ID W9CDP2_SCLBF Unreviewed; 547 AA.
AC W9CDP2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN ORFNames=SBOR_5666 {ECO:0000313|EMBL:ESZ93963.1};
OS Sclerotinia borealis (strain F-4128).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=1432307 {ECO:0000313|EMBL:ESZ93963.1, ECO:0000313|Proteomes:UP000019487};
RN [1] {ECO:0000313|EMBL:ESZ93963.1, ECO:0000313|Proteomes:UP000019487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-4157 {ECO:0000313|Proteomes:UP000019487};
RX PubMed=24459262; DOI=10.1128/genomeA.01175-13;
RA Mardanov A.V., Beletsky A.V., Kadnikov V.V., Ignatov A.N., Ravin N.V.;
RT "Draft genome sequence of Sclerotinia borealis, a psychrophilic plant
RT pathogenic fungus.";
RL Genome Announc. 2:E0117513-E0117513(2014).
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, 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:ESZ93963.1}.
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DR EMBL; AYSA01000277; ESZ93963.1; -; Genomic_DNA.
DR AlphaFoldDB; W9CDP2; -.
DR STRING; 1432307.W9CDP2; -.
DR HOGENOM; CLU_002865_6_3_1; -.
DR OrthoDB; 3714148at2759; -.
DR Proteomes; UP000019487; 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:SF123; GMC OXIDOREDUCTASE (AFU_ORTHOLOGUE AFUA_2G01770)-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:UP000019487}.
FT DOMAIN 85..108
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 258..272
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 490
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 528
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 222
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 547 AA; 58716 MW; 55382D6E43A2C246 CRC64;
MAETSNYHYI IIGGGIAGSV VASRLHEKHP SLSILLIEAG PDVSDNPLVT DSANGPFLVG
SELDWGYSTV PQRHLNNRAL PNNAGKALGG GSAINAGGWI RGDANDYNAW GKLVNDPRWS
YAGFLPYFHR TEQYHKAGLD TQHGYEGPLY TQSVSSTDRN YPLRENIRKA WESIGINYNA
DANSGSPQGL GELVENRKDG QRQVASTAYP LTGVQVMTST LVARVLMDTQ GLIPRATAVE
LADGRKIVAT KEIIISAGAF RTPQILLLSG IGTKGELAIH GIQQIVDAPY VGKNLHDHMS
VAQWWKLKNP EAGYALGSPL FNNPNFKKGT PMDWVVTYTV PHEGLKAALA KDEGIVDDMH
PLLSPARSHV ECFTVYVGVN KSDPIIPMDG SHVTTVVLGG LPTSRGSVKL ASTDPTAAPV
IDPNYFSTEA DRYVLRTGLR KIMEAMLSTA EGQALIETET VAAGEKSLDW KAEDAELDER
IKARGKTVYH PAGTAAMGKV VDSSLCVYGV QGLRVVDASV LPLPIAAHYQ ACIYALAEQA
AEIIGAS
//