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P17067

- CAHC_PEA

UniProt

P17067 - CAHC_PEA

Protein

Carbonic anhydrase, chloroplastic

Gene
N/A
Organism
Pisum sativum (Garden pea)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Aug 1990)
      Previous versions | rss
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    Functioni

    Reversible hydration of carbon dioxide.

    Catalytic activityi

    H2CO3 = CO2 + H2O.

    GO - Molecular functioni

    1. carbonate dehydratase activity Source: UniProtKB-EC
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. carbon utilization Source: InterPro

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonic anhydrase, chloroplastic (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase
    Cleaved into the following 2 chains:
    OrganismiPisum sativum (Garden pea)
    Taxonomic identifieri3888 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast stroma Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi159 – 1591C → S: 100% loss of activity. 1 Publication
    Mutagenesisi168 – 1681H → N: Small loss of activity. 1 Publication
    Mutagenesisi203 – 2031E → A: 100% loss of activity. 1 Publication
    Mutagenesisi208 – 2081H → N: Small loss of activity. 1 Publication
    Mutagenesisi219 – 2191H → N: 100% loss of activity. 1 Publication
    Mutagenesisi222 – 2221C → S: 100% loss of activity. 1 Publication
    Mutagenesisi275 – 2751E → A: Small loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 7070Chloroplast1 PublicationAdd
    BLAST
    Chaini71 – 328258Carbonic anhydrase, 27 kDa isoformPRO_0000004269Add
    BLAST
    Chaini108 – 328221Carbonic anhydrase, 25 kDa isoformPRO_0000004270Add
    BLAST

    Proteomic databases

    ProMEXiP17067.

    Interactioni

    Subunit structurei

    Homohexamer.

    Structurei

    Secondary structure

    1
    328
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi120 – 13415
    Turni135 – 1373
    Helixi140 – 1467
    Beta strandi153 – 1597
    Helixi162 – 1643
    Helixi166 – 1694
    Beta strandi176 – 1827
    Helixi183 – 1853
    Turni192 – 1943
    Helixi196 – 20712
    Beta strandi212 – 22110
    Helixi223 – 2308
    Beta strandi239 – 2413
    Helixi242 – 2465
    Helixi247 – 2493
    Helixi250 – 25910
    Helixi265 – 28420
    Helixi288 – 2958
    Beta strandi300 – 3078
    Turni308 – 3114
    Beta strandi312 – 3187

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EKJX-ray1.93A/B/C/D/E/F/G/H108-328[»]
    ProteinModelPortaliP17067.
    SMRiP17067. Positions 109-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17067.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P17067-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTSSINGFS LSSLSPAKTS TKRTTLRPFV SASLNTSSSS SSSTFPSLIQ    50
    DKPVFASSSP IITPVLREEM GKGYDEAIEE LQKLLREKTE LKATAAEKVE 100
    QITAQLGTTS SSDGIPKSEA SERIKTGFLH FKKEKYDKNP ALYGELAKGQ 150
    SPPFMVFACS DSRVCPSHVL DFQPGEAFVV RNVANLVPPY DQAKYAGTGA 200
    AIEYAVLHLK VSNIVVIGHS ACGGIKGLLS FPFDGTYSTD FIEEWVKIGL 250
    PAKAKVKAQH GDAPFAELCT HCEKEAVNAS LGNLLTYPFV REGLVNKTLA 300
    LKGGYYDFVK GSFELWGLEF GLSSTFSV 328
    Length:328
    Mass (Da):35,377
    Last modified:August 1, 1990 - v1
    Checksum:iDD26766D96483B2B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311S → F in AAA33652. (PubMed:16667962)Curated
    Sequence conflicti43 – 431S → SS in AAA33652. (PubMed:16667962)Curated
    Sequence conflicti176 – 1761E → K in AAA33652. (PubMed:16667962)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52558 mRNA. Translation: CAA36792.1.
    M63627 mRNA. Translation: AAA33652.1.
    PIRiS10200.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52558 mRNA. Translation: CAA36792.1 .
    M63627 mRNA. Translation: AAA33652.1 .
    PIRi S10200.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EKJ X-ray 1.93 A/B/C/D/E/F/G/H 108-328 [» ]
    ProteinModelPortali P17067.
    SMRi P17067. Positions 109-328.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    ProMEXi P17067.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P17067.

    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. "Nucleotide sequence of pea cDNA encoding chloroplast carbonic anhydrase."
      Roeske C.A., Ogren W.L.
      Nucleic Acids Res. 18:3413-3413(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "Isolation and characterization of a cDNA coding for pea chloroplastic carbonic anhydrase."
      Majeau N., Coleman J.R.
      Plant Physiol. 95:264-268(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Processing of the chloroplast transit peptide of pea carbonic anhydrase in chloroplasts and in Escherichia coli. Identification of two cleavage sites."
      Johansson I.-M., Forsman C.
      FEBS Lett. 314:232-236(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 71-76 AND 108-113, PROTEOLYTIC PROCESSING.
    4. "Characterization of pea chloroplastic carbonic anhydrase. Expression in Escherichia coli and site-directed mutagenesis."
      Provart N.J., Majeau N., Coleman J.R.
      Plant Mol. Biol. 22:937-943(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    5. "The active site architecture of Pisum sativum beta-carbonic anhydrase is a mirror image of that of alpha-carbonic anhydrases."
      Kimber M.S., Pai E.F.
      EMBO J. 19:1407-1418(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 108-328.

    Entry informationi

    Entry nameiCAHC_PEA
    AccessioniPrimary (citable) accession number: P17067
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 91 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3