ID   ALDA_STAHJ              Reviewed;         497 AA.
AC   Q4L919;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Putative aldehyde dehydrogenase AldA;
DE            EC=1.2.1.3;
GN   Name=aldA; OrderedLocusNames=SH0547;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE03856.1; -; Genomic_DNA.
DR   RefSeq; WP_011274872.1; NC_007168.1.
DR   AlphaFoldDB; Q4L919; -.
DR   SMR; Q4L919; -.
DR   STRING; 279808.SH0547; -.
DR   PRIDE; Q4L919; -.
DR   EnsemblBacteria; BAE03856; BAE03856; SH0547.
DR   GeneID; 58063262; -.
DR   KEGG; sha:SH0547; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_1_9; -.
DR   OMA; HGIGYYP; -.
DR   OrthoDB; 744602at2; -.
DR   Proteomes; UP000000543; 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..497
FT                   /note="Putative aldehyde dehydrogenase AldA"
FT                   /id="PRO_0000056463"
FT   ACT_SITE        257
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        291
FT                   /evidence="ECO:0000250"
FT   BINDING         213..219
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   497 AA;  54119 MW;  6BBC0B29CBED6B8E CRC64;
     MAKVNVRDFI EEQYGLFING EFQASESGDT LTVTNPANGE DLAKVAKASK SDVDKAVQAA
     QDAFDSWSKT SKEERADYLL EISRRIHEKV EHFATIESLQ NGKPYRETST IDVPLTANQF
     KYFASVLTTD EGSVNEIDEN TMSLVVNEPV GVVGAVVAWN FPILLASWKL APALAAGNTI
     VIQPSSSTPL SLIELAKIFQ EVLPKGVVNV LTGKGSESGD AIFNHEGVNK LSFTGSTDVG
     YGVAKAGAER IVPTTLELGG KSANIIFDDA NLDQVVEGAQ LGILFNQGEV CSAGSRLLVQ
     SSIYDKVMPK LKEAFENIKV GDPFDEDVKM SAQTGPEQLE KIESYVKIAE EDSNANILTG
     GHRLTDNGRD KGYFFEPTII EIKDNSHQLA QEEIFGPVVV VEKFEDEAEA IKIANDSEYG
     LAGGIFTTNI NRALNVAKAM RTGRIWINTY NQFPAGAPFG GYKKSGIGRE IYKDAIKNYQ
     QVKNIFIDTS NQTKGLY