ID   ALD1_STAES              Reviewed;         475 AA.
AC   Q8CNI5;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Putative aldehyde dehydrogenase SE_1720;
DE            EC=1.2.1.3;
GN   OrderedLocusNames=SE_1720;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; 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; AAO05319.1; -; Genomic_DNA.
DR   RefSeq; NP_765275.1; NC_004461.1.
DR   RefSeq; WP_001832742.1; NZ_WBME01000021.1.
DR   AlphaFoldDB; Q8CNI5; -.
DR   SMR; Q8CNI5; -.
DR   STRING; 176280.SE_1720; -.
DR   EnsemblBacteria; AAO05319; AAO05319; SE_1720.
DR   GeneID; 50018180; -.
DR   KEGG; sep:SE_1720; -.
DR   PATRIC; fig|176280.10.peg.1680; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_2_9; -.
DR   OMA; RRMDTGQ; -.
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   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..475
FT                   /note="Putative aldehyde dehydrogenase SE_1720"
FT                   /id="PRO_0000293561"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        279
FT                   /evidence="ECO:0000250"
FT   BINDING         201..207
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   475 AA;  51890 MW;  905E024191EE75D1 CRC64;
     MRNFTKQYIN GEWVDSASGE TIDVINPATE EVMGKIAKGN EEDVNKAVDA ADKVYLEFRH
     SSVEERRELL DKIVKEYQNR KNDLIEAITD ELGAPLSVSE NVHYQMGLNH FTAARDALDS
     FQFEEQRGDD LVVKEAIGVA GLVTPWNFPT NQTSLKLAAA FAAGSPVVLK PSEETPFAAI
     ILAEIFDKVG VPKGVFNLVN GDGSGVGNPL SEHPKVRMMS FTGSGPTGSK IMEKAAKDFK
     KVSLELGGKS PYIVLDDVDV EEAANATTKK VVNNTGQVCT AGTRVLIPES IKEDYLTAVK
     EAFSKVKVGQ PREEGTQVGP IISKKQFDQV QDYIDKGINE GAELFYGGPG KPEGLDKGYF
     ARPTIFINVD NHMTIAQEEI FGPVMSVITY NNLDEAIEIA NDTKYGLAGY VIGKDKDTLR
     HVARSIEAGT IEINEAGRKP DLPFGGYKES GLGREWGDYG IEEFLEVKSI AGYFK