ID N4UN19_FUSC1 Unreviewed; 362 AA.
AC N4UN19;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=D-amino-acid oxidase {ECO:0000313|EMBL:ENH72732.1};
GN ORFNames=FOC1_g10013399 {ECO:0000313|EMBL:ENH72732.1};
OS Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH72732.1, ECO:0000313|Proteomes:UP000016928};
RN [1] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
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; KB730093; ENH72732.1; -; Genomic_DNA.
DR AlphaFoldDB; N4UN19; -.
DR STRING; 1229664.N4UN19; -.
DR VEuPathDB; FungiDB:FOC1_g10013399; -.
DR HOGENOM; CLU_034311_1_0_1; -.
DR OMA; WERRTWI; -.
DR Proteomes; UP000016928; 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; IPR006181; D-amino_acid_oxidase_CS.
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.
DR PROSITE; PS00677; DAO; 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:UP000016928};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..362
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004121233"
FT DOMAIN 5..350
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT BINDING 193
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ SEQUENCE 362 AA; 39566 MW; ABDAC1BA77154CA5 CRC64;
MTNTVVVIGA GVIGLTSALL LAKEGNKVTV VGKHMPGDYD AEYASPWAGA NVIPLSPKDA
SRWERRTWIA LKKLVEETPE AGIHFQTTHV LRRNKDTESA KSGFSAHFYA DNPWFKEIFN
NFRNNHPSEV ATGYDSGFQY QGVCINTAIY LPWLLGQCLK YGVILKRAIL THINEAKYLS
HTGEKANIIV NATGLGSLKL GGVQDTTVAP ARGQIVLVRN ETPKNLPLFM CSSALDESGE
EIYAMQRAAG GGTVIGGTYQ IGNWDTQPDP NTANRIMQRI VDLCPDIAGG KGITGLSVIR
HGVGFRPYRK GGLRLEEEKL DDETWVIHNY GHSGWGYMGS YGCAEGVVEL VDKVTDKTRA
KL
//
