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Protein

Malonyl-CoA reductase

Gene

mcr

Organism
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. Can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA.1 Publication

Catalytic activityi

Malonate semialdehyde + CoA + NADP+ = malonyl-CoA + NADPH.1 Publication

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Divalent metal cations such as Mg2+ and Mn2+ ions at 5 mM.1 Publication

Enzyme regulationi

Activated by dithioerythritol (5 mM) and inhibited by the thiol-blocking agent iodoacetamide (0.1 mM).1 Publication

Kineticsi

  1. KM=25 µM for NADP (with 0.2 mM malonyl-CoA)1 Publication
  2. KM=40 µM for malonyl-CoA (with 0.5 mM NADP)1 Publication

    pH dependencei

    Optimum pH is 7.2, with half-maximal activities at pH 6 and 8.1 Publication

    Temperature dependencei

    Optimum temperature is 85 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei153Acyl-thioester intermediateBy similarity1
    Active sitei248Proton acceptorBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi16 – 19NADPBy similarity4
    Nucleotide bindingi183 – 184NADPBy similarity2
    Nucleotide bindingi335 – 336NADPBy similarity2

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP, RNA-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13611.
    BRENDAi1.2.1.75. 6166.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malonyl-CoA reductase (EC:1.2.1.75)
    Gene namesi
    Name:mcr
    Synonyms:scr
    Ordered Locus Names:STK_21710
    OrganismiSulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
    Taxonomic identifieri273063 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
    Proteomesi
    • UP000001015 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004188551 – 359Malonyl-CoA reductaseAdd BLAST359

    Interactioni

    Subunit structurei

    Homodimer and possibly a tetramer.1 Publication

    Protein-protein interaction databases

    STRINGi273063.ST2171.

    Structurei

    Secondary structure

    1359
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi8 – 12Combined sources5
    Turni13 – 16Combined sources4
    Helixi20 – 28Combined sources9
    Beta strandi31 – 41Combined sources11
    Turni42 – 45Combined sources4
    Helixi48 – 51Combined sources4
    Beta strandi56 – 58Combined sources3
    Helixi62 – 65Combined sources4
    Helixi74 – 76Combined sources3
    Beta strandi82 – 85Combined sources4
    Turni89 – 91Combined sources3
    Helixi92 – 101Combined sources10
    Beta strandi105 – 108Combined sources4
    Turni112 – 115Combined sources4
    Turni124 – 126Combined sources3
    Helixi128 – 132Combined sources5
    Helixi133 – 141Combined sources9
    Beta strandi144 – 149Combined sources6
    Helixi153 – 168Combined sources16
    Beta strandi171 – 180Combined sources10
    Helixi182 – 185Combined sources4
    Helixi192 – 195Combined sources4
    Helixi204 – 218Combined sources15
    Helixi230 – 232Combined sources3
    Beta strandi234 – 238Combined sources5
    Beta strandi248 – 258Combined sources11
    Helixi262 – 270Combined sources9
    Helixi275 – 278Combined sources4
    Beta strandi288 – 292Combined sources5
    Helixi300 – 303Combined sources4
    Turni307 – 311Combined sources5
    Beta strandi313 – 323Combined sources11
    Beta strandi326 – 333Combined sources8
    Turni335 – 340Combined sources6
    Helixi341 – 353Combined sources13

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4DPKX-ray2.05A/B/C/D1-359[»]
    4DPLX-ray1.90A/B/C/D1-359[»]
    4DPMX-ray2.30A/B/C/D/E/F1-359[»]
    ProteinModelPortaliQ96YK1.
    SMRiQ96YK1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiarCOG00494. Archaea.
    COG0136. LUCA.
    HOGENOMiHOG000013358.
    KOiK15017.
    OMAiDATTHRI.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR005676. Asp_semi-ald_DH_pep-lack.
    IPR012080. Asp_semialdehyde_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR000534. Semialdehyde_DH_NAD-bd.
    IPR012280. Semialdhyde_DH_dimer_dom.
    [Graphical view]
    PfamiPF01118. Semialdhyde_dh. 1 hit.
    PF02774. Semialdhyde_dhC. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000148. ASA_dh. 1 hit.
    SMARTiSM00859. Semialdhyde_dh. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR00978. asd_EA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q96YK1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MILMRRTLKA AILGATGLVG IEYVRMLSNH PYIKPAYLAG KGSVGKPYGE
    60 70 80 90 100
    VVRWQTVGQV PKEIADMEIK PTDPKLMDDV DIIFSPLPQG AAGPVEEQFA
    110 120 130 140 150
    KEGFPVISNS PDHRFDPDVP LLVPELNPHT ISLIDEQRKR REWKGFIVTT
    160 170 180 190 200
    PLCTAQGAAI PLGAIFKDYK MDGAFITTIQ SLSGAGYPGI PSLDVVDNIL
    210 220 230 240 250
    PLGDGYDAKT IKEIFRILSE VKRNVDEPKL EDVSLAATTH RIATIHGHYE
    260 270 280 290 300
    VLYVSFKEET AAEKVKETLE NFRGEPQDLK LPTAPSKPII VMNEDTRPQV
    310 320 330 340 350
    YFDRWAGDIP GMSVVVGRLK QVNKRMIRLV SLIHNTVRGA AGGGILAAEL

    LVEKGYIEK
    Length:359
    Mass (Da):39,560
    Last modified:December 1, 2001 - v1
    Checksum:i426AAE51597DD0E8
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000023 Genomic DNA. Translation: BAB67276.1.

    Genome annotation databases

    EnsemblBacteriaiBAB67276; BAB67276; STK_21710.
    KEGGisto:STK_21710.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000023 Genomic DNA. Translation: BAB67276.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4DPKX-ray2.05A/B/C/D1-359[»]
    4DPLX-ray1.90A/B/C/D1-359[»]
    4DPMX-ray2.30A/B/C/D/E/F1-359[»]
    ProteinModelPortaliQ96YK1.
    SMRiQ96YK1.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi273063.ST2171.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAB67276; BAB67276; STK_21710.
    KEGGisto:STK_21710.

    Phylogenomic databases

    eggNOGiarCOG00494. Archaea.
    COG0136. LUCA.
    HOGENOMiHOG000013358.
    KOiK15017.
    OMAiDATTHRI.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13611.
    BRENDAi1.2.1.75. 6166.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR005676. Asp_semi-ald_DH_pep-lack.
    IPR012080. Asp_semialdehyde_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR000534. Semialdehyde_DH_NAD-bd.
    IPR012280. Semialdhyde_DH_dimer_dom.
    [Graphical view]
    PfamiPF01118. Semialdhyde_dh. 1 hit.
    PF02774. Semialdhyde_dhC. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000148. ASA_dh. 1 hit.
    SMARTiSM00859. Semialdhyde_dh. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR00978. asd_EA. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMCR_SULTO
    AccessioniPrimary (citable) accession number: Q96YK1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: December 1, 2001
    Last modified: November 2, 2016
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This enzyme contains bound RNA, but the physiological role is not known.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.