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O53521

- FAC15_MYCTU

UniProt

O53521 - FAC15_MYCTU

Protein

Long-chain-fatty-acid--CoA ligase FadD15

Gene

fadD15

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 3 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Catalyzes the activation of long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension.1 Publication

    Catalytic activityi

    ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.

    Pathwayi

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. long-chain fatty acid-CoA ligase activity Source: MTBBASE

    GO - Biological processi

    1. Actinobacterium-type cell wall biogenesis Source: UniProtKB
    2. fatty acid biosynthetic process Source: UniProtKB-UniPathway
    3. lipid biosynthetic process Source: UniProtKB
    4. long-chain fatty acid metabolic process Source: MTBBASE

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMTBRV:RV2187-MONOMER.
    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Long-chain-fatty-acid--CoA ligase FadD15 (EC:6.2.1.3)
    Short name:
    FACL
    Alternative name(s):
    Acyl-CoA synthetase
    Gene namesi
    Name:fadD15
    Ordered Locus Names:Rv2187
    OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    Taxonomic identifieri83332 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    ProteomesiUP000001584: Chromosome

    Organism-specific databases

    TubercuListiRv2187.

    Subcellular locationi

    GO - Cellular componenti

    1. cell wall Source: MTBBASE
    2. plasma membrane Source: MTBBASE

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 600600Long-chain-fatty-acid--CoA ligase FadD15PRO_0000406784Add
    BLAST

    Proteomic databases

    PRIDEiO53521.

    PTM databases

    PhosSiteiP12071722.

    Interactioni

    Protein-protein interaction databases

    STRINGi83332.Rv2187.

    Structurei

    3D structure databases

    ProteinModelPortaliO53521.
    SMRiO53521. Positions 29-545.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1022.
    HOGENOMiHOG000229985.
    KOiK01897.
    OMAiFRELAIN.
    OrthoDBiEOG64FKGZ.
    PhylomeDBiO53521.

    Family and domain databases

    InterProiIPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    [Graphical view]
    PROSITEiPS00455. AMP_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O53521-1 [UniParc]FASTAAdd to Basket

    « Hide

    MREISVPAPF TVGEHDNVAA MVFEHERDDP DYVIYQRLID GVWTDVTCAE    50
    AANQIRAAAL GLISLGVQAG DRVVIFSATR YEWAILDFAI LAVGAVTVPT 100
    YETSSAEQVR WVLQDSEAVV LFAETDSHAT MVAELSGSVP ALREVLQIAG 150
    SGPNALDRLT EAGASVDPAE LTARLAALRS TDPATLIYTS GTTGRPKGCQ 200
    LTQSNLVHEI KGARAYHPTL LRKGERLLVF LPLAHVLARA ISMAAFHSKV 250
    TVGFTSDIKN LLPMLAVFKP TVVVSVPRVF EKVYNTAEQN AANAGKGRIF 300
    AIAAQTAVDW SEACDRGGPG LLLRAKHAVF DRLVYRKLRA ALGGNCRAAV 350
    SGGAPLGARL GHFYRGAGLT IYEGYGLSGT SGGVAISQFN DLKIGTVGKP 400
    VPGNSLRIAD DGELLVRGGV VFSGYWRNEQ ATTEAFTDGW FKTGDLGAVD 450
    EDGFLTITGR KKEIIVTAGG KNVAPAVLED QLRAHPLISQ AVVVGDAKPF 500
    IGALITIDPE AFEGWKQRNS KTAGASVGDL ATDPDLIAEI DAAVKQANLA 550
    VSHAESIRKF RILPVDFTED TGELTPTMKV KRKVVAEKFA SDIEAIYNKE 600
    Length:600
    Mass (Da):64,035
    Last modified:July 5, 2004 - v3
    Checksum:iDCA7C09033C3CEBA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL123456 Genomic DNA. Translation: CCP44964.1.
    PIRiE70937.
    RefSeqiNP_216703.1. NC_000962.3.
    YP_006515606.1. NC_018143.2.

    Genome annotation databases

    EnsemblBacteriaiCCP44964; CCP44964; Rv2187.
    GeneIDi13318875.
    887456.
    KEGGimtu:Rv2187.
    mtv:RVBD_2187.
    PATRICi18153420. VBIMycTub87468_2438.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL123456 Genomic DNA. Translation: CCP44964.1 .
    PIRi E70937.
    RefSeqi NP_216703.1. NC_000962.3.
    YP_006515606.1. NC_018143.2.

    3D structure databases

    ProteinModelPortali O53521.
    SMRi O53521. Positions 29-545.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 83332.Rv2187.

    PTM databases

    PhosSitei P12071722.

    Proteomic databases

    PRIDEi O53521.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CCP44964 ; CCP44964 ; Rv2187 .
    GeneIDi 13318875.
    887456.
    KEGGi mtu:Rv2187.
    mtv:RVBD_2187.
    PATRICi 18153420. VBIMycTub87468_2438.

    Organism-specific databases

    TubercuListi Rv2187.

    Phylogenomic databases

    eggNOGi COG1022.
    HOGENOMi HOG000229985.
    KOi K01897.
    OMAi FRELAIN.
    OrthoDBi EOG64FKGZ.
    PhylomeDBi O53521.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .
    BioCyci MTBRV:RV2187-MONOMER.

    Family and domain databases

    InterProi IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view ]
    Pfami PF00501. AMP-binding. 1 hit.
    [Graphical view ]
    PROSITEi PS00455. AMP_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 25618 / H37Rv.
    2. "Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria."
      Trivedi O.A., Arora P., Sridharan V., Tickoo R., Mohanty D., Gokhale R.S.
      Nature 428:441-445(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN ACYL-COA SYNTHETASE.
      Strain: ATCC 25618 / H37Rv.
    3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ATCC 25618 / H37Rv.

    Entry informationi

    Entry nameiFAC15_MYCTU
    AccessioniPrimary (citable) accession number: O53521
    Secondary accession number(s): L0T8V6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 5, 2011
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 89 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: 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