ID V2WVC3_MONRO Unreviewed; 593 AA.
AC V2WVC3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Aryl-alcohol oxidase {ECO:0000313|EMBL:ESK84506.1};
GN ORFNames=Moror_6152 {ECO:0000313|EMBL:ESK84506.1};
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:ESK84506.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK84506.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK84506.1,
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}.
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:ESK84506.1}.
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DR EMBL; AWSO01001289; ESK84506.1; -; Genomic_DNA.
DR RefSeq; XP_007856185.1; XM_007857994.1.
DR AlphaFoldDB; V2WVC3; -.
DR KEGG; mrr:Moror_6152; -.
DR HOGENOM; CLU_002865_6_3_1; -.
DR OrthoDB; 3215324at2759; -.
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; 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:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 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|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..593
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004713175"
FT DOMAIN 304..318
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 524
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 568
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 112
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 120..123
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 264
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 593 AA; 64514 MW; 69CB44C54FFB4A20 CRC64;
MLVGFLLLAL TAEVSAAIVE RWEDLPREEF DFIVVGGGTA GNVIANRLTE NPSWSVLVLE
AGGSNQNTPL DPVPQIPHLC GQLAGSALDW NYTASLGSGA QGRKTLLPRG FVLGGSSSIN
CMVYARGSKG DWDRYAQVTG DSGWSWDGIQ PYIRKNERFT PPFDNHDTTG EFDPRVHGFD
GINSVTLSGF RHDLDRWVIN ASKNVPEELK AFKFNLDTNS GFQLGVGYAQ STVRNGTRSS
SATSYLADKF IRRPNLHVLL HSHVTRILSK KEELLEFERV EFSQDGGKKL RTITAKKEIV
LSAGTIGSPQ ILLLSGIGDT AELSSIGVPT LKHLPSVGRN MTEQPVVQSS FQVNTTDTSD
TSAQNQTVAD EQMRLWLEQR KGPLADGPLS DVGWLRVPIE EGLVDPAGDS ETAHLGVLFL
NGGFPPATQG NFIIANAIVV SPASRGYMKL KSSDPFEYPE IDLNLLASPF DVFALREGIR
TIHRFLTSRL FDGFVISSVL PISPDASDEE FDAHIRNTAF IISHITGTAA MTANDAEWGV
VNPDLKVKGM KGVRVVDASI LPFIPSSHTQ APVYIVAEKG ADLIKAAWSW TQE
//
