ID CAN_ECOLI Reviewed; 220 AA. AC P61517; P36857; P75656; Q8KJQ4; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2004, sequence version 1. DT 27-MAR-2024, entry version 154. DE RecName: Full=Carbonic anhydrase 2; DE EC=4.2.1.1 {ECO:0000269|PubMed:11316870}; DE AltName: Full=Carbonate dehydratase 2; GN Name=can; Synonyms=cynT2, yadF; OrderedLocusNames=b0126, JW0122; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8202364; DOI=10.1093/nar/22.9.1637; RA Fujita N., Mori H., Yura T., Ishihama A.; RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4- RT 4.1 min (110,917-193,643 bp) region."; RL Nucleic Acids Res. 22:1637-1639(1994). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION. 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 [4] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=B / BL21; RX PubMed=10493123; RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q; RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.; RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite RT chromatography."; RL Electrophoresis 20:2181-2195(1999). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC ION, CATALYTIC RP ACTIVITY, AND SUBUNIT. RX PubMed=11316870; DOI=10.1110/ps.46301; RA Cronk J.D., Endrizzi J.A., Cronk M.R., O'neill J.W., Zhang K.Y.J.; RT "Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an RT unusual pH-dependent activity."; RL Protein Sci. 10:911-922(2001). 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; CC Evidence={ECO:0000269|PubMed:11316870}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:11316870}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11316870}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11316870}. CC -!- INTERACTION: CC P61517; P0CE47: tufA; NbExp=2; IntAct=EBI-562106, EBI-301077; 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; U00096; AAC73237.1; -; Genomic_DNA. DR EMBL; AP009048; BAB96701.2; -; Genomic_DNA. DR PIR; F64735; F64735. DR RefSeq; NP_414668.1; NC_000913.3. DR RefSeq; WP_000651599.1; NZ_STEB01000010.1. DR PDB; 1I6O; X-ray; 2.20 A; A/B=1-220. DR PDB; 1I6P; X-ray; 2.00 A; A=1-220. DR PDB; 1T75; X-ray; 2.50 A; A/B/D/E=1-220. DR PDB; 2ESF; X-ray; 2.25 A; A/B=1-220. DR PDB; 7SEV; X-ray; 2.30 A; A=1-220. DR PDBsum; 1I6O; -. DR PDBsum; 1I6P; -. DR PDBsum; 1T75; -. DR PDBsum; 2ESF; -. DR PDBsum; 7SEV; -. DR AlphaFoldDB; P61517; -. DR SMR; P61517; -. DR BioGRID; 4259733; 31. DR DIP; DIP-36168N; -. DR IntAct; P61517; 11. DR STRING; 511145.b0126; -. DR jPOST; P61517; -. DR PaxDb; 511145-b0126; -. DR EnsemblBacteria; AAC73237; AAC73237; b0126. DR GeneID; 75202059; -. DR GeneID; 944832; -. DR KEGG; ecj:JW0122; -. DR KEGG; eco:b0126; -. DR PATRIC; fig|1411691.4.peg.2156; -. DR EchoBASE; EB2224; -. DR eggNOG; COG0288; Bacteria. DR HOGENOM; CLU_053879_3_0_6; -. DR InParanoid; P61517; -. DR OMA; WHYIIET; -. DR OrthoDB; 9797527at2; -. DR PhylomeDB; P61517; -. DR BioCyc; EcoCyc:EG12319-MONOMER; -. DR BioCyc; MetaCyc:EG12319-MONOMER; -. DR BRENDA; 4.2.1.1; 2026. DR EvolutionaryTrace; P61517; -. DR PRO; PR:P61517; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; 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; IBA:GO_Central. DR GO; GO:0051289; P:protein homotetramerization; IDA:EcoCyc. DR CDD; cd00883; beta_CA_cladeA; 1. DR Gene3D; 3.40.1050.10; Carbonic anhydrase; 1. DR InterPro; IPR001765; Carbonic_anhydrase. DR InterPro; IPR015892; Carbonic_anhydrase_CS. DR InterPro; IPR036874; Carbonic_anhydrase_sf. DR PANTHER; PTHR11002; CARBONIC ANHYDRASE; 1. DR PANTHER; PTHR11002:SF83; CARBONIC ANHYDRASE; 1. DR Pfam; PF00484; Pro_CA; 1. DR SMART; SM00947; Pro_CA; 1. DR SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 1. DR PROSITE; PS00704; PROK_CO2_ANHYDRASE_1; 1. DR PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Lyase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1..220 FT /note="Carbonic anhydrase 2" FT /id="PRO_0000077465" FT BINDING 42 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:11316870, FT ECO:0007744|PDB:1I6O, ECO:0007744|PDB:1I6P" FT BINDING 44 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:11316870, FT ECO:0007744|PDB:1I6O, ECO:0007744|PDB:1I6P" FT BINDING 98 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:11316870, FT ECO:0007744|PDB:1I6O, ECO:0007744|PDB:1I6P" FT BINDING 101 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:11316870, FT ECO:0007744|PDB:1I6O, ECO:0007744|PDB:1I6P" FT HELIX 4..19 FT /evidence="ECO:0007829|PDB:1I6P" FT TURN 23..26 FT /evidence="ECO:0007829|PDB:1I6P" FT HELIX 27..30 FT /evidence="ECO:0007829|PDB:1I6P" FT STRAND 36..42 FT /evidence="ECO:0007829|PDB:1I6P" FT HELIX 49..53 FT /evidence="ECO:0007829|PDB:1I6P" FT STRAND 59..65 FT /evidence="ECO:0007829|PDB:1I6P" FT HELIX 75..86 FT /evidence="ECO:0007829|PDB:1I6P" FT STRAND 91..98 FT /evidence="ECO:0007829|PDB:1I6P" FT HELIX 102..109 FT /evidence="ECO:0007829|PDB:1I6P" FT HELIX 116..129 FT /evidence="ECO:0007829|PDB:1I6P" FT HELIX 131..134 FT /evidence="ECO:0007829|PDB:1I6P" FT HELIX 139..141 FT /evidence="ECO:0007829|PDB:1I6P" FT HELIX 142..160 FT /evidence="ECO:0007829|PDB:1I6P" FT HELIX 162..169 FT /evidence="ECO:0007829|PDB:1I6P" FT STRAND 175..181 FT /evidence="ECO:0007829|PDB:1I6P" FT TURN 183..185 FT /evidence="ECO:0007829|PDB:1I6P" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:1I6P" FT STRAND 195..197 FT /evidence="ECO:0007829|PDB:1I6P" FT HELIX 198..214 FT /evidence="ECO:0007829|PDB:1I6P" SQ SEQUENCE 220 AA; 25097 MW; 48A9086BE9428452 CRC64; MKDIDTLISN NALWSKMLVE EDPGFFEKLA QAQKPRFLWI GCSDSRVPAE RLTGLEPGEL FVHRNVANLV IHTDLNCLSV VQYAVDVLEV EHIIICGHYG CGGVQAAVEN PELGLINNWL LHIRDIWFKH SSLLGEMPQE RRLDTLCELN VMEQVYNLGH STIMQSAWKR GQKVTIHGWA YGIHDGLLRD LDVTATNRET LEQRYRHGIS NLKLKHANHK //