ID   DHA_STAES               Reviewed;         371 AA.
AC   Q8CNW8;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 41.
DE   RecName: Full=Alanine dehydrogenase;
DE            EC=1.4.1.1;
GN   Name=ald; OrderedLocusNames=SE_1384;
OS   Staphylococcus epidermidis (strain ATCC 12228).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22832016; PubMed=12950922;
RX   DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J.,
RA   Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z.,
RA   Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04983.1; -; Genomic_DNA.
DR   RefSeq; NP_764939.1; -.
DR   HSSP; O52942; 1SAY.
DR   GeneID; 1055853; -.
DR   GenomeReviews; AE015929_GR; SE_1384.
DR   KEGG; sep:SE1384; -.
DR   HOGENOM; Q8CNW8; -.
DR   OMA; Q8CNW8; VAHGHEV.
DR   BioCyc; SEPI176280:SE_1384-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    371       Alanine dehydrogenase.
FT                                /FTId=PRO_0000199007.
FT   NP_BIND     169    199       NAD (By similarity).
FT   ACT_SITE     95     95       Potential.
SQ   SEQUENCE   371 AA;  40195 MW;  78541923F8E7CD6F CRC64;
     MKIGIPKEIK NNENRVGLSP SGVHALVDQG HEVLVETNAG LGSYFEDGDY QEAGAKIVDE
     QSKAWDVDMV IKVKEPLESE YKFFKEELIL FTYLHLANEQ KLTQALVDNK VISIAYETVQ
     LPDGSLPLLT PMSEVAGRMS TQVGAEFLQR FNGGMGILLG GIPGVPKGKV TIIGGGQAGT
     NAAKIALGLG AEVTILDVNP KRLEELEDLF DGRVRTIMSN PLNIEMYVKE SDLVIGAVLI
     PGAKAPNLVT EDMIKEMKDG SVIVDIAIDQ GGIFETTDKI TTHDNPTYTK HGVVHYAVAN
     MPGAVPRTST IGLNNATLPY AQLLANKGYR EAFKVNHPLS LGLNTFNGHV TNKNVADTFN
     FEYTSIEDAL K
//