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P0A953

- FABB_ECOLI

UniProt

P0A953 - FABB_ECOLI

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Protein

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

Gene

fabB

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

  1. 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: EcoCyc

GO - Biological processi

  1. fatty acid biosynthetic process Source: EcoCyc
  2. 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.
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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10274. fabB.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiFNPEYAE.
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:
EMBL
GenBank
DDBJ
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.
YP_490565.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75383; AAC75383; b2323.
BAA16180; BAA16180; BAA16180.
GeneIDi12931799.
946799.
KEGGiecj:Y75_p2289.
eco:b2323.
PATRICi32120019. VBIEscCol129921_2419.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A31284. SYECA1.
RefSeqi NP_416826.1. NC_000913.3.
YP_490565.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DD8 X-ray 2.30 A/B/C/D 1-406 [» ]
1EK4 X-ray 1.85 A/B/C/D 1-406 [» ]
1F91 X-ray 2.40 A/B/C/D 1-406 [» ]
1FJ4 X-ray 2.35 A/B/C/D 1-406 [» ]
1FJ8 X-ray 2.27 A/B/C/D 1-406 [» ]
1G5X X-ray 2.45 A/B/C/D 1-406 [» ]
1H4F X-ray 2.00 A/B/C/D 1-406 [» ]
2AQ7 X-ray 2.30 A/B/C/D 1-406 [» ]
2AQB X-ray 2.19 A/B/C/D 1-406 [» ]
2BUH X-ray 1.90 A/B/C/D 1-406 [» ]
2BUI X-ray 2.40 A/B/C/D 1-406 [» ]
2BYW X-ray 1.70 A/B/C/D 5-406 [» ]
2BYX X-ray 2.00 A/B/C/D 5-406 [» ]
2BYY X-ray 2.20 A/B/C/D 1-406 [» ]
2BYZ X-ray 1.95 A/B/C/D 1-406 [» ]
2BZ3 X-ray 2.00 A/B/C/D 1-406 [» ]
2BZ4 X-ray 1.86 A/B/C/D 1-406 [» ]
2CDH X-ray 4.20 A/B/C/D/E/F 1-406 [» ]
2CF2 X-ray 4.30 A/J 1-406 [» ]
2VB7 X-ray 1.60 A/B/C/D 1-406 [» ]
2VB8 X-ray 1.52 A/B/C/D 1-406 [» ]
2VB9 X-ray 1.50 A/B/C/D 1-406 [» ]
2VBA X-ray 1.36 A/B/C/D 1-406 [» ]
ProteinModelPortali P0A953.
SMRi P0A953. Positions 1-406.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29379N.
IntActi P0A953. 9 interactions.
MINTi MINT-1235843.
STRINGi 511145.b2323.

Chemistry

BindingDBi P0A953.
ChEMBLi CHEMBL4913.
DrugBanki DB01034. Cerulenin.

Proteomic databases

PaxDbi P0A953.
PRIDEi P0A953.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75383 ; AAC75383 ; b2323 .
BAA16180 ; BAA16180 ; BAA16180 .
GeneIDi 12931799.
946799.
KEGGi ecj:Y75_p2289.
eco:b2323.
PATRICi 32120019. VBIEscCol129921_2419.

Organism-specific databases

EchoBASEi EB0270.
EcoGenei EG10274. fabB.

Phylogenomic databases

eggNOGi COG0304.
HOGENOMi HOG000060165.
InParanoidi P0A953.
KOi K00647.
OMAi FNPEYAE.
OrthoDBi EOG6DG2SR.
PhylomeDBi P0A953.

Enzyme and pathway databases

UniPathwayi UPA00094 .
BioCyci EcoCyc:FABB-MONOMER.
ECOL316407:JW2320-MONOMER.
MetaCyc:FABB-MONOMER.
RETL1328306-WGS:GSTH-112-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A953.
PROi P0A953.

Gene expression databases

Genevestigatori P0A953.

Family and domain databases

Gene3Di 3.40.47.10. 2 hits.
InterProi IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view ]
Pfami PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view ]
SUPFAMi SSF53901. SSF53901. 2 hits.
PROSITEi PS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 93 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