ID   A2RZB8_BURM9            Unreviewed;       415 AA.
AC   A2RZB8;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 2.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Putative D-amino acid dehydrogenase, small subunit {ECO:0000313|EMBL:ABM99655.2};
GN   OrderedLocusNames=BMA10229_1235 {ECO:0000313|EMBL:ABM99655.2};
OS   Burkholderia mallei (strain NCTC 10229).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=412022 {ECO:0000313|EMBL:ABM99655.2, ECO:0000313|Proteomes:UP000002283};
RN   [1] {ECO:0000313|EMBL:ABM99655.2, ECO:0000313|Proteomes:UP000002283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10229 {ECO:0000313|EMBL:ABM99655.2,
RC   ECO:0000313|Proteomes:UP000002283};
RA   DeShazer D., Woods D.E., Nierman W.C.;
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- PATHWAY: Amino-acid degradation; D-alanine degradation; NH(3) and
CC       pyruvate from D-alanine: step 1/1. {ECO:0000256|ARBA:ARBA00004960}.
CC   -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00009410}.
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; CP000545; ABM99655.2; -; Genomic_DNA.
DR   RefSeq; WP_004196258.1; NC_008835.1.
DR   AlphaFoldDB; A2RZB8; -.
DR   GeneID; 56596898; -.
DR   KEGG; bml:BMA10229_1235; -.
DR   HOGENOM; CLU_007884_9_2_4; -.
DR   Proteomes; UP000002283; Chromosome II.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR13847:SF280; D-AMINO ACID DEHYDROGENASE; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          2..398
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   415 AA;  44745 MW;  10A28891B4C6BCAC CRC64;
     MRICVLGAGV VGLTSAYCLA REGHDVTVLE ARPDAVLDAS FANGGQLSYS YVAPLADPAV
     LGKLPAWLAR RDSALRFVPR LDVDQWLWCA AFLAACRTAR ARRTAAEMLE LGALSRIALH
     ALVERETLDF DYARNGKLVV YRDRREFDRA RRAMDHLIAA GARQQALDTA ACVALEPALA
     PASGLLAGGI HTPSEEVGDC RRFGIELARV LRERLRVAIH YETPVDTLRT EGATIVAART
     PRGEIAADAF VLSAGNGSAP MLRRLGMRLP IYPLTGYSLT LPARHDATPR VSVTDLHRKI
     VYAPLGARLR IAGMVEIAGL RSSGAARRLA LLAQQAQEIF PHAGDYAHGE TWCGHRPATP
     DGKPLIGATP FRNLWLNTGH GALGFTLACG SARVLADLIA GRPPALDTRA YALHR
//