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Database: UniProt/SWISS-PROT
Entry: ALDH_STAAW
LinkDB: ALDH_STAAW
Original site: ALDH_STAAW 
ID   ALDH_STAAW              Reviewed;         475 AA.
AC   Q8NVG4;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   05-DEC-2018, entry version 90.
DE   RecName: Full=Putative aldehyde dehydrogenase {ECO:0000305};
DE            EC=1.2.1.3 {ECO:0000305};
GN   OrderedLocusNames=MW2046;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A.,
RA   Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L.,
RA   Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-
RT   acquired MRSA.";
RL   Lancet 359:1819-1827(2002).
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; BA000033; BAB95911.1; -; Genomic_DNA.
DR   RefSeq; WP_001206105.1; NC_003923.1.
DR   ProteinModelPortal; Q8NVG4; -.
DR   SMR; Q8NVG4; -.
DR   EnsemblBacteria; BAB95911; BAB95911; BAB95911.
DR   KEGG; sam:MW2046; -.
DR   HOGENOM; HOG000271505; -.
DR   KO; K00128; -.
DR   OMA; KTIWIAL; -.
DR   BioCyc; SAUR196620:G1G3G-2294-MONOMER; -.
DR   Proteomes; UP000000418; 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   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    475       Putative aldehyde dehydrogenase.
FT                                /FTId=PRO_0000293557.
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;  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
//
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