Protein profile

KP13_03769

Histidinol-phosphate aminotransferase

Genome: KpKP13

Gene: AHE43694.1 hisC Structure source: Experimental + ColabFold UniProt A6TBC4
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Amino acids 353
Annotations 6
Features 17
PDB binders 4
Druggability 0.775

Overview

Basic information about this protein and its source genome.

Accession
KP13_03769
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE43694.1 hisC
Status
annotated
Amino acids
353
Structure source
Experimental + ColabFold
GO
GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. GO:0004400 Catalysis of the reaction: L-histidinol-phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid. GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones. GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2. 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 (%)
30.734
Human E-value
1.3e-08
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
59.195
DEG E-value
5.989999999999999e-159
Localization
Cytoplasmic
ColabFold pLDDT
97.3

Selected Druggability evidence

PDB experimental structure

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 0.775
Structure 7SZP
Pocket Pocket 1
P2Rank 0.811
Structure 7SZP
Pocket Pocket 1
ColabFold model
FPocket 0.439 · Pocket 1
P2Rank 0.878 · Pocket 1
Core conservation Accessory gene
Roary core
CoreCruncher accessory
Gut microbiome 139 / 4744 genomes with a hit
Normalized 0.029

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

6
  • GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
  • GO:0004400 Catalysis of the reaction: L-histidinol-phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate.
  • GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.
  • GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.
  • GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

17 records
Show feature table
Start End DB Term Name
8 349 NCBIfam TIGR01141 histidinol-phosphate transaminase
8 349 InterPro IPR005861 Histidinol-phosphate aminotransferase family
28 348 CDD cd00609 AAT_like
6 352 Hamap MF_01023 Histidinol-phosphate aminotransferase [hisC].
6 352 InterPro IPR005861 Histidinol-phosphate aminotransferase family
6 344 Gene3D G3DSA:3.90.1150.10 Aspartate Aminotransferase, domain 1
6 344 InterPro IPR015422 Pyridoxal phosphate-dependent transferase, small domain
208 217 ProSitePatterns PS00599 Aminotransferases class-II pyridoxal-phosphate attachment site.
208 217 InterPro IPR001917 Aminotransferase, class-II, pyridoxal-phosphate binding site
51 255 Gene3D G3DSA:3.40.640.10 -
51 255 InterPro IPR015421 Pyridoxal phosphate-dependent transferase, major domain
44 348 Pfam PF00155 Aminotransferase class I and II
44 348 InterPro IPR004839 Aminotransferase, class I/classII
5 349 SUPERFAMILY SSF53383 PLP-dependent transferases
5 349 InterPro IPR015424 Pyridoxal phosphate-dependent transferase
7 348 PANTHER PTHR42885 HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED
51 255 FunFam G3DSA:3.40.640.10:FF:000032 Histidinol-phosphate aminotransferase

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

1 + 1

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

Entry Method Resolution Chain Coverage Links Status
PDB 7SZP
X-ray 20.00 Å - —
PDBe RCSB PDBj File
Viewing
ColabFold KP13_03769
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 0.915
4 0.601
3 0.511
5 0.448

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 34.26 0.949
2 32.82 0.945
3 31.46 0.939
4 28.68 0.927
5 6.17 0.307

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.

54 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
144
3CQ5
Q9KJU4 122.1 Da LogP -1.72 TPSA 60.7 ✓ Ro5 ✓ Clean C[N+](CO)(CO)CO
HSA
1FG3
P06986 221.2 Da LogP -0.61 TPSA 121.5 ✓ Ro5 ✓ Clean c1c(nc[nH]1)CC(COP(=O)(O)O)N
PMP
1FG7
P06986 248.2 Da LogP 0.16 TPSA 125.9 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)COP(=O)(O)O)CN)O
SIN
4R5Z
P9WML5 118.1 Da LogP -0.06 TPSA 74.6 ✓ Ro5 ✓ Clean C(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.