ID B6QDV0_TALMQ Unreviewed; 348 AA.
AC B6QDV0;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=D-amino acid oxidase, putative {ECO:0000313|EMBL:EEA24860.1};
GN ORFNames=PMAA_088330 {ECO:0000313|EMBL:EEA24860.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA24860.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995901; EEA24860.1; -; Genomic_DNA.
DR RefSeq; XP_002148371.1; XM_002148335.1.
DR AlphaFoldDB; B6QDV0; -.
DR STRING; 441960.B6QDV0; -.
DR VEuPathDB; FungiDB:PMAA_088330; -.
DR HOGENOM; CLU_034311_1_0_1; -.
DR OrthoDB; 1385925at2759; -.
DR PhylomeDB; B6QDV0; -.
DR Proteomes; UP000001294; 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:UP000001294}.
FT DOMAIN 8..331
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT BINDING 190
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ SEQUENCE 348 AA; 38348 MW; E557F35957C95D68 CRC64;
MSSQTLNIIV LGAGVAGLTT AHSLLAKLPP TKINLTIVAK HLPGDINQTE YCSPQAGANW
RSFEKELNQY GEYDKIAFER FLQIARESPE SGVKRFPMRL VFGPEHDRSK AGLWFEKLVG
GIVDVPKDEL PEGAGWGIDL VTFMVNPAVY CNWLFASLIK RGVKVVRRSY GHVDSLMSDF
PNTTAIFNCT GLGARHLGGV EDTKVHPTKA KRMTIWTQPS IFPPGEFCHV FPRPLGGGII
IGGVRLENDW DDSFDESRVE RIKQRACQLA PELGKPEDLQ IVRNNVGLRP SREGGARVDI
EDRKGAWLVH NYGAGGAGYQ SSWGTAEHAV ALFTQKLDSD LGVRQAKL
//
