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Database: UniProt/SWISS-PROT
Entry: ALDH_STAAR
LinkDB: ALDH_STAAR
Original site: ALDH_STAAR 
ID   ALDH_STAAR              Reviewed;         475 AA.
AC   Q6GEV3;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JAN-2019, entry version 88.
DE   RecName: Full=Putative aldehyde dehydrogenase {ECO:0000305};
DE            EC=1.2.1.3 {ECO:0000305};
GN   OrderedLocusNames=SAR2210;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
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.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence 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(+) +
CC         NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3;
CC         Evidence={ECO:0000305};
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
DR   EMBL; BX571856; CAG41191.1; -; Genomic_DNA.
DR   RefSeq; WP_001206107.1; NC_002952.2.
DR   ProteinModelPortal; Q6GEV3; -.
DR   SMR; Q6GEV3; -.
DR   EnsemblBacteria; CAG41191; CAG41191; SAR2210.
DR   KEGG; sar:SAR2210; -.
DR   HOGENOM; HOG000271505; -.
DR   KO; K00128; -.
DR   OMA; KTIWIAL; -.
DR   OrthoDB; 618655at2; -.
DR   BioCyc; SAUR282458:G1G3O-2391-MONOMER; -.
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       Putative aldehyde dehydrogenase.
FT                                /FTId=PRO_0000293554.
FT   NP_BIND     146    147       NAD. {ECO:0000250|UniProtKB:P25526}.
FT   NP_BIND     223    224       NAD. {ECO:0000250|UniProtKB:P25526}.
FT   ACT_SITE    245    245       Proton acceptor.
FT                                {ECO:0000250|UniProtKB:P25526}.
FT   ACT_SITE    279    279       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P25526}.
FT   BINDING     246    246       NAD; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P25526}.
FT   BINDING     379    379       NAD. {ECO:0000250|UniProtKB:P25526}.
SQ   SEQUENCE   475 AA;  51968 MW;  6D88272B7D42A6BC 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 AGTRVLVPNK IKDAFLAELK
     EQFSQVRVGN PREDGTQVGP IISKKQFDQV QNYINKGIEE GAELFYGGPG KPEGLEKGYF
     ARPTIFINVD NQMTIAQEEI FGPVMSVITY NDLDEAIQIA NDTKYGLAGY VIGKDKETLH
     KVARSIEAGT VEINEAGRKP DLPFGGYKQS GLGREWGDYG IEEFLEVKSI AGYFK
//
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