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P43711

- FABH_HAEIN

UniProt

P43711 - FABH_HAEIN

Protein

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

Gene

fabH

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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 sitei112 – 1121UniRule annotation
    Active sitei243 – 2431UniRule annotation
    Active sitei273 – 2731UniRule 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:HI_0157
    OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
    Taxonomic identifieri71421 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
    ProteomesiUP000000579: Chromosome

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3163163-oxoacyl-[acyl-carrier-protein] synthase 3PRO_0000110432Add
    BLAST

    Proteomic databases

    PRIDEiP43711.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi71421.HI0157.

    Structurei

    Secondary structure

    1
    316
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 115
    Beta strandi16 – 183
    Helixi19 – 235
    Helixi30 – 367
    Beta strandi41 – 433
    Helixi51 – 6616
    Helixi70 – 723
    Beta strandi75 – 795
    Beta strandi86 – 883
    Helixi90 – 978
    Beta strandi104 – 1085
    Helixi111 – 1133
    Helixi114 – 12714
    Beta strandi132 – 14110
    Helixi142 – 1443
    Turni151 – 1566
    Beta strandi159 – 17113
    Beta strandi174 – 1818
    Beta strandi188 – 1903
    Helixi208 – 22821
    Turni229 – 2313
    Turni234 – 2363
    Beta strandi239 – 2424
    Helixi247 – 25610
    Helixi261 – 2633
    Helixi268 – 2714
    Helixi275 – 2773
    Helixi278 – 28811
    Beta strandi297 – 3048
    Turni305 – 3073
    Beta strandi308 – 3158

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3IL3X-ray2.70A1-316[»]
    ProteinModelPortaliP43711.
    SMRiP43711. Positions 1-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP43711.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni244 – 2485ACP-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.
    KOiK00648.
    OMAiAHIVEET.
    OrthoDBiEOG6J74XN.
    PhylomeDBiP43711.

    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.

    P43711-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNSRILSTGS YLPSHIRTNA DLEKMVDTSD EWIVTRSGIR ERRIAAEDET    50
    VATMGFEAAK NAIEAAQINP QDIELIIVAT TSHSHAYPSA ACQVQGLLNI 100
    DDAISFDLAA ACTGFVYALS VADQFIRAGK VKKALVIGSD LNSRKLDETD 150
    RSTVVLFGDG AGAVILEASE QEGIISTHLH ASADKNNALV LAQPERGIEK 200
    SGYIEMQGNE TFKLAVRELS NVVEETLLAN NLDKKDLDWL VPHQANLRII 250
    TATAKKLEMD MSQVVVTLDK YANNSAATVP VALDEAIRDG RIQRGQLLLL 300
    EAFGGGWTWG SALVRF 316
    Length:316
    Mass (Da):34,280
    Last modified:November 1, 1995 - v1
    Checksum:i2D00ADD61DCB6A66
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42023 Genomic DNA. Translation: AAC21826.1.
    PIRiF64051.
    RefSeqiNP_438327.1. NC_000907.1.

    Genome annotation databases

    EnsemblBacteriaiAAC21826; AAC21826; HI_0157.
    GeneIDi951067.
    KEGGihin:HI0157.
    PATRICi20188811. VBIHaeInf48452_0162.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42023 Genomic DNA. Translation: AAC21826.1 .
    PIRi F64051.
    RefSeqi NP_438327.1. NC_000907.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3IL3 X-ray 2.70 A 1-316 [» ]
    ProteinModelPortali P43711.
    SMRi P43711. Positions 1-316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 71421.HI0157.

    Chemistry

    BindingDBi P43711.
    ChEMBLi CHEMBL3822.

    Proteomic databases

    PRIDEi P43711.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC21826 ; AAC21826 ; HI_0157 .
    GeneIDi 951067.
    KEGGi hin:HI0157.
    PATRICi 20188811. VBIHaeInf48452_0162.

    Phylogenomic databases

    eggNOGi COG0332.
    KOi K00648.
    OMAi AHIVEET.
    OrthoDBi EOG6J74XN.
    PhylomeDBi P43711.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .

    Miscellaneous databases

    EvolutionaryTracei P43711.
    PROi P43711.

    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: ATCC 51907 / DSM 11121 / KW20 / Rd.
    2. "Identification, substrate specificity, and inhibition of the Streptococcus pneumoniae beta-ketoacyl-acyl carrier protein synthase III (FabH)."
      Khandekar S.S., Gentry D.R., Van Aller G.S., Warren P., Xiang H., Silverman C., Doyle M.L., Chambers P.A., Konstantinidis A.K., Brandt M., Daines R.A., Lonsdale J.T.
      J. Biol. Chem. 276:30024-30030(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITION BY ANTIBIOTICS.

    Entry informationi

    Entry nameiFABH_HAEIN
    AccessioniPrimary (citable) accession number: P43711
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Inhibited by the SB418011 antibiotic. Not inhibited by cerulenin, and weakly inhibited by thiolactomycin.

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Haemophilus influenzae
      Haemophilus influenzae (strain Rd): entries and gene names
    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