ID   ALDA_STAAR              Reviewed;         495 AA.
AC   Q6GKD8;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Putative aldehyde dehydrogenase AldA;
DE            EC=1.2.1.3;
GN   Name=aldA; OrderedLocusNames=SAR0169;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.3;
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; BX571856; CAG39196.1; -; Genomic_DNA.
DR   RefSeq; WP_000290401.1; NC_002952.2.
DR   AlphaFoldDB; Q6GKD8; -.
DR   SMR; Q6GKD8; -.
DR   KEGG; sar:SAR0169; -.
DR   HOGENOM; CLU_005391_0_2_9; -.
DR   OMA; HGIGYYP; -.
DR   OrthoDB; 744602at2; -.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..495
FT                   /note="Putative aldehyde dehydrogenase AldA"
FT                   /id="PRO_0000056458"
FT   ACT_SITE        256
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000250"
FT   BINDING         212..218
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   495 AA;  53646 MW;  2F53D449813860B1 CRC64;
     MAVNVRDYIA ENYGLFINGE FVKGSSDETI EVTNPATGET LSHITRAKDK DVDHAVKVAQ
     EAFESWSLTS KSERAQMLRD IGDKLMAQKD KIAMIETLNN GKPIRETTAI DIPFAARHFH
     YFASVIETEE GTVNDIDKDT MSIVRHEPIG VVGAVVAWNF PMLLAAWKIA PAIAAGNTIV
     IQPSSSTPLS LLEVAKIFQE VLPNGVVNIL TGKGSESGNA IFNHDGVDKL SFTGSTDVGY
     QVAEAAAKHL VPATLELGGK SANIILDDAN LDLAVEGIQL GILFNQGEVC SAGSRLLVHE
     KIYDQLVPRL QEAFSNIKVG DPQDEATQMG SQTGKDQLDK IQSYIDAAKE SDAQILAGGH
     RLTENGLDKG FFFEPTLIAV PDNHHKLAQE EIFGPVLTVI KVKDDQEAID IANDSEYGLA
     GGVFSQNITR ALNIAKAVRT GRIWINTYNQ VPEGAPFGGY KKSGIGRETY KGALSNYQQV
     KNIYIDTSNA LKGLY