ID   ALDA_STAAN              Reviewed;         495 AA.
AC   Q7A825;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Putative aldehyde dehydrogenase AldA;
DE            EC=1.2.1.3;
GN   Name=aldA; OrderedLocusNames=SA0162;
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;
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; BA000018; BAB41382.1; -; Genomic_DNA.
DR   PIR; C89778; C89778.
DR   RefSeq; WP_000290397.1; NC_002745.2.
DR   AlphaFoldDB; Q7A825; -.
DR   SMR; Q7A825; -.
DR   SWISS-2DPAGE; Q7A825; -.
DR   EnsemblBacteria; BAB41382; BAB41382; BAB41382.
DR   KEGG; sau:SA0162; -.
DR   HOGENOM; CLU_005391_0_2_9; -.
DR   OMA; HGIGYYP; -.
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   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   1: Evidence at protein level;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..495
FT                   /note="Putative aldehyde dehydrogenase AldA"
FT                   /id="PRO_0000056457"
FT   ACT_SITE        256
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000250"
FT   BINDING         212..218
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   495 AA;  53660 MW;  36B448F85BFECD02 CRC64;
     MAVNVRDYIA ENYGLFINGE FVKGSSDETI EVTNPATGET LSHITRAKDK DVDHAVKVAQ
     EAFESWSLTS KSERAQMLRD IGDKLMAQKD KIAMIETLNN GKPIRETTAI DIPFAARHFH
     YFASVIETEE GTVNDIDKDT MSIVRHEPIG VVGAVVAWNF PMLLAAWKIA PAIAAGNTIV
     IQPSSSTPLS LLEVAKIFQE VLPKGVVNIL TGKGSESGNA IFNHDGVDKL SFTGSTDVGY
     QVAEAAAKHL VPATLELGGK SANIILDDAN LDLAVEGIQL GILFNQGEVC SAGSRLLVHE
     KIYDQLVPRL QEAFSNIKVG DPQDEATQMG SQTGKDQLDK IQSYIDAAKE SDAQILAGGH
     RLTENGLDKG FFFEPTLIAV PDNHHKLAQE EIFGPVLTVI KVKDDQEAID IANDSEYGLA
     GGVFSQNITR ALNIAKAVRT GRIWINTYNQ VPEGAPFGGY KKSGIGRETY KGALSNYQQV
     KNIYIDTSNA LKGLY