ID   DHA1_STAAB              Reviewed;         372 AA.
AC   Q2YY66;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Alanine dehydrogenase 1;
DE            EC=1.4.1.1;
GN   Name=ald1; OrderedLocusNames=SAB1304c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI80993.1; -; Genomic_DNA.
DR   RefSeq; WP_000959414.1; NC_007622.1.
DR   AlphaFoldDB; Q2YY66; -.
DR   SMR; Q2YY66; -.
DR   KEGG; sab:SAB1304c; -.
DR   HOGENOM; CLU_003376_3_0_9; -.
DR   OMA; GHQVILQ; -.
DR   UniPathway; UPA00527; UER00585.
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; 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   PROSITE; PS00837; ALADH_PNT_2; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..372
FT                   /note="Alanine dehydrogenase 1"
FT                   /id="PRO_0000287318"
FT   ACT_SITE        94
FT                   /evidence="ECO:0000255"
FT   BINDING         170..200
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   372 AA;  40145 MW;  91FD28D3AECA3130 CRC64;
     MLVAVVKELK QGEGRVACTP ENVRKLTAAG HKVIVEKNAG IGSGFSNDMY EKEGAKIVTH
     EQAWEADLVI KVKEPHESEY QYFKKNQIIW GFLHLASSKE IVEKMQGVGV IAISGETIIK
     NGKAELLAPM SAIAGQRSAI MGAYYSEAQH GGQGTLVTGV HENVDIPGST YVIFGGGVAA
     TNAANVALGL NAKVIIIELN DDRIKYLEDM YAEKDVTVVK STPENLAEQI KKADVFISTI
     LIPGAKPPKL VTREMVKSMK KGSVLIDIAI DQGGTIETIR PTTISDPVYE EEGVIHYGVP
     NQPGAVPRTS TMALAQGNID YILEICDKGL EQAIKDNEAL SAGVNIYQGQ ETNQGLATSH
     DLDYKEILNV IE