Protein profile

PA4977

hypothetical protein

Genome: NC_002516.2

Gene: PA4977 aruI Structure source: AlphaFold UniProt Q9HUI8
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Amino acids 559
Annotations 11
Features 22
PDB binders 34
Druggability 0.521

Overview

Basic information about this protein and its source genome.

Accession
PA4977
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA4977 aruI
Status
annotated
Amino acids
559
Structure source
AlphaFold
EC
4.1.1.75
GO
GO:0005948 A dimeric (a large and a small chain) or tetrameric (two large and two small chains) enzyme complex. Catalyzes the formation of acetolactate from pyruvate. GO:0047435 Catalysis of the reaction: 5-guanidino-2-oxopentanoate + H+ = 4-guanidinobutanal + CO2. GO:0003984 Catalysis of the reaction: H+ + 2 pyruvate = (2S)-2-acetolactate + CO2. Can also convert 2-oxobutanoate and pyruvate to (S)-2-ethyl-2-hydroxy-3-oxobutanoate. GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. GO:0000287 Binding to a magnesium (Mg) ion. GO:0030976 Binding to thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
40.217
Human E-value
2.46e-10
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
Cytoplasmic

Selected Druggability evidence

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 0.521
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

10
  • GO:0005948 A dimeric (a large and a small chain) or tetrameric (two large and two small chains) enzyme complex. Catalyzes the formation of acetolactate from pyruvate.
  • GO:0047435 Catalysis of the reaction: 5-guanidino-2-oxopentanoate + H+ = 4-guanidinobutanal + CO2.
  • GO:0003984 Catalysis of the reaction: H+ + 2 pyruvate = (2S)-2-acetolactate + CO2. Can also convert 2-oxobutanoate and pyruvate to (S)-2-ethyl-2-hydroxy-3-oxobutanoate.
  • GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
  • GO:0000287 Binding to a magnesium (Mg) ion.
  • GO:0030976 Binding to thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases.
  • GO:0009097 OBSOLETE. The chemical reactions and pathways resulting in the formation of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid.
  • GO:0019545 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of L-arginine into other compounds, including succinate.
  • GO:0009099 The chemical reactions and pathways resulting in the formation of valine, 2-amino-3-methylbutanoic acid.
  • 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.

22 records
Show feature table
Start End DB Term Name
216 384 Gene3D G3DSA:3.40.50.1220 -
388 554 CDD cd00568 TPP_enzymes
221 350 Pfam PF00205 Thiamine pyrophosphate enzyme, central domain
221 350 InterPro IPR012000 Thiamine pyrophosphate enzyme, central domain
22 204 SUPERFAMILY SSF52518 Thiamin diphosphate-binding fold (THDP-binding)
22 204 InterPro IPR029061 Thiamin diphosphate-binding fold
29 553 PANTHER PTHR18968 THIAMINE PYROPHOSPHATE ENZYMES
29 553 InterPro IPR045229 Thiamine pyrophosphate enzyme
31 199 Pfam PF02776 Thiamine pyrophosphate enzyme, N-terminal TPP binding domain
31 199 InterPro IPR012001 Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain
386 557 SUPERFAMILY SSF52518 Thiamin diphosphate-binding fold (THDP-binding)
386 557 InterPro IPR029061 Thiamin diphosphate-binding fold
34 190 CDD cd07035 TPP_PYR_POX_like
385 558 Gene3D G3DSA:3.40.50.970 -
414 552 Pfam PF02775 Thiamine pyrophosphate enzyme, C-terminal TPP binding domain
414 552 InterPro IPR011766 Thiamine pyrophosphate enzyme, TPP-binding
184 377 SUPERFAMILY SSF52467 DHS-like NAD/FAD-binding domain
184 377 InterPro IPR029035 DHS-like NAD/FAD-binding domain superfamily
24 204 FunFam G3DSA:3.40.50.970:FF:000084 Probable 2-ketoarginine decarboxylase AruI
20 206 Gene3D G3DSA:3.40.50.970 -
443 462 ProSitePatterns PS00187 Thiamine pyrophosphate enzymes signature.
443 462 InterPro IPR000399 TPP-binding enzyme, conserved site

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 + 1

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA4977
AlphaFold — — full sequence — Viewing
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 0.521

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.

116 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
1IQ
1Z8N
P17597 311.3 Da LogP 2.22 TPSA 91.7 ✓ Ro5 ✓ Clean CC(C)[C@@]1(C(=O)NC(=N1)c2c(cc3ccccc3n2)C(=O)O)C
1MM
1T9D
P07342 381.4 Da LogP 0.49 TPSA 149.5 ✓ Ro5 ✓ Clean Cc1nc(nc(n1)OC)NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC
1MS
3E9Y
P17597 337.3 Da LogP 1.20 TPSA 144.2 ✓ Ro5 ✓ Clean Cc1ccnc(n1)NC(=O)NS(=O)(=O)c2ccccc2[N+](=O)[O-]
1SM
1T9C
P07342 364.4 Da LogP 1.39 TPSA 127.3 ✓ Ro5 ✓ Clean Cc1cc(nc(n1)NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC)C
1TB
1T9A
P07342 395.4 Da LogP 0.51 TPSA 140.7 ✓ Ro5 ✓ Clean Cc1nc(nc(n1)OC)N(C)C(=O)NS(=O)(=O)c2ccccc2C(=O)…
2SM
3EA4
P17597 350.4 Da LogP 1.08 TPSA 127.3 ✓ Ro5 ✓ Clean Cc1ccnc(n1)NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC
60G
5FEM
P07342 410.4 Da LogP 0.93 TPSA 145.8 ✓ Ro5 ✓ Clean COc1cc(nc(n1)NC(=O)NS(=O)(=O)Cc2ccccc2C(=O)OC)OC
6QK
5K2O
P17597 326.8 Da LogP 3.00 TPSA 81.5 ✓ Ro5 ✓ Clean COc1cc(nc(n1)Sc2cccc(c2C(=O)O)Cl)OC
6QL
5K3S
P17597 430.4 Da LogP 2.58 TPSA 144.2 1 viol. ✓ Clean COc1cc(nc(n1)Oc2cccc(c2C(=O)O)Oc3nc(cc(n3)OC)OC…
6R4
5K6T
P17597 398.4 Da LogP 0.10 TPSA 138.6 ✓ Ro5 ✓ Clean CCCOC1=NN(C(=O)N1C)C(=O)NS(=O)(=O)c2ccccc2C(=O)…
6R5
5K6R
P17597 390.4 Da LogP -0.31 TPSA 138.6 1 viol. ✓ Clean Cc1c(c(cs1)C(=O)OC)S(=O)(=O)NC(=O)N2C(=O)N(C(=N…
8GF
6WO1
Q96VZ6 109.1 Da LogP 0.37 TPSA 51.8 ✓ Ro5 ✓ Clean Cc1nccc(n1)N
AUJ
5WKC
P07342 — — — Cc1ncc(c(n1)N)C[N]2=C(SC(=C2C)CCOP(=O)(O)OP(=O)…
AYD
1N0H
P07342 382.3 Da LogP 0.98 TPSA 177.1 ✓ Ro5 ✓ Clean Cc1ncc(c(n1)N)CN/C(=C/CCO[P@@](=O)(O)OP(=O)(O)O…
CIE
1YBH
P17597 414.8 Da LogP 1.83 TPSA 136.6 ✓ Ro5 ✓ Clean CCOC(=O)c1ccccc1S(=O)(=O)NC(=O)Nc2nc(cc(n2)Cl)OC
CO2
6BD3
P07342 44.0 Da LogP -0.58 TPSA 34.1 ✓ Ro5 ✓ Clean C(=O)=O
DPO
6WO1
Q96VZ6 173.9 Da LogP -3.34 TPSA 135.6 ✓ Ro5 ✓ Clean [O-]P(=O)([O-])OP(=O)([O-])[O-]
DTT
1N0H
P07342 154.3 Da LogP -0.43 TPSA 40.5 ✓ Ro5 ✓ Clean C([C@@H]([C@H](CS)O)O)S
F50
5WJ1
P17597 76.1 Da LogP 0.02 TPSA 46.5 ✓ Ro5 ✓ Clean CC(=O)OO
FAB
3E9Y
P17597 855.6 Da LogP -2.87 TPSA 373.8 3 viol. Alert Cc1cc2c(cc1C)[N+](=C3C(=O)NC(=O)N=C3N2C[C@@H]([…
HTL
6BD3
P07342 467.4 Da LogP 1.04 TPSA 186.0 ✓ Ro5 ✓ Clean Cc1c(sc([n+]1Cc2cnc(nc2N)C)C(=O)C)CCO[P@@](=O)(…
NSP
1T9B
P07342 138.2 Da LogP -0.17 TPSA 77.8 ✓ Ro5 ✓ Clean Cc1ncc(c(n1)N)CN
OXY
5IMS
P07342 32.0 Da LogP 0.07 TPSA 34.1 ✓ Ro5 ✓ Clean O=O
P22
1YBH
P17597 206.0 Da LogP 0.23 TPSA 113.3 ✓ Ro5 ✓ Clean CCO[P@](=O)(O)OP(=O)(O)O
P23
1T9A
P07342 220.1 Da LogP 0.62 TPSA 113.3 ✓ Ro5 ✓ Clean CCCO[P@@](=O)(O)OP(=O)(O)O
P25
1T9B
P07342 248.1 Da LogP 1.40 TPSA 113.3 ✓ Ro5 ✓ Clean CCCCCO[P@@](=O)(O)OP(=O)(O)O
PXD
5WJ1
P17597 483.4 Da LogP 2.61 TPSA 116.9 ✓ Ro5 ✓ Clean COc1cnc(n2c1nc(n2)NS(=O)(=O)c3c(cccc3OCC(F)F)C(…
PYD
1T9D
P07342 123.2 Da LogP 0.68 TPSA 51.8 ✓ Ro5 ✓ Clean Cc1cnc(nc1N)C
PYR
6BD9
P07342 88.1 Da LogP -0.34 TPSA 54.4 ✓ Ro5 ✓ Clean CC(=O)C(=O)O
TDM
3E9Y
P17597 468.4 Da LogP 2.51 TPSA 188.6 ✓ Ro5 ✓ Clean Cc1ncc(c(n1)N)CN\2C(=C(S/C2=C(\C)/O)CCO[P@@](=O…
TP9
5K2O
P17597 412.3 Da LogP -0.03 TPSA 182.8 1 viol. ✓ Clean Cc1ncc(c(n1)N)CN/C(=C(/CCO[P@](=O)([O-])O[P@@](…
TZD
5K6T
P17597 440.3 Da LogP 0.72 TPSA 187.1 ✓ Ro5 ✓ Clean Cc1ncc(c(n1)N)CN2C(=C(SC2=O)CCO[P@@](=O)(O)OP(=…
YF3
1T9A
P07342 212.3 Da LogP 0.78 TPSA 63.8 ✓ Ro5 ✓ Clean Cc1ncc(c(n1)N)CNC(C)CS
YF4
1T9A
P07342 180.3 Da LogP 0.82 TPSA 55.0 ✓ Ro5 ✓ Clean CCN(C)Cc1cnc(nc1N)C

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.