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P61517 (CAN_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbonic anhydrase 2

EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase 2
Gene names
Name:can
Synonyms:cynT2, yadF
Ordered Locus Names:b0126, JW0122
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length220 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Binds 1 zinc ion per subunit.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the beta-class carbonic anhydrase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 220220Carbonic anhydrase 2
PRO_0000077465

Sites

Metal binding421Zinc
Metal binding441Zinc
Metal binding981Zinc
Metal binding1011Zinc

Secondary structure

.................................... 220
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61517 [UniParc].

Last modified May 24, 2004. Version 1.
Checksum: 48A9086BE9428452

FASTA22025,097
        10         20         30         40         50         60 
MKDIDTLISN NALWSKMLVE EDPGFFEKLA QAQKPRFLWI GCSDSRVPAE RLTGLEPGEL 

        70         80         90        100        110        120 
FVHRNVANLV IHTDLNCLSV VQYAVDVLEV EHIIICGHYG CGGVQAAVEN PELGLINNWL 

       130        140        150        160        170        180 
LHIRDIWFKH SSLLGEMPQE RRLDTLCELN VMEQVYNLGH STIMQSAWKR GQKVTIHGWA 

       190        200        210        220 
YGIHDGLLRD LDVTATNRET LEQRYRHGIS NLKLKHANHK 

« Hide

References

« Hide 'large scale' references
[1]"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
Fujita N., Mori H., Yura T., Ishihama A.
Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography."
Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.
Electrophoresis 20:2181-2195(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
Strain: B / BL21.
[5]"Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity."
Cronk J.D., Endrizzi J.A., Cronk M.R., O'neill J.W., Zhang K.Y.J.
Protein Sci. 10:911-922(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC73237.1.
AP009048 Genomic DNA. Translation: BAB96701.2.
PIRF64735.
RefSeqNP_414668.1. NC_000913.3.
YP_488429.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I6OX-ray2.20A/B1-220[»]
1I6PX-ray2.00A1-220[»]
1T75X-ray2.50A/B/D/E1-220[»]
2ESFX-ray2.25A/B1-220[»]
ProteinModelPortalP61517.
SMRP61517. Positions 2-215.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36168N.
IntActP61517. 10 interactions.
STRING511145.b0126.

Proteomic databases

PaxDbP61517.
PRIDEP61517.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73237; AAC73237; b0126.
BAB96701; BAB96701; BAB96701.
GeneID12930739.
944832.
KEGGecj:Y75_p0123.
eco:b0126.
PATRIC32115355. VBIEscCol129921_0129.

Organism-specific databases

EchoBASEEB2224.
EcoGeneEG12319. can.

Phylogenomic databases

eggNOGCOG0288.
HOGENOMHOG000125184.
KOK01673.
OMAVQEAWAR.
OrthoDBEOG6FFSB8.
PhylomeDBP61517.
ProtClustDBPRK10437.

Enzyme and pathway databases

BioCycEcoCyc:EG12319-MONOMER.
ECOL316407:JW0122-MONOMER.
BRENDA4.2.1.1. 2026.

Gene expression databases

GenevestigatorP61517.

Family and domain databases

Gene3D3.40.1050.10. 1 hit.
InterProIPR001765. Carbonic_anhydrase.
IPR015892. Carbonic_anhydrase_CS.
[Graphical view]
PANTHERPTHR11002. PTHR11002. 1 hit.
PfamPF00484. Pro_CA. 1 hit.
[Graphical view]
SMARTSM00947. Pro_CA. 1 hit.
[Graphical view]
SUPFAMSSF53056. SSF53056. 1 hit.
PROSITEPS00704. PROK_CO2_ANHYDRASE_1. 1 hit.
PS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP61517.
PROP61517.

Entry information

Entry nameCAN_ECOLI
AccessionPrimary (citable) accession number: P61517
Secondary accession number(s): P36857, P75656, Q8KJQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: April 16, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene