ID   ALD1_STAEQ              Reviewed;         475 AA.
AC   Q5HMA0;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Putative aldehyde dehydrogenase SERP1729;
DE            EC=1.2.1.3;
GN   OrderedLocusNames=SERP1729;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Bacillota; 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; AAW55043.1; -; Genomic_DNA.
DR   RefSeq; WP_001832742.1; NC_002976.3.
DR   AlphaFoldDB; Q5HMA0; -.
DR   SMR; Q5HMA0; -.
DR   STRING; 176279.SERP1729; -.
DR   GeneID; 50018180; -.
DR   KEGG; ser:SERP1729; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_2_9; -.
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   GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
DR   CDD; cd07138; ALDH_CddD_SSP0762; 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   PANTHER; PTHR42804; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42804:SF1; 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; Reference proteome.
FT   CHAIN           1..475
FT                   /note="Putative aldehyde dehydrogenase SERP1729"
FT                   /id="PRO_0000293562"
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
//