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ECOLI:CYNS

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) cynS (synonyms: cnt)
Protein Name(s) Cyanate hydratase

Cyanase Cyanate hydrolase Cyanate lyase

External Links
UniProt P00816
EMBL M17891
M23219
U73857
U00096
AP009048
PIR A91850
RefSeq NP_414874.1
YP_488634.1
PDB 1DW9
1DWK
2IU7
2IUO
2IV1
2IVB
2IVG
2IVQ
PDBsum 1DW9
1DWK
2IU7
2IUO
2IV1
2IVB
2IVG
2IVQ
ProteinModelPortal P00816
SMR P00816
DIP DIP-9365N
IntAct P00816
STRING 511145.b0340
PRIDE P00816
EnsemblBacteria AAC73443
BAE76122
GeneID 12934193
948998
KEGG ecj:Y75_p0329
eco:b0340
PATRIC 32115813
EchoBASE EB0172
EcoGene EG10175
eggNOG COG1513
HOGENOM HOG000043436
InParanoid P00816
KO K01725
OMA FPDRGRA
OrthoDB EOG63FW2F
PhylomeDB P00816
BioCyc EcoCyc:CYANLY-MONOMER
ECOL316407:JW0331-MONOMER
MetaCyc:CYANLY-MONOMER
EvolutionaryTrace P00816
PRO PR:P00816
Proteomes UP000000318
UP000000625
Genevestigator P00816
GO GO:0005737
GO:0008824
GO:0003677
GO:0009440
Gene3D 1.10.260.40
3.30.1160.10
HAMAP MF_00535
InterPro IPR008076
IPR003712
IPR010982
Pfam PF02560
PIRSF PIRSF001263
PRINTS PR01693
SUPFAM SSF47413
SSF55234
TIGRFAMs TIGR00673

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0008824

cyanate hydratase activity

PMID:3309165[1]

ECO:0000315

F

Table 9 shows that wild-type E. coli strains were able to grow on medium containing 0.5 M urea and mutants lacking cyanase were not.

complete
CACAO 4067

part_of

GO:0005737

cytoplasm

PMID:8083164[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0009440

cyanate catabolic process

PMID:3309165[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008824

cyanate hydratase activity

PMID:3651424[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010982

F

Seeded From UniProt

complete

enables

GO:0008824

cyanate hydratase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR008076

F

Seeded From UniProt

complete

involved_in

GO:0009439

cyanate metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003712
InterPro:IPR008076
InterPro:IPR036581

P

Seeded From UniProt

complete

enables

GO:0008824

cyanate hydratase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.2.1.104

F

Seeded From UniProt

complete

enables

GO:0008824

cyanate hydratase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000094089

F

Seeded From UniProt

complete

involved_in

GO:0009439

cyanate metabolic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000094089

P

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Guilloton, M & Karst, F (1987) Isolation and characterization of Escherichia coli mutants lacking inducible cyanase. J. Gen. Microbiol. 133 645-53 PubMed GONUTS page
  2. Kozliak, EI et al. (1994) Expression of proteins encoded by the Escherichia coli cyn operon: carbon dioxide-enhanced degradation of carbonic anhydrase. J. Bacteriol. 176 5711-7 PubMed GONUTS page
  3. Anderson, PM et al. (1987) Interaction of mono- and dianions with cyanase: evidence for apparent half-site binding. Biochemistry 26 3938-43 PubMed GONUTS page