPSDQASG NKAGVSWVPS SLDYTNQTRS
YSRVAHYDRV ISSRPNYHLL TMHTVSKVLF SDDNAATGVE YFSRETGEVS TVTASKEVII
AAGAVHTPQI LQLSGIGPKA LLDSLDIPVV KDLSGVGHNL QDHPAIYTQW NFSNLPLPSV
ESLDVNQTQI DEALFLYRTN RTGAFTQVDR GGNQAAFVPL SKLLSSSPST YASILALAAS
TSPTDIYPPS TPPSVLAGYI QQLARIIPQL SSPTEPVYEF TSGGSSTLPV VFLKSLSRGT
VAITSTNAST QPRVDYRTIR APSDIAVVRA ALRWARTLMR TDAMLEMEPH ESLPGASAQD
DAALDDVIRA NANPGYQHVT ASCAMMPEEW GGVVDSRLRV YGVERVRIVD ASIMPVIPGT
HTSSTVYAVA EKAADIVKKD HGITIGMLKG H
//
