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Protein

Crotonyl-CoA reductase

Gene

ccr

Organism
Streptomyces collinus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in supplying butyryl-CoA for straight-chain fatty acid biosynthesis. Catalyzes the conversion of crotonyl-CoA to butyryl-CoA. It shows a high substrate specificity for crotonyl-CoA, a short-chain-length (C4), but no measurable activity is observed with shorter (C3) or longer-chain-length enoyl-CoA thioesters.1 Publication

Catalytic activityi

Butanoyl-CoA + NADP+ = (E)-but-2-enoyl-CoA + NADPH.1 Publication

Enzyme regulationi

Inhibited by divalent cations (30-100%), beta-chloromercuribenzoate (85%), iodoacetamide (40%) and N-ethylmaleamide (80%). The presence of CoA thioesters containing 12-20 carbon atoms results in inhibition of enzyme activity. The greatest degree of inhibition is observed in the presence of palmitoyl-CoA and myristoyl-CoA. The branched-chain fatty acids, isopalmitoyl-CoA and isomyristoyl-CoA are less effective inhibitors of the crotonyl-CoA reductase. Concentrations of NADPH above 200 µM lead to inhibition of enzyme activity.1 Publication

Kineticsi

  1. KM=18 µM for crotonyl-CoA (with NADP at pH 7.5)1 Publication

    pH dependencei

    Optimum pH is 6.5.1 Publication

    Temperature dependencei

    Optimum temperature is 40 degrees Celsius.1 Publication

    GO - Molecular functioni

    • crotonyl-CoA reductase activity Source: UniProtKB
    • NADP binding Source: UniProtKB
    • zinc ion binding Source: InterPro
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, NADP, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Crotonyl-CoA reductase (EC:1.3.1.86)
    Gene namesi
    Name:ccr
    OrganismiStreptomyces collinus
    Taxonomic identifieri42684 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 447447Crotonyl-CoA reductasePRO_0000418532Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Structurei

    Secondary structure

    1
    447
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 119Combined sources
    Helixi17 – 215Combined sources
    Beta strandi27 – 359Combined sources
    Helixi36 – 383Combined sources
    Turni39 – 446Combined sources
    Helixi47 – 493Combined sources
    Helixi52 – 554Combined sources
    Beta strandi57 – 626Combined sources
    Beta strandi70 – 8011Combined sources
    Helixi82 – 898Combined sources
    Helixi96 – 1027Combined sources
    Helixi107 – 1104Combined sources
    Beta strandi115 – 1184Combined sources
    Beta strandi124 – 1307Combined sources
    Beta strandi142 – 1454Combined sources
    Helixi155 – 1573Combined sources
    Helixi161 – 1633Combined sources
    Turni170 – 1723Combined sources
    Beta strandi173 – 1764Combined sources
    Beta strandi178 – 1869Combined sources
    Helixi187 – 1893Combined sources
    Beta strandi190 – 1923Combined sources
    Helixi199 – 2035Combined sources
    Helixi206 – 21611Combined sources
    Turni219 – 2224Combined sources
    Beta strandi229 – 2324Combined sources
    Turni233 – 2364Combined sources
    Helixi238 – 24912Combined sources
    Beta strandi253 – 2608Combined sources
    Helixi261 – 2699Combined sources
    Beta strandi274 – 2774Combined sources
    Turni278 – 2825Combined sources
    Beta strandi285 – 2906Combined sources
    Helixi294 – 30815Combined sources
    Beta strandi313 – 3186Combined sources
    Helixi322 – 33110Combined sources
    Beta strandi332 – 34110Combined sources
    Beta strandi346 – 3527Combined sources
    Helixi353 – 3575Combined sources
    Turni358 – 3603Combined sources
    Beta strandi362 – 3654Combined sources
    Helixi371 – 38212Combined sources
    Beta strandi390 – 3956Combined sources
    Helixi396 – 3983Combined sources
    Helixi399 – 4079Combined sources
    Beta strandi412 – 4209Combined sources
    Beta strandi422 – 4254Combined sources
    Helixi431 – 44111Combined sources
    Helixi442 – 4443Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HZZX-ray2.40A/B/C/D1-447[»]
    ProteinModelPortaliQ53865.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ53865.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    KOiK17829.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002085. ADH_SF_Zn-type.
    IPR010085. Crot_CoA_red.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR020843. PKS_ER.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 4 hits.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SMARTiSM00829. PKS_ER. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    SSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR01751. crot-CoA-red. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q53865-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTVKDILDAI QSKDATSADF AALQLPESYR AITVHKDETE MFAGLETRDK
    60 70 80 90 100
    DPRKSIHLDE VPVPELGPGE ALVAVMASSV NYNSVWTSIF EPVSTFAFLE
    110 120 130 140 150
    RYGKLSPLTK RHDLPYHIIG SDLAGVVLRT GPGVNAWQPG DEVVAHCLSV
    160 170 180 190 200
    ELESPDGHDD TMLDPEQRIW GFETNFGGLA EIALVKTNQL MPKPKHLTWE
    210 220 230 240 250
    EAAAPGLVNS TAYRQLVSRN GAAMKQGDNV LIWGASGGLG SYATQFALAG
    260 270 280 290 300
    GANPICVVSS PQKAEICRSM GAEAIIDRNA EGYKFWKDEH TQDPKEWKRF
    310 320 330 340 350
    GKRIRELTGG EDIDIVFEHP GRETFGASVY VTRKGGTITT CASTSGYMHE
    360 370 380 390 400
    YDNRYLWMSL KRIIGSHFAN YREAYEANRL IAKGKIHPTL SKTYSLEETG
    410 420 430 440
    QAAYDVHRNL HQGKVGVLCL APEEGLGVRD AEMRAQHIDA INRFRNV
    Length:447
    Mass (Da):49,364
    Last modified:November 1, 1996 - v1
    Checksum:iC275C04F80AB4A5A
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U37135 Genomic DNA. Translation: AAA92890.1.
    PIRiS72400.

    Genome annotation databases

    KEGGiag:AAA92890.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U37135 Genomic DNA. Translation: AAA92890.1.
    PIRiS72400.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HZZX-ray2.40A/B/C/D1-447[»]
    ProteinModelPortaliQ53865.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAA92890.

    Phylogenomic databases

    KOiK17829.

    Miscellaneous databases

    EvolutionaryTraceiQ53865.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002085. ADH_SF_Zn-type.
    IPR010085. Crot_CoA_red.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR020843. PKS_ER.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 4 hits.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SMARTiSM00829. PKS_ER. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    SSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR01751. crot-CoA-red. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "Purification of crotonyl-CoA reductase from Streptomyces collinus and cloning, sequencing and expression of the corresponding gene in Escherichia coli."
      Wallace K.K., Bao Z.Y., Dai H., Digate R., Schuler G., Speedie M.K., Reynolds K.A.
      Eur. J. Biochem. 233:954-962(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A CROTONYL-COA REDUCTASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT.
      Strain: Tu 1892.
    2. "Structure of Streptomycs collinus crotonyl COA carboxylase/reductase."
      Scarsdale J.N., Musayev F.N., Hazzard C., Florova G., Reynolds K., Wright H.T.
      Submitted (JUN-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiCCR_STRCU
    AccessioniPrimary (citable) accession number: Q53865
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: November 1, 1996
    Last modified: May 11, 2016
    This is version 68 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

    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.