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Protein

3-oxoacyl-[acyl-carrier-protein] synthase 1

Gene

fabB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids.1 Publication

Catalytic activityi

Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1631

GO - Molecular functioni

  • 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: EcoCyc

GO - Biological processi

  • fatty acid biosynthetic process Source: EcoCyc
  • lipid biosynthetic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciEcoCyc:FABB-MONOMER.
ECOL316407:JW2320-MONOMER.
MetaCyc:FABB-MONOMER.
BRENDAi2.3.1.41. 2026.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 1 (EC:2.3.1.41)
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase I
Beta-ketoacyl-ACP synthase I
Short name:
KAS I
Gene namesi
Name:fabB
Synonyms:fabC
Ordered Locus Names:b2323, JW2320
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10274. fabB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4913.
DrugBankiDB01034. Cerulenin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001803111 – 4063-oxoacyl-[acyl-carrier-protein] synthase 1Add BLAST406

Proteomic databases

EPDiP0A953.
PaxDbiP0A953.
PRIDEiP0A953.

Expressioni

Inductioni

Mainly activated by FadR, but minor repression is also conferred by FabR (PubMed:11859088, PubMed:21276098).2 Publications

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4260793. 224 interactors.
DIPiDIP-29379N.
IntActiP0A953. 9 interactors.
MINTiMINT-1235843.
STRINGi511145.b2323.

Chemistry databases

BindingDBiP0A953.

Structurei

Secondary structure

1406
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 13Combined sources10
Beta strandi16 – 18Combined sources3
Helixi19 – 28Combined sources10
Beta strandi33 – 35Combined sources3
Helixi37 – 41Combined sources5
Beta strandi48 – 50Combined sources3
Turni57 – 59Combined sources3
Helixi62 – 65Combined sources4
Helixi70 – 86Combined sources17
Helixi90 – 93Combined sources4
Beta strandi99 – 104Combined sources6
Beta strandi106 – 108Combined sources3
Helixi110 – 120Combined sources11
Turni123 – 125Combined sources3
Helixi126 – 129Combined sources4
Helixi133 – 137Combined sources5
Helixi141 – 147Combined sources7
Turni148 – 151Combined sources4
Beta strandi156 – 160Combined sources5
Helixi162 – 164Combined sources3
Helixi165 – 178Combined sources14
Beta strandi183 – 191Combined sources9
Helixi195 – 203Combined sources9
Turni210 – 213Combined sources4
Helixi215 – 217Combined sources3
Beta strandi234 – 242Combined sources9
Helixi243 – 248Combined sources6
Beta strandi255 – 264Combined sources10
Beta strandi269 – 271Combined sources3
Helixi275 – 285Combined sources11
Beta strandi294 – 296Combined sources3
Helixi303 – 317Combined sources15
Helixi318 – 320Combined sources3
Beta strandi323 – 325Combined sources3
Helixi328 – 331Combined sources4
Helixi335 – 337Combined sources3
Helixi338 – 352Combined sources15
Beta strandi362 – 364Combined sources3
Helixi366 – 368Combined sources3
Beta strandi371 – 373Combined sources3
Beta strandi384 – 391Combined sources8
Turni392 – 394Combined sources3
Beta strandi395 – 402Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DD8X-ray2.30A/B/C/D1-406[»]
1EK4X-ray1.85A/B/C/D1-406[»]
1F91X-ray2.40A/B/C/D1-406[»]
1FJ4X-ray2.35A/B/C/D1-406[»]
1FJ8X-ray2.27A/B/C/D1-406[»]
1G5XX-ray2.45A/B/C/D1-406[»]
1H4FX-ray2.00A/B/C/D1-406[»]
2AQ7X-ray2.30A/B/C/D1-406[»]
2AQBX-ray2.19A/B/C/D1-406[»]
2BUHX-ray1.90A/B/C/D1-406[»]
2BUIX-ray2.40A/B/C/D1-406[»]
2BYWX-ray1.70A/B/C/D5-406[»]
2BYXX-ray2.00A/B/C/D5-406[»]
2BYYX-ray2.20A/B/C/D1-406[»]
2BYZX-ray1.95A/B/C/D1-406[»]
2BZ3X-ray2.00A/B/C/D1-406[»]
2BZ4X-ray1.86A/B/C/D1-406[»]
2CDHX-ray4.20A/B/C/D/E/F1-406[»]
2CF2X-ray4.30A/J1-406[»]
2VB7X-ray1.60A/B/C/D1-406[»]
2VB8X-ray1.52A/B/C/D1-406[»]
2VB9X-ray1.50A/B/C/D1-406[»]
2VBAX-ray1.36A/B/C/D1-406[»]
ProteinModelPortaliP0A953.
SMRiP0A953.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A953.

Family & Domainsi

Sequence similaritiesi

Belongs to the beta-ketoacyl-ACP synthases family.Curated

Phylogenomic databases

eggNOGiENOG4105C0Q. Bacteria.
COG0304. LUCA.
HOGENOMiHOG000060165.
InParanoidiP0A953.
KOiK00647.
OMAiHCIGTAL.
PhylomeDBiP0A953.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
InterProiIPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
SMARTiSM00825. PKS_KS. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 2 hits.
PROSITEiPS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A953-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRAVITGLG IVSSIGNNQQ EVLASLREGR SGITFSQELK DSGMRSHVWG
60 70 80 90 100
NVKLDTTGLI DRKVVRFMSD ASIYAFLSME QAIADAGLSP EAYQNNPRVG
110 120 130 140 150
LIAGSGGGSP RFQVFGADAM RGPRGLKAVG PYVVTKAMAS GVSACLATPF
160 170 180 190 200
KIHGVNYSIS SACATSAHCI GNAVEQIQLG KQDIVFAGGG EELCWEMACE
210 220 230 240 250
FDAMGALSTK YNDTPEKASR TYDAHRDGFV IAGGGGMVVV EELEHALARG
260 270 280 290 300
AHIYAEIVGY GATSDGADMV APSGEGAVRC MKMAMHGVDT PIDYLNSHGT
310 320 330 340 350
STPVGDVKEL AAIREVFGDK SPAISATKAM TGHSLGAAGV QEAIYSLLML
360 370 380 390 400
EHGFIAPSIN IEELDEQAAG LNIVTETTDR ELTTVMSNSF GFGGTNATLV

MRKLKD
Length:406
Mass (Da):42,613
Last modified:July 19, 2005 - v1
Checksum:i489D8BAD23E78113
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti4A → T in strain: MA-1 / fabB3. 1
Natural varianti140S → F in strain: K1060 / fabB5. 1
Natural varianti299G → S in strain: MA-1 / fabB3. 1
Natural varianti329A → V in strain: M5 / fabB15. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24427 Genomic DNA. Translation: AAC67304.1.
AJ012161 Genomic DNA. Translation: CAA09932.1.
AJ012162 Genomic DNA. Translation: CAA09933.1.
AJ012163 Genomic DNA. Translation: CAA09934.1.
U00096 Genomic DNA. Translation: AAC75383.1.
AP009048 Genomic DNA. Translation: BAA16180.1.
PIRiA31284. SYECA1.
RefSeqiNP_416826.1. NC_000913.3.
WP_000817178.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75383; AAC75383; b2323.
BAA16180; BAA16180; BAA16180.
GeneIDi946799.
KEGGiecj:JW2320.
eco:b2323.
PATRICi32120019. VBIEscCol129921_2419.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24427 Genomic DNA. Translation: AAC67304.1.
AJ012161 Genomic DNA. Translation: CAA09932.1.
AJ012162 Genomic DNA. Translation: CAA09933.1.
AJ012163 Genomic DNA. Translation: CAA09934.1.
U00096 Genomic DNA. Translation: AAC75383.1.
AP009048 Genomic DNA. Translation: BAA16180.1.
PIRiA31284. SYECA1.
RefSeqiNP_416826.1. NC_000913.3.
WP_000817178.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DD8X-ray2.30A/B/C/D1-406[»]
1EK4X-ray1.85A/B/C/D1-406[»]
1F91X-ray2.40A/B/C/D1-406[»]
1FJ4X-ray2.35A/B/C/D1-406[»]
1FJ8X-ray2.27A/B/C/D1-406[»]
1G5XX-ray2.45A/B/C/D1-406[»]
1H4FX-ray2.00A/B/C/D1-406[»]
2AQ7X-ray2.30A/B/C/D1-406[»]
2AQBX-ray2.19A/B/C/D1-406[»]
2BUHX-ray1.90A/B/C/D1-406[»]
2BUIX-ray2.40A/B/C/D1-406[»]
2BYWX-ray1.70A/B/C/D5-406[»]
2BYXX-ray2.00A/B/C/D5-406[»]
2BYYX-ray2.20A/B/C/D1-406[»]
2BYZX-ray1.95A/B/C/D1-406[»]
2BZ3X-ray2.00A/B/C/D1-406[»]
2BZ4X-ray1.86A/B/C/D1-406[»]
2CDHX-ray4.20A/B/C/D/E/F1-406[»]
2CF2X-ray4.30A/J1-406[»]
2VB7X-ray1.60A/B/C/D1-406[»]
2VB8X-ray1.52A/B/C/D1-406[»]
2VB9X-ray1.50A/B/C/D1-406[»]
2VBAX-ray1.36A/B/C/D1-406[»]
ProteinModelPortaliP0A953.
SMRiP0A953.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260793. 224 interactors.
DIPiDIP-29379N.
IntActiP0A953. 9 interactors.
MINTiMINT-1235843.
STRINGi511145.b2323.

Chemistry databases

BindingDBiP0A953.
ChEMBLiCHEMBL4913.
DrugBankiDB01034. Cerulenin.

Proteomic databases

EPDiP0A953.
PaxDbiP0A953.
PRIDEiP0A953.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75383; AAC75383; b2323.
BAA16180; BAA16180; BAA16180.
GeneIDi946799.
KEGGiecj:JW2320.
eco:b2323.
PATRICi32120019. VBIEscCol129921_2419.

Organism-specific databases

EchoBASEiEB0270.
EcoGeneiEG10274. fabB.

Phylogenomic databases

eggNOGiENOG4105C0Q. Bacteria.
COG0304. LUCA.
HOGENOMiHOG000060165.
InParanoidiP0A953.
KOiK00647.
OMAiHCIGTAL.
PhylomeDBiP0A953.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciEcoCyc:FABB-MONOMER.
ECOL316407:JW2320-MONOMER.
MetaCyc:FABB-MONOMER.
BRENDAi2.3.1.41. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A953.
PROiP0A953.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
InterProiIPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
SMARTiSM00825. PKS_KS. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 2 hits.
PROSITEiPS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFABB_ECOLI
AccessioniPrimary (citable) accession number: P0A953
Secondary accession number(s): P14926
, Q9R828, Q9R829, Q9R830
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: November 2, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.