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Protein

Carbonic anhydrase 2

Gene

can

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

H2CO3 = CO2 + H2O.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi42ZincCombined sources1 Publication1
Metal bindingi44ZincCombined sources1 Publication1
Metal bindingi98Zinc; via tele nitrogenCombined sources1 Publication1
Metal bindingi101ZincCombined sources1 Publication1

GO - Molecular functioni

  • carbonate dehydratase activity Source: EcoCyc
  • zinc ion binding Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG12319-MONOMER.
ECOL316407:JW0122-MONOMER.
MetaCyc:EG12319-MONOMER.
BRENDAi4.2.1.1. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 2 (EC:4.2.1.11 Publication)
Alternative name(s):
Carbonate dehydratase 2
Gene namesi
Name:can
Synonyms:cynT2, yadF
Ordered Locus Names:b0126, JW0122
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12319. can.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000774651 – 220Carbonic anhydrase 2Add BLAST220

Proteomic databases

EPDiP61517.
PaxDbiP61517.
PRIDEiP61517.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4259733. 14 interactors.
DIPiDIP-36168N.
IntActiP61517. 10 interactors.
STRINGi511145.b0126.

Structurei

Secondary structure

1220
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 19Combined sources16
Turni23 – 26Combined sources4
Helixi27 – 30Combined sources4
Beta strandi36 – 42Combined sources7
Helixi49 – 53Combined sources5
Beta strandi59 – 65Combined sources7
Helixi75 – 86Combined sources12
Beta strandi91 – 98Combined sources8
Helixi102 – 109Combined sources8
Helixi116 – 129Combined sources14
Helixi131 – 134Combined sources4
Helixi139 – 141Combined sources3
Helixi142 – 160Combined sources19
Helixi162 – 169Combined sources8
Beta strandi175 – 181Combined sources7
Turni183 – 185Combined sources3
Beta strandi188 – 190Combined sources3
Beta strandi195 – 197Combined sources3
Helixi198 – 214Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I6OX-ray2.20A/B1-220[»]
1I6PX-ray2.00A1-220[»]
1T75X-ray2.50A/B/D/E1-220[»]
2ESFX-ray2.25A/B1-220[»]
ProteinModelPortaliP61517.
SMRiP61517.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61517.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG41077A9. Bacteria.
COG0288. LUCA.
HOGENOMiHOG000125184.
InParanoidiP61517.
KOiK01673.
OMAiVQEAWAR.
PhylomeDBiP61517.

Family and domain databases

Gene3Di3.40.1050.10. 1 hit.
InterProiIPR001765. Carbonic_anhydrase.
IPR015892. Carbonic_anhydrase_CS.
[Graphical view]
PANTHERiPTHR11002. PTHR11002. 1 hit.
PfamiPF00484. Pro_CA. 1 hit.
[Graphical view]
SMARTiSM00947. Pro_CA. 1 hit.
[Graphical view]
SUPFAMiSSF53056. SSF53056. 1 hit.
PROSITEiPS00704. PROK_CO2_ANHYDRASE_1. 1 hit.
PS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P61517-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKDIDTLISN NALWSKMLVE EDPGFFEKLA QAQKPRFLWI GCSDSRVPAE
60 70 80 90 100
RLTGLEPGEL FVHRNVANLV IHTDLNCLSV VQYAVDVLEV EHIIICGHYG
110 120 130 140 150
CGGVQAAVEN PELGLINNWL LHIRDIWFKH SSLLGEMPQE RRLDTLCELN
160 170 180 190 200
VMEQVYNLGH STIMQSAWKR GQKVTIHGWA YGIHDGLLRD LDVTATNRET
210 220
LEQRYRHGIS NLKLKHANHK
Length:220
Mass (Da):25,097
Last modified:May 24, 2004 - v1
Checksum:i48A9086BE9428452
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC73237.1.
AP009048 Genomic DNA. Translation: BAB96701.2.
PIRiF64735.
RefSeqiNP_414668.1. NC_000913.3.
WP_000651599.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73237; AAC73237; b0126.
BAB96701; BAB96701; BAB96701.
GeneIDi944832.
KEGGiecj:JW0122.
eco:b0126.
PATRICi32115355. VBIEscCol129921_0129.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC73237.1.
AP009048 Genomic DNA. Translation: BAB96701.2.
PIRiF64735.
RefSeqiNP_414668.1. NC_000913.3.
WP_000651599.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I6OX-ray2.20A/B1-220[»]
1I6PX-ray2.00A1-220[»]
1T75X-ray2.50A/B/D/E1-220[»]
2ESFX-ray2.25A/B1-220[»]
ProteinModelPortaliP61517.
SMRiP61517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259733. 14 interactors.
DIPiDIP-36168N.
IntActiP61517. 10 interactors.
STRINGi511145.b0126.

Proteomic databases

EPDiP61517.
PaxDbiP61517.
PRIDEiP61517.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73237; AAC73237; b0126.
BAB96701; BAB96701; BAB96701.
GeneIDi944832.
KEGGiecj:JW0122.
eco:b0126.
PATRICi32115355. VBIEscCol129921_0129.

Organism-specific databases

EchoBASEiEB2224.
EcoGeneiEG12319. can.

Phylogenomic databases

eggNOGiENOG41077A9. Bacteria.
COG0288. LUCA.
HOGENOMiHOG000125184.
InParanoidiP61517.
KOiK01673.
OMAiVQEAWAR.
PhylomeDBiP61517.

Enzyme and pathway databases

BioCyciEcoCyc:EG12319-MONOMER.
ECOL316407:JW0122-MONOMER.
MetaCyc:EG12319-MONOMER.
BRENDAi4.2.1.1. 2026.

Miscellaneous databases

EvolutionaryTraceiP61517.
PROiP61517.

Family and domain databases

Gene3Di3.40.1050.10. 1 hit.
InterProiIPR001765. Carbonic_anhydrase.
IPR015892. Carbonic_anhydrase_CS.
[Graphical view]
PANTHERiPTHR11002. PTHR11002. 1 hit.
PfamiPF00484. Pro_CA. 1 hit.
[Graphical view]
SMARTiSM00947. Pro_CA. 1 hit.
[Graphical view]
SUPFAMiSSF53056. SSF53056. 1 hit.
PROSITEiPS00704. PROK_CO2_ANHYDRASE_1. 1 hit.
PS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAN_ECOLI
AccessioniPrimary (citable) accession number: P61517
Secondary accession number(s): P36857, P75656, Q8KJQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: November 2, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.