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Protein

3-hydroxypropionyl-coenzyme A dehydratase

Gene

Msed_2001

Organism
Metallosphaera sedula (strain ATCC 51363 / DSM 5348)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in autotrophic carbon fixation via the 3-hydroxypropionate/4-hydroxybutyrate cycle. Catalyzes the reversible dehydration of 3-hydroxypropionyl-CoA to form acryloyl-CoA, and the reversible dehydration of (S)-3-hydroxybutyryl-CoA to form crotonyl-CoA. Inactive towards (R)-3-hydroxybutyryl-CoA.1 Publication

Catalytic activityi

3-hydroxypropanoyl-CoA = acryloyl-CoA + H2O.1 Publication

Kineticsi

  1. KM=60 µM for 3-hydroxypropionyl-CoA1 Publication
  2. KM=75 µM for (S)-3-hydroxybutyryl-CoA1 Publication

    pH dependencei

    Optimum pH is 8.1 at room temperature. Retains half maximum activity at pH 6.5 and pH 9.5 at room temperature.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei113 – 1131NucleophileSequence analysis
    Active sitei133 – 1331Proton acceptorSequence analysis

    GO - Molecular functioni

    • 3-hydroxypropionyl-CoA dehydratase activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13729.
    MSED399549:GH1O-2032-MONOMER.
    RETL1328306-WGS:GSTH-1756-MONOMER.
    BRENDAi4.2.1.116. 7245.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-hydroxypropionyl-coenzyme A dehydratase1 Publication (EC:4.2.1.116)
    Short name:
    3-hydroxypropionyl-CoA dehydratase1 Publication
    Gene namesi
    Ordered Locus Names:Msed_2001
    OrganismiMetallosphaera sedula (strain ATCC 51363 / DSM 5348)
    Taxonomic identifieri399549 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeMetallosphaera
    Proteomesi
    • UP000000242 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2592593-hydroxypropionyl-coenzyme A dehydratasePRO_0000404649Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi399549.Msed_2001.

    Structurei

    3D structure databases

    ProteinModelPortaliA4YI89.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the enoyl-CoA hydratase/isomerase family.Sequence analysis

    Phylogenomic databases

    eggNOGiENOG4102TIM. Archaea.
    COG1024. LUCA.
    HOGENOMiHOG000027939.
    KOiK15019.
    OMAiAGRSMPR.

    Family and domain databases

    Gene3Di1.10.12.10. 1 hit.
    3.90.226.10. 1 hit.
    InterProiIPR029045. ClpP/crotonase-like_dom.
    IPR014748. Crontonase_C.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    [Graphical view]
    PfamiPF00378. ECH_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF52096. SSF52096. 1 hit.
    PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A4YI89-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEFETIETKK EGNLFWITLN RPDKLNALNA KLLEELDRAV SQAESDPEIR
    60 70 80 90 100
    VIIITGKGKA FCAGADITQF NQLTPAEAWK FSKKGREIMD KIEALSKPTI
    110 120 130 140 150
    AMINGYALGG GLELALACDI RIAAEEAQLG LPEINLGIYP GYGGTQRLTR
    160 170 180 190 200
    VIGKGRALEM MMTGDRIPGK DAEKYGLVNR VVPLANLEQE TRKLAEKIAK
    210 220 230 240 250
    KSPISLALIK EVVNRGLDSP LLSGLALESV GWGVVFSTED KKEGVSAFLE

    KREPTFKGK
    Length:259
    Mass (Da):28,316
    Last modified:May 29, 2007 - v1
    Checksum:i5B58E3747F1410BE
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000682 Genomic DNA. Translation: ABP96141.1.
    RefSeqiWP_012021928.1. NC_009440.1.

    Genome annotation databases

    EnsemblBacteriaiABP96141; ABP96141; Msed_2001.
    GeneIDi5103388.
    KEGGimse:Msed_2001.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000682 Genomic DNA. Translation: ABP96141.1.
    RefSeqiWP_012021928.1. NC_009440.1.

    3D structure databases

    ProteinModelPortaliA4YI89.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi399549.Msed_2001.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABP96141; ABP96141; Msed_2001.
    GeneIDi5103388.
    KEGGimse:Msed_2001.

    Phylogenomic databases

    eggNOGiENOG4102TIM. Archaea.
    COG1024. LUCA.
    HOGENOMiHOG000027939.
    KOiK15019.
    OMAiAGRSMPR.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13729.
    MSED399549:GH1O-2032-MONOMER.
    RETL1328306-WGS:GSTH-1756-MONOMER.
    BRENDAi4.2.1.116. 7245.

    Family and domain databases

    Gene3Di1.10.12.10. 1 hit.
    3.90.226.10. 1 hit.
    InterProiIPR029045. ClpP/crotonase-like_dom.
    IPR014748. Crontonase_C.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    [Graphical view]
    PfamiPF00378. ECH_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF52096. SSF52096. 1 hit.
    PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism."
      Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.
      Appl. Environ. Microbiol. 74:682-692(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51363 / DSM 5348.
    2. "3-hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales."
      Teufel R., Kung J.W., Kockelkorn D., Alber B.E., Fuchs G.
      J. Bacteriol. 191:4572-4581(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry nameiHPCD_METS5
    AccessioniPrimary (citable) accession number: A4YI89
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 8, 2011
    Last sequence update: May 29, 2007
    Last modified: November 11, 2015
    This is version 55 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. 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.