ID   ALDH_STAAS              Reviewed;         475 AA.
AC   Q6G7I8;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Putative aldehyde dehydrogenase {ECO:0000305};
DE            EC=1.2.1.3 {ECO:0000305};
GN   OrderedLocusNames=SAS2025;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX571857; CAG43833.1; -; Genomic_DNA.
DR   RefSeq; WP_001206105.1; NC_002953.3.
DR   AlphaFoldDB; Q6G7I8; -.
DR   SMR; Q6G7I8; -.
DR   KEGG; sas:SAS2025; -.
DR   HOGENOM; CLU_005391_0_2_9; -.
DR   OMA; RRMDTGQ; -.
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_0000293555"
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;  51982 MW;  6D8F555E7F35D4C9 CRC64;
     MRDYTKQYIN GEWVESNSNE TIEVINPATE EVIGKVAKGN KADVDKAVEA ADNVYLEFRH
     TSVKERQALL DKIVKEYENR KDDIVQAITD ELGAPLSLSE RVHYQMGLNH FVAARDALDN
     YEFEERRGDD LVVKEAIGVS GLITPWNFPT NQTSLKLAAA FAAGSPVVLK PSEETPFAAV
     ILAEIFDKVG VPKGVFNLVN GDGAGVGNPL SEHPKVRMMS FTGSGPTGSK IMEKAAKDFK
     KVSLELGGKS PYIVLDDVDI KEAAKATTGK VVNNTGQVCT AGTRVLVPKK IKDAFLAELK
     EQFSQVRVGN PREDGTQVGP IISKKQFDQV QNYINKGIEE GAELFYGGPG KPEGLEKGYF
     ARPTIFINVD NQMTIAQEEI FGPVMSVITY NDLDEAIQIA NDTKYGLAGY VIGKDKETLH
     KVARSIEAGT VEINEAGRKP DLPFGGYKQS GLGREWGDYG IEEFLEVKSI AGYFK