Protein profile

PA3639

acetyl-CoA carboxylase carboxyltransferase subunit alpha

Genome: NC_002516.2

Gene: PA3639 accA Structure source: AlphaFold UniProt Q9HXZ2

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Amino acids 316

Annotations 8

Features 27

PDB binders 4

Druggability 0.896

Overview

Basic information about this protein and its source genome.

Accession: PA3639
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA3639 accA
Status: annotated
Amino acids: 316
Structure source: AlphaFold

2.1.3.15

GO:0009317 A protein complex that catalyzes the first step in long-chain fatty acid biosynthesis. For example, in E. coli the complex is heterohexameric and composed of biotin carbonyl carrier protein, biotin carboxylase and the acetate CoA-transferase complex. GO:0003989 Catalysis of the reaction: ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0016743 Catalysis of the transfer of a carboxyl- or carbamoyl group from one compound (donor) to another (acceptor). GO:0006633 The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes. GO:2001295 The chemical reactions and pathways resulting in the formation of malonyl-CoA, the S-malonyl derivative of coenzyme A.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): Y
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 0.896

Structure –

Pocket –

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)

2.1.3.15

Gene Ontology (GO)

GO:0009317 A protein complex that catalyzes the first step in long-chain fatty acid biosynthesis. For example, in E. coli the complex is heterohexameric and composed of biotin carbonyl carrier protein, biotin carboxylase and the acetate CoA-transferase complex.
GO:0003989 Catalysis of the reaction: ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0016743 Catalysis of the transfer of a carboxyl- or carbamoyl group from one compound (donor) to another (acceptor).
GO:0006633 The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
GO:2001295 The chemical reactions and pathways resulting in the formation of malonyl-CoA, the S-malonyl derivative of coenzyme A.
GO:0016874 Catalysis of the joining of two molecules, or two groups within a single molecule, using the energy from the hydrolysis of ATP, a similar triphosphate, or a pH gradient.

Sequence Features

Domain/signature hits from InterPro and related databases.

27 records

Show feature table

Start	End	DB	Term	Name
30	50	Coils	Coil	Coil
1	315	Gene3D	G3DSA:3.90.226.10	-
39	293	ProSiteProfiles	PS50989	Acetyl-coenzyme A (CoA) carboxyltransferase C-terminal domain profile.
39	293	InterPro	IPR011763	Acetyl-coenzyme A carboxyltransferase, C-terminal
3	314	PANTHER	PTHR42853	ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA
3	314	InterPro	IPR001095	Acetyl-CoA carboxylase, alpha subunit
153	166	PRINTS	PR01069	Acetyl-CoA carboxylase carboxyl transferase alpha subunit signature
153	166	InterPro	IPR001095	Acetyl-CoA carboxylase, alpha subunit
169	182	PRINTS	PR01069	Acetyl-CoA carboxylase carboxyl transferase alpha subunit signature
169	182	InterPro	IPR001095	Acetyl-CoA carboxylase, alpha subunit
88	99	PRINTS	PR01069	Acetyl-CoA carboxylase carboxyl transferase alpha subunit signature
88	99	InterPro	IPR001095	Acetyl-CoA carboxylase, alpha subunit
113	131	PRINTS	PR01069	Acetyl-CoA carboxylase carboxyl transferase alpha subunit signature
113	131	InterPro	IPR001095	Acetyl-CoA carboxylase, alpha subunit
134	150	PRINTS	PR01069	Acetyl-CoA carboxylase carboxyl transferase alpha subunit signature
134	150	InterPro	IPR001095	Acetyl-CoA carboxylase, alpha subunit
197	206	PRINTS	PR01069	Acetyl-CoA carboxylase carboxyl transferase alpha subunit signature
197	206	InterPro	IPR001095	Acetyl-CoA carboxylase, alpha subunit
2	315	NCBIfam	TIGR00513	acetyl-CoA carboxylase carboxyl transferase subunit alpha
2	315	InterPro	IPR001095	Acetyl-CoA carboxylase, alpha subunit
5	316	Hamap	MF_00823	Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha [accA].
5	316	InterPro	IPR001095	Acetyl-CoA carboxylase, alpha subunit
4	316	FunFam	G3DSA:3.90.226.10:FF:000008	Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
6	148	Pfam	PF03255	Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit
6	148	InterPro	IPR001095	Acetyl-CoA carboxylase, alpha subunit
5	314	SUPERFAMILY	SSF52096	ClpP/crotonase
5	314	InterPro	IPR029045	ClpP/crotonase-like domain superfamily

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 PA3639	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				0.896
5				0.273

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.

54 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

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.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
1VU	1XNY	Q9X4K7	823.6 Da LogP -0.93 TPSA 363.6	3 viol.	✓ Clean	`CCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COP(=O)(O…`
BTI	6YBP	C5AP75	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`
HXC	5INF	A0ACI9	865.7 Da LogP 0.25 TPSA 363.6	3 viol.	✓ Clean	`CCCCCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P@@…`
YT5	5KDR	Q2FXM7	453.5 Da LogP 1.98 TPSA 121.4	✓ Ro5	✓ Clean	`C/C=C/C=C/C(=O)N[C@@H](CC(=O)N[C@@H](C(C)C)C(=O…`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC34603442	0.703	215.3 Da LogP 0.28 TPSA 67.1	✓ Ro5	✓ Clean	`NCCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC34182012	0.667	230.3 Da LogP 0.70 TPSA 61.4	✓ Ro5	✓ Clean	`O=C1N[C@@H]2[C@H](CCCCCO)SC[C@@H]2N1`
ZINC1532548	0.634	244.3 Da LogP 0.80 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)CCCC[C@H]1SC[C@@H]2NC(=O)N[C@@H]21`
ZINC2169825	0.634	244.3 Da LogP 0.80 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)CCCC[C@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC2169827	0.634	244.3 Da LogP 0.80 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)CCCC[C@H]1SC[C@@H]2NC(=O)N[C@H]21`
ZINC3869709	0.634	243.3 Da LogP 0.20 TPSA 84.2	✓ Ro5	✓ Clean	`NC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21`
ZINC3869710	0.634	243.3 Da LogP 0.20 TPSA 84.2	✓ Ro5	✓ Clean	`NC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC3869711	0.634	243.3 Da LogP 0.20 TPSA 84.2	✓ Ro5	✓ Clean	`NC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC3869712	0.634	243.3 Da LogP 0.20 TPSA 84.2	✓ Ro5	✓ Clean	`NC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]12`
ZINC22052067	0.609	301.4 Da LogP -0.09 TPSA 107.5	✓ Ro5	✓ Clean	`O=C(O)CNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC59286406	0.609	300.4 Da LogP -0.69 TPSA 113.3	✓ Ro5	✓ Clean	`NC(=O)CNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC222024244	0.600	283.4 Da LogP 0.99 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]12)NC1CC1`
ZINC48391181	0.600	283.4 Da LogP 0.99 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12)NC1CC1`
ZINC53464107	0.600	283.4 Da LogP 0.99 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21)NC1CC1`
ZINC53464111	0.600	283.4 Da LogP 0.99 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@H]2NC(=O)N[C@H]21)NC1CC1`
ZINC2121285	0.578	258.3 Da LogP 0.89 TPSA 67.4	✓ Ro5	✓ Clean	`COC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC4038545	0.578	258.3 Da LogP 0.89 TPSA 67.4	✓ Ro5	✓ Clean	`COC(=O)CCCC[C@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC5005298	0.578	258.3 Da LogP 0.89 TPSA 67.4	✓ Ro5	✓ Clean	`COC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21`
ZINC5224322	0.578	258.3 Da LogP 0.89 TPSA 67.4	✓ Ro5	✓ Clean	`COC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC90514224	0.578	258.3 Da LogP 0.89 TPSA 67.4	✓ Ro5	✓ Clean	`COC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]12`
ZINC27065097	0.574	311.5 Da LogP 1.77 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12)NC1CCCC1`
ZINC5157321	0.574	287.4 Da LogP -0.18 TPSA 90.5	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12)NCCO`
ZINC206908803	0.571	315.4 Da LogP 0.00 TPSA 96.5	✓ Ro5	✓ Clean	`COC(=O)CNC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21`
ZINC334161970	0.571	315.4 Da LogP 0.00 TPSA 96.5	✓ Ro5	✓ Clean	`COC(=O)CNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]…`
ZINC62001297	0.571	315.4 Da LogP 0.00 TPSA 96.5	✓ Ro5	✓ Clean	`COC(=O)CNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC75611263	0.571	315.4 Da LogP 0.00 TPSA 96.5	✓ Ro5	✓ Clean	`COC(=O)CNC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC104112886	0.568	242.3 Da LogP 0.57 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)/C=C\CC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21`
ZINC13543600	0.568	242.3 Da LogP 0.57 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)/C=C\CC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC4216800	0.568	242.3 Da LogP 0.57 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)/C=C/CC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC5082085	0.568	242.3 Da LogP 0.57 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)/C=C/CC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21`
ZINC5082088	0.568	242.3 Da LogP 0.57 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)/C=C/CC[C@@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC5082090	0.568	242.3 Da LogP 0.57 TPSA 78.4	✓ Ro5	✓ Clean	`O=C(O)/C=C/CC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]12`
ZINC77273222	0.568	428.6 Da LogP 1.36 TPSA 119.6	✓ Ro5	✓ Clean	`O=C1N[C@@H]2[C@H](CCCC(CCC[C@@H]3SC[C@@H]4NC(=O…`
ZINC107559942	0.563	283.4 Da LogP 1.01 TPSA 70.2	✓ Ro5	✓ Clean	`C=CCNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC12624504	0.563	339.5 Da LogP 2.55 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12)NC1CCCCC…`
ZINC13509480	0.563	315.4 Da LogP 0.30 TPSA 107.5	✓ Ro5	✓ Clean	`O=C(O)CCNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC141396702	0.563	303.5 Da LogP 0.76 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12)NCCS`
ZINC149421996	0.563	286.4 Da LogP -0.21 TPSA 96.2	✓ Ro5	✓ Clean	`NCCNC(=O)CCCC[C@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC22048411	0.563	286.4 Da LogP -0.21 TPSA 96.2	✓ Ro5	✓ Clean	`NCCNC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21`
ZINC222218978	0.563	284.4 Da LogP 1.44 TPSA 67.4	✓ Ro5	✓ Clean	`C=CCOC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]12`
ZINC222438745	0.563	339.5 Da LogP 2.55 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]12)NC1CCCC…`
ZINC34440530	0.563	301.4 Da LogP 0.21 TPSA 90.5	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12)NCCCO`
ZINC39935771	0.563	286.4 Da LogP -0.21 TPSA 96.2	✓ Ro5	✓ Clean	`NCCNC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC39935772	0.563	286.4 Da LogP -0.21 TPSA 96.2	✓ Ro5	✓ Clean	`NCCNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@@H]12`
ZINC5192432	0.563	286.4 Da LogP -0.21 TPSA 96.2	✓ Ro5	✓ Clean	`NCCNC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC80301665	0.563	284.4 Da LogP 1.44 TPSA 67.4	✓ Ro5	✓ Clean	`C=CCOC(=O)CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12`
ZINC95966269	0.563	284.4 Da LogP 1.44 TPSA 67.4	✓ Ro5	✓ Clean	`C=CCOC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21`
ZINC95966271	0.563	284.4 Da LogP 1.44 TPSA 67.4	✓ Ro5	✓ Clean	`C=CCOC(=O)CCCC[C@@H]1SC[C@H]2NC(=O)N[C@H]21`
ZINC9691512	0.563	339.5 Da LogP 2.55 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@H]2NC(=O)N[C@@H]21)NC1CCCCC…`
ZINC9691514	0.563	339.5 Da LogP 2.55 TPSA 70.2	✓ Ro5	✓ Clean	`O=C(CCCC[C@@H]1SC[C@H]2NC(=O)N[C@H]21)NC1CCCCCC1`

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.