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   03-AUG-2022, entry version 121.
DE   RecName: Full=Alanine dehydrogenase;
DE            EC=1.4.1.1;
GN   Name=ald; OrderedLocusNames=SH1216;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
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., Lee J.C.,
RA   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: 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; AP006716; BAE04525.1; -; Genomic_DNA.
DR   RefSeq; WP_011275515.1; NC_007168.1.
DR   AlphaFoldDB; Q4L750; -.
DR   SMR; Q4L750; -.
DR   STRING; 279808.SH1216; -.
DR   EnsemblBacteria; BAE04525; BAE04525; SH1216.
DR   GeneID; 58062585; -.
DR   KEGG; sha:SH1216; -.
DR   eggNOG; COG0686; Bacteria.
DR   HOGENOM; CLU_003376_3_0_9; -.
DR   OMA; HPYYHLY; -.
DR   OrthoDB; 673280at2; -.
DR   UniPathway; UPA00527; UER00585.
DR   Proteomes; UP000000543; 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..373
FT                   /note="Alanine dehydrogenase"
FT                   /id="PRO_0000287324"
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   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