ID V2X9B7_MONRO Unreviewed; 500 AA.
AC V2X9B7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Glucooligosaccharide oxidase {ECO:0000313|EMBL:ESK89075.1};
GN ORFNames=Moror_5350 {ECO:0000313|EMBL:ESK89075.1};
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:ESK89075.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK89075.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK89075.1,
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 -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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:ESK89075.1}.
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DR EMBL; AWSO01000593; ESK89075.1; -; Genomic_DNA.
DR RefSeq; XP_007851643.1; XM_007853452.1.
DR AlphaFoldDB; V2X9B7; -.
DR STRING; 1381753.V2X9B7; -.
DR KEGG; mrr:Moror_5350; -.
DR HOGENOM; CLU_018354_10_1_1; -.
DR OrthoDB; 1094055at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..500
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004712057"
FT DOMAIN 56..228
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 500 AA; 54048 MW; 4719AB14D3DBFB40 CRC64;
MYPSHTILQV IIISYLAIVA HAANDLLAQL NNAGIKSYGP EDQEYASASK AFNLRYTYQP
AAIAFPTSAA AVSKAVAIGA SKNLNIVARS GGHSYIANGT GGKNGALVID LSKMKNIVFN
SSTKVATVET GNRLGDVALR LNRDGRGIPH GTCPYVGIGG HTSFGGFGHT SRMWGLTLDA
VSALNVVLAD GTAVRASRES QQDLFWAMRG AGPSFGITTS IEFNTHPVPT YAYVYHYIWQ
LPAEQAASAF KSFQTFAHTN IPKELSCYVY LSKGVSRGSV SFEFTGAWYG PKEQLDSVVL
GFVNTMPKPN SVSVVGNGTY IDAVVQAGGM GNLDTSKPDQ SQKFYAKSLT VPEGGMLSDD
AMKSFMGYLG DAGTRVSQDM HWFMLVELFG GSNSKINSVA ANDTSYARRD TLFTIQFYIS
MVNPQSAFPN GGFDFLDGAV NSIVSRMPFN WDYGAYTNYV DDRLGTNATK LYYSSHYQRL
KSVKKAVDPN NVFMFPTSIQ
//
