Cyanate hydratase - Escherichia coli (strain K12)

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P00816 (CYNS_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 126. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	156 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Keywords
Molecular function	Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cyanate catabolic process Inferred from mutant phenotype PubMed 3309165. Source: EcoCyc
Cellular_component	cytoplasm Inferred from direct assay PubMed 8083164. Source: EcoliWiki
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro cyanate hydratase activity Inferred from direct assay PubMed 3651424. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 156

156

Cyanate hydratase HAMAP-Rule MF_00535

PRO_0000187523

Sites

Active site

122

Experimental info

Sequence conflict

D → N Ref.3

Sequence conflict

D → N Ref.3

Sequence conflict

L → S Ref.3

Sequence conflict

125

N → D Ref.3

Secondary structure

156

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00816 [UniParc].

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

FASTA

156

17,049

        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' referencesShow '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 277:1453-1474(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.

PIR

YNEC. A91850.

RefSeq

NP_414874.1. NC_000913.2.
YP_488634.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P00816.

SMR

P00816. Positions 1-156.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9365N.

IntAct

P00816. 3 interactions.

STRING

511145.b0340.

Proteomic databases

PRIDE

P00816.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73443; AAC73443; b0340.
BAE76122; BAE76122; BAE76122.

GeneID

12934193.
948998.

KEGG

ecj:Y75_p0329.
eco:b0340.

PATRIC

32115813. VBIEscCol129921_0348.

Organism-specific databases

EchoBASE

EB0172.

EcoGene

EG10175. cynS.

Phylogenomic databases

eggNOG

COG1513.

HOGENOM

HOG000043436.

K01725.

OMA

IYRFHEM.

ProtClustDB

PRK02866.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P00816.

Family and domain databases

Gene3D

1.10.260.40. 1 hit.
3.30.1160.10. 1 hit.

HAMAP

MF_00535. Cyanate_hydrat.

InterPro

IPR008076. Cyanase.
IPR003712. Cyanate_lyase_C.
IPR010982. Lambda_DNA-bd_dom.
[Graphical view]

Pfam

PF02560. Cyanate_lyase. 1 hit.
[Graphical view]

PIRSF

PIRSF001263. Cyanate_hydratas. 1 hit.

PRINTS

PR01693. CYANASE.

SUPFAM

SSF55234. Cyanate_lyase_C. 1 hit.
SSF47413. Lambda_like_DNA. 1 hit.

TIGRFAMs

TIGR00673. cynS. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P00816.

Entry information

Entry name

CYNS_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Recent format changes

Overview of recent format changes

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents