CAN_ECOLI
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 03-AUG-2022, entry version 146.
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; Proteobacteria; 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; P61517; -.
DR PRIDE; P61517; -.
DR EnsemblBacteria; AAC73237; AAC73237; b0126.
DR EnsemblBacteria; BAB96701; BAB96701; BAB96701.
DR GeneID; 66671585; -.
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; PANEIIG; -.
DR PhylomeDB; P61517; -.
DR BioCyc; EcoCyc:EG12319-MON; -.
DR BioCyc; MetaCyc:EG12319-MON; -.
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 Gene3D; 3.40.1050.10; -; 1.
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 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
