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P00816

- CYNS_ECOLI

UniProt

P00816 - CYNS_ECOLI

Protein

Cyanate hydratase

Gene

cynS

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.

    Catalytic activityi

    Cyanate + HCO3- + 2 H+ = NH3 + 2 CO2.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei96 – 961
    Active sitei99 – 991
    Active sitei122 – 1221

    GO - Molecular functioni

    1. cyanate hydratase activity Source: EcoCyc
    2. DNA binding Source: InterPro

    GO - Biological processi

    1. cyanate catabolic process Source: EcoCyc

    Keywords - Molecular functioni

    Lyase

    Enzyme and pathway databases

    BioCyciEcoCyc:CYANLY-MONOMER.
    ECOL316407:JW0331-MONOMER.
    MetaCyc:CYANLY-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyanate hydratase (EC:4.2.1.104)
    Short name:
    Cyanase
    Alternative name(s):
    Cyanate hydrolase
    Cyanate lyase
    Gene namesi
    Name:cynS
    Synonyms:cnt
    Ordered Locus Names:b0340, JW0331
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10175. cynS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: EcoliWiki

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 156156Cyanate hydratasePRO_0000187523Add
    BLAST

    Proteomic databases

    PRIDEiP00816.

    Expressioni

    Gene expression databases

    GenevestigatoriP00816.

    Interactioni

    Subunit structurei

    Homodecamer composed of five homodimers.

    Protein-protein interaction databases

    DIPiDIP-9365N.
    IntActiP00816. 3 interactions.
    STRINGi511145.b0340.

    Structurei

    Secondary structure

    1
    156
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 2416
    Helixi29 – 335
    Beta strandi36 – 383
    Helixi40 – 478
    Helixi55 – 6410
    Helixi69 – 746
    Beta strandi85 – 884
    Helixi92 – 11524
    Beta strandi118 – 13417
    Beta strandi138 – 15215

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DW9X-ray1.65A/B/C/D/E/F/G/H/I/J1-156[»]
    1DWKX-ray1.65A/B/C/D/E/F/G/H/I/J1-156[»]
    2IU7X-ray1.91A/B/C/D/E/F/G/H/I/J1-156[»]
    2IUOX-ray1.90A/B/C/D/E/F/G/H/I/J1-156[»]
    2IV1X-ray1.88A/B/C/D/E/F/G/H/I/J1-156[»]
    2IVBX-ray1.95A/B/C/D/E/F/G/H/I/J1-156[»]
    2IVGX-ray1.87A/B/C/D/E/F/G/H/I/J1-156[»]
    2IVQX-ray2.10A/B/C/D/E/F/G/H/I/J1-156[»]
    ProteinModelPortaliP00816.
    SMRiP00816. Positions 1-156.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00816.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cyanase family.Curated

    Phylogenomic databases

    eggNOGiCOG1513.
    HOGENOMiHOG000043436.
    KOiK01725.
    OMAiDSHKANE.
    OrthoDBiEOG63FW2F.
    PhylomeDBiP00816.

    Family and domain databases

    Gene3Di1.10.260.40. 1 hit.
    3.30.1160.10. 1 hit.
    HAMAPiMF_00535. Cyanate_hydrat.
    InterProiIPR008076. Cyanase.
    IPR003712. Cyanate_lyase_C.
    IPR010982. Lambda_DNA-bd_dom.
    [Graphical view]
    PfamiPF02560. Cyanate_lyase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001263. Cyanate_hydratas. 1 hit.
    PRINTSiPR01693. CYANASE.
    SUPFAMiSSF47413. SSF47413. 1 hit.
    SSF55234. SSF55234. 1 hit.
    TIGRFAMsiTIGR00673. cynS. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P00816-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIQSQINRNI RLDLADAILL SKAKKDLSFA EIADGTGLAE AFVTAALLGQ    50
    QALPADAARL VGAKLDLDED SILLLQMIPL RGCIDDRIPT DPTMYRFYEM 100
    LQVYGTTLKA LVHEKFGDGI ISAINFKLDV KKVADPEGGE RAVITLDGKY 150
    LPTKPF 156
    Length:156
    Mass (Da):17,049
    Last modified:July 1, 1989 - v2
    Checksum:i13AC830926313CED
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti34 – 341D → N(PubMed:3049588)Curated
    Sequence conflicti68 – 681D → N(PubMed:3049588)Curated
    Sequence conflicti74 – 741L → S(PubMed:3049588)Curated
    Sequence conflicti125 – 1251N → D(PubMed:3049588)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17891 Genomic DNA. Translation: AAA23629.1.
    M23219 Genomic DNA. Translation: AAA23626.1.
    U73857 Genomic DNA. Translation: AAB18064.1.
    U00096 Genomic DNA. Translation: AAC73443.1.
    AP009048 Genomic DNA. Translation: BAE76122.1.
    PIRiA91850. YNEC.
    RefSeqiNP_414874.1. NC_000913.3.
    YP_488634.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73443; AAC73443; b0340.
    BAE76122; BAE76122; BAE76122.
    GeneIDi12934193.
    948998.
    KEGGiecj:Y75_p0329.
    eco:b0340.
    PATRICi32115813. VBIEscCol129921_0348.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17891 Genomic DNA. Translation: AAA23629.1 .
    M23219 Genomic DNA. Translation: AAA23626.1 .
    U73857 Genomic DNA. Translation: AAB18064.1 .
    U00096 Genomic DNA. Translation: AAC73443.1 .
    AP009048 Genomic DNA. Translation: BAE76122.1 .
    PIRi A91850. YNEC.
    RefSeqi NP_414874.1. NC_000913.3.
    YP_488634.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DW9 X-ray 1.65 A/B/C/D/E/F/G/H/I/J 1-156 [» ]
    1DWK X-ray 1.65 A/B/C/D/E/F/G/H/I/J 1-156 [» ]
    2IU7 X-ray 1.91 A/B/C/D/E/F/G/H/I/J 1-156 [» ]
    2IUO X-ray 1.90 A/B/C/D/E/F/G/H/I/J 1-156 [» ]
    2IV1 X-ray 1.88 A/B/C/D/E/F/G/H/I/J 1-156 [» ]
    2IVB X-ray 1.95 A/B/C/D/E/F/G/H/I/J 1-156 [» ]
    2IVG X-ray 1.87 A/B/C/D/E/F/G/H/I/J 1-156 [» ]
    2IVQ X-ray 2.10 A/B/C/D/E/F/G/H/I/J 1-156 [» ]
    ProteinModelPortali P00816.
    SMRi P00816. Positions 1-156.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9365N.
    IntActi P00816. 3 interactions.
    STRINGi 511145.b0340.

    Proteomic databases

    PRIDEi P00816.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73443 ; AAC73443 ; b0340 .
    BAE76122 ; BAE76122 ; BAE76122 .
    GeneIDi 12934193.
    948998.
    KEGGi ecj:Y75_p0329.
    eco:b0340.
    PATRICi 32115813. VBIEscCol129921_0348.

    Organism-specific databases

    EchoBASEi EB0172.
    EcoGenei EG10175. cynS.

    Phylogenomic databases

    eggNOGi COG1513.
    HOGENOMi HOG000043436.
    KOi K01725.
    OMAi DSHKANE.
    OrthoDBi EOG63FW2F.
    PhylomeDBi P00816.

    Enzyme and pathway databases

    BioCyci EcoCyc:CYANLY-MONOMER.
    ECOL316407:JW0331-MONOMER.
    MetaCyc:CYANLY-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P00816.
    PROi P00816.

    Gene expression databases

    Genevestigatori P00816.

    Family and domain databases

    Gene3Di 1.10.260.40. 1 hit.
    3.30.1160.10. 1 hit.
    HAMAPi MF_00535. Cyanate_hydrat.
    InterProi IPR008076. Cyanase.
    IPR003712. Cyanate_lyase_C.
    IPR010982. Lambda_DNA-bd_dom.
    [Graphical view ]
    Pfami PF02560. Cyanate_lyase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001263. Cyanate_hydratas. 1 hit.
    PRINTSi PR01693. CYANASE.
    SUPFAMi SSF47413. SSF47413. 1 hit.
    SSF55234. SSF55234. 1 hit.
    TIGRFAMsi TIGR00673. cynS. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The amino acid sequence of Escherichia coli cyanase."
      Chin C.C.Q., Anderson P.M., Wold F.
      J. Biol. Chem. 258:276-282(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    2. "Characterization of high-level expression and sequencing of the Escherichia coli K-12 cynS gene encoding cyanase."
      Sung Y.-C., Anderson P.M., Fuchs J.A.
      J. Bacteriol. 169:5224-5230(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. "Characterization of the cyn operon in Escherichia coli K12."
      Sung Y.-C., Fuchs J.A.
      J. Biol. Chem. 263:14769-14775(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    7. "Structural properties of cyanase. Denaturation, renaturation, and role of sulfhydryls and oligomeric structure in catalytic activity."
      Little R.M., Anderson P.M.
      J. Biol. Chem. 262:10120-10126(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    8. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    9. "Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site."
      Walsh M.A., Otwinowski Z., Perrakis A., Anderson P.M., Joachimiak A.
      Structure 8:505-514(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).

    Entry informationi

    Entry nameiCYNS_ECOLI
    AccessioniPrimary (citable) accession number: P00816
    Secondary accession number(s): Q2MC84
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3