ID   DHA1_STAAS              Reviewed;         372 AA.
AC   Q6G9C3;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Alanine dehydrogenase 1;
DE            EC=1.4.1.1;
GN   Name=ald1; OrderedLocusNames=SAS1382;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571857; CAG43158.1; -; Genomic_DNA.
DR   RefSeq; WP_000959432.1; NC_002953.3.
DR   AlphaFoldDB; Q6G9C3; -.
DR   SMR; Q6G9C3; -.
DR   KEGG; sas:SAS1382; -.
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; 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 1"
FT                   /id="PRO_0000198999"
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;  40234 MW;  7FF131E5E18D4035 CRC64;
     MLVAVVKELK QGEGRVACTP ENVRKLTDAG HKVIVEKNAG IGSGFSNDMY EKEGAKIVTH
     EQAWEADLVI KVKEPHESEY QYFKKNQIIW GFLHLASSKE IVEKMQEVGV TAISGETIIK
     NGKAELLAPM SAIAGQRSAI MGAYYSEAQH GGQGTLVTGV HENVDIPGST YVIFGGGVAA
     TNAANVALGL NAKVIIIELN DDRIKYLQDM YAEKDVTVVK STPENLAEQI KKADVFISTI
     LIPGAKPPKL VTREMVKSMK KGSVLIDIAI DQGGTIETIR PTTISDPVYE EEGVIHYGVP
     NQPGAVPRTS TMALAQGNID YILEICDKGL EQAIKDNEAL STGVNIYQGQ VTNQGLASSH
     DLDYKEILNV IE