ID   ALDA_STAAB              Reviewed;         495 AA.
AC   Q2YV11;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Putative aldehyde dehydrogenase AldA;
DE            EC=1.2.1.3;
GN   Name=aldA; OrderedLocusNames=SAB0108;
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   -!- 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; AJ938182; CAI79796.1; -; Genomic_DNA.
DR   RefSeq; WP_000290390.1; NC_007622.1.
DR   AlphaFoldDB; Q2YV11; -.
DR   SMR; Q2YV11; -.
DR   KEGG; sab:SAB0108; -.
DR   HOGENOM; CLU_005391_0_2_9; -.
DR   OMA; HGIGYYP; -.
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_0000290787"
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;  53688 MW;  BA85E006A728C036 CRC64;
     MAVNVRDYIA ENYGLFINGE FVKGSSDETI EVTNPATGET LSHITRAKDK DVDHAVEVAQ
     EAFESWSLTS KSERAQMLRD IGDKLMAQKD KIAMIETLNN GKPIRETTAI DIPFAARHFH
     YFASVIETEE GTVNDIDKDT MSIVRHEPIG VVGAVVAWNF PMLLAAWKIA PAIAAGNTIV
     IQPSSSTPLS LLEVAKIFQE VLPKGVVNIL TGKGSESGNA IFNHDGVDKL SFTGSTDVGY
     QVAEAAAKHL VPATLELGGK SANIILDDAN LDLAVEGIQL GILFNQGEVC SAGSRLLVHE
     KIYDQLVPRL QEAFSNIKVG DPQDEATQMG SQTGKDQLDK IQSYIDVAKE SDAQILAGGH
     RLTENGLDKG FFFEPTLIAV PDNHHKLAQE EIFGPVLTVI KVKDDQEAID IANDSKYGLA
     GGVFSQNITR ALNIAKAVRT GRIWINTYNQ VPEGAPFGGY KKSGIGRETY KGALSNYQQV
     KNIYIDTSNA LKGLY