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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei163 – 1631

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.
RETL1328306-WGS:GSTH-112-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 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

DrugBankiDB01034. Cerulenin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4064063-oxoacyl-[acyl-carrier-protein] synthase 1PRO_0000180311Add
BLAST

Proteomic databases

PaxDbiP0A953.
PRIDEiP0A953.

Expressioni

Gene expression databases

GenevestigatoriP0A953.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

DIPiDIP-29379N.
IntActiP0A953. 9 interactions.
MINTiMINT-1235843.
STRINGi511145.b2323.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1310Combined sources
Beta strandi16 – 183Combined sources
Helixi19 – 2810Combined sources
Beta strandi33 – 353Combined sources
Helixi37 – 415Combined sources
Beta strandi48 – 503Combined sources
Turni57 – 593Combined sources
Helixi62 – 654Combined sources
Helixi70 – 8617Combined sources
Helixi90 – 934Combined sources
Beta strandi99 – 1046Combined sources
Beta strandi106 – 1083Combined sources
Helixi110 – 12011Combined sources
Turni123 – 1253Combined sources
Helixi126 – 1294Combined sources
Helixi133 – 1375Combined sources
Helixi141 – 1477Combined sources
Turni148 – 1514Combined sources
Beta strandi156 – 1605Combined sources
Helixi162 – 1643Combined sources
Helixi165 – 17814Combined sources
Beta strandi183 – 1919Combined sources
Helixi195 – 2039Combined sources
Turni210 – 2134Combined sources
Helixi215 – 2173Combined sources
Beta strandi234 – 2429Combined sources
Helixi243 – 2486Combined sources
Beta strandi255 – 26410Combined sources
Beta strandi269 – 2713Combined sources
Helixi275 – 28511Combined sources
Beta strandi294 – 2963Combined sources
Helixi303 – 31715Combined sources
Helixi318 – 3203Combined sources
Beta strandi323 – 3253Combined sources
Helixi328 – 3314Combined sources
Helixi335 – 3373Combined sources
Helixi338 – 35215Combined sources
Beta strandi362 – 3643Combined sources
Helixi366 – 3683Combined sources
Beta strandi371 – 3733Combined sources
Beta strandi384 – 3918Combined sources
Turni392 – 3943Combined sources
Beta strandi395 – 4028Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-406.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A953.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0304.
HOGENOMiHOG000060165.
InParanoidiP0A953.
KOiK00647.
OMAiIGNAMEQ.
OrthoDBiEOG6DG2SR.
PhylomeDBiP0A953.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
InterProiIPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41A → T in strain: MA-1 / fabB3.
Natural varianti140 – 1401S → F in strain: K1060 / fabB5.
Natural varianti299 – 2991G → S in strain: MA-1 / fabB3.
Natural varianti329 – 3291A → V in strain: M5 / fabB15.

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.

Genome annotation databases

EnsemblBacteriaiAAC75383; AAC75383; b2323.
BAA16180; BAA16180; BAA16180.
GeneIDi946799.
KEGGiecj:Y75_p2289.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29379N.
IntActiP0A953. 9 interactions.
MINTiMINT-1235843.
STRINGi511145.b2323.

Chemistry

BindingDBiP0A953.
ChEMBLiCHEMBL4913.
DrugBankiDB01034. Cerulenin.

Proteomic databases

PaxDbiP0A953.
PRIDEiP0A953.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75383; AAC75383; b2323.
BAA16180; BAA16180; BAA16180.
GeneIDi946799.
KEGGiecj:Y75_p2289.
eco:b2323.
PATRICi32120019. VBIEscCol129921_2419.

Organism-specific databases

EchoBASEiEB0270.
EcoGeneiEG10274. fabB.

Phylogenomic databases

eggNOGiCOG0304.
HOGENOMiHOG000060165.
InParanoidiP0A953.
KOiK00647.
OMAiIGNAMEQ.
OrthoDBiEOG6DG2SR.
PhylomeDBiP0A953.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciEcoCyc:FABB-MONOMER.
ECOL316407:JW2320-MONOMER.
MetaCyc:FABB-MONOMER.
RETL1328306-WGS:GSTH-112-MONOMER.
BRENDAi2.3.1.41. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A953.
PROiP0A953.

Gene expression databases

GenevestigatoriP0A953.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
InterProiIPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 2 hits.
PROSITEiPS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Beta-ketoacyl-ACP synthase I of Escherichia coli: nucleotide sequence of the fabB gene and identification of the cerulenin binding residue."
    Kauppinen S., Siggaard-Andersen M., von Wettstein-Knowles P.
    Carlsberg Res. Commun. 53:357-370(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19 AND 158-168.
    Strain: B.
  2. "Catalytic residues of beta-ketoacyl-ACP synthases."
    Siggaard-Andersen M., von Wettstein-Knowles P., Gotthardt-Olsen J., Bangera G., Chuck J.-A., Pontoppidan B.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K1060 / fabB5, M5 / fabB15 and MA-1 / fabB3.
  3. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Role of Escherichia coli beta-ketoacyl-ACP synthase I in unsaturated fatty acid synthesis."
    Siggaard-Andersen M.
    Carlsberg Res. Commun. 53:371-379(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UNSATURATED FATTY ACID SYNTHESIS.
  7. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  8. "The X-ray crystal structure of beta-ketoacyl [acyl carrier-protein] synthase I."
    Olsen J.G., Kadziola A., von Wettstein-Knowles P., Siggaard-Andersen M., Lindquist Y., Larsen S.
    FEBS Lett. 460:46-52(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

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: May 27, 2015
This is version 97 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

External Data

Dasty 3

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 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.