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Protein

2-deoxy-scyllo-inosose synthase

Gene

btrC

Organism
Bacillus circulans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the intramolecular carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose (DOI).

Catalytic activityi

D-glucose-6-phosphate = 2-deoxy-L-scyllo-inosose + phosphate.3 Publications

Cofactori

Protein has several cofactor binding sites:
  • NAD+
  • Co2+Note: Binds 1 Co2+ ion per subunit.

Enzyme regulationi

Strongly inhibited by EDTA, zinc and Cu2+.

Kineticsi

  1. KM=900 µM for glucose-6-phosphate (at pH 7.7 and 46 degrees Celsius)1 Publication
  2. KM=170 µM for NAD+ (at pH 7.7 and 46 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 7.5-8.5.1 Publication

    Temperature dependencei

    Optimum temperature is 46 degrees Celsius.1 Publication

    Pathwayi: 2-deoxystreptamine biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes 2-deoxystreptamine from D-glucose 6-phosphate.
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. 2-deoxy-scyllo-inosose synthase (btrC)
    2. L-glutamine:2-deoxy-scyllo-inosose aminotransferase (btrR)
    3. no protein annotated in this organism
    4. L-glutamine:2-deoxy-scyllo-inosose aminotransferase (btrR)
    This subpathway is part of the pathway 2-deoxystreptamine biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-deoxystreptamine from D-glucose 6-phosphate, the pathway 2-deoxystreptamine biosynthesis and in Metabolic intermediate biosynthesis.

    Pathwayi: butirosin biosynthesis

    This protein is involved in the pathway butirosin biosynthesis, which is part of Antibiotic biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway butirosin biosynthesis and in Antibiotic biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei141 – 1411Curated
    Metal bindingi183 – 1831CobaltSequence analysis
    Metal bindingi246 – 2461CobaltSequence analysis
    Metal bindingi262 – 2621CobaltSequence analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi102 – 11110NADSequence analysis

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Antibiotic biosynthesis

    Keywords - Ligandi

    Cobalt, Metal-binding, NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17225.
    BRENDAi4.2.3.124. 649.
    SABIO-RKQ9S5E2.
    UniPathwayiUPA00907; UER00921.
    UPA00964.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-deoxy-scyllo-inosose synthase (EC:4.2.3.124)
    Short name:
    DOI synthase
    Short name:
    DOIS
    Gene namesi
    Name:btrC
    OrganismiBacillus circulans
    Taxonomic identifieri1397 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3683682-deoxy-scyllo-inosose synthasePRO_0000234034Add
    BLAST

    Interactioni

    Subunit structurei

    Was isolated as a heterodimeric enzyme comprising of BtrC and a smaller polypeptide further identified as PdxT by sequence homology.1 Publication

    Structurei

    Secondary structure

    1
    368
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86Combined sources
    Beta strandi11 – 188Combined sources
    Helixi22 – 276Combined sources
    Beta strandi35 – 428Combined sources
    Helixi47 – 5711Combined sources
    Turni58 – 603Combined sources
    Beta strandi63 – 686Combined sources
    Helixi72 – 743Combined sources
    Helixi77 – 8913Combined sources
    Beta strandi96 – 1038Combined sources
    Helixi104 – 11613Combined sources
    Beta strandi122 – 1276Combined sources
    Helixi130 – 1345Combined sources
    Turni135 – 1373Combined sources
    Beta strandi141 – 1466Combined sources
    Beta strandi149 – 1568Combined sources
    Beta strandi160 – 1656Combined sources
    Helixi166 – 1705Combined sources
    Helixi174 – 19017Combined sources
    Helixi200 – 2023Combined sources
    Helixi211 – 22919Combined sources
    Beta strandi235 – 2373Combined sources
    Helixi238 – 2436Combined sources
    Helixi246 – 25510Combined sources
    Turni256 – 2583Combined sources
    Helixi262 – 27918Combined sources
    Helixi285 – 29713Combined sources
    Turni298 – 3025Combined sources
    Helixi310 – 3189Combined sources
    Beta strandi322 – 3276Combined sources
    Beta strandi329 – 3357Combined sources
    Beta strandi338 – 3403Combined sources
    Beta strandi353 – 3564Combined sources
    Helixi357 – 36610Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D2XX-ray2.30A/B1-368[»]
    2GRUX-ray2.15A/B1-368[»]
    ProteinModelPortaliQ9S5E2.
    SMRiQ9S5E2. Positions 2-368.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9S5E2.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    KOiK13546.
    K13551.

    Family and domain databases

    InterProiIPR030963. DHQ_synth_fam.
    IPR030960. DHQS/DOIS.
    [Graphical view]
    PfamiPF01761. DHQ_synthase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001455. DHQ_synth. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9S5E2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTTKQICFAD RCFNFAFGEH VLESVESYIP RDEFDQYIMI SDSGVPDSIV
    60 70 80 90 100
    HYAAEYFGKL APVHILRFQG GEEYKTLSTV TNLQERAIAL GANRRTAIVA
    110 120 130 140 150
    VGGGLTGNVA GVAAGMMFRG IALIHVPTTF LAASDSVLSI KQAVNLTSGK
    160 170 180 190 200
    NLVGFYYPPR FVFADTRILS ESPPRQVKAG MCELVKNMLI LENDNKEFTE
    210 220 230 240 250
    DDLNSANVYS PKQLETFINF CISAKMSVLS EDIYEKKKGL IFEYGHTIGH
    260 270 280 290 300
    AIELAEQGGI THGEAIAVGM IYAAKIANRM NLMPEHDVSA HYWLLNKIGA
    310 320 330 340 350
    LQDIPLKSDP DSIFHYLIHD NKRGYIKLDE DNLGMILLSG VGKPAMYNQT
    360
    LLTPVRKTLI KEVIREGL
    Length:368
    Mass (Da):40,747
    Last modified:May 1, 2000 - v1
    Checksum:i88391DD153B67671
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB019237 Genomic DNA. Translation: BAA83344.1.
    AJ781030 Genomic DNA. Translation: CAG77421.1.
    AB097196 Genomic DNA. Translation: BAE07067.1.

    Genome annotation databases

    KEGGiag:BAE07067.
    ag:BAE07068.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB019237 Genomic DNA. Translation: BAA83344.1.
    AJ781030 Genomic DNA. Translation: CAG77421.1.
    AB097196 Genomic DNA. Translation: BAE07067.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D2XX-ray2.30A/B1-368[»]
    2GRUX-ray2.15A/B1-368[»]
    ProteinModelPortaliQ9S5E2.
    SMRiQ9S5E2. Positions 2-368.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:BAE07067.
    ag:BAE07068.

    Phylogenomic databases

    KOiK13546.
    K13551.

    Enzyme and pathway databases

    UniPathwayiUPA00907; UER00921.
    UPA00964.
    BioCyciMetaCyc:MONOMER-17225.
    BRENDAi4.2.3.124. 649.
    SABIO-RKQ9S5E2.

    Miscellaneous databases

    EvolutionaryTraceiQ9S5E2.

    Family and domain databases

    InterProiIPR030963. DHQ_synth_fam.
    IPR030960. DHQS/DOIS.
    [Graphical view]
    PfamiPF01761. DHQ_synthase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001455. DHQ_synth. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiDOIS_BACCI
    AccessioniPrimary (citable) accession number: Q9S5E2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2006
    Last sequence update: May 1, 2000
    Last modified: January 20, 2016
    This is version 71 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, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.