ID K2SYL0_MACPH Unreviewed; 629 AA.
AC K2SYL0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Major facilitator superfamily {ECO:0000313|EMBL:EKG21685.1};
GN ORFNames=MPH_00995 {ECO:0000313|EMBL:EKG21685.1};
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:EKG21685.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG21685.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG21685.1,
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|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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:EKG21685.1}.
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DR EMBL; AHHD01000041; EKG21685.1; -; Genomic_DNA.
DR AlphaFoldDB; K2SYL0; -.
DR STRING; 1126212.K2SYL0; -.
DR VEuPathDB; FungiDB:MPH_00995; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_2_1; -.
DR InParanoid; K2SYL0; -.
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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-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; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT DOMAIN 106..129
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 298..312
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 263
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 629 AA; 67407 MW; 861CEDA5BD766BE8 CRC64;
MASPENSTTN GTAAALPALA TSASDFLAHA YDYIIIGGGT AGLVLAARLT EDPSIRVGVL
EAGANRLNDA LVDTPALFPQ MLGNPSYEWN MKTAGNHNRT HHLPRGKLLG GSSGINYMLY
VRGSARDYDD WATLTSDPSW SAAALAPYVR KHQALQAIPD TIANRVAMRT QPAYHGTSGP
IHTSFNDTRL ELEDAWLLAA EEACGVTAKV ADAWSGDHYG FYNGMGSVYG QGRLKGRRCY
AARGYFEENA GRENLKVLCD ASVARILLEE GSAVGVEFIH AGETYSAKAE KEVLLCGGAI
HSPQILELSG IGDPEVLKKA GVEVKVELPS VGENLQDHVI GGCAYQLAPG EVSMDSLFHP
DAFAEAQKAF VENGSGPLTC VLSGQGFVSY KQLAPKEEFE KTIASIRKTQ EISNEFQKRQ
LELVIQHLED DRSANLQYVM CPASPVFEEE AVADQSKMWP PGDPNSPGFA SACCLQYPVS
RGSVHITSAD VTHPPSIDPA YLRHPADVAV LGTGVKFADR MVKVPVLAAR VGARTFPAPE
IDMDDQKAAE EAVRDWIIGE YHVAGSCAMG DTVDSRLRVK GVSRLRVVDA SVFPNHVSGN
IQSSVYTLAE RAADIIKEDN GHTAAGKLA
//