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Q8G1E0

- FABH_BRUSU

UniProt

Q8G1E0 - FABH_BRUSU

Protein

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

Gene

fabH

Organism
Brucella suis biovar 1 (strain 1330)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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. 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. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.UniRule annotation

    Catalytic activityi

    Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei113 – 1131UniRule annotation
    Active sitei250 – 2501UniRule annotation
    Active sitei280 – 2801UniRule annotation

    GO - Molecular functioni

    1. 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: InterPro
    2. beta-ketoacyl-acyl-carrier-protein synthase III activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

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

    Enzyme and pathway databases

    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-oxoacyl-[acyl-carrier-protein] synthase 3UniRule annotation (EC:2.3.1.180UniRule annotation)
    Alternative name(s):
    3-oxoacyl-[acyl-carrier-protein] synthase IIIUniRule annotation
    Beta-ketoacyl-ACP synthase IIIUniRule annotation
    Short name:
    KAS IIIUniRule annotation
    Gene namesi
    Name:fabHUniRule annotation
    Ordered Locus Names:BR0777, BS1330_I0773
    OrganismiBrucella suis biovar 1 (strain 1330)
    Taxonomic identifieri204722 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
    ProteomesiUP000000824: Chromosome I, UP000007104: Chromosome I

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3233233-oxoacyl-[acyl-carrier-protein] synthase 3PRO_0000110408Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi204722.BR0777.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8G1E0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni251 – 2555ACP-bindingUniRule annotation

    Domaini

    The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.UniRule annotation

    Sequence similaritiesi

    Belongs to the FabH family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0332.
    HOGENOMiHOG000246674.
    KOiK00648.
    OMAiAHIVEET.
    OrthoDBiEOG6J74XN.

    Family and domain databases

    Gene3Di3.40.47.10. 2 hits.
    HAMAPiMF_01815. FabH.
    InterProiIPR013751. ACP_syn_III.
    IPR013747. ACP_syn_III_C.
    IPR004655. FabH_synth.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view]
    PfamiPF08545. ACP_syn_III. 1 hit.
    PF08541. ACP_syn_III_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF53901. SSF53901. 1 hit.
    TIGRFAMsiTIGR00747. fabH. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8G1E0-1 [UniParc]FASTAAdd to Basket

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    MIRSVVRGIG SALPKRVMKN TDFEGIVETS DEWIVQRTGI RERHIAGEGE    50
    TTVSLGAAAA RAAIENAGLQ PSDIDLVLLA TSTPNNTFPA SAVAIQRELG 100
    ITRGFAFDLQ AVCSGFIYAI TTADLYIRGG MARRVLVIGA ETFSHILDWT 150
    DRTTCVLFGD GAGAIVLEAA EGHGLTSDRG ILAANLRSDG NHKEKLYVDG 200
    GPSTTQTVGH LRMEGREVFK HAVGMITDVI EASFEATGLT AEDIDWFVPH 250
    QANKRIIDAS AKKLHIAEEK VVITVDRHGN TSAASVPLAL ATAVADGRIK 300
    KGDLVLLEAM GGGFTWGAVL VRW 323
    Length:323
    Mass (Da):34,429
    Last modified:March 1, 2003 - v1
    Checksum:iF9105FF67D1237BB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014291 Genomic DNA. Translation: AAN29706.1.
    CP002997 Genomic DNA. Translation: AEM18123.1.
    RefSeqiNP_697791.1. NC_004310.3.
    YP_005615615.1. NC_017251.1.

    Genome annotation databases

    EnsemblBacteriaiAAN29706; AAN29706; BR0777.
    AEM18123; AEM18123; BS1330_I0773.
    GeneIDi1166442.
    12137096.
    KEGGibms:BR0777.
    bsi:BS1330_I0773.
    PATRICi17789846. VBIBruSui107850_0787.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014291 Genomic DNA. Translation: AAN29706.1 .
    CP002997 Genomic DNA. Translation: AEM18123.1 .
    RefSeqi NP_697791.1. NC_004310.3.
    YP_005615615.1. NC_017251.1.

    3D structure databases

    ProteinModelPortali Q8G1E0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 204722.BR0777.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN29706 ; AAN29706 ; BR0777 .
    AEM18123 ; AEM18123 ; BS1330_I0773 .
    GeneIDi 1166442.
    12137096.
    KEGGi bms:BR0777.
    bsi:BS1330_I0773.
    PATRICi 17789846. VBIBruSui107850_0787.

    Phylogenomic databases

    eggNOGi COG0332.
    HOGENOMi HOG000246674.
    KOi K00648.
    OMAi AHIVEET.
    OrthoDBi EOG6J74XN.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .

    Family and domain databases

    Gene3Di 3.40.47.10. 2 hits.
    HAMAPi MF_01815. FabH.
    InterProi IPR013751. ACP_syn_III.
    IPR013747. ACP_syn_III_C.
    IPR004655. FabH_synth.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view ]
    Pfami PF08545. ACP_syn_III. 1 hit.
    PF08541. ACP_syn_III_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53901. SSF53901. 1 hit.
    TIGRFAMsi TIGR00747. fabH. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 1330.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 1330.

    Entry informationi

    Entry nameiFABH_BRUSU
    AccessioniPrimary (citable) accession number: Q8G1E0
    Secondary accession number(s): G0K8S5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 15, 2003
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 78 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

    Complete proteome, Multifunctional enzyme

    Documents

    1. Brucella suis
      Brucella suis (strain 1330): entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3