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PR01693

Identifier
CYANASE  [View Relations]  [View Alignment]  
Accession
PR01693
No. of Motifs
5
Creation Date
25-MAR-2002
Title
Cyanase signature
Database References

PFAM; PF02560 Cyanate_lyase
INTERPRO; IPR003712
UMBBD; e0369
PDB; 1DW9
SCOP; 1DW9
CATH; 1DW9
Literature References
1. CHIN, C.C., ANDERSON, P.M. AND WOLD, F. 
The amino acid sequence of Escherichia coli cyanase. 
J.BIOL.CHEM. 258 276-282 (1983).
 
2. SUNG, Y.C. AND FUCHS, J.A. 
Characterization of the cyn operon in Escherichia coli K12. 
J.BIOL.CHEM. 263(29) 14769-14775 (1988).
 
3. LITTLE, R.M. AND ANDERSON, P.M. 
Structural properties of cyanase. Denaturation, renaturation, and role of 
sulphydrils and oligomeric structure in catalytic activity. 
J.BIOL.CHEM. 262 10120-10126 (1987).
 
4. WALSH, M.A., OTWINOWSKI, Z., PERRAKIS, A., ANDERSON, P.M. AND 
JOACHIMIAK, A.
Structure of cyanase reveals that a novel dimeric and decameric arrangement
of subunits is required for formation of the enzyme active site. 
STRUCTURE 8 505-514 (2000).

Documentation
Cyanase, an enzyme found in bacteria and plants, catalyses the reaction
of cyanate with bicarbonate to produce ammonia and carbon dioxide, allowing
the host organisms to overcome the toxicity of environmental cyanate [2].
The enzyme is also known as cyanase lyase and cyanase hydrolase. 
 
The cyanate lyase monomer is composed of two domains: an N-terminal domain
that shows structural similarity to the DNA-binding alpha-helix bundle
motif, and a C-terminal domain that has an 'open fold' that shows no 
structural similarity to other proteins [2,4].
 
The enzyme is active as a homodecamer of 17kDa subunits, and displays
half-site binding of substrates or substrate analogues. The dimer structure
reveals the C-terminal domains to be intertwined; the decamer is formed
from a pentamer of these dimers. The active site of the enzyme is located
between dimers and comprises residues from four adjacent subunits
of the homodecamer [4].
 
CYANASE is a 5-element fingerprint that provides a signature for the
cyanases. The fingerprint was derived from an initial alignment of 4
sequences: the motifs were drawn from conserved regions spanning the full
alignment length - motif 1 spans the C-terminus of alpha-helix 1 and helix
2; motif 2 spans helix 3 and the N-terminus of helix 4; motif 3 encodes the
N-terminus of helix 6, and includes the active site arginine and glutamate
residues; motif 4 spans the C-terminus of helix 6 and the N-terminal portion
of beta-strand 1, including the active site serine; and motif 5 encodes
strand 2. Two iterations on SPTR40_18f were required to reach convergence,
at which point a true set comprising 7 sequences was identified.
Summary Information
7 codes involving  5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
577777
400000
300000
200000
12345
True Positives
CYNS_ECOLI    CYNS_SYNP7    CYNS_SYNY3    O22683        
O66587 Q9FWK4 Q9I263
Sequence Titles
CYNS_ECOLI  Cyanate lyase (EC 4.3.99.1) (Cyanate hydrolase) (Cyanase) - Escherichia coli. 
CYNS_SYNP7 Cyanate lyase (EC 4.3.99.1) (Cyanate hydrolase) (Cyanase) - Synechococcus sp. (strain PCC 7942) (Anacystis nidulans R2).
CYNS_SYNY3 Cyanate lyase (EC 4.3.99.1) (Cyanate hydrolase) (Cyanase) - Synechocystis sp. (strain PCC 6803).
O22683 CYANASE (EC 4.3.99.1) (CYANATE LYASE) (CYANATE HYDROLASE) (CYANASE HYDROLASE) - Arabidopsis thaliana (Mouse-ear cress).
O66587 CYANATE HYDROLASE - Aquifex aeolicus.
Q9FWK4 PUTATIVE CYANASE - Oryza sativa (Rice).
Q9I263 CYANATE LYASE - Pseudomonas aeruginosa.
Scan History
SPTR40_18f 2  120  NSINGLE    
Initial Motifs
Motif 1  width=16
Element Seqn Id St Int Rpt
KSASGKTFSQLAAETG O22683 17 17 -
KAKKDLSFAEIADGTG CYNS_ECOLI 22 22 -
KAESRKSFSEIGEEAG Q9FWK4 77 77 -
KKNLGLTWEDVSRKLG O66587 16 16 -

Motif 2 width=18
Element Seqn Id St Int Rpt
YVAQLLRRQAQLKPDTVP O22683 37 4 -
FVTAALLGQQALPADAAR CYNS_ECOLI 42 4 -
YVAQLLRRQAQLKPETAP Q9FWK4 97 4 -
YCAMLFYGYAQADDEEVK O66587 36 4 -

Motif 3 width=15
Element Seqn Id St Int Rpt
EPTIYRLNEAVMHFG O22683 86 31 -
DPTMYRFYEMLQVYG CYNS_ECOLI 91 31 -
DTQGTRLNEAVMHFG Q9FWK4 247 132 -
DPFVYRLYEVVILYG O66587 85 31 -

Motif 4 width=17
Element Seqn Id St Int Rpt
KEIINEDFGDGIMSAID O22683 104 3 -
KALVHEKFGDGIISAIN CYNS_ECOLI 109 3 -
KEIINEEFGDGIMSAID Q9FWK4 265 3 -
KDVAHEMFGDGIMSAID O66587 103 3 -

Motif 5 width=11
Element Seqn Id St Int Rpt
RVVVTLDGKYL O22683 136 15 -
RAVITLDGKYL CYNS_ECOLI 141 15 -
RVVVTFDGKYL Q9FWK4 297 15 -
RMVLTFNGKWL O66587 134 14 -
Final Motifs
Motif 1  width=16
Element Seqn Id St Int Rpt
KKAKGITFADLEQLLG CYNS_SYNY3 17 17 -
KSASGKTFSQLAAETG O22683 17 17 -
KKAKGITFTELEQLLG CYNS_SYNP7 13 13 -
KARLGLSWQDLADGTG Q9I263 22 22 -
KAKKDLSFAEIADGTG CYNS_ECOLI 22 22 -
KAESRKSFSEIGEEAG Q9FWK4 77 77 -
KKNLGLTWEDVSRKLG O66587 16 16 -

Motif 2 width=18
Element Seqn Id St Int Rpt
WIAAVIYRQASASVDEAE CYNS_SYNY3 37 4 -
YVAQLLRRQAQLKPDTVP O22683 37 4 -
WIASVFYRQSTASPEEAE CYNS_SYNP7 33 4 -
FVTAALLGQHALPEAAAR Q9I263 42 4 -
FVTAALLGQQALPADAAR CYNS_ECOLI 42 4 -
YVAQLLRRQAQLKPETAP Q9FWK4 97 4 -
YCAMLFYGYAQADDEEVK O66587 36 4 -

Motif 3 width=15
Element Seqn Id St Int Rpt
DPLIYRFYEIMQVYG CYNS_SYNY3 85 30 -
EPTIYRLNEAVMHFG O22683 86 31 -
DPLIYRFYEIMQVYG CYNS_SYNP7 82 31 -
DPTIYRFYEMLQVYG Q9I263 91 31 -
DPTMYRFYEMLQVYG CYNS_ECOLI 91 31 -
DTQGTRLNEAVMHFG Q9FWK4 247 132 -
DPFVYRLYEVVILYG O66587 85 31 -

Motif 4 width=17
Element Seqn Id St Int Rpt
KEVIHEKFGDGIMSAID CYNS_SYNY3 103 3 -
KEIINEDFGDGIMSAID O22683 104 3 -
KDVIQEKFGDGIMSAID CYNS_SYNP7 100 3 -
KALVHEQFGDGIISAIN Q9I263 109 3 -
KALVHEKFGDGIISAIN CYNS_ECOLI 109 3 -
KEIINEEFGDGIMSAID Q9FWK4 265 3 -
KDVAHEMFGDGIMSAID O66587 103 3 -

Motif 5 width=11
Element Seqn Id St Int Rpt
RVKVTMNGKFL CYNS_SYNY3 134 14 -
RVVVTLDGKYL O22683 136 15 -
RVKVTMCGKFL CYNS_SYNP7 131 14 -
RAVITLDGKYL Q9I263 141 15 -
RAVITLDGKYL CYNS_ECOLI 141 15 -
RVVVTFDGKYL Q9FWK4 297 15 -
RMVLTFNGKWL O66587 134 14 -