ID   ALD1_STAS1              Reviewed;         475 AA.
AC   Q49Z69;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Putative aldehyde dehydrogenase SSP0762;
DE            EC=1.2.1.3;
GN   OrderedLocusNames=SSP0762;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE17907.1; -; Genomic_DNA.
DR   RefSeq; WP_011302667.1; NZ_MTGA01000032.1.
DR   AlphaFoldDB; Q49Z69; -.
DR   SMR; Q49Z69; -.
DR   STRING; 342451.SSP0762; -.
DR   PRIDE; Q49Z69; -.
DR   EnsemblBacteria; BAE17907; BAE17907; SSP0762.
DR   KEGG; ssp:SSP0762; -.
DR   PATRIC; fig|342451.11.peg.764; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_2_9; -.
DR   OMA; RRMDTGQ; -.
DR   OrthoDB; 618655at2; -.
DR   Proteomes; UP000006371; 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   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..475
FT                   /note="Putative aldehyde dehydrogenase SSP0762"
FT                   /id="PRO_0000293564"
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;  51651 MW;  9A71EA22E5FE487B CRC64;
     MRNFTKQYIN GEWVESTSGE TLEVINPATE EVAGTIAKGN KEDVEKAVEA ADNVYLEFRH
     TSVKERQDLL DQIVQEYKNR KEDLIQAITD ELGAPLSVAE NVHYQMGLDH FEAARDALND
     FQFEERRGDD LVVKEAIGVS GLITPWNFPT NQTSLKLAAA FAAGSPVVFK PSEETPFAAI
     ILAEIFDKVG VPKGVFNLVN GDGQGVGNPL SEHPKVRMMS FTGSGPTGSS IMKKAAEDFK
     KVSLELGGKS PYIILDDADI DGAASAAANK VVFNTGQVCT AGTRTIVPAS IKEDFLTAVK
     EKFSQVKVGN PREEGTQVGP IISKKQFDQV QAYIDKGIEE GAELLYGGPG KPEGLDKGYF
     ARPTIFNNVD NSMTIAQEEI FGPVMSVITY NDLDEAIKIA NDTKYGLAGY VYGSDKDTLH
     KVARSIEAGT VEINEAGRKP DLPFGGYKQS GLGREWGDYG IEEFLEVKSI AGYYN