Protein profile

KP13_03250

Oxaloacetate decarboxylase alpha chain

Genome: KpKP13

Gene: AHE45629.1 Structure source: Experimental + AlphaFold + ColabFold UniProt P13187
Export view
Amino acids 590
Annotations 8
Features 25
PDB binders 10
Druggability 0.3

Overview

Basic information about this protein and its source genome.

Accession
KP13_03250
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE45629.1
Status
annotated
Amino acids
590
Structure source
Experimental + AlphaFold + ColabFold
EC
7.2.4.2
GO
GO:0008948 Catalysis of the reaction: H+ + oxaloacetate = CO2 + pyruvate. 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:0006814 The directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0015451 Primary active transport of a solute across a membrane driven by decarboxylation of a cytoplasmic substrate. Primary active transport is catalysis of the transport of a solute across a membrane, up the solute's concentration gradient, by binding the solute and undergoing a series of conformational changes. Transport works equally well in either direction and is driven by a primary energy source. GO:0004736 Catalysis of the reaction: ATP + bicarbonate + pyruvate = ADP + 2 H+ + oxaloacetate + phosphate.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
38.095
Human E-value
3.66e-06
Gut microbiome off-target
hit
Essential (DEG)
N
DEG identity (%)
0.0
Localization
Cytoplasmic
ColabFold pLDDT
90.47

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 0.3
Structure P13187
Pocket Pocket 5
P2Rank 0.911
Structure P13187
Pocket Pocket 1
ColabFold model
FPocket 0.258 · Pocket 9
P2Rank 0.898 · Pocket 1
Core conservation Accessory gene
Roary accessory
CoreCruncher accessory
Gut microbiome 765 / 4744 genomes with a hit
Normalized 0.161

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:0008948 Catalysis of the reaction: H+ + oxaloacetate = CO2 + pyruvate.
  • 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:0006814 The directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0015451 Primary active transport of a solute across a membrane driven by decarboxylation of a cytoplasmic substrate. Primary active transport is catalysis of the transport of a solute across a membrane, up the solute's concentration gradient, by binding the solute and undergoing a series of conformational changes. Transport works equally well in either direction and is driven by a primary energy source.
  • GO:0004736 Catalysis of the reaction: ATP + bicarbonate + pyruvate = ADP + 2 H+ + oxaloacetate + phosphate.
  • GO:0006094 The formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol.

Sequence Features

Domain/signature hits from InterPro and related databases.

25 records
Show feature table
Start End DB Term Name
514 589 Gene3D G3DSA:2.40.50.100 -
517 590 ProSiteProfiles PS50968 Biotinyl/lipoyl domain profile.
517 590 InterPro IPR000089 Biotin/lipoyl attachment
290 489 Pfam PF02436 Conserved carboxylase domain
290 489 InterPro IPR003379 Carboxylase, conserved domain
5 279 CDD cd07937 DRE_TIM_PC_TC_5S
546 563 ProSitePatterns PS00188 Biotin-requiring enzymes attachment site.
546 563 InterPro IPR001882 Biotin-binding site
5 586 NCBIfam TIGR01108 sodium-extruding oxaloacetate decarboxylase subunit alpha
5 586 InterPro IPR005776 Oxaloacetate decarboxylase, alpha subunit
3 263 ProSiteProfiles PS50991 Pyruvate carboxyltransferase domain.
3 263 InterPro IPR000891 Pyruvate carboxyltransferase
524 589 CDD cd06850 biotinyl_domain
515 589 SUPERFAMILY SSF51230 Single hybrid motif
515 589 InterPro IPR011053 Single hybrid motif
5 589 PANTHER PTHR45266 OXALOACETATE DECARBOXYLASE ALPHA CHAIN
515 590 FunFam G3DSA:2.40.50.100:FF:000003 Acetyl-CoA carboxylase biotin carboxyl carrier protein
3 298 SUPERFAMILY SSF51569 Aldolase
524 589 Pfam PF00364 Biotin-requiring enzyme
524 589 InterPro IPR000089 Biotin/lipoyl attachment
295 454 SUPERFAMILY SSF89000 post-HMGL domain-like
1 462 Gene3D G3DSA:3.20.20.70 Aldolase class I
1 462 InterPro IPR013785 Aldolase-type TIM barrel
3 268 Pfam PF00682 HMGL-like
3 268 InterPro IPR000891 Pyruvate carboxyltransferase

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 + 2

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

Entry Method Resolution Chain Coverage Links Status
PDB 6ROJ
X-ray 20.00 Å - —
PDBe RCSB PDBj File
Viewing
AlphaFold AF_P13187
AlphaFold — — full sequence — Loaded
ColabFold KP13_03250
ColabFold — — full sequence — Loaded
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

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.

60 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
2KT
1RR2
Q70AC7 102.1 Da LogP 0.05 TPSA 54.4 ✓ Ro5 ✓ Clean CCC(=O)C(=O)O
3PY
4MFE
Q2K340 104.1 Da LogP -1.37 TPSA 74.6 ✓ Ro5 ✓ Clean C(C(=O)C(=O)O)O
AGS
2QF7
Q2K340 523.2 Da LogP -1.51 TPSA 262.1 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
BPV
4MIM
Q2K340 167.0 Da LogP 0.03 TPSA 54.4 ✓ Ro5 ✓ Clean C(C(=O)C(=O)O)Br
BTI
3BG5
A0A0H3JRU9 228.3 Da LogP 0.91 TPSA 58.2 ✓ Ro5 ✓ Clean C1[C@H]2[C@@H]([C@@H](S1)CCCCC=O)NC(=O)N2
BYT
4M6V
Q2K340 372.5 Da LogP 0.41 TPSA 133.6 ✓ Ro5 ✓ Clean C1[C@H]2[C@@H]([C@@H](S1)CCCCC(=O)NCCCC[C@@H](C…
OAA
1RQE
Q70AC7 131.1 Da LogP -2.22 TPSA 94.5 ✓ Ro5 ✓ Clean C(C(=O)C(=O)O)C(=O)[O-]
OXL
4MFD
Q2K340 88.0 Da LogP -3.51 TPSA 80.3 ✓ Ro5 ✓ Clean C(=O)(C(=O)[O-])[O-]
PAE
3TW6
Q2K340 140.0 Da LogP -0.75 TPSA 94.8 ✓ Ro5 ✓ Clean C(C(=O)O)P(=O)(O)O
PYR
4JX5
Q2K340 88.1 Da LogP -0.34 TPSA 54.4 ✓ Ro5 ✓ Clean CC(=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.