Protein profile

KP13_00029

Glucosamine--fructose-6-phosphate aminotransferase isomerizing

Genome: KpKP13

Gene: AHE47138.1 glmS Structure source: AlphaFold + ColabFold UniProt A0A0H3H4X5

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Amino acids 609

Annotations 11

Features 33

PDB binders 7

Druggability 0.989

Overview

Basic information about this protein and its source genome.

Accession: KP13_00029
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE47138.1 glmS
Status: annotated
Amino acids: 609
Structure source: AlphaFold + ColabFold

2.6.1.16

GO:1901135 The chemical reactions and pathways involving carbohydrate derivative. GO:0097367 Binding to a carbohydrate derivative. GO:0004360 Catalysis of the reaction: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate. GO:1901137 The chemical reactions and pathways resulting in the formation of carbohydrate derivative. GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0046349 The chemical reactions and pathways resulting in the formation of any amino sugar, sugars containing an amino group in place of a hydroxyl group.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 40.93
Human E-value: 4.81e-94
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 92.447
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 94.29

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 0.989

Structure A0A0H3H4X5

Pocket Pocket 1

P2Rank 0.712

Structure A0A0H3H4X5

Pocket Pocket 1

ColabFold model

FPocket 0.962 · Pocket 1

P2Rank 0.759 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 277 / 4744 genomes with a hit

Normalized 0.058

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)

2.6.1.16

Gene Ontology (GO)

GO:1901135 The chemical reactions and pathways involving carbohydrate derivative.
GO:0097367 Binding to a carbohydrate derivative.
GO:0004360 Catalysis of the reaction: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate.
GO:1901137 The chemical reactions and pathways resulting in the formation of carbohydrate derivative.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0046349 The chemical reactions and pathways resulting in the formation of any amino sugar, sugars containing an amino group in place of a hydroxyl group.
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:0006002 The chemical reactions and pathways involving fructose 6-phosphate, also known as F6P. The D-enantiomer is an important intermediate in glycolysis, gluconeogenesis, and fructose metabolism.
GO:0006487 A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of an asparagine residue.
GO:0006047 The chemical reactions and pathways involving UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.

Sequence Features

Domain/signature hits from InterPro and related databases.

33 records

Show feature table

Start	End	DB	Term	Name
2	241	Gene3D	G3DSA:3.60.20.10	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
2	241	InterPro	IPR029055	Nucleophile aminohydrolases, N-terminal
286	426	ProSiteProfiles	PS51464	SIS domain profile.
286	426	InterPro	IPR001347	SIS domain
2	609	NCBIfam	TIGR01135	glutamine--fructose-6-phosphate transaminase (isomerizing)
2	609	InterPro	IPR005855	Glucosamine-fructose-6-phosphate aminotransferase, isomerising
447	594	Gene3D	G3DSA:3.40.50.10490	-
2	232	SUPERFAMILY	SSF56235	N-terminal nucleophile aminohydrolases (Ntn hydrolases)
2	232	InterPro	IPR029055	Nucleophile aminohydrolases, N-terminal
458	599	ProSiteProfiles	PS51464	SIS domain profile.
458	599	InterPro	IPR001347	SIS domain
453	607	CDD	cd05009	SIS_GlmS_GlmD_2
453	607	InterPro	IPR035490	GlmS/FrlB, SIS domain 2
451	594	FunFam	G3DSA:3.40.50.10490:FF:000002	Glutamine--fructose-6-phosphate aminotransferase [isomerizing]
1	609	Hamap	MF_00164	Glutamine--fructose-6-phosphate aminotransferase [isomerizing] [glmS].
1	609	InterPro	IPR005855	Glucosamine-fructose-6-phosphate aminotransferase, isomerising
289	418	Pfam	PF01380	SIS domain
289	418	InterPro	IPR001347	SIS domain
462	591	Pfam	PF01380	SIS domain
462	591	InterPro	IPR001347	SIS domain
248	608	Gene3D	G3DSA:3.40.50.10490	-
2	218	ProSiteProfiles	PS51278	Glutamine amidotransferase type 2 domain profile.
2	218	InterPro	IPR017932	Glutamine amidotransferase type 2 domain
2	240	FunFam	G3DSA:3.60.20.10:FF:000006	Glutamine--fructose-6-phosphate aminotransferase [isomerizing]
295	421	CDD	cd05008	SIS_GlmS_GlmD_1
295	421	InterPro	IPR035466	GlmS/AgaS, SIS domain 1
1	609	PANTHER	PTHR10937	GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING
66	174	Pfam	PF13522	Glutamine amidotransferase domain
245	609	SUPERFAMILY	SSF53697	SIS domain
245	609	InterPro	IPR046348	SIS domain superfamily
2	215	CDD	cd00714	GFAT
2	215	InterPro	IPR047084	Glucosamine-fructose-6-phosphate aminotransferase, isomerising, N-terminal domain
247	450	FunFam	G3DSA:3.40.50.10490:FF:000001	Glutamine--fructose-6-phosphate aminotransferase [isomerizing]

3D Structure

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

Loading 3D structure...

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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_A0A0H3H4X5	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_00029	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
1				0.989
35				0.362

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	Score	Probability
1	6.66	0.338
2	4.42	0.186
3	2.84	0.089
4	2.44	0.066
5	1.83	0.035

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
1				0.962

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	Score	Probability
1	8.37	0.446
2	4.84	0.216
3	3.33	0.118
4	1.67	0.028
5	1.45	0.019

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

58 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
AGP	1MOS	P17169	261.2 Da LogP -3.50 TPSA 173.7	1 viol.	✓ Clean	`C([C@@H]([C@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O)…`
F6R	4AMV	P17169	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`C([C@H]([C@H]([C@@H](C(=O)CO)O)O)O)OP(=O)(O)O`
G6Q	1JXA	P17169	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`C([C@H]([C@H]([C@@H]([C@H](C=O)O)O)O)O)OP(=O)(O…`
HGA	1XFG	P17169	162.1 Da LogP -1.32 TPSA 112.7	✓ Ro5	✓ Clean	`C(CC(=O)NO)[C@@H](C(=O)O)N`
M6R	2PUV	P53704	261.2 Da LogP -3.50 TPSA 173.7	1 viol.	✓ Clean	`C([C@H]([C@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O)N…`
UD1	2PUT	P53704	607.4 Da LogP -4.65 TPSA 305.9	3 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@]…`
UD2	6SVM	Q06210-2	607.4 Da LogP -4.65 TPSA 305.9	3 viol.	✓ Clean	`CC(=O)N[C@@H]1[C@H]([C@H]([C@H](O[C@@H]1O[P@@](…`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL1911372	Q06210	6.82	225.0 Da LogP -1.09 TPSA 92.4	✓ Ro5	✓ Clean	`N[C@@H](CNC(=O)CBr)C(=O)O`

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC100033330	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC100065511	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC100067275	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC100085043	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC100889630	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC104861723	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O…`
ZINC104869937	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC12503760	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC12503763	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@H](O)[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC13537943	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC19850142	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC2508229	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC4545927	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@@H](O)COP(=O)(…`
ZINC4545928	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)[C@H](O)COP(=O)(O…`
ZINC4545929	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)COP(=O)(O…`
ZINC85994845	1.000	260.1 Da LogP -3.26 TPSA 164.8	1 viol.	✓ Clean	`O=C(CO)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC5132038	0.897	290.2 Da LogP -3.90 TPSA 185.0	1 viol.	✓ Clean	`O=C(CO)[C@@H](O)[C@H](O)[C@H](O)[C@H](O)COP(=O)…`
ZINC1530556	0.889	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC22116391	0.889	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC3606137	0.889	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC3869426	0.889	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC8551307	0.889	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC8551308	0.889	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC1529626	0.793	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC1532567	0.793	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC1532851	0.793	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC30320708	0.793	230.1 Da LogP -2.62 TPSA 144.5	✓ Ro5	✓ Clean	`O=C(CO)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC1532601	0.750	200.1 Da LogP -1.98 TPSA 124.3	✓ Ro5	✓ Clean	`O=C[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC32786787	0.750	200.1 Da LogP -1.98 TPSA 124.3	✓ Ro5	✓ Clean	`O=C[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC12502210	0.742	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@H](O)[C@@H](O)COP(=O…`
ZINC12502212	0.742	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@H](O)[C@H](O)COP(=O)…`
ZINC12502214	0.742	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@@H](O)[C@@H](O)COP(=…`
ZINC12502216	0.742	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@H](O)[C@@H](O)[C@H](O)COP(=O…`
ZINC4523251	0.742	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@@H](O)[C@@H](O)COP(…`
ZINC4523255	0.742	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@@H](O)[C@H](O)COP(=…`
ZINC4523257	0.742	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@H](O)[C@@H](O)COP(=…`
ZINC4523259	0.742	340.1 Da LogP -3.14 TPSA 211.3	1 viol.	✓ Clean	`O=C(COP(=O)(O)O)[C@@H](O)[C@H](O)[C@H](O)COP(=O…`
ZINC2516111	0.724	262.2 Da LogP -3.47 TPSA 167.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)CO`
ZINC2522704	0.724	262.2 Da LogP -3.47 TPSA 167.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H](O)[C@H](O)[C@@H](O)[C@@H](O)CO`
ZINC3869812	0.724	262.2 Da LogP -3.47 TPSA 167.9	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO`
ZINC100657408	0.710	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@H](C=O)[C@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC215934438	0.710	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@H](C=O)[C@H](O)[C@@H](O)[C@@H](O)COP(=O)(O)O`
ZINC255961849	0.710	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@H](C=O)[C@H](O)[C@H](O)[C@@H](O)COP(=O)(O)O`
ZINC255961850	0.710	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@H](C=O)[C@H](O)[C@@H](O)[C@H](O)COP(=O)(O)O`
ZINC5132021	0.710	259.2 Da LogP -3.30 TPSA 170.5	1 viol.	✓ Clean	`N[C@@H](C=O)[C@@H](O)[C@H](O)[C@H](O)COP(=O)(O)O`
ZINC1532902	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC13518200	0.688	276.2 Da LogP -2.32 TPSA 144.5	1 viol.	✓ Clean	`O=C[C@H](O)[C@@H](O)[C@H](O)[C@H](S)COP(=O)(O)O`
ZINC3593496	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.