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P00816

- CYNS_ECOLI

UniProt

P00816 - CYNS_ECOLI

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Protein
Cyanate hydratase
Gene
cynS, cnt, b0340, JW0331
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. cyanate catabolic process Source: EcoCyc
Complete GO annotation...

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
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 156156Cyanate hydrataseUniRule annotation
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP00816.

Family & Domainsi

Sequence similaritiesi

Belongs to the cyanase family.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341D → N1 Publication
Sequence conflicti68 – 681D → N1 Publication
Sequence conflicti74 – 741L → S1 Publication
Sequence conflicti125 – 1251N → D1 Publication

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

« Hide 'large scale' publications
  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: May 14, 2014
This is version 133 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

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