ID DADA_PSEU5 Reviewed; 432 AA. AC A4VGT8; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 16-JUN-2009, entry version 17. DE RecName: Full=D-amino acid dehydrogenase small subunit; DE EC=1.4.99.1; GN Name=dadA; OrderedLocusNames=PST_0483; OS Pseudomonas stutzeri (strain A1501). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=379731; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Yan Y., Yang J., Dou Y., Ping S., Chen M., Yao Z., Li H., Lu W., RA Zhang W., Peng J., Liu W., He S., Geng L., Zhang X., Yang F., Li D., RA Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.; RT "Complete genome sequence of the metabolically versatile and root- RT associated nitrogen-fixing bacterium Pseudomonas stutzeri A1501."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000304; ABP78189.1; -; Genomic_DNA. DR RefSeq; YP_001171031.1; -. DR GeneID; 5094833; -. DR GenomeReviews; CP000304_GR; PST_0483. DR KEGG; psa:PST_0483; -. DR OMA; A4VGT8; MFQKHAP. DR GO; GO:0005488; F:binding; IEA:InterPro. 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 InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. 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 1 432 D-amino acid dehydrogenase small subunit. FT /FTId=PRO_1000066109. FT NP_BIND 3 17 FAD (Potential). SQ SEQUENCE 432 AA; 47281 MW; B90145203F385F0B CRC64; MRVLVLGSGV VGTASAYYLA RAGFEVVVVD RQPAVAMETS FANAGQVSPG YASPWAAPGV PLKAMKWLLQ RHAPLAIKLT GDIDQYLWMA QMLRNCTAAR YAVNKERMVR LSEYSRDCLD ELRAETGIAY EGRQLGTTQL FRTQAQLDAA AKDIAVLERS GVPYELLDRA SIARVEPALA KVSHKLSGAL RLPNDQTGDC QLFTTRLAEM ARALGVEFRF EQNIQRLEHA GDRIAGVWID GKLETADRYV LALGSYSPQM LKPLGIRAPV YPLKGYSLTV PISDPAMAPQ STVLDETYKV AITRFDQRIR VGGMAEIAGH DLSLDPRRRE TLEMVVGDLY PQGGDPSDAV FWTGLRPATP DGTPIIGATP YRNLFLNTGH GTLGWTMACG SGRVLADLLA SKRPQISTEG LDIFRYGKHK ENHKHAHPAA AH //