Entry Information
Protein Name GatY
Accession No P37192
Protein description Tagatose-1,6-bisphosphate aldolase GatY
pI/Mw (Da)
Theoretical Experimental
5.87/30811.93 -
Protein function and expression Catalyzes the reversible condensation of dihydroxyacetone phosphate with glyceraldehyde 3-phosphate to produce tagatose 1,6-bisphosphate. Induced by low pH during aerobic or anaerobic growth, and increases in the physiological short-term adaptation to glucose-limitation.
Reference(s) Blankenhorn, D., J. Phillips, and J. L. Slonczewski. 1999. Acid- and base-induced proteins during aerobic and anaerobic growth of Escherichia coli revealed by two-dimensional gel electrophoresis. J. Bacteriol. 181:2209-2216. (NCBI)

Wick, L. M., M. Quadroni, and T. Egli. 2001. Short- and long-term changes in proteome composition and kinetic properties in a culture of Escherichia coli during transition from glucose-excess to glucose-limited growth conditions in continuous culture and vice versa. Environ. Microbiol. 3:588-599. (NCBI)

Yohannes, E., D. M. Barnhart, and J. L. Slonczewski. 2004. pH-dependent catabolic protein expression during anaerobic growth of Escherichia coli K-12. J. Bacteriol. 186:192-199. (NCBI)

2D gels information
Map ID27
Reference(s)Blankenhorn, D., J. Phillips, and J. L. Slonczewski. 1999. Acid- and base-induced proteins during aerobic and anaerobic growth of Escherichia coli revealed by two-dimensional gel electrophoresis. J. Bacteriol. 181:2209-2216. (NCBI)
Protein function and expression(s)Map: AA AB AC AD BA BB BC BD
Spot: 10
Method of Identity: N-terminal sequecing
N-terminal sequence: MYVVSTKQMLNN

AA
Proteins expressed during growth with aeration. Media contained LBK buffered with 100 mM HOMOPIPES, pH 4.4.
AB
Proteins expressed during growth with aeration. Media contained LBK buffered with 100 mM MES-50 mM propionic acid, pH 6.
AC
Proteins expressed during growth with aeration. Media contained LBK buffered with 100 mM MOPS, pH 7.0.
AD
Proteins expressed during growth with aeration. Media contained LBK buffered with 100 mM AMPSO, pH 9.2.
BA
Proteins expressed during anaerobic growth. Media contained LBK buffered with 100 mM HOMOPIPES, pH 4.4.
BB
Proteins expressed during anaerobic growth. Media contained LBK buffered with 100 mM MES-50 mM propionic acid, pH 6.
BC
Proteins expressed during anaerobic growth. Media contained LBK buffered with 100 mM MOPS, pH 7.0.
BD
Proteins expressed during anaerobic growth. Media contained LBK buffered with 100 mM AMPSO, pH 9.2.
Map ID38
Reference(s)Champion, K. M., J. C. Nishihara, J. C. Joly, and D. Arnott. 2001. Similarity of the Escherichia coli proteome upon completion of different biopharmaceutical fermentation processes. Proteomics 1:1133-1148. (NCBI)
Protein function and expression(s)Map: A
pI/Mw: 6.04/30907

A
2-DE profile of E. coli proteins at the end of anti-CD18 blank run fermentation.
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: A A A B B B B CA
Spot: 7


A
The membrane proteins of the wild type strain.
B
The membrane proteins of the E. coli transformant producing recombinant human cytochrome P450 2E1 and cytochrome P450 reductase
CA
The membrane proteins of E. coli producing human cytochrome P450 2D6 were solubilized with 0.5% sodium cholate. Cholate was exchanged against 7 M urea, 2 M thiourea and 4% CHAPS.
Map ID311
Reference(s)Wick, L. M., M. Quadroni, and T. Egli. 2001. Short- and long-term changes in proteome composition and kinetic properties in a culture of Escherichia coli during transition from glucose-excess to glucose-limited growth conditions in continuous culture and vice versa. Environ. Microbiol. 3:588-599. (NCBI)
Protein function and expression(s)Map: A B
Spot: 10
Functional category: Catabolism

A
Proteins expressed in a culture of E. coli K12 during growth under glucose-excess batch.
B
Proteins expressed in a culture of E. coli K12 during growth under glucose-limited continuous.
Map ID323
Reference(s)Yohannes, E., D. M. Barnhart, and J. L. Slonczewski. 2004. pH-dependent catabolic protein expression during anaerobic growth of Escherichia coli K-12. J. Bacteriol. 186:192-199. (NCBI)
Protein function and expression(s)Map: A B
Spot: 15
Acid induced
LDE(the mean logarithmic differential expression ratio of pH 8.5 cultures to pH 5.5 cultures)
A: -1

A
pH-dependent protein profiles after anaerobic growth. In the layered view shown two composite images, one representing growth at pH 8.5 (pink) and one representing growth at pH 5.5 (green), are superimposed. Cultures grown in LBK buffered with 100 mM MES (pH 5.5) or 100 mM TAPS (pH 8.5).
B
pH-dependent protein profiles after anaerobic growth. In the layered view shown two composite images, one representing growth at pH 8.5 (pink) and one representing growth at pH 5.5 (green), are superimposed. Cultures grown in LBK buffered with a mixture of 50 mM MES and 50 mM1TAPS for both pH 5.5 and pH 8.5.
Swiss-Prot Database Reference

Entry information
Entry Name GATY_ECOLI
Primary accession number P37192
Secondary accession numbers P76415 
Integrated into Swiss-Prot on 1994-10-01
Sequence was last modified on 2001-04-27 (Sequence version 4)
Annotations were last modified on 2006-06-27 (Entry version 51)
Name and origin of the protein
Protein name Tagatose-1,6-bisphosphate aldolase gatY
Synonyms EC 4.1.2.- Tagatose-1,6-bisphosphate aldolase gatY
TBPA
Gene name Name : gatY
OrderedLocusName : b2096
From Escherichia coli [TaxID:562] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia;
References
[1] NUCLEOTIDE SEQUENCE [GENOMIC DNA].
strain = EC3132
DOI=10.1016/0167-4781(95)00053-J;PubMed=7772602[NCBI, ExPASy, EBI, Israel, Japan]
Nobelmann B. , Lengeler J.W. ,
"Sequence of the gat operon for galactitol utilization from a wild-type strain EC3132 of Escherichia coli."
Biochim. Biophys. Acta1262:69-72(1995) 
[2] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / W3110 / ATCC 27325 / DSM 5911
DOI=10.1093/dnares/3.6.379;PubMed=9097040[NCBI, ExPASy, EBI, Israel, Japan]
Itoh T. , Aiba H. , Baba T. , Fujita K. , Hayashi K. , Inada T. , Isono K. , Kasai H. , Kimura S. , Kitakawa M. , Kitagawa M. , Makino K. , Miki T. , Mizobuchi K. , Mori H. , Mori T. , Motomura K. , Nakade S. , Nakamura Y. , Nashimoto H. , Nishio Y. , Oshima T. , Saito N. , Sampei G. , Seki Y. , Sivasundaram S. , Tagami H. , Takeda J. , Takemoto K. , Wada C. , Yamamoto Y. , Horiuchi T. ,
"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
DNA Res.3:379-392(1996) 
[3] 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) 
[4] 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) 
Comments
  • FUNCTION : Catalyzes the reversible condensation of dihydroxyacetone phosphate with glyceraldehyde 3-phosphate to produce tagatose 1,6-bisphosphate
  • CATALYTIC ACTIVITY : D-tagatose 1,6-bisphosphate 1,6-bisphosphate = glycerone-phosphate + D-glyceraldehyde 3-phosphate
  • COFACTOR : Binds 1 zinc ion per subunit (By similarity)
  • PATHWAY : Galacticol utilization
  • SIMILARITY : Belongs to the class II fructose-bisphosphate aldolase 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 X79837;CAA56226.1;ALT_INIT;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    U00096;AAC75157.1;ALT_INIT;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    AP009048;BAA15966.1;ALT_INIT;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    3D structure databases
    HSSP P42908;1GVF[HSSP ENTRY / PDB].
    ModBase P37192
    Protein-protein interaction databases
    IntAct P37192;-.
    DIP P37192
    Enzyme and pathway databases
    BioCyc EcoCyc:TAGAALDOL2-MONOMER;-.
    2D gel databases
    SWISS-2DPAGE Get region on 2D PAGE
    Organism-specific gene databases
    EchoBASE EB2318;-.
    EcoGene EG12419;gatY.
    HOGENOM [Family / Alignment / Tree]
    Family and domain databases
    InterPro IPR000771;K_bP_aldolase.
    IPR011288;Tag_bisphos_ald.
    Graphical view of domain structure
    Pfam PF01116;F_bP_aldolase;1.
    Pfam graphical view of domain structure
    ProDom PD002376;K_bP_aldolase;1.
    [Domain structure / List of seq. sharing at least 1 domain]
    TIGRFAMs TIGR00167;cbbA;1.
    TIGR01858;tag_bisphos_ald;1.
    BLOCKS P37192
    PROSITE PS00602;ALDOLASE_CLASS_II_1;1.
    PS00806;ALDOLASE_CLASS_II_2;1.
    Genome annotation databases
    GenomeReviews U00096_GR;b2096.
    Other
    ProtoNet P37192
    UniRef View cluster of proteins with at least 50% / 90% / 100% identity
    Keyword
    Complete proteome; Galactitol metabolism; Lyase; Metal-binding; Zinc;
    Features
    Feature table viewer Feature aligner
    Key  From   To Length  Description  FTId
    CHAIN    1   284    284  Tagatose-1,6-bisphosphate aldolase gatY  PRO_0000178766
    METAL   83    83    Zinc(by similarity)  
    METAL  180   180    Zinc(by similarity)  
    METAL  208   208    Zinc(by similarity)  
    CONFLICT   93    94    KV -> NL: (in Ref. 1)  
    CONFLICT  153   153    L -> F: (in Ref. 1)  
    CONFLICT  188   188    A -> V: (in Ref. 1)  
    CONFLICT  249   249    E -> A: (in Ref. 1)  
    Sequence information
    Length: 284AA [This is the length of the unprocessed precursor] Molecular weight: 30812Da [This is the MW of the unprocessed precursor] CRC64: D414AA3921BBFE2B[This is a checksum on the sequence]
            10         20         30         40         50         60
    MYVVSTKQML NNAQRGGYAV PAFNIHNLET MQVVVETAAN LHAPVIIAGT PGTFTHAGTE
            70         80         90        100        110        120
    NLLALVSAMA KQYHHPLAIH LDHHTKFDDI AQKVRSGVRS VMIDASHLPF AQNISRVKEV
           130        140        150        160        170        180
    VDFCHRFDVS VEAELGQLGG QEDDVQVNEA DALYTNPAQA REFAEATGID SLAVAIGTAH
           190        200        210        220        230        240
    GMYASAPALD FSRLENIRQW VNLPLVLHGA SGLSTKDIQQ TIKLGICKIN VATELKNAFS
           250        260        270        280 
    QALKNYLTEH PEATDPRDYL QSAKSAMRDV VSKVIADCGC EGRA
    P37192 in FASTA format