Protein profile

KP13_04728

putative glucose-6-phosphate 1-epimerase

Genome: KpKP13

Gene: AHE45074.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GRG2
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Amino acids 294
Annotations 7
Features 11
PDB binders 0
Druggability 0.171

Overview

Basic information about this protein and its source genome.

Accession
KP13_04728
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE45074.1
Status
annotated
Amino acids
294
Structure source
AlphaFold + ColabFold
EC
5.1.3.15
GO
GO:0016853 Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5. GO:0030246 Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates. GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. 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:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0047938 Catalysis of the reaction: alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate.

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
97.97

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 0.171
Structure A0A0H3GRG2
Pocket Pocket 7
P2Rank 0.732
Structure A0A0H3GRG2
Pocket Pocket 1
ColabFold model
FPocket 0.361 · Pocket 8
P2Rank 0.853 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 106 / 4744 genomes with a hit
Normalized 0.022

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

6
  • GO:0016853 Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.
  • GO:0030246 Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.
  • GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
  • 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:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0047938 Catalysis of the reaction: alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate.

Sequence Features

Domain/signature hits from InterPro and related databases.

11 records
Show feature table
Start End DB Term Name
28 268 Pfam PF01263 Aldose 1-epimerase
28 268 InterPro IPR008183 Aldose 1-/Glucose-6-phosphate 1-epimerase
1 294 Gene3D G3DSA:2.70.98.10 -
1 294 InterPro IPR014718 Glycoside hydrolase-type carbohydrate-binding
8 274 SUPERFAMILY SSF74650 Galactose mutarotase-like
8 274 InterPro IPR011013 Galactose mutarotase-like domain superfamily
10 294 PIRSF PIRSF016020 PHexose_mutarotase
10 294 InterPro IPR025532 Glucose-6-phosphate 1-epimerase
29 290 CDD cd09020 D-hex-6-P-epi_like
29 290 InterPro IPR025532 Glucose-6-phosphate 1-epimerase
26 291 PANTHER PTHR11122 APOSPORY-ASSOCIATED PROTEIN C-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

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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_A0A0H3GRG2
AlphaFold — — full sequence — Viewing
ColabFold KP13_04728
ColabFold — — full sequence — Loaded
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

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 11.89 0.63
2 2.04 0.045
3 1.29 0.013