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Protein

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

Gene

kbaY

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

Functioni

Catalytic subunit of the tagatose-1,6-bisphosphate aldolase KbaYZ, 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 KbaZ subunit for full activity and stability.2 Publications

Catalytic activityi

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

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Kineticsi

The catalytic efficiency measured with tagatose-1,6-bisphosphate as substrate is 340-fold higher than that with fructose-1,6-bisphosphate.

  1. KM=0.26 mM for tagatose-1,6-bisphosphate1 Publication
  2. KM=1.3 mM for fructose-1,6-bisphosphate1 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 donor1 Publication
    Metal bindingi83 – 831Zinc; catalytic1 Publication
    Metal bindingi180 – 1801Zinc; catalytic1 Publication
    Binding sitei181 – 1811Dihydroxyacetone phosphate; via amide nitrogen
    Metal bindingi208 – 2081Zinc; catalytic1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:TAGAALDOL1-MONOMER.
    ECOL316407:JW3106-MONOMER.
    MetaCyc:TAGAALDOL1-MONOMER.
    BRENDAi4.1.2.40. 2026.
    SABIO-RKP0AB74.
    UniPathwayiUPA00704; UER00716.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-tagatose-1,6-bisphosphate aldolase subunit KbaY (EC:4.1.2.40)
    Short name:
    TBPA
    Short name:
    TagBP aldolase
    Alternative name(s):
    D-tagatose-bisphosphate aldolase class II
    Ketose 1,6-bisphosphate aldolase class II
    Tagatose-bisphosphate aldolase
    Gene namesi
    Name:kbaY
    Synonyms:agaY, kba, yraC
    Ordered Locus Names:b3137, JW3106
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG12768. kbaY.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 286286D-tagatose-1,6-bisphosphate aldolase subunit KbaYPRO_0000178763Add
    BLAST

    Proteomic databases

    PaxDbiP0AB74.
    PRIDEiP0AB74.

    Interactioni

    Subunit structurei

    Homotetramer. Forms a complex with KbaZ.2 Publications

    Protein-protein interaction databases

    BioGridi4261155. 23 interactions.
    DIPiDIP-47961N.
    IntActiP0AB74. 7 interactions.
    MINTiMINT-1279079.
    STRINGi511145.b3137.

    Structurei

    Secondary structure

    1
    286
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 1610Combined sources
    Beta strandi20 – 245Combined sources
    Helixi28 – 4114Combined sources
    Beta strandi46 – 494Combined sources
    Helixi53 – 564Combined sources
    Helixi59 – 7214Combined sources
    Beta strandi77 – 848Combined sources
    Helixi87 – 959Combined sources
    Beta strandi100 – 1034Combined sources
    Helixi110 – 12617Combined sources
    Beta strandi130 – 1367Combined sources
    Helixi157 – 16711Combined sources
    Beta strandi170 – 1745Combined sources
    Helixi191 – 20010Combined sources
    Beta strandi205 – 2073Combined sources
    Helixi215 – 2239Combined sources
    Beta strandi226 – 2316Combined sources
    Helixi233 – 24917Combined sources
    Helixi256 – 27823Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GVFX-ray1.45A/B1-286[»]
    ProteinModelPortaliP0AB74.
    SMRiP0AB74. Positions 2-284.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AB74.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105D2N. Bacteria.
    COG0191. LUCA.
    HOGENOMiHOG000227793.
    InParanoidiP0AB74.
    KOiK08302.
    OMAiVNTREMF.
    OrthoDBiEOG6HXJ7B.
    PhylomeDBiP0AB74.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01293. TagBP_aldolase_KbaY.
    InterProiIPR013785. Aldolase_TIM.
    IPR000771. Ketose_bisP_aldolase_II.
    IPR023788. TagBP_ald_KbaY.
    IPR011288. TagBP_ald_KbaY/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.

    P0AB74-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSIISTKYLL QDAQANGYAV PAFNIHNAET IQAILEVCSE MRSPVILAGT
    60 70 80 90 100
    PGTFKHIALE EIYALCSAYS TTYNMPLALH LDHHESLDDI RRKVHAGVRS
    110 120 130 140 150
    AMIDGSHFPF AENVKLVKSV VDFCHSQDCS VEAELGRLGG VEDDMSVDAE
    160 170 180 190 200
    SAFLTDPQEA KRFVELTGVD SLAVAIGTAH GLYSKTPKID FQRLAEIREV
    210 220 230 240 250
    VDVPLVLHGA SDVPDEFVRR TIELGVTKVN VATELKIAFA GAVKAWFAEN
    260 270 280
    PQGNDPRYYM RVGMDAMKEV VRNKINVCGS ANRISA
    Length:286
    Mass (Da):31,294
    Last modified:November 8, 2005 - v1
    Checksum:iCAA42DF05C2B918B
    GO

    Mass spectrometryi

    Molecular mass is 31165.9±2.95 Da from positions 2 - 286. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U18997 Genomic DNA. Translation: AAA57940.1.
    U00096 Genomic DNA. Translation: AAC76171.1.
    AP009048 Genomic DNA. Translation: BAE77183.1.
    PIRiE65103.
    RefSeqiNP_417606.1. NC_000913.3.
    WP_000022766.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76171; AAC76171; b3137.
    BAE77183; BAE77183; BAE77183.
    GeneIDi947644.
    KEGGiecj:JW3106.
    eco:b3137.
    PATRICi32121692. VBIEscCol129921_3232.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U18997 Genomic DNA. Translation: AAA57940.1.
    U00096 Genomic DNA. Translation: AAC76171.1.
    AP009048 Genomic DNA. Translation: BAE77183.1.
    PIRiE65103.
    RefSeqiNP_417606.1. NC_000913.3.
    WP_000022766.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GVFX-ray1.45A/B1-286[»]
    ProteinModelPortaliP0AB74.
    SMRiP0AB74. Positions 2-284.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261155. 23 interactions.
    DIPiDIP-47961N.
    IntActiP0AB74. 7 interactions.
    MINTiMINT-1279079.
    STRINGi511145.b3137.

    Proteomic databases

    PaxDbiP0AB74.
    PRIDEiP0AB74.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76171; AAC76171; b3137.
    BAE77183; BAE77183; BAE77183.
    GeneIDi947644.
    KEGGiecj:JW3106.
    eco:b3137.
    PATRICi32121692. VBIEscCol129921_3232.

    Organism-specific databases

    EchoBASEiEB2621.
    EcoGeneiEG12768. kbaY.

    Phylogenomic databases

    eggNOGiENOG4105D2N. Bacteria.
    COG0191. LUCA.
    HOGENOMiHOG000227793.
    InParanoidiP0AB74.
    KOiK08302.
    OMAiVNTREMF.
    OrthoDBiEOG6HXJ7B.
    PhylomeDBiP0AB74.

    Enzyme and pathway databases

    UniPathwayiUPA00704; UER00716.
    BioCyciEcoCyc:TAGAALDOL1-MONOMER.
    ECOL316407:JW3106-MONOMER.
    MetaCyc:TAGAALDOL1-MONOMER.
    BRENDAi4.1.2.40. 2026.
    SABIO-RKP0AB74.

    Miscellaneous databases

    EvolutionaryTraceiP0AB74.
    PROiP0AB74.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01293. TagBP_aldolase_KbaY.
    InterProiIPR013785. Aldolase_TIM.
    IPR000771. Ketose_bisP_aldolase_II.
    IPR023788. TagBP_ald_KbaY.
    IPR011288. TagBP_ald_KbaY/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 / MG1655 / ATCC 47076.
    2. "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.
    3. "Novel phosphotransferase genes revealed by bacterial genome sequencing: a gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in Escherichia coli."
      Reizer J., Ramseier T.M., Reizer A., Charbit A., Saier M.H. Jr.
      Microbiology 142:231-250(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISCUSSION OF SEQUENCE.
    4. "Exploring substrate binding and discrimination in fructose 1,6-bisphosphate and tagatose 1,6-bisphosphate aldolases."
      Zgiby S.M., Thomson G.J., Qamar S., Berry A.
      Eur. J. Biochem. 267:1858-1868(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, MASS SPECTROMETRY, SUBUNIT.
      Strain: K12 / MG1655 / ATCC 47076.
    5. "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, COMPLEX WITH KBAZ.
      Strain: K12.
    6. "Structure of tagatose-1,6-bisphosphate aldolase. Insight into chiral discrimination, mechanism, and specificity of class II aldolases."
      Hall D.R., Bond C.S., Leonard G.A., Watt C.I., Berry A., Hunter W.N.
      J. Biol. Chem. 277:22018-22024(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH ZINC AND TRANSITION STATE ANALOG, ACTIVE SITE.

    Entry informationi

    Entry nameiKBAY_ECOLI
    AccessioniPrimary (citable) accession number: P0AB74
    Secondary accession number(s): P42908, Q2M973
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: November 8, 2005
    Last modified: June 8, 2016
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In contrast to E.coli strains C and EC3132, K-12 strains cannot grow on N-acetylgalactosamine and D-galactosamine, because they carry a deletion and thus lack active PTS systems specific for these compounds. Therefore, KbaYZ in K-12 strains is not involved in the degradation of these compounds.

    Keywords - Technical termi

    3D-structure, Complete proteome, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.