Protein profile

KP13_00556

N-acetyl-gamma-glutamyl-phosphate reductase

Genome: KpKP13

Gene: argC AHE47032.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GH05
Export view
Amino acids 334
Annotations 9
Features 20
PDB binders 8
Druggability 0.239

Overview

Basic information about this protein and its source genome.

Accession
KP13_00556
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
argC AHE47032.1
Status
annotated
Amino acids
334
Structure source
AlphaFold + ColabFold
EC
1.2.1.38
GO
GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH. GO:0016620 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces NAD or NADP. GO:0046983 The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. GO:0070401 Binding to the oxidized form, NADP+, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions. GO:0003942 Catalysis of the reaction: N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH + H+. GO:0006526 The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
88.024
DEG E-value
0.0
Localization
Cytoplasmic
ColabFold pLDDT
98.45

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 0.239
Structure A0A0H3GH05
Pocket Pocket 11
P2Rank 0.937
Structure A0A0H3GH05
Pocket Pocket 1
ColabFold model
FPocket 0.326 · Pocket 16
P2Rank 0.921 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 147 / 4744 genomes with a hit
Normalized 0.031

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:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
  • GO:0016620 Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces NAD or NADP.
  • GO:0046983 The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
  • GO:0070401 Binding to the oxidized form, NADP+, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions.
  • GO:0003942 Catalysis of the reaction: N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH + H+.
  • GO:0006526 The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
  • GO:0008652 The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

Sequence Features

Domain/signature hits from InterPro and related databases.

20 records
Show feature table
Start End DB Term Name
154 308 SUPERFAMILY SSF55347 Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
1 171 SUPERFAMILY SSF51735 NAD(P)-binding Rossmann-fold domains
1 171 InterPro IPR036291 NAD(P)-binding domain superfamily
4 164 FunFam G3DSA:3.40.50.720:FF:000117 N-acetyl-gamma-glutamyl-phosphate reductase
163 311 Pfam PF02774 Semialdehyde dehydrogenase, dimerisation domain
163 311 InterPro IPR012280 Semialdehyde dehydrogenase, dimerisation domain
2 334 Hamap MF_00150 N-acetyl-gamma-glutamyl-phosphate reductase [argC].
2 334 InterPro IPR000706 N-acetyl-gamma-glutamyl-phosphate reductase, type 1
3 333 PANTHER PTHR32338 N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED
149 165 ProSitePatterns PS01224 N-acetyl-gamma-glutamyl-phosphate reductase active site.
149 165 InterPro IPR023013 N-acetyl-gamma-glutamyl-phosphate reductase, active site
6 330 Gene3D G3DSA:3.40.50.720 -
3 146 SMART SM00859 Semialdhyde_dh_3
3 146 InterPro IPR000534 Semialdehyde dehydrogenase, NAD-binding
5 146 Pfam PF01118 Semialdehyde dehydrogenase, NAD binding domain
5 146 InterPro IPR000534 Semialdehyde dehydrogenase, NAD-binding
152 308 FunFam G3DSA:3.30.360.10:FF:000014 N-acetyl-gamma-glutamyl-phosphate reductase
3 333 NCBIfam TIGR01850 N-acetyl-gamma-glutamyl-phosphate reductase
3 333 InterPro IPR000706 N-acetyl-gamma-glutamyl-phosphate reductase, type 1
153 312 Gene3D G3DSA:3.30.360.10 Dihydrodipicolinate Reductase; domain 2

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_A0A0H3GH05
AlphaFold — — full sequence — Viewing
ColabFold KP13_00556
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
11 0.239

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 19.6 0.842
2 1.8 0.034

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

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
AZI
2OZP
Q5SH26 42.0 Da LogP 0.87 TPSA 58.7 ✓ Ro5 Alert [N-]=[N+]=[N-]
BTB
2I3A
P9WPZ9 209.2 Da LogP -3.01 TPSA 104.4 ✓ Ro5 ✓ Clean C(CO)N(CCO)C(CO)(CO)CO
MLA
1YS4
Q57658 104.1 Da LogP -0.45 TPSA 74.6 ✓ Ro5 ✓ Clean C(C(=O)O)C(=O)O
MLT
3DR3
P59310 134.1 Da LogP -1.09 TPSA 94.8 ✓ Ro5 ✓ Clean C([C@H](C(=O)O)O)C(=O)O
MYI
7NOT
P9WPZ9 205.2 Da LogP 1.80 TPSA 62.3 ✓ Ro5 ✓ Clean COc1ccc2c(c1)c(c[nH]2)CC(=O)O
UJQ
7NNR
P9WPZ9 226.2 Da LogP 3.01 TPSA 46.5 ✓ Ro5 ✓ Clean c1ccc2c(c1)C(c3ccccc3O2)C(=O)O
UKE
7NPH
P9WPZ9 193.2 Da LogP 1.53 TPSA 72.6 ✓ Ro5 ✓ Clean COc1ccc2c(c1)nc(o2)C(=O)O
UKK
7NPJ
P9WPZ9 186.2 Da LogP 2.46 TPSA 48.1 ✓ Ro5 Alert c1ccc(cc1)Oc2ccc(cn2)N

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.