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Protein

D-tagatose-1,6-bisphosphate aldolase subunit GatY

Gene

gatY

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic subunit of the tagatose-1,6-bisphosphate aldolase GatYZ, which catalyzes the reversible aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate (TBP). Requires GatZ subunit for full activity and stability. Is involved in the catabolism of galactitol.2 Publications

Catalytic activityi

D-tagatose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Kineticsi

  1. KM=1.0 mM for tagatose-1,6-bisphosphate (when expressed alone)1 Publication
  2. KM=0.3 mM for tagatose-1,6-bisphosphate (when expressed with GatZ)1 Publication

    Pathwayi: D-tagatose 6-phosphate degradation

    This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. D-tagatose-1,6-bisphosphate aldolase subunit GatZ (gatZ), D-tagatose-1,6-bisphosphate aldolase subunit GatY (gatY), D-tagatose-1,6-bisphosphate aldolase subunit KbaY (kbaY), D-tagatose-1,6-bisphosphate aldolase subunit KbaZ (kbaZ)
    This subpathway is part of the pathway D-tagatose 6-phosphate degradation, which is itself part of Carbohydrate metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate, the pathway D-tagatose 6-phosphate degradation and in Carbohydrate metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei82 – 821Proton donorBy similarity
    Metal bindingi83 – 831Zinc; catalyticBy similarity
    Metal bindingi180 – 1801Zinc; catalyticBy similarity
    Binding sitei181 – 1811Dihydroxyacetone phosphate; via amide nitrogenBy similarity
    Metal bindingi208 – 2081Zinc; catalyticBy similarity

    GO - Molecular functioni

    • tagatose-bisphosphate aldolase activity Source: EcoCyc
    • zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Galactitol metabolism

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:TAGAALDOL2-MONOMER.
    MetaCyc:TAGAALDOL2-MONOMER.
    SABIO-RKP0C8J6.
    UniPathwayiUPA00704; UER00716.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-tagatose-1,6-bisphosphate aldolase subunit GatY (EC:4.1.2.40)
    Short name:
    TBPA
    Short name:
    TagBP aldolase
    Alternative name(s):
    D-tagatose-bisphosphate aldolase class II
    Tagatose-bisphosphate aldolase
    Gene namesi
    Name:gatY
    Synonyms:yegF
    Ordered Locus Names:b2096, JW5343
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG12419. gatY.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 284284D-tagatose-1,6-bisphosphate aldolase subunit GatYPRO_0000178766Add
    BLAST

    Proteomic databases

    PaxDbiP0C8J6.
    PRIDEiP0C8J6.

    Expressioni

    Inductioni

    Constitutively expressed. Up-regulated under low pH conditions.2 Publications

    Interactioni

    Subunit structurei

    Forms a complex with GatZ.

    Protein-protein interaction databases

    BioGridi4260432. 7 interactions.
    DIPiDIP-48239N.
    IntActiP0C8J6. 13 interactions.
    MINTiMINT-1266244.
    STRINGi511145.b2096.

    Structurei

    3D structure databases

    ProteinModelPortaliP0C8J6.
    SMRiP0C8J6. Positions 3-283.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni209 – 2113Dihydroxyacetone phosphate bindingBy similarity
    Regioni230 – 2334Dihydroxyacetone phosphate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105D2N. Bacteria.
    COG0191. LUCA.
    HOGENOMiHOG000227793.
    InParanoidiP0C8J6.
    KOiK08302.
    OMAiLESGMGE.
    OrthoDBiEOG6HXJ7B.
    PhylomeDBiP0C8J6.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01294. TagBP_aldolase_GatY.
    InterProiIPR013785. Aldolase_TIM.
    IPR000771. Ketose_bisP_aldolase_II.
    IPR011288. TagBP_ald_KbaY/GatY.
    IPR023955. TagBP_aldolase_GatY.
    [Graphical view]
    PfamiPF01116. F_bP_aldolase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
    TIGRFAMsiTIGR00167. cbbA. 1 hit.
    TIGR01858. tag_bisphos_ald. 1 hit.
    PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
    PS00806. ALDOLASE_CLASS_II_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0C8J6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MYVVSTKQML NNAQRGGYAV PAFNIHNLET MQVVVETAAN LHAPVIIAGT
    60 70 80 90 100
    PGTFTHAGTE NLLALVSAMA KQYHHPLAIH LDHHTKFDDI AQKVRSGVRS
    110 120 130 140 150
    VMIDASHLPF AQNISRVKEV VDFCHRFDVS VEAELGQLGG QEDDVQVNEA
    160 170 180 190 200
    DALYTNPAQA REFAEATGID SLAVAIGTAH GMYASAPALD FSRLENIRQW
    210 220 230 240 250
    VNLPLVLHGA SGLSTKDIQQ TIKLGICKIN VATELKNAFS QALKNYLTEH
    260 270 280
    PEATDPRDYL QSAKSAMRDV VSKVIADCGC EGRA
    Length:284
    Mass (Da):30,812
    Last modified:November 25, 2008 - v1
    Checksum:iD414AA3921BBFE2B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75157.2.
    AP009048 Genomic DNA. Translation: BAA15966.2.
    PIRiS55901.
    RefSeqiNP_416599.2. NC_000913.3.
    WP_001307281.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75157; AAC75157; b2096.
    BAA15966; BAA15966; BAA15966.
    GeneIDi946636.
    KEGGiecj:JW5343.
    eco:b2096.
    PATRICi32119525. VBIEscCol129921_2173.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75157.2.
    AP009048 Genomic DNA. Translation: BAA15966.2.
    PIRiS55901.
    RefSeqiNP_416599.2. NC_000913.3.
    WP_001307281.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP0C8J6.
    SMRiP0C8J6. Positions 3-283.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260432. 7 interactions.
    DIPiDIP-48239N.
    IntActiP0C8J6. 13 interactions.
    MINTiMINT-1266244.
    STRINGi511145.b2096.

    Proteomic databases

    PaxDbiP0C8J6.
    PRIDEiP0C8J6.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75157; AAC75157; b2096.
    BAA15966; BAA15966; BAA15966.
    GeneIDi946636.
    KEGGiecj:JW5343.
    eco:b2096.
    PATRICi32119525. VBIEscCol129921_2173.

    Organism-specific databases

    EchoBASEiEB2318.
    EcoGeneiEG12419. gatY.

    Phylogenomic databases

    eggNOGiENOG4105D2N. Bacteria.
    COG0191. LUCA.
    HOGENOMiHOG000227793.
    InParanoidiP0C8J6.
    KOiK08302.
    OMAiLESGMGE.
    OrthoDBiEOG6HXJ7B.
    PhylomeDBiP0C8J6.

    Enzyme and pathway databases

    UniPathwayiUPA00704; UER00716.
    BioCyciEcoCyc:TAGAALDOL2-MONOMER.
    MetaCyc:TAGAALDOL2-MONOMER.
    SABIO-RKP0C8J6.

    Miscellaneous databases

    PROiP0C8J6.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01294. TagBP_aldolase_GatY.
    InterProiIPR013785. Aldolase_TIM.
    IPR000771. Ketose_bisP_aldolase_II.
    IPR011288. TagBP_ald_KbaY/GatY.
    IPR023955. TagBP_aldolase_GatY.
    [Graphical view]
    PfamiPF01116. F_bP_aldolase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
    TIGRFAMsiTIGR00167. cbbA. 1 hit.
    TIGR01858. tag_bisphos_ald. 1 hit.
    PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
    PS00806. ALDOLASE_CLASS_II_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Acid- and base-induced proteins during aerobic and anaerobic growth of Escherichia coli revealed by two-dimensional gel electrophoresis."
      Blankenhorn D., Phillips J., Slonczewski J.L.
      J. Bacteriol. 181:2209-2216(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-12, INDUCTION AT LOW PH.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "A role of RnlA in the RNase LS activity from Escherichia coli."
      Otsuka Y., Koga M., Iwamoto A., Yonesaki T.
      Genes Genet. Syst. 82:291-299(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-8.
      Strain: K12.
    6. "Molecular analysis of the gat genes from Escherichia coli and of their roles in galactitol transport and metabolism."
      Nobelmann B., Lengeler J.W.
      J. Bacteriol. 178:6790-6795(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ROLE IN GALACTITOL CATABOLISM, INDUCTION.
      Strain: K12.
    7. "Two class II D-tagatose-bisphosphate aldolases from enteric bacteria."
      Brinkkoetter A., Shakeri-Garakani A., Lengeler J.W.
      Arch. Microbiol. 177:410-419(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, KINETIC PARAMETERS, COMPLEX WITH GATZ.
      Strain: K12.

    Entry informationi

    Entry nameiGATY_ECOLI
    AccessioniPrimary (citable) accession number: P0C8J6
    Secondary accession number(s): P37192, P76415
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 25, 2008
    Last sequence update: November 25, 2008
    Last modified: January 20, 2016
    This is version 68 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.