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   03-AUG-2022, entry version 115.
DE   RecName: Full=Alanine dehydrogenase;
DE            EC=1.4.1.1;
GN   Name=ald; OrderedLocusNames=SE_1384;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; 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., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   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: Catalyzes the reversible reductive amination of pyruvate to
CC       L-alanine. May play a role in cell wall synthesis as L-alanine is an
CC       important constituent of the peptidoglycan layer (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-alanine + NAD(+) = H(+) + NADH + NH4(+) + pyruvate;
CC         Xref=Rhea:RHEA:18405, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:57972; EC=1.4.1.1;
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via
CC       dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1.
CC   -!- SUBUNIT: Homohexamer. Trimer of dimer (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR   EMBL; AE015929; AAO04983.1; -; Genomic_DNA.
DR   RefSeq; NP_764939.1; NC_004461.1.
DR   RefSeq; WP_001830775.1; NZ_WBME01000042.1.
DR   AlphaFoldDB; Q8CNW8; -.
DR   SMR; Q8CNW8; -.
DR   STRING; 176280.SE_1384; -.
DR   EnsemblBacteria; AAO04983; AAO04983; SE_1384.
DR   GeneID; 50018502; -.
DR   KEGG; sep:SE_1384; -.
DR   PATRIC; fig|176280.10.peg.1352; -.
DR   eggNOG; COG0686; Bacteria.
DR   HOGENOM; CLU_003376_3_0_9; -.
DR   OMA; HPYYHLY; -.
DR   UniPathway; UPA00527; UER00585.
DR   Proteomes; UP000001411; Chromosome.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0000286; F:alanine dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006524; P:alanine catabolic process; ISS:UniProtKB.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05305; L-AlaDH; 1.
DR   InterPro; IPR008141; Ala_DH.
DR   InterPro; IPR008143; Ala_DH/PNT_CS2.
DR   InterPro; IPR008142; AlaDH/PNT_CS1.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42795; PTHR42795; 1.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   PIRSF; PIRSF000183; Alanine_dh; 1.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 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   NAD; Nucleotide-binding; Oxidoreductase.
FT   CHAIN           1..371
FT                   /note="Alanine dehydrogenase"
FT                   /id="PRO_0000199007"
FT   ACT_SITE        95
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        269
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         177..178
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         238..239
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         266..269
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         298..301
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
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