位置:首页 > 蛋白库 > CYNT_ECOLI
CYNT_ECOLI
ID   CYNT_ECOLI              Reviewed;         219 AA.
AC   P0ABE9; P17582; P78278; Q2MC85;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Carbonic anhydrase 1;
DE            EC=4.2.1.1 {ECO:0000269|PubMed:1740425};
DE   AltName: Full=Carbonate dehydratase 1;
GN   Name=cynT {ECO:0000303|PubMed:3049588}; OrderedLocusNames=b0339, JW0330;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
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   [2]
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   [3]
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   [4]
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   [5]
RP   PROTEIN SEQUENCE OF 1-20, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT,
RP   AND INDUCTION.
RX   PubMed=1740425; DOI=10.1016/s0021-9258(19)50586-5;
RA   Guilloton M.B., Korte J.J., Lamblin A.-F.J., Fuchs J.A., Anderson P.M.;
RT   "Carbonic anhydrase in Escherichia coli. A product of the cyn operon.";
RL   J. Biol. Chem. 267:3731-3734(1992).
CC   -!- FUNCTION: Reversible hydration of carbon dioxide. Carbon dioxide formed
CC       in the bicarbonate-dependent decomposition of cyanate by cyanase (CynS)
CC       diffuses out of the cell faster than it would be hydrated to
CC       bicarbonate, so the apparent function of this enzyme is to catalyze the
CC       hydration of carbon dioxide and thus prevent depletion of cellular
CC       bicarbonate. {ECO:0000269|PubMed:1740425}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000269|PubMed:1740425};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:1740425};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:1740425};
CC   -!- SUBUNIT: Oligomer. {ECO:0000269|PubMed:1740425}.
CC   -!- INDUCTION: By cyanate. {ECO:0000269|PubMed:1740425}.
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M23219; AAA23625.1; -; Genomic_DNA.
DR   EMBL; U73857; AAB18063.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73442.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76121.1; -; Genomic_DNA.
DR   PIR; C64761; QRECTC.
DR   RefSeq; NP_414873.1; NC_000913.3.
DR   RefSeq; WP_000658652.1; NZ_STEB01000036.1.
DR   AlphaFoldDB; P0ABE9; -.
DR   SMR; P0ABE9; -.
DR   BioGRID; 4259815; 4.
DR   DIP; DIP-47965N; -.
DR   IntAct; P0ABE9; 1.
DR   STRING; 511145.b0339; -.
DR   PaxDb; P0ABE9; -.
DR   PRIDE; P0ABE9; -.
DR   EnsemblBacteria; AAC73442; AAC73442; b0339.
DR   EnsemblBacteria; BAE76121; BAE76121; BAE76121.
DR   GeneID; 66671357; -.
DR   GeneID; 946548; -.
DR   KEGG; ecj:JW0330; -.
DR   KEGG; eco:b0339; -.
DR   PATRIC; fig|1411691.4.peg.1938; -.
DR   EchoBASE; EB0173; -.
DR   eggNOG; COG0288; Bacteria.
DR   HOGENOM; CLU_053879_5_3_6; -.
DR   InParanoid; P0ABE9; -.
DR   OMA; WHYIIET; -.
DR   PhylomeDB; P0ABE9; -.
DR   BioCyc; EcoCyc:CARBODEHYDRAT-MON; -.
DR   BioCyc; MetaCyc:CARBODEHYDRAT-MON; -.
DR   PRO; PR:P0ABE9; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR   GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR   GO; GO:0009440; P:cyanate catabolic process; IMP:EcoCyc.
DR   CDD; cd00884; beta_CA_cladeB; 1.
DR   Gene3D; 3.40.1050.10; -; 1.
DR   InterPro; IPR045066; Beta_CA_cladeB.
DR   InterPro; IPR001765; Carbonic_anhydrase.
DR   InterPro; IPR015892; Carbonic_anhydrase_CS.
DR   InterPro; IPR036874; Carbonic_anhydrase_sf.
DR   PANTHER; PTHR11002; PTHR11002; 1.
DR   Pfam; PF00484; Pro_CA; 1.
DR   SMART; SM00947; Pro_CA; 1.
DR   SUPFAM; SSF53056; SSF53056; 1.
DR   PROSITE; PS00704; PROK_CO2_ANHYDRASE_1; 1.
DR   PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lyase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..219
FT                   /note="Carbonic anhydrase 1"
FT                   /id="PRO_0000077459"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPJ7"
FT   BINDING         41
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPJ7"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPJ7"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPJ7"
FT   CONFLICT        174..176
FT                   /note="RIA -> GS (in Ref. 1; AAA23625)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="P -> R (in Ref. 1; AAA23625)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   219 AA;  23764 MW;  5EB41F125EC4D731 CRC64;
     MKEIIDGFLK FQREAFPKRE ALFKQLATQQ SPRTLFISCS DSRLVPELVT QREPGDLFVI
     RNAGNIVPSY GPEPGGVSAS VEYAVAALRV SDIVICGHSN CGAMTAIASC QCMDHMPAVS
     HWLRYADSAR VVNEARPHSD LPSKAAAMVR ENVIAQLANL QTHPSVRLAL EEGRIALHGW
     VYDIESGSIA AFDGATRQFV PLAANPRVCA IPLRQPTAA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024