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O53551

- FAC17_MYCTU

UniProt

O53551 - FAC17_MYCTU

Protein

Long-chain-fatty-acid--CoA ligase FadD17

Gene

fadD17

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 85 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      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. lipid biosynthetic process Source: UniProtKB
    3. long-chain fatty acid biosynthetic 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:RV3506-MONOMER.
    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Long-chain-fatty-acid--CoA ligase FadD17 (EC:6.2.1.3)
    Short name:
    FACL
    Alternative name(s):
    Acyl-CoA synthetase
    Gene namesi
    Name:fadD17
    Ordered Locus Names:Rv3506
    OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    Taxonomic identifieri83332 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    ProteomesiUP000001584: Chromosome

    Organism-specific databases

    TubercuListiRv3506.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: MTBBASE
    2. plasma membrane Source: MTBBASE

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 502502Long-chain-fatty-acid--CoA ligase FadD17PRO_0000406787Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi83332.Rv3506.

    Structurei

    3D structure databases

    ProteinModelPortaliO53551.
    SMRiO53551. Positions 42-491.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0318.
    HOGENOMiHOG000052047.
    KOiK00666.
    OMAiNTHKEMA.
    OrthoDBiEOG6VF30G.
    PhylomeDBiO53551.

    Family and domain databases

    InterProiIPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view]
    PROSITEiPS00455. AMP_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O53551-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTPTHPTVTE LLLPLSEIDD RGVYFEDSFT SWRDHIRHGA AIAAALRERL    50
    DPARPPHVGV LLQNTPFFSA TLVAGALSGI VPVGLNPVRR GAALAGDIAK 100
    ADCQLVLTGS GSAEVPADVE HINVDSPEWT DEVAAHRDTE VRFRSADLAD 150
    LFMLIFTSGT SGDPKAVKCS HRKVAIAGVT ITQRFSLGRD DVCYVSMPLF 200
    HSNAVLVGWA VAAACQGSMA LRRKFSASQF LADVRRYGAT YANYVGKPLS 250
    YVLATPELPD DADNPLRAVY GNEGVPGDID RFGRRFGCVV MDGFGSTEGG 300
    VAITRTLDTP AGALGPLPGG IQIVDPDTGE PCPTGVVGEL VNTAGPGGFE 350
    GYYNDEAAEA ERMAGGVYHS GDLAYRDDAG YAYFAGRLGD WMRVDGENLG 400
    TAPIERVLMR YPDATEVAVY PVPDPVVGDQ VMAALVLAPG TKFDADKFRA 450
    FLTEQPDLGH KQWPSYVRVS AGLPRTMTFK VIKRQLSAEG VACADPVWPI 500
    RR 502
    Length:502
    Mass (Da):53,739
    Last modified:June 1, 1998 - v1
    Checksum:i0AF9A7B3B9C83A4D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL123456 Genomic DNA. Translation: CCP46328.1.
    PIRiD70806.
    RefSeqiNP_218023.1. NC_000962.3.
    YP_006516995.1. NC_018143.2.

    Genome annotation databases

    EnsemblBacteriaiCCP46328; CCP46328; Rv3506.
    GeneIDi13317113.
    888251.
    KEGGimtu:Rv3506.
    mtv:RVBD_3506.
    PATRICi18156406. VBIMycTub87468_3913.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL123456 Genomic DNA. Translation: CCP46328.1 .
    PIRi D70806.
    RefSeqi NP_218023.1. NC_000962.3.
    YP_006516995.1. NC_018143.2.

    3D structure databases

    ProteinModelPortali O53551.
    SMRi O53551. Positions 42-491.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 83332.Rv3506.

    Chemistry

    ChEMBLi CHEMBL5783.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CCP46328 ; CCP46328 ; Rv3506 .
    GeneIDi 13317113.
    888251.
    KEGGi mtu:Rv3506.
    mtv:RVBD_3506.
    PATRICi 18156406. VBIMycTub87468_3913.

    Organism-specific databases

    TubercuListi Rv3506.

    Phylogenomic databases

    eggNOGi COG0318.
    HOGENOMi HOG000052047.
    KOi K00666.
    OMAi NTHKEMA.
    OrthoDBi EOG6VF30G.
    PhylomeDBi O53551.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .
    BioCyci MTBRV:RV3506-MONOMER.

    Family and domain databases

    InterProi IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view ]
    Pfami PF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 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 nameiFAC17_MYCTU
    AccessioniPrimary (citable) accession number: O53551
    Secondary accession number(s): L0TCQ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 5, 2011
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 85 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, 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