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Protein

Probable enoyl-CoA hydratase 1

Gene

Rv0130

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in the hydration of fatty acids for production of polyhydroxylalkanoates.1 Publication

Catalytic activityi

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.1 Publication

Kineticsi

  1. KM=55 µM for 2-butenoyl-CoA1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei40 – 401Important for catalytic activity
    Sitei42 – 421Transition state stabilizerSequence analysis
    Sitei45 – 451Important for catalytic activity
    Binding sitei124 – 1241Substrate; in homodimeric partnerCurated
    Binding sitei148 – 1481Substrate; in homodimeric partnerCurated

    GO - Molecular functioni

    • 3-hydroxyacyl-CoA dehydratase activity Source: MTBBASE
    • enoyl-CoA hydratase activity Source: MTBBASE

    GO - Biological processi

    • fatty acid biosynthetic process Source: MTBBASE
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Chemistry

    SwissLipidsiSLP:000001286.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable enoyl-CoA hydratase 1 (EC:4.2.1.17)
    Alternative name(s):
    N-related protein
    Nodulation protein
    Gene namesi
    Ordered Locus Names:Rv0130
    OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    Taxonomic identifieri83332 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    Proteomesi
    • UP000001584 Componenti: Chromosome

    Organism-specific databases

    TubercuListiRv0130.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi40 – 401D → N: 27% loss of activity. 1 Publication
    Mutagenesisi45 – 451H → Q: Total loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 151151Probable enoyl-CoA hydratase 1PRO_0000262761Add
    BLAST

    Proteomic databases

    PaxDbiP9WNP3.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi83332.Rv0130.

    Structurei

    Secondary structure

    1
    151
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 64Combined sources
    Helixi7 – 126Combined sources
    Turni13 – 153Combined sources
    Beta strandi16 – 205Combined sources
    Helixi28 – 3811Combined sources
    Helixi43 – 464Combined sources
    Helixi48 – 525Combined sources
    Helixi63 – 686Combined sources
    Helixi70 – 756Combined sources
    Beta strandi79 – 824Combined sources
    Beta strandi84 – 9512Combined sources
    Beta strandi105 – 11915Combined sources
    Beta strandi122 – 13312Combined sources
    Beta strandi140 – 15011Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C2IX-ray1.80A/B1-151[»]
    ProteinModelPortaliP9WNP3.
    SMRiP9WNP3. Positions 2-150.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 132122MaoC-likeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni60 – 634Substrate-bindingCurated
    Regioni86 – 894Substrate-binding (in homodimeric partner)Curated
    Regioni97 – 993Substrate-bindingCurated

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi11 – 144Poly-Ala

    Sequence similaritiesi

    Contains 1 MaoC-like domain.Curated

    Phylogenomic databases

    eggNOGiENOG4108ZPG. Bacteria.
    COG2030. LUCA.
    OMAiKLGESEW.
    PhylomeDBiP9WNP3.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    InterProiIPR029069. HotDog_dom.
    IPR002539. MaoC_dom.
    [Graphical view]
    PfamiPF01575. MaoC_dehydratas. 1 hit.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P9WNP3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRTFESVADL AAAAGEKVGQ SDWVTITQEE VNLFADATGD HQWIHVDPER
    60 70 80 90 100
    AAAGPFGTTI AHGFMTLALL PRLQHQMYTV KGVKLAINYG LNKVRFPAPV
    110 120 130 140 150
    PVGSRVRATS SLVGVEDLGN GTVQATVSTT VEVEGSAKPA CVAESIVRYV

    A
    Length:151
    Mass (Da):16,007
    Last modified:April 16, 2014 - v1
    Checksum:i7A2613466BBFCD57
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL123456 Genomic DNA. Translation: CCP42855.1.
    PIRiE70615.
    RefSeqiNP_214644.1. NC_000962.3.
    WP_003400912.1. NZ_KK339370.1.

    Genome annotation databases

    EnsemblBacteriaiCCP42855; CCP42855; Rv0130.
    GeneIDi886876.
    KEGGimtu:Rv0130.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL123456 Genomic DNA. Translation: CCP42855.1.
    PIRiE70615.
    RefSeqiNP_214644.1. NC_000962.3.
    WP_003400912.1. NZ_KK339370.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C2IX-ray1.80A/B1-151[»]
    ProteinModelPortaliP9WNP3.
    SMRiP9WNP3. Positions 2-150.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv0130.

    Chemistry

    SwissLipidsiSLP:000001286.

    Proteomic databases

    PaxDbiP9WNP3.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCCP42855; CCP42855; Rv0130.
    GeneIDi886876.
    KEGGimtu:Rv0130.

    Organism-specific databases

    TubercuListiRv0130.

    Phylogenomic databases

    eggNOGiENOG4108ZPG. Bacteria.
    COG2030. LUCA.
    OMAiKLGESEW.
    PhylomeDBiP9WNP3.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    InterProiIPR029069. HotDog_dom.
    IPR002539. MaoC_dom.
    [Graphical view]
    PfamiPF01575. MaoC_dehydratas. 1 hit.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiECH1_MYCTU
    AccessioniPrimary (citable) accession number: P9WNP3
    Secondary accession number(s): L0T2P7, P96807, Q7DAF4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2014
    Last sequence update: April 16, 2014
    Last modified: December 9, 2015
    This is version 16 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, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.