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O67185

- FABH_AQUAE

UniProt

O67185 - FABH_AQUAE

Protein

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

Gene

fabH

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      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 sitei111 – 1111UniRule annotation
    Active sitei236 – 2361UniRule annotation
    Active sitei266 – 2661UniRule 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

    BioCyciAAEO224324:GJBH-783-MONOMER.
    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:aq_1099
    OrganismiAquifex aeolicus (strain VF5)
    Taxonomic identifieri224324 [NCBI]
    Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
    ProteomesiUP000000798: 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 – 3093093-oxoacyl-[acyl-carrier-protein] synthase 3PRO_0000110392Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi224324.aq_1099.

    Structurei

    Secondary structure

    1
    309
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 119
    Beta strandi14 – 185
    Helixi19 – 235
    Helixi30 – 378
    Beta strandi41 – 444
    Helixi50 – 6516
    Helixi69 – 713
    Beta strandi73 – 786
    Beta strandi83 – 875
    Helixi89 – 979
    Beta strandi103 – 1086
    Helixi110 – 1123
    Helixi113 – 12614
    Beta strandi131 – 14010
    Helixi141 – 1433
    Turni150 – 1556
    Beta strandi158 – 16710
    Beta strandi169 – 1713
    Beta strandi173 – 1819
    Helixi183 – 1886
    Beta strandi189 – 1913
    Beta strandi197 – 1993
    Helixi201 – 22323
    Helixi227 – 2293
    Beta strandi231 – 2355
    Helixi240 – 24910
    Helixi254 – 2563
    Helixi261 – 2644
    Helixi268 – 2703
    Helixi271 – 28111
    Beta strandi290 – 2978
    Turni298 – 3003
    Beta strandi301 – 3088

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EBDX-ray2.10A/B1-309[»]
    ProteinModelPortaliO67185.
    SMRiO67185. Positions 1-309.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO67185.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni237 – 2415ACP-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.

    O67185-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGTKIIGTGV YLPKNVLTNF DLEKIVDTSD EWITTRTGIK ERRIAKEETI    50
    TYMATQAAKE ALREANLSPE ELDLIILATL TPQKRFPSTA CLVQAQLKAK 100
    GVYAFDISAA CSGFIYALDI ADSFIKSGKA KNVLVIGAEK LSEAVDWEDR 150
    STCVLFGDGA GAVVVTRSED KSDILATRMY AEGSLEELLH ADNCGYIRMK 200
    GRELFKVAVR SMEEVCREVL EKAGVKPEEV SLVIPHQANV RIINALAEKL 250
    NIPKEKVFVN IQKYGNTSAA SIPIALHEAI KEGKVKRGDL ILMTAMGGGL 300
    TWGAVLLRY 309
    Length:309
    Mass (Da):33,825
    Last modified:August 1, 1998 - v1
    Checksum:iEB97518DB168140D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000657 Genomic DNA. Translation: AAC07144.1.
    PIRiF70394.
    RefSeqiNP_213748.1. NC_000918.1.
    WP_010880686.1. NC_000918.1.

    Genome annotation databases

    EnsemblBacteriaiAAC07144; AAC07144; aq_1099.
    GeneIDi1193819.
    KEGGiaae:aq_1099.
    PATRICi20959474. VBIAquAeo85532_0857.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000657 Genomic DNA. Translation: AAC07144.1 .
    PIRi F70394.
    RefSeqi NP_213748.1. NC_000918.1.
    WP_010880686.1. NC_000918.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EBD X-ray 2.10 A/B 1-309 [» ]
    ProteinModelPortali O67185.
    SMRi O67185. Positions 1-309.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224324.aq_1099.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC07144 ; AAC07144 ; aq_1099 .
    GeneIDi 1193819.
    KEGGi aae:aq_1099.
    PATRICi 20959474. VBIAquAeo85532_0857.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00094 .
    BioCyci AAEO224324:GJBH-783-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei O67185.

    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: VF5.
    2. "Crystal structure of 3-oxoacyl-[acyl-carrier-protein] synthase III from Aquifex aeolicus VF5."
      RIKEN structural genomics initiative (RSGI)
      Submitted (AUG-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
      Strain: VF5.

    Entry informationi

    Entry nameiFABH_AQUAE
    AccessioniPrimary (citable) accession number: O67185
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 95 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, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3