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Protein

dTDP-4-dehydro-6-deoxyglucose 3-epimerase

Gene

chmJ

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

Functioni

Catalyzes the conversion of dTDP-4-oxo-6-deoxyglucose to dTDP-4-oxo-6-deoxyallose, via a C-3 epimerization. This is a step in the biosynthesis of the mycinose moiety of the chalcomycin antibiotic.1 Publication

Catalytic activityi

dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-allose.1 Publication

Kineticsi

kcat is 6.4 sec(-1).

  1. KM=04 mM for dTDP-4-dehydro-6-deoxy-alpha-D-glucose

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei21Substrate1
    Binding sitei26Substrate1
    Binding sitei45Substrate1
    Binding sitei57Substrate1
    Active sitei60Proton acceptor1 Publication1
    Binding sitei70Substrate1
    Binding sitei117Substrate1
    Active sitei130Proton donor1 Publication1
    Binding sitei136Substrate1
    Binding sitei141Substrate1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Antibiotic biosynthesis, Carbohydrate metabolism

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    dTDP-4-dehydro-6-deoxyglucose 3-epimerase (EC:5.1.3.27)
    Alternative name(s):
    dTDP-4-dehydro-6-deoxy-D-glucose 3-epimerase
    dTDP-4-keto-6-deoxyglucose epimerase
    dTDP-4-oxo-6-deoxy-D-glucose epimerase
    Gene namesi
    Name:chmJ
    OrganismiStreptomyces bikiniensis
    Taxonomic identifieri1896 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi60H → N: No effect on substrate affinity, but 2400-fold reduction in activity. 1 Publication1
    Mutagenesisi130Y → F: Slight decrease in substrate affinity, and 1650-fold reduction in activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004251061 – 196dTDP-4-dehydro-6-deoxyglucose 3-epimeraseAdd BLAST196

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1196
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi9 – 12Combined sources4
    Beta strandi16 – 19Combined sources4
    Beta strandi22 – 29Combined sources8
    Helixi30 – 37Combined sources8
    Beta strandi45 – 51Combined sources7
    Beta strandi55 – 62Combined sources8
    Beta strandi64 – 66Combined sources3
    Beta strandi70 – 84Combined sources15
    Turni91 – 94Combined sources4
    Beta strandi96 – 102Combined sources7
    Turni103 – 105Combined sources3
    Beta strandi108 – 111Combined sources4
    Beta strandi116 – 121Combined sources6
    Beta strandi126 – 134Combined sources9
    Helixi138 – 140Combined sources3
    Beta strandi141 – 143Combined sources3
    Turni149 – 151Combined sources3
    Helixi165 – 168Combined sources4
    Helixi173 – 178Combined sources6
    Helixi185 – 196Combined sources12

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4HMZX-ray2.00A/B/C/D1-196[»]
    4HN0X-ray2.20A/B/C/D1-196[»]
    4HN1X-ray1.60A/B/C/D1-196[»]
    ProteinModelPortaliQ5SFD1.
    SMRiQ5SFD1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di2.60.120.10. 1 hit.
    InterProiIPR000888. dTDP_sugar_isom.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view]
    PANTHERiPTHR21047. PTHR21047. 1 hit.
    PfamiPF00908. dTDP_sugar_isom. 1 hit.
    [Graphical view]
    ProDomiPD001462. dTDP_sugar_isom. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF51182. SSF51182. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q5SFD1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MHPLSIEGAW SQEPVIHSDH RGRSHEWFRG ESFRQAFGHD FPVAQVNVAV
    60 70 80 90 100
    SHRGALRGIH YTEIPPGQAK YSVCVRGAGL DVVVDVRIGS PTFGRWEIVP
    110 120 130 140 150
    MDAERNTAVY LTAGLGRAFL SLTDDATLVY LCSSGYAPAR EHSVNPLDPD
    160 170 180 190
    LGIAWPDDIE PLLSDRDENA PTLATAERLG LLPTYQAWQE QQQAQR
    Length:196
    Mass (Da):21,683
    Last modified:December 21, 2004 - v1
    Checksum:i26C8CD880701F1CA
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY509120 Genomic DNA. Translation: AAS79451.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY509120 Genomic DNA. Translation: AAS79451.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4HMZX-ray2.00A/B/C/D1-196[»]
    4HN0X-ray2.20A/B/C/D1-196[»]
    4HN1X-ray1.60A/B/C/D1-196[»]
    ProteinModelPortaliQ5SFD1.
    SMRiQ5SFD1.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Family and domain databases

    Gene3Di2.60.120.10. 1 hit.
    InterProiIPR000888. dTDP_sugar_isom.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view]
    PANTHERiPTHR21047. PTHR21047. 1 hit.
    PfamiPF00908. dTDP_sugar_isom. 1 hit.
    [Graphical view]
    ProDomiPD001462. dTDP_sugar_isom. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF51182. SSF51182. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCHMJ_STRBI
    AccessioniPrimary (citable) accession number: Q5SFD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 22, 2014
    Last sequence update: December 21, 2004
    Last modified: November 2, 2016
    This is version 36 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.