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Q96YK1

- MCR_SULTO

UniProt

Q96YK1 - MCR_SULTO

Protein

Malonyl-CoA reductase

Gene

mcr

Organism
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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

    Divalent cations such as magnesium or manganese 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

    1. aspartate-semialdehyde dehydrogenase activity Source: InterPro
    2. N-acetyl-gamma-glutamyl-phosphate reductase activity Source: InterPro
    3. NAD binding Source: InterPro
    4. NADP binding Source: InterPro
    5. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. aspartate metabolic process Source: InterPro
    2. isoleucine biosynthetic process Source: InterPro
    3. lysine biosynthetic process via diaminopimelate Source: InterPro
    4. methionine biosynthetic process Source: InterPro
    5. threonine biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP, RNA-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13611.
    STOK273063:GJC7-2380-MONOMER.

    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: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    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 – 125
    Turni13 – 164
    Helixi20 – 289
    Beta strandi31 – 4111
    Turni42 – 454
    Helixi48 – 514
    Beta strandi56 – 583
    Helixi62 – 654
    Helixi74 – 763
    Beta strandi82 – 854
    Turni89 – 913
    Helixi92 – 10110
    Beta strandi105 – 1084
    Turni112 – 1154
    Turni124 – 1263
    Helixi128 – 1325
    Helixi133 – 1419
    Beta strandi144 – 1496
    Helixi153 – 16816
    Beta strandi171 – 18010
    Helixi182 – 1854
    Helixi192 – 1954
    Helixi204 – 21815
    Helixi230 – 2323
    Beta strandi234 – 2385
    Beta strandi248 – 25811
    Helixi262 – 2709
    Helixi275 – 2784
    Beta strandi288 – 2925
    Helixi300 – 3034
    Turni307 – 3115
    Beta strandi313 – 32311
    Beta strandi326 – 3338
    Turni335 – 3406
    Helixi341 – 35313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiRISAACN.

    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

    MILMRRTLKA AILGATGLVG IEYVRMLSNH PYIKPAYLAG KGSVGKPYGE    50
    VVRWQTVGQV PKEIADMEIK PTDPKLMDDV DIIFSPLPQG AAGPVEEQFA 100
    KEGFPVISNS PDHRFDPDVP LLVPELNPHT ISLIDEQRKR REWKGFIVTT 150
    PLCTAQGAAI PLGAIFKDYK MDGAFITTIQ SLSGAGYPGI PSLDVVDNIL 200
    PLGDGYDAKT IKEIFRILSE VKRNVDEPKL EDVSLAATTH RIATIHGHYE 250
    VLYVSFKEET AAEKVKETLE NFRGEPQDLK LPTAPSKPII VMNEDTRPQV 300
    YFDRWAGDIP GMSVVVGRLK QVNKRMIRLV SLIHNTVRGA AGGGILAAEL 350
    LVEKGYIEK 359
    Length:359
    Mass (Da):39,560
    Last modified:December 1, 2001 - v1
    Checksum:i426AAE51597DD0E8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000023 Genomic DNA. Translation: BAB67276.1 .
    RefSeqi NP_378167.1. NC_003106.2.
    WP_010980251.1. NC_003106.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4DPK X-ray 2.05 A/B/C/D 1-359 [» ]
    4DPL X-ray 1.90 A/B/C/D 1-359 [» ]
    4DPM X-ray 2.30 A/B/C/D/E/F 1-359 [» ]
    ProteinModelPortali Q96YK1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 273063.ST2171.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB67276 ; BAB67276 ; STK_21710 .
    GeneIDi 1460244.
    KEGGi sto:ST2171.

    Phylogenomic databases

    eggNOGi COG0136.
    HOGENOMi HOG000013358.
    KOi K15017.
    OMAi RISAACN.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-13611.
    STOK273063:GJC7-2380-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR005676. 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 ]
    Pfami PF01118. Semialdhyde_dh. 1 hit.
    PF02774. Semialdhyde_dhC. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000148. ASA_dh. 1 hit.
    SMARTi SM00859. Semialdhyde_dh. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00978. asd_EA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 73 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