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Protein

Carbonic anhydrase 2

Gene

can

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionLyase
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG12319-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: EcoCyc

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

Binary interactionsi

WithEntry#Exp.IntActNotes
tufAP0CE472EBI-562106,EBI-301077

Protein-protein interaction databases

BioGridi425973331 interactors.
DIPiDIP-36168N
IntActiP61517 11 interactors.
STRINGi316385.ECDH10B_0106

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
OMAiAWERGQD
PhylomeDBiP61517

Family and domain databases

Gene3Di3.40.1050.101 hit
InterProiView protein in InterPro
IPR001765 Carbonic_anhydrase
IPR015892 Carbonic_anhydrase_CS
IPR036874 Carbonic_anhydrase_sf
PfamiView protein in Pfam
PF00484 Pro_CA, 1 hit
SMARTiView protein in SMART
SM00947 Pro_CA, 1 hit
SUPFAMiSSF53056 SSF53056, 1 hit
PROSITEiView protein in PROSITE
PS00704 PROK_CO2_ANHYDRASE_1, 1 hit
PS00705 PROK_CO2_ANHYDRASE_2, 1 hit

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
PATRICifig|1411691.4.peg.2156

Similar proteinsi

Entry informationi

Entry nameiCAN_ECOLI
AccessioniPrimary (citable) accession number: P61517
Secondary accession number(s): P36857, P75656, Q8KJQ4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: March 28, 2018
This is version 122 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome