ID   DHA_STAHJ               Reviewed;         373 AA.
AC   Q4L750;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Alanine dehydrogenase;
DE            EC=1.4.1.1;
GN   Name=ald; OrderedLocusNames=SH1216;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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.
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DR   EMBL; AP006716; BAE04525.1; -; Genomic_DNA.
DR   RefSeq; YP_253131.1; -.
DR   GeneID; 3482407; -.
DR   GenomeReviews; AP006716_GR; SH1216.
DR   KEGG; sha:SH1216; -.
DR   NMPDR; fig|279808.3.peg.2455; -.
DR   HOGENOM; Q4L750; -.
DR   OMA; Q4L750; VAHGHEV.
DR   BioCyc; SHAE279808:SH1216-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    373       Alanine dehydrogenase.
FT                                /FTId=PRO_0000287324.
FT   NP_BIND     169    199       NAD (By similarity).
FT   ACT_SITE     95     95       Potential.
SQ   SEQUENCE   373 AA;  39966 MW;  66E91EE689108294 CRC64;
     MKIGIPKEIK NNENRVGLSP SGVHALVEQG HTVLVEKDAG LGSFFEDKDY KDAGADIVSE
     QSSVWDVEMV IKVKEPLEEE YKYFKEGLIL FTYLHLANEE KLTQALVDNK VVGIAYETVQ
     LPDRSLPLLT PMSEVAGRMS AQVGSQFLQK FNGGMGILLG GVPGVPKGKV SIIGGGQAGT
     NAAKIALGLG ANVTILDVNP KRLAELDDLF DGRVNTIMSN PLNIENAVKE SDLVIGAVLI
     PGAKAPSLVT EDMIKQMKDG SVIVDIAIDQ GGIFETTDKI TTHDDPTYVK HGVVHYAVAN
     MPGAVPRTST IALNNATLPY AQLLASKGYR EAFKANHALS LGLNTYKGHV THKGVAEAFG
     LEYTSVEDAL KED
//