ID   ALDH_STAAC              Reviewed;         475 AA.
AC   Q5HE78;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Putative aldehyde dehydrogenase {ECO:0000305};
DE            EC=1.2.1.3 {ECO:0000305};
GN   OrderedLocusNames=SACOL2114;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
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; Evidence={ECO:0000305};
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000046; AAW38424.1; -; Genomic_DNA.
DR   RefSeq; WP_001206093.1; NC_002951.2.
DR   AlphaFoldDB; Q5HE78; -.
DR   SMR; Q5HE78; -.
DR   EnsemblBacteria; AAW38424; AAW38424; SACOL2114.
DR   KEGG; sac:SACOL2114; -.
DR   HOGENOM; CLU_005391_0_2_9; -.
DR   OMA; RRMDTGQ; -.
DR   Proteomes; UP000000530; 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:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
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   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 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"
FT                   /id="PRO_0000293553"
FT   ACT_SITE        245
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P25526"
FT   ACT_SITE        279
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P25526"
FT   BINDING         146..147
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25526"
FT   BINDING         223..224
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25526"
FT   BINDING         246
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25526"
FT   BINDING         379
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25526"
SQ   SEQUENCE   475 AA;  51969 MW;  03C66ED0B87BC09A CRC64;
     MRDYTKQYIN GEWVESNSNE TIEVINPATE EVIGKVAKGN KADVDKAVEA ADDVYLEFRH
     TSVKERQALL DKIVKEYENR KDDIVQAITD ELGAPLSLSE RVHYQMGLNH FVAARDALDN
     YEFEERRGDD LVVKEAIGVS GLITPWNFPT NQTSLKLAAA FAAGSPVVLK PSEETPFAAV
     ILAEIFDKVG VPKGVFNLVN GDGAGVGNPL SEHPKVRMMS FTGSGPTGSK IMEKAAKDFK
     KVSLELGGKS PYIVLDDVDI KEAAKATTGK VVNNTGQVCT AGTRVLVPNK IKDAFLAELK
     EQFSQVRVGN PREDGTQVGP IISKKQFDQV QNYINKGIEE GAELFYGGPG KPEGLEKGYF
     ARPTIFINVD NQMTIAQEEI FGPVMSVITY NDLDEAIQIA NDTKYGLAGY VIGKDKETLH
     KVARSIEAGT VEINEAGRKP DLPFGGYKQS GLGREWGDYG IEEFLEVKSI AGYFK