ID   DHA_STAS1               Reviewed;         371 AA.
AC   Q49YD9;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-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=SSP1057;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 /
OS   DSM 20229).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K.,
RA   Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S.,
RA   Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE18202.1; -; Genomic_DNA.
DR   RefSeq; YP_301147.1; -.
DR   GeneID; 3615425; -.
DR   GenomeReviews; AP008934_GR; SSP1057.
DR   KEGG; ssp:SSP1057; -.
DR   NMPDR; fig|342451.4.peg.1117; -.
DR   HOGENOM; Q49YD9; -.
DR   OMA; Q49YD9; VAHGHEV.
DR   BioCyc; SSAP342451:SSP1057-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; FALSE_NEG.
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_0000287325.
FT   NP_BIND     169    199       NAD (By similarity).
FT   ACT_SITE     95     95       Potential.
SQ   SEQUENCE   371 AA;  39903 MW;  9BC859AAC3B4AF64 CRC64;
     MIIGIPKEIK NNENRVSLSP SGVHALVEQG HTVIVEKSAG LGSYFEDVDY TEAGASIVNE
     QAEVWNVDMV MKVKEPLEEE FQYFKEGLIL FTYLHLANEE KLTRALLENK VVGIAYETVQ
     LPDRTLPLLT PMSEVAGRMS AQIGAEFLQK YKGGMGILLG GVPGVSKGRV SIIGGGQAGT
     NAAKIALGLG ADVTILDVNP KRLQELEDLF DGRVHTIMSN PLNIEQCVKD SDLVIGAVLI
     PGAKAPNLVT EDMVKEMRDG AVIVDIAIDQ GGIFETTDRI STHDDPTYKK HGVVHYAVAN
     MPGAVPRTST IALNNATLPY AQQLASKGYL KALQDNHALS LGLNTINGEL TNKGVAEALN
     LSYTDIESAL K
//