UniProtKB - P0A6R0 (FABH_ECOLI)
Protein
3-oxoacyl-[acyl-carrier-protein] synthase 3
Gene
fabH
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain (PubMed:7592873, PubMed:8631920, PubMed:8910376, PubMed:10629181). Can also use propionyl-CoA, with lower efficiency (PubMed:8631920, PubMed:10629181).4 Publications
Miscellaneous
Inhibited by the SB418011 antibiotic. Not inhibited by cerulenin and thiolactomycin.
Catalytic activityi
- EC:2.3.1.180UniRule annotation4 PublicationsThis reaction proceeds in the forward4 Publications direction.
- This reaction proceeds in the forward2 Publications direction.
Activity regulationi
Negatively regulated by acyl-ACP, possibly by binding to either the free enzyme or the acyl-enzyme intermediate.1 Publication
Kineticsi
- KM=40 µM for acetyl-CoA1 Publication
- KM=5 µM for malonyl-[ACP]1 Publication
: fatty acid biosynthesis Pathwayi
This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotationView all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 112 | 3 Publications | 1 | |
Active sitei | 244 | 3 Publications | 1 | |
Active sitei | 274 | 3 Publications | 1 |
GO - Molecular functioni
- 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: InterPro
- beta-ketoacyl-acyl-carrier-protein synthase III activity Source: EcoCyc
GO - Biological processi
- fatty acid biosynthetic process Source: UniProtKB-UniRule
- fatty acid metabolic process Source: CACAO
Keywordsi
Molecular function | Acyltransferase, Multifunctional enzyme, Transferase |
Biological process | Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism |
Enzyme and pathway databases
BioCyci | EcoCyc:FABH-MONOMER MetaCyc:FABH-MONOMER |
BRENDAi | 2.3.1.180, 2026 |
UniPathwayi | UPA00094 |
Chemistry databases
SwissLipidsi | SLP:000000852 |
Names & Taxonomyi
Protein namesi | Recommended name: 3-oxoacyl-[acyl-carrier-protein] synthase 3UniRule annotation (EC:2.3.1.180UniRule annotation4 Publications)Alternative name(s): 3-oxoacyl-[acyl-carrier-protein] synthase IIIUniRule annotation Beta-ketoacyl-ACP synthase IIIUniRule annotation Short name: KAS IIIUniRule annotation EcFabH |
Gene namesi | Name:fabH Ordered Locus Names:b1091, JW1077 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
- Cytoplasm UniRule annotation
GO - Cellular componenti
- cytosol Source: EcoCyc
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 112 | C → S: Loss of activity. | 1 | |
Mutagenesisi | 214 | K → E or A: Strongly reduces the binding to malonyl-ACP but not that of the substrate. 1 Publication | 1 | |
Mutagenesisi | 244 | H → A: Loss of activity. | 1 | |
Mutagenesisi | 249 | R → E or A: Abolishes the binding to malonyl-ACP but not that of the substrate. 1 Publication | 1 | |
Mutagenesisi | 253 | A → Y: Abolishes both binding to malonyl-ACP and binding to substrate. 1 Publication | 1 | |
Mutagenesisi | 256 – 257 | KK → AA: Strongly reduces both binding to malonyl-ACP and binding to substrate. 1 Publication | 2 | |
Mutagenesisi | 256 – 257 | KK → EE: Abolishes the binding to malonyl-ACP but not that of the substrate. 1 Publication | 2 | |
Mutagenesisi | 274 | N → A: Loss of activity. | 1 |
Chemistry databases
ChEMBLi | CHEMBL4914 |
DrugBanki | DB02316, 1-(5-Carboxypentyl)-5-[(2,6-Dichlorobenzyl)Oxy]-1 H-Indole-2-Carboxylic Acid DB01034, Cerulenin DB01992, Coenzyme A DB03661, L-cysteic acid DB04524, Malonyl-CoA DB02039, S-Acetyl-Cysteine |
DrugCentrali | P0A6R0 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000110424 | 1 – 317 | 3-oxoacyl-[acyl-carrier-protein] synthase 3Add BLAST | 317 |
Proteomic databases
jPOSTi | P0A6R0 |
PaxDbi | P0A6R0 |
PRIDEi | P0A6R0 |
PTM databases
CarbonylDBi | P0A6R0 |
Interactioni
Subunit structurei
Homodimer.
UniRule annotationProtein-protein interaction databases
BioGRIDi | 4261031, 467 interactors |
DIPi | DIP-48255N |
IntActi | P0A6R0, 5 interactors |
STRINGi | 511145.b1091 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A6R0 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A6R0 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 245 – 249 | ACP-binding | 5 |
Domaini
The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.UniRule annotation1 Publication
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0332, Bacteria |
HOGENOMi | CLU_039592_4_1_6 |
InParanoidi | P0A6R0 |
PhylomeDBi | P0A6R0 |
Family and domain databases
CDDi | cd00830, KAS_III, 1 hit |
Gene3Di | 3.40.47.10, 1 hit |
HAMAPi | MF_01815, FabH, 1 hit |
InterProi | View protein in InterPro IPR013751, ACP_syn_III IPR013747, ACP_syn_III_C IPR004655, FabH_synth IPR016039, Thiolase-like |
Pfami | View protein in Pfam PF08545, ACP_syn_III, 1 hit PF08541, ACP_syn_III_C, 1 hit |
SUPFAMi | SSF53901, SSF53901, 1 hit |
TIGRFAMsi | TIGR00747, fabH, 1 hit |
i Sequence
Sequence statusi: Complete.
P0A6R0-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MYTKIIGTGS YLPEQVRTNA DLEKMVDTSD EWIVTRTGIR ERHIAAPNET
60 70 80 90 100
VSTMGFEAAT RAIEMAGIEK DQIGLIVVAT TSATHAFPSA ACQIQSMLGI
110 120 130 140 150
KGCPAFDVAA ACAGFTYALS VADQYVKSGA VKYALVVGSD VLARTCDPTD
160 170 180 190 200
RGTIIIFGDG AGAAVLAASE EPGIISTHLH ADGSYGELLT LPNADRVNPE
210 220 230 240 250
NSIHLTMAGN EVFKVAVTEL AHIVDETLAA NNLDRSQLDW LVPHQANLRI
260 270 280 290 300
ISATAKKLGM SMDNVVVTLD RHGNTSAASV PCALDEAVRD GRIKPGQLVL
310
LEAFGGGFTW GSALVRF
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M77744 Genomic DNA Translation: AAA23749.1 M96793 Genomic DNA Translation: AAB59065.1 U00096 Genomic DNA Translation: AAC74175.1 AP009048 Genomic DNA Translation: BAA35899.2 M87040 Genomic DNA Translation: AAA23741.1 Z11565 Genomic DNA Translation: CAA77659.1 |
PIRi | A42431 |
RefSeqi | NP_415609.1, NC_000913.3 WP_000288132.1, NZ_STEB01000016.1 |
Genome annotation databases
EnsemblBacteriai | AAC74175; AAC74175; b1091 BAA35899; BAA35899; BAA35899 |
GeneIDi | 58461211 946003 |
KEGGi | ecj:JW1077 eco:b1091 |
PATRICi | fig|1411691.4.peg.1177 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M77744 Genomic DNA Translation: AAA23749.1 M96793 Genomic DNA Translation: AAB59065.1 U00096 Genomic DNA Translation: AAC74175.1 AP009048 Genomic DNA Translation: BAA35899.2 M87040 Genomic DNA Translation: AAA23741.1 Z11565 Genomic DNA Translation: CAA77659.1 |
PIRi | A42431 |
RefSeqi | NP_415609.1, NC_000913.3 WP_000288132.1, NZ_STEB01000016.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1EBL | X-ray | 1.80 | A/B | 1-317 | [»] | |
1HN9 | X-ray | 2.00 | A/B | 1-317 | [»] | |
1HND | X-ray | 1.60 | A | 1-317 | [»] | |
1HNH | X-ray | 1.90 | A | 1-317 | [»] | |
1HNJ | X-ray | 1.46 | A | 1-317 | [»] | |
1HNK | X-ray | 1.90 | A | 1-317 | [»] | |
1MZS | X-ray | 2.10 | A | 1-317 | [»] | |
2EFT | X-ray | 2.00 | A/B | 1-317 | [»] | |
2GYO | X-ray | 2.00 | A/B | 1-317 | [»] | |
3IL9 | X-ray | 1.85 | A/B | 1-317 | [»] | |
4Z8D | X-ray | 2.00 | A/B | 1-317 | [»] | |
5BNM | X-ray | 1.70 | A/B | 1-317 | [»] | |
5BNR | X-ray | 1.89 | A | 1-317 | [»] | |
5BNS | X-ray | 2.20 | A/B | 1-317 | [»] | |
SMRi | P0A6R0 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4261031, 467 interactors |
DIPi | DIP-48255N |
IntActi | P0A6R0, 5 interactors |
STRINGi | 511145.b1091 |
Chemistry databases
ChEMBLi | CHEMBL4914 |
DrugBanki | DB02316, 1-(5-Carboxypentyl)-5-[(2,6-Dichlorobenzyl)Oxy]-1 H-Indole-2-Carboxylic Acid DB01034, Cerulenin DB01992, Coenzyme A DB03661, L-cysteic acid DB04524, Malonyl-CoA DB02039, S-Acetyl-Cysteine |
DrugCentrali | P0A6R0 |
SwissLipidsi | SLP:000000852 |
PTM databases
CarbonylDBi | P0A6R0 |
Proteomic databases
jPOSTi | P0A6R0 |
PaxDbi | P0A6R0 |
PRIDEi | P0A6R0 |
Genome annotation databases
EnsemblBacteriai | AAC74175; AAC74175; b1091 BAA35899; BAA35899; BAA35899 |
GeneIDi | 58461211 946003 |
KEGGi | ecj:JW1077 eco:b1091 |
PATRICi | fig|1411691.4.peg.1177 |
Organism-specific databases
EchoBASEi | EB0273 |
Phylogenomic databases
eggNOGi | COG0332, Bacteria |
HOGENOMi | CLU_039592_4_1_6 |
InParanoidi | P0A6R0 |
PhylomeDBi | P0A6R0 |
Enzyme and pathway databases
UniPathwayi | UPA00094 |
BioCyci | EcoCyc:FABH-MONOMER MetaCyc:FABH-MONOMER |
BRENDAi | 2.3.1.180, 2026 |
Miscellaneous databases
EvolutionaryTracei | P0A6R0 |
PROi | PR:P0A6R0 |
Family and domain databases
CDDi | cd00830, KAS_III, 1 hit |
Gene3Di | 3.40.47.10, 1 hit |
HAMAPi | MF_01815, FabH, 1 hit |
InterProi | View protein in InterPro IPR013751, ACP_syn_III IPR013747, ACP_syn_III_C IPR004655, FabH_synth IPR016039, Thiolase-like |
Pfami | View protein in Pfam PF08545, ACP_syn_III, 1 hit PF08541, ACP_syn_III_C, 1 hit |
SUPFAMi | SSF53901, SSF53901, 1 hit |
TIGRFAMsi | TIGR00747, fabH, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | FABH_ECOLI | |
Accessioni | P0A6R0Primary (citable) accession number: P0A6R0 Secondary accession number(s): P24249 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 10, 2005 |
Last sequence update: | May 10, 2005 | |
Last modified: | February 10, 2021 | |
This is version 137 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families