ID   ALDH_STAAN              Reviewed;         475 AA.
AC   Q7A4D8;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Putative aldehyde dehydrogenase {ECO:0000305};
DE            EC=1.2.1.3 {ECO:0000305};
GN   OrderedLocusNames=SA1924;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=N315;
RX   PubMed=15590099; DOI=10.1016/j.mimet.2004.09.017;
RA   Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y.,
RA   Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C.,
RA   Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.;
RT   "Correlation of proteomic and transcriptomic profiles of Staphylococcus
RT   aureus during the post-exponential phase of growth.";
RL   J. Microbiol. Methods 60:247-257(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=N315;
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT   aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
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; BA000018; BAB43208.1; -; Genomic_DNA.
DR   PIR; G90005; G90005.
DR   RefSeq; WP_001206093.1; NC_002745.2.
DR   AlphaFoldDB; Q7A4D8; -.
DR   SMR; Q7A4D8; -.
DR   SWISS-2DPAGE; Q7A4D8; -.
DR   EnsemblBacteria; BAB43208; BAB43208; BAB43208.
DR   KEGG; sau:SA1924; -.
DR   HOGENOM; CLU_005391_0_2_9; -.
DR   OMA; RRMDTGQ; -.
DR   Proteomes; UP000000751; 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   1: Evidence at protein level;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..475
FT                   /note="Putative aldehyde dehydrogenase"
FT                   /id="PRO_0000293558"
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