ID V2WB91_MONRO Unreviewed; 650 AA.
AC V2WB91;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Alcohol oxidase {ECO:0000313|EMBL:ESK84078.1};
GN ORFNames=Moror_11464 {ECO:0000313|EMBL:ESK84078.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK84078.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK84078.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK84078.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK84078.1}.
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; AWSO01001373; ESK84078.1; -; Genomic_DNA.
DR RefSeq; XP_007856616.1; XM_007858425.1.
DR AlphaFoldDB; V2WB91; -.
DR STRING; 1381753.V2WB91; -.
DR KEGG; mrr:Moror_11464; -.
DR HOGENOM; CLU_002865_5_1_1; -.
DR OrthoDB; 2418107at2759; -.
DR Proteomes; UP000017559; 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 GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 2.
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; 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|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 90..113
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 272..286
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 629..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 229
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 559..560
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 650 AA; 72072 MW; 3C55853A3F3D6E80 CRC64;
MGHPNEVDVI VAGGGPAGCV VAGRLAYADP NLKVMLIEGG ANNRDDPWVY RPGIYVKNMQ
RDGINDKATF YVDTMKSSYL RGRQSIVPCA NILGGGSSIN FQMYTRASAS DWDDFKTPGW
TAKELLPLMK RLENYQKPVN NDTHGYDGPI AISNGGSITA LAQDFLRAAD AIGVPFSDDI
QDLDTAHASE IWAKYINRHT GRRSDAATAY VHSVMDIQSN LYLRTNARVS RVIFEGNKAV
GVAYVPSRNR AHKGQLLETI VKARKYVVLS GGTLGTPQIL ERSGVGDSKL LQKLDIKVVS
DLPGVGEEYQ DHYTTLSIYR VSNESFTTDD FLRGDKEAQK ELFTEWETSP EKARLSSNAI
DAGFKIRPTE EELKEMGPDF NALWDRYFKD KPDKPVMFGS IVSGAYADHA LLPPGKYMTM
FQYLEYPASR GKIHINSPSP YVEPFFDSGF MNHKADFAPI RWSYKKTREV ARRMDAFRGE
LTSHHPHFHP ASPAACRDID IKTAKQIYPD GLTVGIHMGT WHRPSEPYDA DKVHDDIKYT
EEDDKAIDDW IADHVETTWH SLGTCAMKPR EEGGVVDGRL NVFGTQNLKV CDLSICPDNL
GTNTYSSALL VGEKGADLLA EDLGLKIKTP HAPVPHTPVP SGKPATQLVR
//
