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Database: UniProt/SWISS-PROT
Entry: ALD1_STAHJ
LinkDB: ALD1_STAHJ
Original site: ALD1_STAHJ 
ID   ALD1_STAHJ              Reviewed;         475 AA.
AC   Q4L803;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   10-APR-2019, entry version 98.
DE   RecName: Full=Putative aldehyde dehydrogenase SH0913;
DE            EC=1.2.1.3;
GN   OrderedLocusNames=SH0913;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE04222.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AP006716; BAE04222.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_029376675.1; NC_007168.1.
DR   ProteinModelPortal; Q4L803; -.
DR   SMR; Q4L803; -.
DR   STRING; 279808.SH0913; -.
DR   PRIDE; Q4L803; -.
DR   EnsemblBacteria; BAE04222; BAE04222; SH0913.
DR   GeneID; 24246031; -.
DR   KEGG; sha:SH0913; -.
DR   eggNOG; ENOG4105C26; Bacteria.
DR   eggNOG; COG1012; LUCA.
DR   HOGENOM; HOG000271505; -.
DR   KO; K00128; -.
DR   OMA; KTIWIAL; -.
DR   OrthoDB; 618655at2; -.
DR   BioCyc; SHAE279808:G1G27-875-MONOMER; -.
DR   Proteomes; UP000000543; 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   Complete proteome; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN         1    475       Putative aldehyde dehydrogenase SH0913.
FT                                /FTId=PRO_0000293563.
FT   NP_BIND     201    207       NAD. {ECO:0000250}.
FT   ACT_SITE    245    245       {ECO:0000250}.
FT   ACT_SITE    279    279       {ECO:0000250}.
SQ   SEQUENCE   475 AA;  51949 MW;  8B75A796F9CDCCE7 CRC64;
     MRNYTQQYIN GEWIDSDSNE TIEVINPATE EVIGKVAKGN SNDVEKAVEA ANNVYLEFRH
     SSVKERKELL DKIVEEYKNR KQDIIEAITD ELGAPLTLSE NVHYQMGLNH FEEASRALDS
     FEFEERRGDA LVTKEAIGVS GLVTPWNFPT NQTSLKLAAA FAAGSPVVLK PSEETPFAAV
     ILAEIFDKVG VPKGVFNLVN GDGEGVGNPL SEHPKVRMMS FTGSGRTGSK IMEKASKDFK
     KVSLELGGKS PYIVLDDVDV KEAAKATTGK VVNNTGQVCT AGTRILIPES KKEDFLTALK
     EEFSKVKVGD PREEGTQVGP IISKKQFDTV QSYIDKGIEE GAELFYGGPG KPEGLNTGYF
     ARPTIFINVD NDMTIAQEEI FGPVASVITY NNLDEAIKIA NDTKYGLAGY VIGKDKETLQ
     KVARSIEAGR IEINEAGNQP DLPFGGYKQS GIGREWGDYG IEEFLEVKSI AGYFS
//
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