ID   ALDA_STAES              Reviewed;         497 AA.
AC   Q8CN24;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Putative aldehyde dehydrogenase AldA;
DE            EC=1.2.1.3;
GN   Name=aldA; OrderedLocusNames=SE_2071;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05713.1; -; Genomic_DNA.
DR   RefSeq; NP_765626.1; NC_004461.1.
DR   RefSeq; WP_002438147.1; NZ_WBME01000003.1.
DR   AlphaFoldDB; Q8CN24; -.
DR   SMR; Q8CN24; -.
DR   GeneID; 50017843; -.
DR   KEGG; sep:SE_2071; -.
DR   PATRIC; fig|176280.10.peg.2023; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_0_9; -.
DR   OrthoDB; 9762913at2; -.
DR   Proteomes; UP000001411; 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   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   PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR   PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 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_0000056461"
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
//