ID   ALDA_STAEQ              Reviewed;         497 AA.
AC   Q5HLA3;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, 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=SERP2084;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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; CP000029; AAW52930.1; -; Genomic_DNA.
DR   RefSeq; WP_002438147.1; NC_002976.3.
DR   AlphaFoldDB; Q5HLA3; -.
DR   SMR; Q5HLA3; -.
DR   STRING; 176279.SERP2084; -.
DR   EnsemblBacteria; AAW52930; AAW52930; SERP2084.
DR   GeneID; 50017843; -.
DR   KEGG; ser:SERP2084; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_0_9; -.
DR   OMA; HGIGYYP; -.
DR   OrthoDB; 744602at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome.
FT   CHAIN           1..497
FT                   /note="Putative aldehyde dehydrogenase AldA"
FT                   /id="PRO_0000056462"
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;  54247 MW;  DDCD2D2E0F2FDA7E CRC64;
     MTNINVRNYI DESYGLFINN EFQASDSGET LTVSNPANGE DLAKVARAGK KDVDKAVQAA
     HDAFDSWSKI SKEERADYLL EISRRIHEKT EHLATVESLQ NGKPYRETST IDVPQAANQF
     KYFASVLTTD EGSVNEIDQN TMSLVVNEPV GVVGAVVAWN FPILLASWKL GPALAAGNTV
     VIQPSSSTPL SLIELAKIFQ EVLPKGVVNV LTGKGSESGD AIFHHEGVDK LSFTGSTDVG
     YGVAQAGAER IVPTTLELGG KSANIIFDDA NLEQVIEGVQ LGILFNQGEV CSAGSRLLVQ
     SSIYDELLPK LKEAFENIKV GDPFDEDTKM SAQTGPEQLD KIESYIKIAE EDDKANILTG
     GHRITDNGLD KGYFFEPTII EINDNKHQLA QEEIFGPVVV VEKFDDEQEA IEIANDSEYG
     LAGGIFTTDI HRALNVAKAM RTGRIWINTY NQIPAGAPFG GYKKSGIGRE VYKDAIKNYQ
     QVKNIFIDTS NQTKGLY