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Database: UniProt/SWISS-PROT
Entry: ALDA_STAAR
LinkDB: ALDA_STAAR
Original site: ALDA_STAAR 
ID   ALDA_STAAR              Reviewed;         495 AA.
AC   Q6GKD8;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   28-FEB-2018, entry version 79.
DE   RecName: Full=Putative aldehyde dehydrogenase AldA;
DE            EC=1.2.1.3;
GN   Name=aldA; OrderedLocusNames=SAR0169;
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: An aldehyde + NAD(+) + H(2)O = a carboxylate +
CC       NADH.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
DR   EMBL; BX571856; CAG39196.1; -; Genomic_DNA.
DR   RefSeq; WP_000290401.1; NC_002952.2.
DR   ProteinModelPortal; Q6GKD8; -.
DR   SMR; Q6GKD8; -.
DR   EnsemblBacteria; CAG39196; CAG39196; SAR0169.
DR   KEGG; sar:SAR0169; -.
DR   HOGENOM; HOG000271505; -.
DR   KO; K00128; -.
DR   OMA; TFVQEDV; -.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 2.
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.
FT   CHAIN         1    495       Putative aldehyde dehydrogenase AldA.
FT                                /FTId=PRO_0000056458.
FT   NP_BIND     212    218       NAD. {ECO:0000250}.
FT   ACT_SITE    256    256       {ECO:0000250}.
FT   ACT_SITE    290    290       {ECO:0000250}.
SQ   SEQUENCE   495 AA;  53646 MW;  2F53D449813860B1 CRC64;
     MAVNVRDYIA ENYGLFINGE FVKGSSDETI EVTNPATGET LSHITRAKDK DVDHAVKVAQ
     EAFESWSLTS KSERAQMLRD IGDKLMAQKD KIAMIETLNN GKPIRETTAI DIPFAARHFH
     YFASVIETEE GTVNDIDKDT MSIVRHEPIG VVGAVVAWNF PMLLAAWKIA PAIAAGNTIV
     IQPSSSTPLS LLEVAKIFQE VLPNGVVNIL 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
//
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