Entry Information
Protein Name GldA
Accession No P0A9S5
Protein description Glycerol dehydrogenase
pI/Mw (Da)
Theoretical Experimental
4.81/38712.2 -
Protein function and expression Induced by hydroxyacetone and stationary phase growth conditions.
Reference(s) Lopez-Campistrous, A., P. Semchuk, L. Burke, T. Palmer-Stone, S. J. Brokx, G. Broderick, D. Bottorff, S. Bolch, J. H. Weiner, and M. J. Ellison. 2005. Localization, annotation & comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell. Proteomics 4:1205-1209. (NCBI)

2D gels information
Map ID68
Reference(s)Fountoulakis, M., and R. Gasser. 2003. Proteomic analysis of the cell envelope fraction of Escherichia coli. Amino Acids 24:19-41. (NCBI)
Protein function and expression(s)Map: B
Spot: 4


B
The membrane proteins of the E. coli transformant producing recombinant human cytochrome P450 2E1 and cytochrome P450 reductase
Swiss-Prot Database Reference

Entry information
Entry Name GLDA_ECOLI
Primary accession number P0A9S5
Secondary accession numbers P32665 P78132 Q2M8P1 
Integrated into Swiss-Prot on 2005-07-19
Sequence was last modified on 2005-07-19 (Sequence version 1)
Annotations were last modified on 2006-06-13 (Entry version 11)
Name and origin of the protein
Protein name Glycerol dehydrogenase
Synonyms EC 1.1.1.6 Glycerol dehydrogenase
GLDH
Gene name Name : gldA
OrderedLocusName : b3945
From Escherichia coli [TaxID:562] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia;
References
[1] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / MG1655 / ATCC 47076
PubMed=8265357[NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R. , Burland V.D. , Plunkett G. III , Sofia H.J. , Daniels D.L. ,
"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
Nucleic Acids Res.21:5408-5417(1993) 
[2] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / MG1655 / ATCC 47076
DOI=10.1126/science.277.5331.1453;PubMed=9278503[NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R. , Plunkett G. III , Bloch C.A. , Perna N.T. , Burland V. , Riley M. , Collado-Vides J. , Glasner J.D. , Rode C.K. , Mayhew G.F. , Gregor J. , Davis N.W. , Kirkpatrick H.A. , Goeden M.A. , Rose D.J. , Mau B. , Shao Y. ,
"The complete genome sequence of Escherichia coli K-12."
Science277:1453-1474(1997) 
[3] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / W3110 / ATCC 27325 / DSM 5911
DOI=10.1038/msb4100049;
Hayashi K. , Morooka N. , Yamamoto Y. , Fujita K. , Isono K. , Choi S. , Ohtsubo E. , Baba T. , Wanner B.L. , Mori H. , Horiuchi T. ,
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Mol. Syst. Biol.2:E1-E5(2006) 
[4] CHARACTERIZATION.PubMed=8132480[NCBI, ExPASy, EBI, Israel, Japan]
Truniger V. , Boos W. ,
"Mapping and cloning of gldA, the structural gene of the Escherichia coli glycerol dehydrogenase."
J. Bacteriol.176:1796-1800(1994) 
Comments
  • CATALYTIC ACTIVITY : Glycerol + NAD(+) = glycerone + NADH
  • COFACTOR : Divalent metal ions (Potential)
  • PATHWAY : Glycerol utilization
  • DEVELOPMENTAL STAGE : Expression is higher in during stationary phase than during logarithmic growth
  • INDUCTION : Full expression of gldA is achieved only by induction with hydroxyacetone and stationary-phase growth conditions
  • SIMILARITY : Belongs to the iron-containing alcohol dehydrogenase family
  • Copyright
    Copyrighted by the UniProt Consortium, see http://www.uniprot.org/. Distributed under the Creative Commons Attribution-NoDerivs License.
    Cross-reference
    Sequence databases
    EMBL U00006;AAC43051.1;ALT_INIT;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    U00096;AAC76927.1;ALT_INIT;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    AP009048;BAE77365.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    3D structure databases
    HSSP Q9WYQ4;1KQ3[HSSP ENTRY / PDB].
    ModBase P0A9S5
    Protein-protein interaction databases
    DIP P0A9S5
    Enzyme and pathway databases
    BioCyc EcoCyc:GLYCDEH-MONOMER;-.
    2D gel databases
    SWISS-2DPAGE Get region on 2D PAGE
    Organism-specific gene databases
    EchoBASE EB1849;-.
    EcoGene EG11904;gldA.
    HOGENOM [Family / Alignment / Tree]
    Family and domain databases
    InterPro IPR001670;Fe_ADH.
    Graphical view of domain structure
    Pfam PF00465;Fe-ADH;1.
    Pfam graphical view of domain structure
    BLOCKS P0A9S5
    PROSITE PS00913;ADH_IRON_1;1.
    PS00060;ADH_IRON_2;1.
    Genome annotation databases
    GenomeReviews U00096_GR;b3945.
    Other
    ProtoNet P0A9S5
    UniRef View cluster of proteins with at least 50% / 90% / 100% identity
    Keyword
    Complete proteome; Glycerol metabolism; NAD; Oxidoreductase;
    Features
    Feature table viewer Feature aligner
    Key  From   To Length  Description  FTId
    CHAIN    1   367    367  Glycerol dehydrogenase  PRO_0000087828
    Sequence information
    Length: 367AA [This is the length of the unprocessed precursor] Molecular weight: 38712Da [This is the MW of the unprocessed precursor] CRC64: F6F3F275B4091F28[This is a checksum on the sequence]
            10         20         30         40         50         60
    MDRIIQSPGK YIQGADVINR LGEYLKPLAE RWLVVGDKFV LGFAQSTVEK SFKDAGLVVE
            70         80         90        100        110        120
    IAPFGGECSQ NEIDRLRGIA ETAQCGAILG IGGGKTLDTA KALAHFMGVP VAIAPTIAST
           130        140        150        160        170        180
    DAPCSALSVI YTDEGEFDRY LLLPNNPNMV IVDTKIVAGA PARLLAAGIG DALATWFEAR
           190        200        210        220        230        240
    ACSRSGATTM AGGKCTQAAL ALAELCYNTL LEEGEKAMLA AEQHVVTPAL ERVIEANTYL
           250        260        270        280        290        300
    SGVGFESGGL AAAHAVHNGL TAIPDAHHYY HGEKVAFGTL TQLVLENAPV EEIETVAALS
           310        320        330        340        350        360
    HAVGLPITLA QLDIKEDVPA KMRIVAEAAC AEGETIHNMP GGATPDQVYA ALLVADQYGQ
    
    RFLQEWE
    P0A9S5 in FASTA format