Protein profile

VK055_2541

[citrate (pro-3S)-lyase] ligase

Genome: KpATCC43816

Gene: AIK81138.1 citC Structure source: AlphaFold + ColabFold UniProt A0A0H3GN23
Export view
Amino acids 342
Annotations 7
Features 24
PDB binders 0
Druggability 0.209

Overview

Basic information about this protein and its source genome.

Accession
VK055_2541
Assembly
Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene
AIK81138.1 citC
Status
annotated
Amino acids
342
Structure source
AlphaFold + ColabFold
EC
6.2.1.22
GO
GO:0016747 Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor). 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: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. GO:0008771 Catalysis of the reaction: ATP + acetate + (citrate (pro-3S)-lyase) (thiol form) = AMP + diphosphate + (citrate (pro-3S)-lyase) (acetyl form). GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.

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 (%)
50.294
DEG E-value
1.47e-118
Localization
Cytoplasmic
ColabFold pLDDT
92.71

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 0.209
Structure A0A0H3GN23
Pocket Pocket 23
P2Rank 0.948
Structure A0A0H3GN23
Pocket Pocket 1
ColabFold model
FPocket 0.797 · Pocket 1
P2Rank 0.943 · Pocket 1
Core conservation Accessory gene
Roary accessory
CoreCruncher accessory
Gut microbiome 78 / 4744 genomes with a hit
Normalized 0.016

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

6
  • GO:0016747 Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor).
  • 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: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.
  • GO:0008771 Catalysis of the reaction: ATP + acetate + (citrate (pro-3S)-lyase) (thiol form) = AMP + diphosphate + (citrate (pro-3S)-lyase) (acetyl form).
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.

Sequence Features

Domain/signature hits from InterPro and related databases.

24 records
Show feature table
Start End DB Term Name
142 342 FunFam G3DSA:3.40.50.620:FF:000071 [Citrate [pro-3S]-lyase] ligase
8 118 Gene3D G3DSA:3.40.630.30 -
145 333 SUPERFAMILY SSF52374 Nucleotidylyl transferase
146 331 SMART SM00764 citrate_ly_lig5
146 331 InterPro IPR013166 Citrate lyase ligase, C-terminal
15 116 SUPERFAMILY SSF55729 Acyl-CoA N-acyltransferases (Nat)
15 116 InterPro IPR016181 Acyl-CoA N-acyltransferase
28 331 CDD cd02169 Citrate_lyase_ligase
28 331 InterPro IPR005216 Citrate lyase ligase
21 103 Pfam PF00583 Acetyltransferase (GNAT) family
21 103 InterPro IPR000182 GNAT domain
1 342 PIRSF PIRSF005751 Acet_citr_lig
1 342 InterPro IPR005216 Citrate lyase ligase
3 339 PANTHER PTHR40599 [CITRATE [PRO-3S]-LYASE] LIGASE
3 339 InterPro IPR005216 Citrate lyase ligase
146 203 NCBIfam TIGR00125 cytidyltransferase-like domain
146 203 InterPro IPR004821 Cytidyltransferase-like domain
5 340 NCBIfam TIGR00124 [citrate (pro-3S)-lyase] ligase
5 340 InterPro IPR005216 Citrate lyase ligase
142 342 Gene3D G3DSA:3.40.50.620 HUPs
142 342 InterPro IPR014729 Rossmann-like alpha/beta/alpha sandwich fold
146 331 Pfam PF08218 Citrate lyase ligase C-terminal domain
1 127 ProSiteProfiles PS51186 Gcn5-related N-acetyltransferase (GNAT) domain profile.
1 127 InterPro IPR000182 GNAT domain

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...

Legend High Medium Low

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_A0A0H3GN23
AlphaFold — — full sequence — Viewing
ColabFold VK055_2541
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
23 0.209

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 24.17 0.896
2 4.51 0.192
3 3.25 0.113