ID R1EKY4_BOTPV Unreviewed; 344 AA.
AC R1EKY4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative d-amino acid oxidase protein {ECO:0000313|EMBL:EOD48217.1};
GN ORFNames=UCRNP2_5007 {ECO:0000313|EMBL:EOD48217.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD48217.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000189-1};
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family.
CC {ECO:0000256|ARBA:ARBA00006730}.
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DR EMBL; KB916238; EOD48217.1; -; Genomic_DNA.
DR RefSeq; XP_007584285.1; XM_007584223.1.
DR AlphaFoldDB; R1EKY4; -.
DR STRING; 1287680.R1EKY4; -.
DR KEGG; npa:UCRNP2_5007; -.
DR eggNOG; KOG3923; Eukaryota.
DR HOGENOM; CLU_034311_1_0_1; -.
DR OMA; GANWSPM; -.
DR OrthoDB; 1385925at2759; -.
DR Proteomes; UP000013521; Unassembled WGS sequence.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0046416; P:D-amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR023209; DAO.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR PANTHER; PTHR11530; D-AMINO ACID OXIDASE; 1.
DR PANTHER; PTHR11530:SF16; D-AMINO ACID OXIDASE (AFU_ORTHOLOGUE AFUA_5G11290); 1.
DR Pfam; PF01266; DAO; 1.
DR PIRSF; PIRSF000189; D-aa_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000189-1};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000189-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013521}.
FT DOMAIN 10..331
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT BINDING 160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 180
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ SEQUENCE 344 AA; 37269 MW; 78F1CBE94FC98650 CRC64;
MAETRIVVLG YSVTVVAKHM PGDYDIEYAS PWAGANYLPV GAPGSNLAEY EKNTWPELQR
LAADVPEAHI HFQPTVLHNR SKDVGSTVGN WFSELLKTDP WWKDVVPDFR VLSKDQLGPG
IDSATAFTSV CINTALYLPW LIGQCRKYGT QFRRGIVSHV ADAAALHHSG QRADVVVNCT
GLSALKLGGV LDTKMYPGRG QIVLVRNSPG VMTSTSGTDD GEDEAVYIME RADGGGTILG
GCLQKGSWES QPDPNLANRI MKRAVELRPE LTGGKGPEAL SVIRHGVGLR PMREGGPRVE
KERIEGVWTV HNYGHGGYGY QASYGSAYAA VKLVDEVVKA KAKL
//
