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Protein

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

Gene

kbaY

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

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.

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 KbaZ (kbaZ), D-tagatose-1,6-bisphosphate aldolase subunit KbaY (kbaY), D-tagatose-1,6-bisphosphate aldolase subunit GatY (gatY), D-tagatose-1,6-bisphosphate aldolase subunit GatZ (gatZ)
    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)DescriptionActionsGraphical viewLength
    Active sitei82Proton donor1 Publication1
    Metal bindingi83Zinc; catalytic1 Publication1
    Metal bindingi180Zinc; catalytic1 Publication1
    Binding sitei181Dihydroxyacetone phosphate; via amide nitrogen1
    Metal bindingi208Zinc; catalytic1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionLyase
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:TAGAALDOL1-MONOMER
    MetaCyc:TAGAALDOL1-MONOMER
    BRENDAi4.1.2.40 2026
    SABIO-RKiP0AB74
    UniPathwayi
    UPA00704;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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG12768 kbaY

    Subcellular locationi

    GO - Cellular componenti

    Pathology & Biotechi

    Chemistry databases

    DrugBankiDB03026 Phosphoglycolohydroxamic Acid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001787631 – 286D-tagatose-1,6-bisphosphate aldolase subunit KbaYAdd BLAST286

    Proteomic databases

    PaxDbiP0AB74
    PRIDEiP0AB74

    Interactioni

    Subunit structurei

    Homotetramer. Forms a complex with KbaZ.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    rplLP0A7K22EBI-543669,EBI-543702

    GO - Molecular functioni

    Protein-protein interaction databases

    BioGridi4261155, 23 interactors
    DIPiDIP-47961N
    IntActiP0AB74, 7 interactors
    STRINGi316385.ECDH10B_3310

    Structurei

    Secondary structure

    1286
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    ProteinModelPortaliP0AB74
    SMRiP0AB74
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AB74

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni209 – 211Dihydroxyacetone phosphate binding3
    Regioni230 – 233Dihydroxyacetone phosphate binding4

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105D2N Bacteria
    COG0191 LUCA
    HOGENOMiHOG000227793
    InParanoidiP0AB74
    KOiK08302
    OMAiELCKDCI
    PhylomeDBiP0AB74

    Family and domain databases

    Gene3Di3.20.20.70, 1 hit
    HAMAPiMF_01293 TagBP_aldolase_KbaY, 1 hit
    InterProiView protein in InterPro
    IPR013785 Aldolase_TIM
    IPR000771 FBA_II
    IPR023788 TagBP_ald_KbaY
    IPR011288 TagBP_ald_KbaY/GatY
    PfamiView protein in Pfam
    PF01116 F_bP_aldolase, 1 hit
    PIRSFiPIRSF001359 F_bP_aldolase_II, 1 hit
    TIGRFAMsiTIGR00167 cbbA, 1 hit
    TIGR01858 tag_bisphos_ald, 1 hit
    PROSITEiView protein in PROSITE
    PS00602 ALDOLASE_CLASS_II_1, 1 hit
    PS00806 ALDOLASE_CLASS_II_2, 1 hit

    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
    PATRICifig|1411691.4.peg.3593

    Similar proteinsi

    Entry informationi

    Entry nameiKBAY_ECOLI
    AccessioniPrimary (citable) accession number: P0AB74
    Secondary accession number(s): P42908, Q2M973
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: November 8, 2005
    Last modified: March 28, 2018
    This is version 100 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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