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P00816 (CYNS_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyanate hydratase

Short name=Cyanase
EC=4.2.1.104
Alternative name(s):
Cyanate hydrolase
Cyanate lyase
Gene names
Name:cynS
Synonyms:cnt
Ordered Locus Names:b0340, JW0331
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length156 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. HAMAP-Rule MF_00535

Catalytic activity

Cyanate + HCO3- + 2 H+ = NH3 + 2 CO2. HAMAP-Rule MF_00535

Subunit structure

Homodecamer composed of five homodimers.

Sequence similarities

Belongs to the cyanase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 156156Cyanate hydratase HAMAP-Rule MF_00535
PRO_0000187523

Sites

Active site961
Active site991
Active site1221

Experimental info

Sequence conflict341D → N Ref.3
Sequence conflict681D → N Ref.3
Sequence conflict741L → S Ref.3
Sequence conflict1251N → D Ref.3

Secondary structure

..................... 156
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00816 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: 13AC830926313CED

FASTA15617,049
        10         20         30         40         50         60 
MIQSQINRNI RLDLADAILL SKAKKDLSFA EIADGTGLAE AFVTAALLGQ QALPADAARL 

        70         80         90        100        110        120 
VGAKLDLDED SILLLQMIPL RGCIDDRIPT DPTMYRFYEM LQVYGTTLKA LVHEKFGDGI 

       130        140        150 
ISAINFKLDV KKVADPEGGE RAVITLDGKY LPTKPF 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRYNEC. A91850.
RefSeqNP_414874.1. NC_000913.3.
YP_488634.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP00816.
SMRP00816. Positions 1-156.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9365N.
IntActP00816. 3 interactions.
STRING511145.b0340.

Proteomic databases

PRIDEP00816.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73443; AAC73443; b0340.
BAE76122; BAE76122; BAE76122.
GeneID12934193.
948998.
KEGGecj:Y75_p0329.
eco:b0340.
PATRIC32115813. VBIEscCol129921_0348.

Organism-specific databases

EchoBASEEB0172.
EcoGeneEG10175. cynS.

Phylogenomic databases

eggNOGCOG1513.
HOGENOMHOG000043436.
KOK01725.
OMAAIDFKMD.
OrthoDBEOG63FW2F.
PhylomeDBP00816.
ProtClustDBPRK02866.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP00816.

Family and domain databases

Gene3D1.10.260.40. 1 hit.
3.30.1160.10. 1 hit.
HAMAPMF_00535. Cyanate_hydrat.
InterProIPR008076. Cyanase.
IPR003712. Cyanate_lyase_C.
IPR010982. Lambda_DNA-bd_dom.
[Graphical view]
PfamPF02560. Cyanate_lyase. 1 hit.
[Graphical view]
PIRSFPIRSF001263. Cyanate_hydratas. 1 hit.
PRINTSPR01693. CYANASE.
SUPFAMSSF47413. SSF47413. 1 hit.
SSF55234. SSF55234. 1 hit.
TIGRFAMsTIGR00673. cynS. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP00816.
PROP00816.

Entry information

Entry nameCYNS_ECOLI
AccessionPrimary (citable) accession number: P00816
Secondary accession number(s): Q2MC84
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene