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C5CAR9

- C5CAR9_MICLC

UniProt

C5CAR9 - C5CAR9_MICLC

Protein

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

Gene

fabH

Organism
Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus)
Status
Unreviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 40 (01 Oct 2014)
      Sequence version 1 (28 Jul 2009)
      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 annotationSAAS annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei123 – 1231UniRule annotation
    Active sitei275 – 2751UniRule annotation
    Active sitei306 – 3061UniRule 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

    AcyltransferaseUniRule annotationSAAS annotation, Transferase

    Keywords - Biological processi

    Fatty acid biosynthesisUniRule annotationSAAS annotation, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Enzyme and pathway databases

    BioCyciMLUT465515:GHH6-929-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
    Gene namesi
    Name:fabHUniRule annotation
    Ordered Locus Names:Mlut_09310Imported
    OrganismiMicrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus)Imported
    Taxonomic identifieri465515 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeMicrococcus
    ProteomesiUP000000738: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotationSAAS annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    CytoplasmUniRule annotationSAAS annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotationSAAS annotation

    Protein-protein interaction databases

    STRINGi465515.Mlut_09310.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4EWPX-ray2.20A/B/C/D/E/F1-350[»]
    ProteinModelPortaliC5CAR9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni276 – 2805ACP-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.
    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.

    C5CAR9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTVTLKQHER PAASRIVAVG AYRPANLVPN EDLIGPIDSS DEWIRQRTGI    50
    VTRQRATAEE TVPVMAVGAA REALERAGLQ GSDLDAVIVS TVTFPHATPS 100
    AAALVAHEIG ATPAPAYDVS AACAGYCYGV AQADALVRSG TARHVLVVGV 150
    ERLSDVVDPT DRSISFLLGD GAGAVIVAAS DEPGISPSVW GSDGERWSTI 200
    SMTHSQLELR DAVEHARTTG DASAITGAEG MLWPTLRQDG PSVFRWAVWS 250
    MAKVAREALD AAGVEPEDLA AFIPHQANMR IIDEFAKQLK LPESVVVARD 300
    IADAGNTSAA SIPLAMHRLL EENPELSGGL ALQIGFGAGL VYGAQVVRLP 350
    Length:350
    Mass (Da):36,749
    Last modified:July 28, 2009 - v1
    Checksum:i7CD8432B19C723B7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001628 Genomic DNA. Translation: ACS30452.1.
    RefSeqiYP_002957006.1. NC_012803.1.

    Genome annotation databases

    EnsemblBacteriaiACS30452; ACS30452; Mlut_09310.
    GeneIDi7986167.
    KEGGimlu:Mlut_09310.
    PATRICi22622508. VBIMicLut29563_0892.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001628 Genomic DNA. Translation: ACS30452.1 .
    RefSeqi YP_002957006.1. NC_012803.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4EWP X-ray 2.20 A/B/C/D/E/F 1-350 [» ]
    ProteinModelPortali C5CAR9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 465515.Mlut_09310.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACS30452 ; ACS30452 ; Mlut_09310 .
    GeneIDi 7986167.
    KEGGi mlu:Mlut_09310.
    PATRICi 22622508. VBIMicLut29563_0892.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00094 .
    BioCyci MLUT465515:GHH6-929-MONOMER.

    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 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230Imported.
    2. "Structure of FabH and factors affecting the distribution of branched fatty acids in Micrococcus luteus."
      Pereira J.H., Goh E.B., Keasling J.D., Beller H.R., Adams P.D.
      Acta Crystallogr. D 68:1320-1328(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).

    Entry informationi

    Entry nameiC5CAR9_MICLC
    AccessioniPrimary (citable) accession number: C5CAR9
    Entry historyi
    Integrated into UniProtKB/TrEMBL: July 28, 2009
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 40 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported, Complete proteome, Multifunctional enzymeUniRule annotationSAAS annotation, Reference proteomeImported

    External Data

    Dasty 3