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P0A953

- FABB_ECOLI

UniProt

P0A953 - FABB_ECOLI

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
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (19 Jul 2005)
      Previous versions | rss
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    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

    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A953.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0304.
    HOGENOMiHOG000060165.
    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

    MKRAVITGLG IVSSIGNNQQ EVLASLREGR SGITFSQELK DSGMRSHVWG    50
    NVKLDTTGLI DRKVVRFMSD ASIYAFLSME QAIADAGLSP EAYQNNPRVG 100
    LIAGSGGGSP RFQVFGADAM RGPRGLKAVG PYVVTKAMAS GVSACLATPF 150
    KIHGVNYSIS SACATSAHCI GNAVEQIQLG KQDIVFAGGG EELCWEMACE 200
    FDAMGALSTK YNDTPEKASR TYDAHRDGFV IAGGGGMVVV EELEHALARG 250
    AHIYAEIVGY GATSDGADMV APSGEGAVRC MKMAMHGVDT PIDYLNSHGT 300
    STPVGDVKEL AAIREVFGDK SPAISATKAM TGHSLGAAGV QEAIYSLLML 350
    EHGFIAPSIN IEELDEQAAG LNIVTETTDR ELTTVMSNSF GFGGTNATLV 400
    MRKLKD 406
    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.
    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.
    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

    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 1, 2014
    This is version 92 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