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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 Mg(2+) 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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei153 – 1531Acyl-thioester intermediateBy similarity
    Active sitei248 – 2481Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi16 – 194NADPBy similarity
    Nucleotide bindingi183 – 1842NADPBy similarity
    Nucleotide bindingi335 – 3362NADPBy similarity

    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.
    STOK273063:GJC7-2380-MONOMER.
    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
    ProteomesiUP000001015 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 359359Malonyl-CoA reductasePRO_0000418855Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer and possibly a tetramer.1 Publication

    Protein-protein interaction databases

    STRINGi273063.ST2171.

    Structurei

    Secondary structure

    1
    359
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 125Combined sources
    Turni13 – 164Combined sources
    Helixi20 – 289Combined sources
    Beta strandi31 – 4111Combined sources
    Turni42 – 454Combined sources
    Helixi48 – 514Combined sources
    Beta strandi56 – 583Combined sources
    Helixi62 – 654Combined sources
    Helixi74 – 763Combined sources
    Beta strandi82 – 854Combined sources
    Turni89 – 913Combined sources
    Helixi92 – 10110Combined sources
    Beta strandi105 – 1084Combined sources
    Turni112 – 1154Combined sources
    Turni124 – 1263Combined sources
    Helixi128 – 1325Combined sources
    Helixi133 – 1419Combined sources
    Beta strandi144 – 1496Combined sources
    Helixi153 – 16816Combined sources
    Beta strandi171 – 18010Combined sources
    Helixi182 – 1854Combined sources
    Helixi192 – 1954Combined sources
    Helixi204 – 21815Combined sources
    Helixi230 – 2323Combined sources
    Beta strandi234 – 2385Combined sources
    Beta strandi248 – 25811Combined sources
    Helixi262 – 2709Combined sources
    Helixi275 – 2784Combined sources
    Beta strandi288 – 2925Combined sources
    Helixi300 – 3034Combined sources
    Turni307 – 3115Combined sources
    Beta strandi313 – 32311Combined sources
    Beta strandi326 – 3338Combined sources
    Turni335 – 3406Combined sources
    Helixi341 – 35313Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0136.
    HOGENOMiHOG000013358.
    KOiK15017.
    OMAiIKPAYLA.

    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]
    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.
    RefSeqiNP_378167.1. NC_003106.2.
    WP_010980251.1. NC_003106.2.

    Genome annotation databases

    EnsemblBacteriaiBAB67276; BAB67276; STK_21710.
    GeneIDi1460244.
    KEGGisto:ST2171.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000023 Genomic DNA. Translation: BAB67276.1.
    RefSeqiNP_378167.1. NC_003106.2.
    WP_010980251.1. NC_003106.2.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi273063.ST2171.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAB67276; BAB67276; STK_21710.
    GeneIDi1460244.
    KEGGisto:ST2171.

    Phylogenomic databases

    eggNOGiCOG0136.
    HOGENOMiHOG000013358.
    KOiK15017.
    OMAiIKPAYLA.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13611.
    STOK273063:GJC7-2380-MONOMER.
    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]
    TIGRFAMsiTIGR00978. asd_EA. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 16993 / JCM 10545 / NBRC 100140 / 7.
    2. "Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for autotrophic carbon fixation in archaeal Metallosphaera and Sulfolobus spp."
      Alber B., Olinger M., Rieder A., Kockelkorn D., Jobst B., Hugler M., Fuchs G.
      J. Bacteriol. 188:8551-8559(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A MALONYL COA REDUCTASE, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY, ENZYME REGULATION, SUBUNIT, RNA BINDING, NOMENCLATURE, CATALYTIC ACTIVITY.

    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: May 27, 2015
    This is version 79 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

    External Data

    Dasty 3

    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 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.