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P61517

- CAN_ECOLI

UniProt

P61517 - CAN_ECOLI

Protein

Carbonic anhydrase 2

Gene

can

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (24 May 2004)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    H2CO3 = CO2 + H2O.

    Cofactori

    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi42 – 421Zinc
    Metal bindingi44 – 441Zinc
    Metal bindingi98 – 981Zinc
    Metal bindingi101 – 1011Zinc

    GO - Molecular functioni

    1. carbonate dehydratase activity Source: EcoCyc
    2. zinc ion binding Source: EcoCyc

    GO - Biological processi

    1. carbon utilization Source: InterPro
    2. metabolic process Source: GOC

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonic anhydrase 2 (EC:4.2.1.1)
    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12319. can.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 220220Carbonic anhydrase 2PRO_0000077465Add
    BLAST

    Proteomic databases

    PaxDbiP61517.
    PRIDEiP61517.

    Expressioni

    Gene expression databases

    GenevestigatoriP61517.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    DIPiDIP-36168N.
    IntActiP61517. 10 interactions.
    STRINGi511145.b0126.

    Structurei

    Secondary structure

    1
    220
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1916
    Turni23 – 264
    Helixi27 – 304
    Beta strandi36 – 427
    Helixi49 – 535
    Beta strandi59 – 657
    Helixi75 – 8612
    Beta strandi91 – 988
    Helixi102 – 1098
    Helixi116 – 12914
    Helixi131 – 1344
    Helixi139 – 1413
    Helixi142 – 16019
    Helixi162 – 1698
    Beta strandi175 – 1817
    Turni183 – 1853
    Beta strandi188 – 1903
    Beta strandi195 – 1973
    Helixi198 – 21417

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 2-215.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP61517.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0288.
    HOGENOMiHOG000125184.
    KOiK01673.
    OMAiCEINVIE.
    OrthoDBiEOG6FFSB8.
    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

    MKDIDTLISN NALWSKMLVE EDPGFFEKLA QAQKPRFLWI GCSDSRVPAE    50
    RLTGLEPGEL FVHRNVANLV IHTDLNCLSV VQYAVDVLEV EHIIICGHYG 100
    CGGVQAAVEN PELGLINNWL LHIRDIWFKH SSLLGEMPQE RRLDTLCELN 150
    VMEQVYNLGH STIMQSAWKR GQKVTIHGWA YGIHDGLLRD LDVTATNRET 200
    LEQRYRHGIS NLKLKHANHK 220
    Length:220
    Mass (Da):25,097
    Last modified:May 24, 2004 - v1
    Checksum:i48A9086BE9428452
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC73237.1.
    AP009048 Genomic DNA. Translation: BAB96701.2.
    PIRiF64735.
    RefSeqiNP_414668.1. NC_000913.3.
    YP_488429.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73237; AAC73237; b0126.
    BAB96701; BAB96701; BAB96701.
    GeneIDi12930739.
    944832.
    KEGGiecj:Y75_p0123.
    eco:b0126.
    PATRICi32115355. VBIEscCol129921_0129.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC73237.1 .
    AP009048 Genomic DNA. Translation: BAB96701.2 .
    PIRi F64735.
    RefSeqi NP_414668.1. NC_000913.3.
    YP_488429.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1I6O X-ray 2.20 A/B 1-220 [» ]
    1I6P X-ray 2.00 A 1-220 [» ]
    1T75 X-ray 2.50 A/B/D/E 1-220 [» ]
    2ESF X-ray 2.25 A/B 1-220 [» ]
    ProteinModelPortali P61517.
    SMRi P61517. Positions 2-215.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36168N.
    IntActi P61517. 10 interactions.
    STRINGi 511145.b0126.

    Proteomic databases

    PaxDbi P61517.
    PRIDEi P61517.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73237 ; AAC73237 ; b0126 .
    BAB96701 ; BAB96701 ; BAB96701 .
    GeneIDi 12930739.
    944832.
    KEGGi ecj:Y75_p0123.
    eco:b0126.
    PATRICi 32115355. VBIEscCol129921_0129.

    Organism-specific databases

    EchoBASEi EB2224.
    EcoGenei EG12319. can.

    Phylogenomic databases

    eggNOGi COG0288.
    HOGENOMi HOG000125184.
    KOi K01673.
    OMAi CEINVIE.
    OrthoDBi EOG6FFSB8.
    PhylomeDBi P61517.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG12319-MONOMER.
    ECOL316407:JW0122-MONOMER.
    BRENDAi 4.2.1.1. 2026.

    Miscellaneous databases

    EvolutionaryTracei P61517.
    PROi P61517.

    Gene expression databases

    Genevestigatori P61517.

    Family and domain databases

    Gene3Di 3.40.1050.10. 1 hit.
    InterProi IPR001765. Carbonic_anhydrase.
    IPR015892. Carbonic_anhydrase_CS.
    [Graphical view ]
    PANTHERi PTHR11002. PTHR11002. 1 hit.
    Pfami PF00484. Pro_CA. 1 hit.
    [Graphical view ]
    SMARTi SM00947. Pro_CA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53056. SSF53056. 1 hit.
    PROSITEi PS00704. PROK_CO2_ANHYDRASE_1. 1 hit.
    PS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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).

    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: October 1, 2014
    This is version 101 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

    External Data

    Dasty 3