Protein profile

KP13_02142

Gamma-glutamyl phosphate reductase

Genome: KpKP13

Gene: proA AHE46148.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GNT9
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Amino acids 417
Annotations 8
Features 20
PDB binders 0
Druggability 0.172

Overview

Basic information about this protein and its source genome.

Accession
KP13_02142
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
proA AHE46148.1
Status
annotated
Amino acids
417
Structure source
AlphaFold + ColabFold
EC
1.2.1.41
GO
GO:0006561 OBSOLETE. The chemical reactions and pathways resulting in the formation of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins. GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. GO:0004350 Catalysis of the reaction: L-glutamate 5-semialdehyde + NADP+ + phosphate = L-glutamyl 5-phosphate + H+ + NADPH. 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:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
36.211
Human E-value
2.64e-82
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
50.529
DEG E-value
3.34e-130
Localization
Cytoplasmic
ColabFold pLDDT
95.86

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 0.172
Structure A0A0H3GNT9
Pocket Pocket 3
P2Rank 0.529
Structure A0A0H3GNT9
Pocket Pocket 1
ColabFold model
FPocket 0.163 · Pocket 3
P2Rank 0.482 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 187 / 4744 genomes with a hit
Normalized 0.039

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

7
  • GO:0006561 OBSOLETE. The chemical reactions and pathways resulting in the formation of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.
  • GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
  • GO:0004350 Catalysis of the reaction: L-glutamate 5-semialdehyde + NADP+ + phosphate = L-glutamyl 5-phosphate + H+ + NADPH.
  • 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:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0055129 The chemical reactions and pathways resulting in the formation of L-proline, an L-enantiomer of a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.

Sequence Features

Domain/signature hits from InterPro and related databases.

20 records
Show feature table
Start End DB Term Name
11 413 Gene3D G3DSA:3.40.605.10 Aldehyde Dehydrogenase; Chain A, domain 1
11 413 InterPro IPR016162 Aldehyde dehydrogenase, N-terminal
9 406 NCBIfam TIGR00407 glutamate-5-semialdehyde dehydrogenase
9 406 InterPro IPR000965 GPR domain
1 417 PIRSF PIRSF000151 GPR
1 417 InterPro IPR012134 Glutamate-5-semialdehyde dehydrogenase
222 374 Gene3D G3DSA:3.40.309.10 Aldehyde Dehydrogenase; Chain A, domain 2
222 374 InterPro IPR016163 Aldehyde dehydrogenase, C-terminal
323 344 ProSitePatterns PS01223 Gamma-glutamyl phosphate reductase signature.
323 344 InterPro IPR020593 Gamma-glutamyl phosphate reductase GPR, conserved site
3 416 PANTHER PTHR11063 GLUTAMATE SEMIALDEHYDE DEHYDROGENASE
222 374 FunFam G3DSA:3.40.309.10:FF:000006 Gamma-glutamyl phosphate reductase
3 412 CDD cd07079 ALDH_F18-19_ProA-GPR
3 412 InterPro IPR000965 GPR domain
8 280 Pfam PF00171 Aldehyde dehydrogenase family
8 280 InterPro IPR015590 Aldehyde dehydrogenase domain
3 415 SUPERFAMILY SSF53720 ALDH-like
3 415 InterPro IPR016161 Aldehyde/histidinol dehydrogenase
1 416 Hamap MF_00412 Gamma-glutamyl phosphate reductase [proA].
1 416 InterPro IPR000965 GPR domain

3D Structure

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

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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_A0A0H3GNT9
AlphaFold — — full sequence — Viewing
ColabFold KP13_02142
ColabFold — — full sequence — Loaded
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

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 6.5 0.329
2 2.32 0.06
3 0.96 0.005
4 0.81 0.003