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   24-JAN-2024, entry version 182.
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; Pseudomonadota; 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; 511145-b0340; -.
DR   EnsemblBacteria; AAC73443; AAC73443; b0340.
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   OrthoDB; 9785870at2; -.
DR   PhylomeDB; P00816; -.
DR   BioCyc; EcoCyc:CYANLY-MONOMER; -.
DR   BioCyc; MetaCyc:CYANLY-MONOMER; -.
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; 3.30.1160.10; Cyanate lyase, C-terminal domain; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 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; IPR048564; CYNS_N.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   NCBIfam; TIGR00673; cynS; 1.
DR   PANTHER; PTHR34186; CYANATE HYDRATASE; 1.
DR   PANTHER; PTHR34186:SF2; CYANATE HYDRATASE; 1.
DR   Pfam; PF02560; Cyanate_lyase; 1.
DR   Pfam; PF21291; CYNS_N; 1.
DR   PIRSF; PIRSF001263; Cyanate_hydratas; 1.
DR   PRINTS; PR01693; CYANASE.
DR   SMART; SM01116; Cyanate_lyase; 1.
DR   SUPFAM; SSF55234; Cyanase C-terminal domain; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 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
//