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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//