ID DHA2_STAA8 Reviewed; 372 AA. AC Q2FXL7; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 22. DE RecName: Full=Alanine dehydrogenase 2; DE EC=1.4.1.1; GN Name=ald2; OrderedLocusNames=SAOUHSC_01818; OS Staphylococcus aureus (strain NCTC 8325). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=93061; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., RA Iandolo J.J.; RT "The Staphylococcus aureus NCTC8325 genome."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May play a role in cell wall synthesis as L-alanine is CC an important constituent of the peptidoglycan layer (By CC similarity). CC -!- CATALYTIC ACTIVITY: L-alanine + H(2)O + NAD(+) = pyruvate + NH(3) CC + NADH. CC -!- PATHWAY: Amino-acid degradation; L-alanine degradation via CC dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step CC 1/1. CC -!- SIMILARITY: Belongs to the AlaDH/PNT 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; CP000253; ABD30886.1; -; Genomic_DNA. DR RefSeq; YP_500323.1; -. DR GeneID; 3919288; -. DR GenomeReviews; CP000253_GR; SAOUHSC_01818. DR KEGG; sao:SAOUHSC_01818; -. DR HOGENOM; Q2FXL7; -. DR OMA; Q2FXL7; VAHGHEV. DR BioCyc; SAUR93061:SAOUHSC_01818-MON; -. DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:EC. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR007698; Ala_DH/PNT_C. DR InterPro; IPR008142; Ala_DH/PNT_CS1. DR InterPro; IPR008143; Ala_DH/PNT_CS2. DR InterPro; IPR007886; Ala_DH/PNT_N. DR InterPro; IPR008141; Ala_DH_PNT. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF01262; AlaDh_PNT_C; 1. DR Pfam; PF05222; AlaDh_PNT_N; 1. DR ProDom; PD000139; FAD_pyr_redox; 1. DR TIGRFAMs; TIGR00518; alaDH; 1. DR PROSITE; PS00836; ALADH_PNT_1; 1. DR PROSITE; PS00837; ALADH_PNT_2; 1. PE 3: Inferred from homology; KW Complete proteome; NAD; Oxidoreductase. FT CHAIN 1 372 Alanine dehydrogenase 2. FT /FTId=PRO_0000287321. FT NP_BIND 169 199 NAD (By similarity). FT ACT_SITE 95 95 Potential. SQ SEQUENCE 372 AA; 40105 MW; 32BA3DA4734EC9FB CRC64; MKIGIPREIK NNENRVGLSP SGVHALVESG HTVLVETNAG SGSFFEDVDY KEAGAEIVAE QAKVWDVDMV IKVKEPLESE YPYFKEGLVL FTYLHLANEE KLTQALIDRK VISIAYETVQ LPDRSLPLLS PMSEVAGRMS AQVGAEFLQK LNGGMGILLG GVPGVPKGKV TIIGGGQAGT NAAKIALGLG ADVTILDVNP KRLQQLDDLF GGRVHTIMSN PLNIELYVKQ SDLVIGAVLI PGAKAPRLVT EDMIKQMKNG SVIIDIAIDQ GGIFETTDKI TTHDDPTYIK HGVVHYAVAN MPGAVPRTST LALNNATLPY ALMLANKGYR EAFKSNQPLS LGLNTYKGHV TNKGVAEAFE MEYKSVEEAL QL //