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Database: UniProt
Entry: Q08XF1_STIAD
LinkDB: Q08XF1_STIAD
Original site: Q08XF1_STIAD 
ID   Q08XF1_STIAD            Unreviewed;       314 AA.
AC   Q08XF1;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=D-amino acid oxidase {ECO:0000313|EMBL:ADO70684.1};
DE            EC=1.4.3.3 {ECO:0000313|EMBL:ADO70684.1};
DE   SubName: Full=D-aspartate oxidase {ECO:0000313|EMBL:EAU65167.1};
DE            EC=1.4.3.1 {ECO:0000313|EMBL:EAU65167.1};
GN   OrderedLocusNames=STAUR_2892 {ECO:0000313|EMBL:ADO70684.1};
GN   ORFNames=STIAU_4200 {ECO:0000313|EMBL:EAU65167.1};
OS   Stigmatella aurantiaca (strain DW4/3-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Archangiaceae; Stigmatella.
OX   NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU65167.1, ECO:0000313|Proteomes:UP000032702};
RN   [1] {ECO:0000313|EMBL:EAU65167.1, ECO:0000313|Proteomes:UP000032702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU65167.1,
RC   ECO:0000313|Proteomes:UP000032702};
RA   Nierman W.C.;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADO70684.1, ECO:0000313|Proteomes:UP000001351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO70684.1,
RC   ECO:0000313|Proteomes:UP000001351};
RX   PubMed=21037205; DOI=10.1093/molbev/msq292;
RA   Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA   Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA   Sogaard-Andersen L.;
RT   "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL   Mol. Biol. Evol. 28:1083-1097(2011).
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; CP002271; ADO70684.1; -; Genomic_DNA.
DR   EMBL; AAMD01000091; EAU65167.1; -; Genomic_DNA.
DR   RefSeq; WP_002615633.1; NZ_AAMD01000091.1.
DR   STRING; 378806.STAUR_2892; -.
DR   KEGG; sur:STAUR_2892; -.
DR   PATRIC; fig|378806.16.peg.4180; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_034311_0_0_7; -.
DR   OrthoDB; 246701at2; -.
DR   Proteomes; UP000001351; Chromosome.
DR   Proteomes; UP000032702; Unassembled WGS sequence.
DR   GO; GO:0008445; F:D-aspartate oxidase activity; IEA:UniProtKB-EC.
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:SF11; D-ASPARTATE OXIDASE; 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   Oxidoreductase {ECO:0000313|EMBL:EAU65167.1}.
FT   DOMAIN          2..307
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   BINDING         38..39
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         152
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         169
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         292..297
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ   SEQUENCE   314 AA;  34223 MW;  1C1D432FC26D6C5E CRC64;
     MDFIVLGGGV SGLSCGIRLL EAGHAVQLWA RELSPHTTSD VAAAMWYPYL ASPKERVLGW
     GQRTYEVLRS LAGRPETGVQ MVHGAELFTE TVQDPWWASS VPGFRRAAPG ELPPGYSEGY
     AFEVPVIEMP RYLPFLLERF HELGGRLRQR EVHSLEEAWS EAPTVVNCTG LGARTLVGDE
     ALFPIRGEVL RVSPSPTPRF LIDESEARGM TYLIPRATDC ILGGTAEGGV DSLTPSATEA
     EGILSRCRRL LPEGTPLNVV EHRVGLRPGR PSVRLEAEHL GERRVIHNYG HGGAGVTLSW
     GCAEEVRALA EAAR
//
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