Protein profile

KP13_03141

Uridine kinase

Genome: KpKP13

Gene: AHE43644.1 udk Structure source: AlphaFold + ColabFold UniProt A0A0H3GVV7
Amino acids 213
Annotations 9
Features 25
PDB binders 12
Druggability 0.556

Overview

Basic information about this protein and its source genome.

Accession
KP13_03141
Gene
AHE43644.1 udk
Status
annotated
Amino acids
213
Structure source
AlphaFold + ColabFold

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
37.624
Human E-value
2.91e-42
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
68.159
DEG E-value
6.6999999999999994e-105
Localization
Cytoplasmic
ColabFold pLDDT
95.52

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 0.556
Structure A0A0H3GVV7
Pocket Pocket 1
P2Rank 0.874
Structure A0A0H3GVV7
Pocket Pocket 1
ColabFold model
FPocket 0.696 · Pocket 1
P2Rank 0.872 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 370 / 4744 genomes with a hit
Normalized 0.078

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

8
  • GO:0016773 Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to an alcohol group (acceptor).
  • GO:0004849 Catalysis of the reaction: ATP + uridine = ADP + UMP.
  • GO:0016301 Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0043771 Catalysis of the reaction: ATP + cytidine = ADP + CMP.
  • GO:0044211 Any process which produces cytidine 5'-triphosphate (CTP) from derivatives of it, without de novo synthesis.
  • GO:0044206 Any process which produces UMP, uridine monophosphate, from derivatives of it (e.g. cytidine, uridine, cytosine) without de novo synthesis.

Sequence Features

Domain/signature hits from InterPro and related databases.

25 records
Show feature table
Start End DB Term Name
10 208 CDD cd02023 UMPK
10 208 InterPro IPR000764 Uridine kinase-like
21 213 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
16 20 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
1 20 Phobius SIGNAL_PEPTIDE Signal peptide region
5 213 Hamap MF_00551 Uridine kinase [udk].
5 213 InterPro IPR026008 Uridine kinase
1 7 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
5 213 Gene3D G3DSA:3.40.50.300 -
5 213 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
7 213 FunFam G3DSA:3.40.50.300:FF:000252 Uridine kinase
10 199 Pfam PF00485 Phosphoribulokinase / Uridine kinase family
10 199 InterPro IPR006083 Phosphoribulokinase/uridine kinase
8 205 SUPERFAMILY SSF52540 P-loop containing nucleoside triphosphate hydrolases
8 205 InterPro IPR027417 P-loop containing nucleoside triphosphate hydrolase
8 15 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
6 213 NCBIfam TIGR00235 uridine kinase
6 213 InterPro IPR000764 Uridine kinase-like
9 190 PANTHER PTHR10285 URIDINE KINASE
157 168 PRINTS PR00988 Uridine kinase signature
8 25 PRINTS PR00988 Uridine kinase signature
87 102 PRINTS PR00988 Uridine kinase signature
143 153 PRINTS PR00988 Uridine kinase signature
179 192 PRINTS PR00988 Uridine kinase signature
42 53 PRINTS PR00988 Uridine kinase signature

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...

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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_A0A0H3GVV7
AlphaFold full sequence Viewing
ColabFold KP13_03141
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 0.556
3 0.484
6 0.455

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 16.6 0.782
2 1.04 0.006

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.

64 records

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
0JR B5XYG3 309.4 Da LogP -0.42 TPSA 111.6 ✓ Ro5 ✓ Clean CC(C)(CO)[C@H](C(=O)NCCC(=O)NCc1cccnc1)O
ACP Q5SKR5 505.2 Da LogP -1.52 TPSA 269.9 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
CTN Q5SKR5 243.2 Da LogP -2.56 TPSA 130.8 ✓ Ro5 ✓ Clean C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…
DTT Q31PL2 154.3 Da LogP -0.43 TPSA 40.5 ✓ Ro5 ✓ Clean C([C@@H]([C@H](CS)O)O)S
G6P Q31PL2 260.1 Da LogP -3.10 TPSA 156.9 1 viol. ✓ Clean C([C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O)O)O)O)OP…
KEA Q9BZX2 348.2 Da LogP -1.13 TPSA 205.9 ✓ Ro5 Alert C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…
OS A0A0H3K6J7 190.2 Da LogP -0.00 TPSA 0.0 ✓ Ro5 ✓ Clean [Os+3]
P6D Q9BZX2 C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…
PN4 B5XYG3 288.4 Da LogP 0.18 TPSA 98.7 ✓ Ro5 ✓ Clean CCCCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO)O
SH2 B5XYG3 366.4 Da LogP -0.04 TPSA 117.1 ✓ Ro5 ✓ Clean CC(C)(CO)[C@H](C(=O)NCCC(=O)NCCc1ccc2c(c1)OCO2)O
UZ0 Q9BZX2 269.2 Da LogP -1.53 TPSA 153.3 ✓ Ro5 Alert C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…
UZR Q9BZX2 350.2 Da LogP -2.18 TPSA 201.4 ✓ Ro5 Alert C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)C…

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.