ID   DHA2_STAAW              Reviewed;         372 AA.
AC   Q8NW54;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Alanine dehydrogenase 2;
DE            EC=1.4.1.1;
GN   Name=ald2; OrderedLocusNames=MW1652;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: May play a role in cell wall synthesis as L-alanine is an
CC       important constituent of the peptidoglycan layer. {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   -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR   EMBL; BA000033; BAB95517.1; -; Genomic_DNA.
DR   RefSeq; WP_000689998.1; NC_003923.1.
DR   AlphaFoldDB; Q8NW54; -.
DR   SMR; Q8NW54; -.
DR   EnsemblBacteria; BAB95517; BAB95517; BAB95517.
DR   KEGG; sam:MW1652; -.
DR   HOGENOM; CLU_003376_3_0_9; -.
DR   OMA; HPYYHLY; -.
DR   UniPathway; UPA00527; UER00585.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-EC.
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; Oxidoreductase.
FT   CHAIN           1..372
FT                   /note="Alanine dehydrogenase 2"
FT                   /id="PRO_0000199006"
FT   ACT_SITE        95
FT                   /evidence="ECO:0000255"
FT   BINDING         169..199
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   372 AA;  40105 MW;  32BA3DA4734EC9FB CRC64;
     MKIGIPREIK NNENRVGLSP SGVHALVESG HTVLVETNAG SGSFFEDVDY KEAGAEIVAE
     QAKVWDVDMV IKVKEPLESE YPYFKEGLVL FTYLHLANEE KLTQALIDRK VISIAYETVQ
     LPDRSLPLLS PMSEVAGRMS AQVGAEFLQK LNGGMGILLG GVPGVPKGKV TIIGGGQAGT
     NAAKIALGLG ADVTILDVNP KRLQQLDDLF GGRVHTIMSN PLNIELYVKQ SDLVIGAVLI
     PGAKAPRLVT EDMIKQMKNG SVIIDIAIDQ GGIFETTDKI TTHDDPTYIK HGVVHYAVAN
     MPGAVPRTST LALNNATLPY ALMLANKGYR EAFKSNQPLS LGLNTYKGHV TNKGVAEAFE
     MEYKSVEEAL QL