ID   DHA2_STAAM              Reviewed;         372 AA.
AC   Q931P7;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Alanine dehydrogenase 2;
DE            EC=1.4.1.1;
GN   Name=ald2; OrderedLocusNames=SAV1709;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000017; BAB57871.1; -; Genomic_DNA.
DR   RefSeq; WP_000690009.1; NC_002758.2.
DR   AlphaFoldDB; Q931P7; -.
DR   SMR; Q931P7; -.
DR   World-2DPAGE; 0002:Q931P7; -.
DR   PaxDb; Q931P7; -.
DR   EnsemblBacteria; BAB57871; BAB57871; SAV1709.
DR   KEGG; sav:SAV1709; -.
DR   HOGENOM; CLU_003376_3_0_9; -.
DR   OMA; HPYYHLY; -.
DR   PhylomeDB; Q931P7; -.
DR   BioCyc; SAUR158878:SAV_RS09170-MON; -.
DR   UniPathway; UPA00527; UER00585.
DR   Proteomes; UP000002481; 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_0000199002"
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;  40083 MW;  3B5FF183743F0F9E CRC64;
     MKIGIPREIK NNENRVGLSP SGVHALVESG HTVLVETNAG SGSFFEDVDY KEAGAEIVAE
     QAKVWDVDMV IKVKEPLESE YTYFKEGLVL FTYLHLANEE KLTQALIDRK VISIAYETVQ
     LPDRSSPLLS 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