CYNS_ECOLI
ID CYNS_ECOLI Reviewed; 156 AA.
AC P00816; Q2MC84;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Cyanate hydratase;
DE Short=Cyanase;
DE EC=4.2.1.104;
DE AltName: Full=Cyanate hydrolase;
DE AltName: Full=Cyanate lyase;
GN Name=cynS; Synonyms=cnt; OrderedLocusNames=b0340, JW0331;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=6336748; DOI=10.1016/s0021-9258(18)33253-8;
RA Chin C.C.Q., Anderson P.M., Wold F.;
RT "The amino acid sequence of Escherichia coli cyanase.";
RL J. Biol. Chem. 258:276-282(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2822670; DOI=10.1128/jb.169.11.5224-5230.1987;
RA Sung Y.-C., Anderson P.M., Fuchs J.A.;
RT "Characterization of high-level expression and sequencing of the
RT Escherichia coli K-12 cynS gene encoding cyanase.";
RL J. Bacteriol. 169:5224-5230(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3049588; DOI=10.1016/s0021-9258(18)68104-9;
RA Sung Y.-C., Fuchs J.A.;
RT "Characterization of the cyn operon in Escherichia coli K12.";
RL J. Biol. Chem. 263:14769-14775(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP CHARACTERIZATION.
RX PubMed=3301828; DOI=10.1016/s0021-9258(18)61086-5;
RA Little R.M., Anderson P.M.;
RT "Structural properties of cyanase. Denaturation, renaturation, and role of
RT sulfhydryls and oligomeric structure in catalytic activity.";
RL J. Biol. Chem. 262:10120-10126(1987).
RN [8]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=10801492; DOI=10.1016/s0969-2126(00)00134-9;
RA Walsh M.A., Otwinowski Z., Perrakis A., Anderson P.M., Joachimiak A.;
RT "Structure of cyanase reveals that a novel dimeric and decameric
RT arrangement of subunits is required for formation of the enzyme active
RT site.";
RL Structure 8:505-514(2000).
CC -!- FUNCTION: Catalyzes the reaction of cyanate with bicarbonate to produce
CC ammonia and carbon dioxide.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+);
CC Xref=Rhea:RHEA:11120, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:29195;
CC EC=4.2.1.104;
CC -!- SUBUNIT: Homodecamer composed of five homodimers.
CC -!- SIMILARITY: Belongs to the cyanase family. {ECO:0000305}.
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DR EMBL; M17891; AAA23629.1; -; Genomic_DNA.
DR EMBL; M23219; AAA23626.1; -; Genomic_DNA.
DR EMBL; U73857; AAB18064.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73443.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76122.1; -; Genomic_DNA.
DR PIR; A91850; YNEC.
DR RefSeq; NP_414874.1; NC_000913.3.
DR RefSeq; WP_000616243.1; NZ_SSZK01000061.1.
DR PDB; 1DW9; X-ray; 1.65 A; A/B/C/D/E/F/G/H/I/J=1-156.
DR PDB; 1DWK; X-ray; 1.65 A; A/B/C/D/E/F/G/H/I/J=1-156.
DR PDB; 2IU7; X-ray; 1.91 A; A/B/C/D/E/F/G/H/I/J=1-156.
DR PDB; 2IUO; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J=1-156.
DR PDB; 2IV1; X-ray; 1.88 A; A/B/C/D/E/F/G/H/I/J=1-156.
DR PDB; 2IVB; X-ray; 1.95 A; A/B/C/D/E/F/G/H/I/J=1-156.
DR PDB; 2IVG; X-ray; 1.87 A; A/B/C/D/E/F/G/H/I/J=1-156.
DR PDB; 2IVQ; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=1-156.
DR PDBsum; 1DW9; -.
DR PDBsum; 1DWK; -.
DR PDBsum; 2IU7; -.
DR PDBsum; 2IUO; -.
DR PDBsum; 2IV1; -.
DR PDBsum; 2IVB; -.
DR PDBsum; 2IVG; -.
DR PDBsum; 2IVQ; -.
DR AlphaFoldDB; P00816; -.
DR SMR; P00816; -.
DR BioGRID; 4263187; 5.
DR DIP; DIP-9365N; -.
DR IntAct; P00816; 3.
DR STRING; 511145.b0340; -.
DR PaxDb; P00816; -.
DR PRIDE; P00816; -.
DR EnsemblBacteria; AAC73443; AAC73443; b0340.
DR EnsemblBacteria; BAE76122; BAE76122; BAE76122.
DR GeneID; 948998; -.
DR KEGG; ecj:JW0331; -.
DR KEGG; eco:b0340; -.
DR PATRIC; fig|1411691.4.peg.1937; -.
DR EchoBASE; EB0172; -.
DR eggNOG; COG1513; Bacteria.
DR HOGENOM; CLU_103452_1_1_6; -.
DR InParanoid; P00816; -.
DR OMA; YELVMIN; -.
DR PhylomeDB; P00816; -.
DR BioCyc; EcoCyc:CYANLY-MON; -.
DR BioCyc; MetaCyc:CYANLY-MON; -.
DR EvolutionaryTrace; P00816; -.
DR PRO; PR:P00816; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008824; F:cyanate hydratase activity; IDA:EcoCyc.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0009440; P:cyanate catabolic process; IMP:EcoCyc.
DR CDD; cd00559; Cyanase_C; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR Gene3D; 3.30.1160.10; -; 1.
DR HAMAP; MF_00535; Cyanate_hydrat; 1.
DR InterPro; IPR008076; Cyanase.
DR InterPro; IPR003712; Cyanate_lyase_C.
DR InterPro; IPR036581; Cyanate_lyase_C_sf.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR PANTHER; PTHR34186; PTHR34186; 1.
DR Pfam; PF02560; Cyanate_lyase; 1.
DR PIRSF; PIRSF001263; Cyanate_hydratas; 1.
DR PRINTS; PR01693; CYANASE.
DR SMART; SM01116; Cyanate_lyase; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR SUPFAM; SSF55234; SSF55234; 1.
DR TIGRFAMs; TIGR00673; cynS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lyase; Reference proteome.
FT CHAIN 1..156
FT /note="Cyanate hydratase"
FT /id="PRO_0000187523"
FT ACT_SITE 96
FT ACT_SITE 99
FT ACT_SITE 122
FT CONFLICT 34
FT /note="D -> N (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="D -> N (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="L -> S (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="N -> D (in Ref. 3)"
FT /evidence="ECO:0000305"
FT HELIX 9..24
FT /evidence="ECO:0007829|PDB:1DW9"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:1DW9"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1DW9"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:1DW9"
FT HELIX 55..64
FT /evidence="ECO:0007829|PDB:1DW9"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:1DW9"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:1DW9"
FT HELIX 92..115
FT /evidence="ECO:0007829|PDB:1DW9"
FT STRAND 118..134
FT /evidence="ECO:0007829|PDB:1DW9"
FT STRAND 138..152
FT /evidence="ECO:0007829|PDB:1DW9"
SQ SEQUENCE 156 AA; 17049 MW; 13AC830926313CED CRC64;
MIQSQINRNI RLDLADAILL SKAKKDLSFA EIADGTGLAE AFVTAALLGQ QALPADAARL
VGAKLDLDED SILLLQMIPL RGCIDDRIPT DPTMYRFYEM LQVYGTTLKA LVHEKFGDGI
ISAINFKLDV KKVADPEGGE RAVITLDGKY LPTKPF
