P9WID3 · PFKB_MYCTU

Function

function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (PubMed:33540748).
Can also catalyze the phosphorylation of tagatose-6-phosphate. The catalytic efficiency with tagatose-6-phosphate is about 1.8 times lower than that with fructose 6-phosphate (PubMed:33540748).
Can use phosphate donors other than ATP (GTP and ITP), with lower efficiency (PubMed:33540748).
In addition, can catalyze the reverse gluconeogenic reaction, albeit with low efficiency (PubMed:33540748).
May support and maintain basic glycolysis and metabolic fluxes during conditions inhibiting PfkA (PubMed:33540748).

Miscellaneous

Activity of PfkB is tenfold lower than that of PfkA (PubMed:33540748).
Activity with tagatose-6-phosphate suggests that PfkA and/or PfkB may substitute for tagatose-6-phosphate kinase and further support glycolysis (PubMed:33540748).
Was identified as a high-confidence drug target.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: The magnesium does not function as an allosteric effector but is essential for glycolytic reaction.

Activity regulation

Not inhibited by an excess of substrates and common allosteric inhibitors. Inhibited by high concentrations of the reaction products, fructose 1,6-bisphosphate and ADP.

Biotechnology

Has strong T-cell and IFN-gamma inducing capacity in human tuberculin skin test positive patients, indicating this might be a good vaccine candidate.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.04 mMfructose 6-phosphate
0.052 mMATP
0.09 mMtagatose-6-phosphate
17.5 mMfructose 1,6-bisphosphate (for gluconeogenic reaction)
12.9 mMADP (for gluconeogenic reaction)
0.27 mMIDP (for gluconeogenic reaction)
0.28 mMGDP (for gluconeogenic reaction)
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
1.2 μmol/min/mgwith fructose 6-phosphate as substrate
0.8 μmol/min/mgwith ATP as substrate
1.5 μmol/min/mgwith tagatose-6-phosphate as substrate
0.39 μmol/min/mgwith fructose 1,6-bisphosphate as substrate (for gluconeogenic reaction)
3.6 μmol/min/mgwith ADP as substrate (for gluconeogenic reaction)
0.37 μmol/min/mgwith IDP as substrate (for gluconeogenic reaction)
0.32 μmol/min/mgwith GDP as substrate (for gluconeogenic reaction)

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site22-24substrate
Binding site37ATP (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site37-39substrate
Binding site49-53substrate
Binding site100-102substrate
Binding site150substrate
Binding site194-196ATP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site199Mg2+ (UniProtKB | ChEBI); catalytic
Binding site233-238ATP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site259K+ (UniProtKB | ChEBI)
Binding site261K+ (UniProtKB | ChEBI)
Active site265
Binding site265substrate
Binding site295K+ (UniProtKB | ChEBI)
Binding site298K+ (UniProtKB | ChEBI)
Binding site300K+ (UniProtKB | ChEBI)
Binding site302K+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function6-phosphofructokinase activity
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functiontagatose-6-phosphate kinase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent 6-phosphofructokinase isozyme 2
  • EC number
  • Short names
    ATP-PFK 2; Phosphofructokinase 2
  • Alternative names
    • Phosphofructokinase B
    • Phosphohexokinase 2
    • Tagatose-6-phosphate kinase
      (EC:2.7.1.144
      ) . EC:2.7.1.144 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      pfkB
    • Ordered locus names
      Rv2029c

Organism names

Accessions

  • Primary accession
    P9WID3
  • Secondary accessions
    • L0T8F1
    • O86352
    • Q7D7L4

Proteomes

Organism-specific databases

Subcellular Location

Phenotypes & Variants

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, cross-link.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylthreonine
ChainPRO_00003929122-339ATP-dependent 6-phosphofructokinase isozyme 2
Cross-link283Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

Keywords

Proteomic databases

PTM databases

Expression

Induction

A member of the dormancy regulon. Induced in response to reduced oxygen tension (hypoxia), low levels of nitric oxide (NO) and carbon monoxide (CO). It is hoped that this regulon will give insight into the latent, or dormant phase of infection.

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the carbohydrate kinase PfkB family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    339
  • Mass (Da)
    35,401
  • Last updated
    2014-04-16 v1
  • Checksum
    D773E363FF73DADD
MTEPAAWDEGKPRIITLTMNPALDITTSVDVVRPTEKMRCGAPRYDPGGGGINVARIVHVLGGCSTALFPAGGSTGSLLMALLGDAGVPFRVIPIAASTRESFTVNESRTAKQYRFVLPGPSLTVAEQEQCLDELRGAAASAAFVVASGSLPPGVAADYYQRVADICRRSSTPLILDTSGGGLQHISSGVFLLKASVRELRECVGSELLTEPEQLAAAHELIDRGRAEVVVVSLGSQGALLATRHASHRFSSIPMTAVSGVGAGDAMVAAITVGLSRGWSLIKSVRLGNAAGAAMLLTPGTAACNRDDVERFFELAAEPTEVGQDQYVWHPIVNPEASP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL123456
EMBL· GenBank· DDBJ
CCP44802.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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