Protein profile

VK055_4807

acetyl-CoA carboxylase, carboxyl transferase, beta subunit

Genome: KpATCC43816

Gene: accD AIK83334.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GT58

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Amino acids 306

Annotations 9

Features 25

PDB binders 6

Druggability 0.533

Overview

Basic information about this protein and its source genome.

Accession: VK055_4807
Assembly: Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene: accD AIK83334.1
Status: annotated
Amino acids: 306
Structure source: AlphaFold + ColabFold

2.1.3.15

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: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:0009329 A heterotetrameric enzyme complex made up of two alpha subunits and two beta subunits. Part of the acetyl-CoA carboxylase complex. Catalyzes the transfer of a carboxyl group to form 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).

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 29.091
Human E-value: 8.11e-06
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 97.059
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 90.26

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 0.533

Structure A0A0H3GT58

Pocket Pocket 19

P2Rank 0.112

Structure A0A0H3GT58

Pocket Pocket 1

ColabFold model

FPocket 0.866 · Pocket 1

P2Rank 0.134 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 528 / 4744 genomes with a hit

Normalized 0.111

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

2.1.3.15

Gene Ontology (GO)

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: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:0009329 A heterotetrameric enzyme complex made up of two alpha subunits and two beta subunits. Part of the acetyl-CoA carboxylase complex. Catalyzes the transfer of a carboxyl group to form 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:0008270 Binding to a zinc ion (Zn).
GO:2001295 The chemical reactions and pathways resulting in the formation of malonyl-CoA, the S-malonyl derivative of coenzyme A.

Sequence Features

Domain/signature hits from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
1	279	Hamap	MF_01395	Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic [accD].
1	279	InterPro	IPR000438	Acetyl-CoA carboxylase carboxyl transferase, beta subunit
23	292	ProSiteProfiles	PS50980	Acetyl-coenzyme A (CoA) carboxyltransferase N-terminal domain profile.
23	292	InterPro	IPR011762	Acetyl-coenzyme A carboxyltransferase, N-terminal
7	279	PANTHER	PTHR42995	ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC
1	281	NCBIfam	TIGR00515	acetyl-CoA carboxylase, carboxyltransferase subunit beta
1	281	InterPro	IPR000438	Acetyl-CoA carboxylase carboxyl transferase, beta subunit
91	238	Pfam	PF01039	Carboxyl transferase domain
91	238	InterPro	IPR034733	Acetyl-CoA carboxylase
23	281	Gene3D	G3DSA:3.90.226.10	-
227	238	PRINTS	PR01070	Acetyl-CoA carboxylase carboxyl transferase beta subunit signature
227	238	InterPro	IPR000438	Acetyl-CoA carboxylase carboxyl transferase, beta subunit
198	215	PRINTS	PR01070	Acetyl-CoA carboxylase carboxyl transferase beta subunit signature
198	215	InterPro	IPR000438	Acetyl-CoA carboxylase carboxyl transferase, beta subunit
161	179	PRINTS	PR01070	Acetyl-CoA carboxylase carboxyl transferase beta subunit signature
161	179	InterPro	IPR000438	Acetyl-CoA carboxylase carboxyl transferase, beta subunit
249	258	PRINTS	PR01070	Acetyl-CoA carboxylase carboxyl transferase beta subunit signature
249	258	InterPro	IPR000438	Acetyl-CoA carboxylase carboxyl transferase, beta subunit
127	141	PRINTS	PR01070	Acetyl-CoA carboxylase carboxyl transferase beta subunit signature
127	141	InterPro	IPR000438	Acetyl-CoA carboxylase carboxyl transferase, beta subunit
23	280	SUPERFAMILY	SSF52096	ClpP/crotonase
23	280	InterPro	IPR029045	ClpP/crotonase-like domain superfamily
24	49	Pfam	PF17848	Acetyl-coA carboxylase zinc finger domain
24	49	InterPro	IPR041010	Acetyl-coA carboxylase zinc finger domain
23	282	FunFam	G3DSA:3.90.226.10:FF:000013	Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

3D Structure

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

Loading 3D structure...

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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_A0A0H3GT58	AlphaFold	—	—	full sequence	—	Viewing
ColabFold VK055_4807	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
22				0.182
1				0.074
15				0.018
21				0.0

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	Score	Probability
1	3.68	0.112
2	2.03	0.037
3	0.97	0.005

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				0.529
23				0.063
3				0.004
10				0.001

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				4.08	0.134
2				2.55	0.058

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.

56 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	3N6R	Q168G2	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`
DXX	1ON3	Q8GBW6	118.1 Da LogP -0.21 TPSA 74.6	✓ Ro5	✓ Clean	`CC(C(=O)O)C(=O)O`
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@@…`
MCA	1ON3	Q8GBW6	867.6 Da LogP -1.61 TPSA 400.9	3 viol.	✓ Clean	`C[C@H](C(=O)O)C(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)…`
YT5	5KDR	Q2FXM6	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.