Protein profile

KP13_02992

Aldose 1-epimerase

Genome: KpKP13

Gene: AHE45625.1 galM Structure source: AlphaFold + ColabFold UniProt A0A0H3GK63
Amino acids 347
Annotations 11
Features 16
PDB binders 0
Druggability 0.3

Overview

Basic information about this protein and its source genome.

Accession
KP13_02992
Gene
AHE45625.1 galM
Status
annotated
Amino acids
347
Structure source
AlphaFold + ColabFold
EC
GO
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:0006012 The chemical reactions and pathways involving galactose, the aldohexose galacto-hexose. D-galactose is widely distributed in combined form in plants, animals and microorganisms as a constituent of oligo- and polysaccharides; it also occurs in galactolipids and as its glucoside in lactose and melibiose. 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:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. GO:0019318 The chemical reactions and pathways involving a hexose, any monosaccharide with a chain of six carbon atoms in the molecule. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
39.037
Human E-value
1.1999999999999999e-35
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
40.356
DEG E-value
2.2e-81
Localization
Periplasmic
ColabFold pLDDT
97.5

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 0.3
Structure A0A0H3GK63
Pocket Pocket 2
P2Rank 0.791
Structure A0A0H3GK63
Pocket Pocket 1
ColabFold model
FPocket 0.225 · Pocket 1
P2Rank 0.693 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 98 / 4744 genomes with a hit
Normalized 0.021

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

10
  • 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:0006012 The chemical reactions and pathways involving galactose, the aldohexose galacto-hexose. D-galactose is widely distributed in combined form in plants, animals and microorganisms as a constituent of oligo- and polysaccharides; it also occurs in galactolipids and as its glucoside in lactose and melibiose.
  • 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:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
  • GO:0019318 The chemical reactions and pathways involving a hexose, any monosaccharide with a chain of six carbon atoms in the molecule.
  • 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:0004034 Catalysis of the reaction: alpha-D-glucose = beta-D-glucose. Also acts on L-arabinose, D-xylose, D-galactose, maltose and lactose.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0033499 The chemical reactions and pathways resulting in the breakdown of galactose, via the intermediate UDP-galactose.
  • GO:0006006 The chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides.

Sequence Features

Domain/signature hits from InterPro and related databases.

16 records
Show feature table
Start End DB Term Name
172 181 ProSitePatterns PS00545 Aldose 1-epimerase putative active site.
172 181 InterPro IPR018052 Aldose 1-epimerase, conserved site
17 342 Pfam PF01263 Aldose 1-epimerase
17 342 InterPro IPR008183 Aldose 1-/Glucose-6-phosphate 1-epimerase
1 347 PIRSF PIRSF005096 GALM
1 347 InterPro IPR015443 Aldose 1-epimerase
3 344 SUPERFAMILY SSF74650 Galactose mutarotase-like
3 344 InterPro IPR011013 Galactose mutarotase-like domain superfamily
17 344 CDD cd09019 galactose_mutarotase_like
17 344 InterPro IPR047215 Galactose mutarotase-like
12 344 NCBIfam TIGR02636 galactose-1-epimerase
12 344 InterPro IPR013458 Aldose 1-epimerase, bacterial
9 345 FunFam G3DSA:2.70.98.10:FF:000002 Aldose 1-epimerase
8 345 Gene3D G3DSA:2.70.98.10 -
8 345 InterPro IPR014718 Glycoside hydrolase-type carbohydrate-binding
18 344 PANTHER PTHR10091 ALDOSE-1-EPIMERASE

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_A0A0H3GK63
AlphaFold full sequence Viewing
ColabFold KP13_02992
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
2 0.3

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 14.58 0.727
2 2.0 0.043