ID   DADA_PSE14              Reviewed;         433 AA.
AC   Q48PZ1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=D-amino acid dehydrogenase small subunit;
DE            EC=1.4.99.1;
GN   Name=dadA; OrderedLocusNames=PSPPH_0223;
OS   Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Crabtree J., Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L.,
RA   Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O.,
RA   Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D.,
RA   Mansfield J.W., Collmer A., Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv.
RT   phaseolicola 1448A reveals divergence among pathovars in genes
RT   involved in virulence and transposition.";
RL   J. Bacteriol. 187:6488-6498(2005).
CC   -!- FUNCTION: Oxidative deamination of D-amino acids (By similarity).
CC   -!- CATALYTIC ACTIVITY: A D-amino acid + H(2)O + acceptor = a 2-oxo
CC       acid + NH(3) + reduced acceptor.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- PATHWAY: Amino-acid degradation; D-alanine degradation; NH(3) and
CC       pyruvate from D-alanine: step 1/1.
CC   -!- SUBUNIT: Heterodimer of a small and a large subunit (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the dadA oxidoreductase family.
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DR   EMBL; CP000058; AAZ34759.1; -; Genomic_DNA.
DR   RefSeq; YP_272528.1; -.
DR   GeneID; 3557319; -.
DR   GenomeReviews; CP000058_GR; PSPPH_0223.
DR   KEGG; psp:PSPPH_0223; -.
DR   NMPDR; fig|264730.3.peg.712; -.
DR   HOGENOM; Q48PZ1; -.
DR   OMA; Q48PZ1; NCQLSRY.
DR   GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0006524; P:alanine catabolic process; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01202; -; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   Pfam; PF01266; DAO; 1.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   3: Inferred from homology;
KW   Complete proteome; FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN         1    433       D-amino acid dehydrogenase small subunit.
FT                                /FTId=PRO_1000066104.
FT   NP_BIND       3     17       FAD (Potential).
SQ   SEQUENCE   433 AA;  47154 MW;  A229B02752C6F5C1 CRC64;
     MRVLVLGSGV IGTTSAYYLA RAGFQVTVVD RQPAAAMETS FANAGQVSPG YASPWAAPGV
     PLKAIKWLLQ RHAPLAIKAT ADIDQYLWMA QMLRNCTASR YTVNKERMVR LSEYSRDCLD
     ELRLETGIAY EGRSLGTTQL FRTQAQLDNA AKDIAVLEQS GVPYELLDRD GIARVEPALA
     GVTGILSGAL RLPNDQTGDC QLFTTRLAEM AVELGVEFRY GQNIERLDHA GDRINGVWID
     GKLETADRYV LALGSYSPQL LKPLGIKAPV YPLKGYSLTV PITNPAMAPT STILDETYKV
     AITRFDNRIR VGGMAEIAGF DLSLNPRRRE TLEMIVGDLY PQGGDLTQAS FWTGLRPTTP
     DGTPIVGATP FRNLFLNTGH GTLGWTMACG SGRLLADLIA RKTPRISAEG LDISRYGNTQ
     ENAQHVNPAP AHQ
//