Protein profile

KP13_04138

putative pyruvate/Phosphoenolpyruvate kinase

Genome: KpKP13

Gene: AHE47488.1 Structure source: AlphaFold + ColabFold UniProt A0A2L1C7S9
Export view
Amino acids 318
Annotations 4
Features 9
PDB binders 0
Druggability 0.732

Overview

Basic information about this protein and its source genome.

Accession
KP13_04138
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE47488.1
Status
annotated
Amino acids
318
Structure source
AlphaFold + ColabFold
GO
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring. GO:0000287 Binding to a magnesium (Mg) ion. GO:0006107 The chemical reactions and pathways involving oxaloacetate, the anion of oxobutanedioic acid, an important intermediate in metabolism, especially as a component of the TCA cycle.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
N
DEG identity (%)
0.0
Localization
Cytoplasmic
ColabFold pLDDT
92.27

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.732
Structure A0A2L1C7S9
Pocket Pocket 13
P2Rank 0.641
Structure A0A2L1C7S9
Pocket Pocket 1
ColabFold model
FPocket 0.698 · Pocket 10
P2Rank 0.543 · Pocket 1
Core conservation Accessory gene
Roary accessory
CoreCruncher accessory
Gut microbiome 20 / 4744 genomes with a hit
Normalized 0.004

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

4
  • GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
  • GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
  • GO:0000287 Binding to a magnesium (Mg) ion.
  • GO:0006107 The chemical reactions and pathways involving oxaloacetate, the anion of oxobutanedioic acid, an important intermediate in metabolism, especially as a component of the TCA cycle.

Sequence Features

Domain/signature hits from InterPro and related databases.

9 records
Show feature table
Start End DB Term Name
4 299 Gene3D G3DSA:3.20.20.60 -
4 299 InterPro IPR040442 Pyruvate kinase-like domain superfamily
1 306 PIRSF PIRSF015582 Cit_lyase_B
1 306 InterPro IPR011206 Citrate lyase beta subunit-like
7 299 Pfam PF15617 C-C_Bond_Lyase of the TIM-Barrel fold
7 299 InterPro IPR039480 C-C bond lyase-like
9 250 SUPERFAMILY SSF51621 Phosphoenolpyruvate/pyruvate domain
9 250 InterPro IPR015813 Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily
11 301 PANTHER PTHR32308 LYASE BETA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13030)-RELATED

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

3D visualization script Full viewer

Loading 3D structure...

Legend High Medium Low

Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A2L1C7S9
AlphaFold — — full sequence — Viewing
ColabFold KP13_04138
ColabFold — — full sequence — Loaded
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET Sticks Spheres Surfaces Druggability Labels Zoom Positions
13 0.732
12 0.304
8 0.294

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 9.05 0.484
2 3.29 0.115
3 2.62 0.076