ID G7UW10_PSEUP Unreviewed; 398 AA.
AC G7UW10;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=D-amino acid oxidase {ECO:0000313|EMBL:AER57668.1};
GN OrderedLocusNames=DSC_15120 {ECO:0000313|EMBL:AER57668.1};
OS Pseudoxanthomonas spadix (strain BD-a59).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER57668.1, ECO:0000313|Proteomes:UP000005870};
RN [1] {ECO:0000313|EMBL:AER57668.1, ECO:0000313|Proteomes:UP000005870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD-a59 {ECO:0000313|EMBL:AER57668.1,
RC ECO:0000313|Proteomes:UP000005870};
RX PubMed=22207748; DOI=10.1128/JB.06436-11;
RA Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT spadix BD-a59.";
RL J. Bacteriol. 194:544-544(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family.
CC {ECO:0000256|ARBA:ARBA00006730}.
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DR EMBL; CP003093; AER57668.1; -; Genomic_DNA.
DR RefSeq; WP_014161841.1; NC_016147.2.
DR AlphaFoldDB; G7UW10; -.
DR STRING; 1045855.DSC_15120; -.
DR KEGG; psd:DSC_15120; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_034311_6_0_6; -.
DR OrthoDB; 246701at2; -.
DR Proteomes; UP000005870; Chromosome.
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; 2.
DR InterPro; IPR023209; DAO.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR11530; D-AMINO ACID OXIDASE; 1.
DR PANTHER; PTHR11530:SF11; D-ASPARTATE OXIDASE; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005870};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..398
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003504464"
FT DOMAIN 119..397
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 398 AA; 42812 MW; 5CE89256DDED6750 CRC64;
MQRRHFLRQA GALAALAGSG RLLAQTPPPS PHAAAAPLGQ LPFAAAKPLA PIKARADRVV
AVTVCTRPFR AQGPRIEAER IGRRTVVHQY GHGGSGWSLS WGSAQQAVRL ALAGGDSEIA
VIGCGAIGIT TARVAQEAGL KVRIYAKETL PASRSFLATG VWSPDSRICT TEHASPAFKA
LWAQMATASF QQYQRMLGLA GAPVEWRDSY VLSEVPLDQP AGGGGEDDEP DYPSLESELL
HGLRPHGLKL DPGEHPFPVP YAARYPGLIF NISAYARMLM EDFLHAGGSF QAREFESPRQ
FADLREKTLI NCTGYGARAL LGDESVIPVR GQTARLIPQP EVDYGLYWRG HNLNVVPRRD
GILVQAQMPG DFNNADTTID RASTDAAVAQ LARLFPAA
//
