P00816 (CYNS_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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)

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 MF_00535
Catalytic activity	Cyanate + HCO3- + 2 H+ = NH3 + 2 CO2. HAMAP 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. Source: EcoCyc
Cellular component	cytoplasm Inferred from direct assay. Source: EcoliWiki
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro cyanate hydratase activity Inferred from direct assay. Source: EcoCyc hydro-lyase activity Inferred from electronic annotation. Source: InterPro
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 MF_00535

PRO_0000187523

Sites

Active site

96

1

Active site

99

1

Active site

122

1

Experimental info

Sequence conflict

34

1

D → N Ref.3

Sequence conflict

68

1

D → N Ref.3

Sequence conflict

74

1

L → S Ref.3

Sequence conflict

125

1

N → D Ref.3

Secondary structure

1

.

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.

.

.

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.

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.

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.

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.

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156

Helix Strand Turn

Details...

Helix

9 – 24

16

Helix

29 – 33

5

Beta strand

36 – 38

3

Helix

40 – 47

8

Helix

55 – 64

10

Helix

69 – 74

6

Beta strand

85 – 88

4

Helix

92 – 115

24

Beta strand

118 – 134

17

Beta strand

138 – 152

15

Sequences

	Sequence		Length	Mass (Da)
	P00816 [UniParc]. Last modified July 1, 1989. Version 2. Checksum: 13AC830926313CED	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

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: 6336748] [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: 2822670] [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: 3049588] [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: 9278503] [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: 16738553] [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: 3301828] [Abstract] Cited for: CHARACTERIZATION.
[8]	"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: 10801492] [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.

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.

2D gel databases

ECO2DBASE

C013.6. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001822; EBESCP00000001822; EBESCG00000001506.
EBESCT00000001823; EBESCP00000001823; EBESCG00000001506.
EBESCT00000015163; EBESCP00000014454; EBESCG00000014223.

GeneID

948998.

GenomeReviews

Gene locus JW0331 in contig AP009048_GR.
Gene locus b0340 in contig U00096_GR.

KEGG

ecj:JW0331.
eco:b0340.

PATRIC

32115813. VBIEscCol129921_0348.

Organism-specific databases

EchoBASE

EB0172.

EcoGene

EG10175. cynS.

Phylogenomic databases

eggNOG

COG1513.

GeneTree

EBGT00050000010564.

HOGENOM

HBG317643.

OMA

QTIPLRG.

PhylomeDB

P00816.

ProtClustDB

PRK02866.

Enzyme and pathway databases

BioCyc

EcoCyc:CYANLY-MONOMER.
MetaCyc:CYANLY-MONOMER.

Gene expression databases

Genevestigator

P00816.

Family and domain databases

HAMAP

MF_00535. Cyanate_hydrat.
[Tree]

InterPro

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

Gene3D

G3DSA:3.30.1160.10. Cyanate_lyase_C. 1 hit.
G3DSA:1.10.260.40. G3DSA:1.10.260.40. 1 hit.

KO

K01725.

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...

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:	January 25, 2012
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program