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P17067 (CAHC_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Carbonic anhydrase, chloroplastic
EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase

Cleaved into the following 2 chains:

  1. Carbonic anhydrase, 27 kDa isoform
  2. Carbonic anhydrase, 25 kDa isoform
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reversible hydration of carbon dioxide.

Catalytic activity

H2CO3 = CO2 + H2O.

Subunit structure

Homohexamer.

Subcellular location

Plastid › chloroplast stroma.

Sequence similarities

Belongs to the beta-class carbonic anhydrase family.

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandZinc
   Molecular functionLyase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcarbon utilization

Inferred from electronic annotation. Source: InterPro

   Cellular_componentchloroplast stroma

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncarbonate dehydratase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 7070Chloroplast Ref.3
Chain71 – 328258Carbonic anhydrase, 27 kDa isoform
PRO_0000004269
Chain108 – 328221Carbonic anhydrase, 25 kDa isoform
PRO_0000004270

Experimental info

Mutagenesis1591C → S: 100% loss of activity.
Mutagenesis1681H → N: Small loss of activity.
Mutagenesis2031E → A: 100% loss of activity.
Mutagenesis2081H → N: Small loss of activity.
Mutagenesis2191H → N: 100% loss of activity.
Mutagenesis2221C → S: 100% loss of activity.
Mutagenesis2751E → A: Small loss of activity.
Sequence conflict311S → F in AAA33652. Ref.2
Sequence conflict431S → SS in AAA33652. Ref.2
Sequence conflict1761E → K in AAA33652. Ref.2

Secondary structure

1 .................................... 328
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17067 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: DD26766D96483B2B

FASTA32835,377
        10         20         30         40         50         60 
MSTSSINGFS LSSLSPAKTS TKRTTLRPFV SASLNTSSSS SSSTFPSLIQ DKPVFASSSP 

        70         80         90        100        110        120 
IITPVLREEM GKGYDEAIEE LQKLLREKTE LKATAAEKVE QITAQLGTTS SSDGIPKSEA 

       130        140        150        160        170        180 
SERIKTGFLH FKKEKYDKNP ALYGELAKGQ SPPFMVFACS DSRVCPSHVL DFQPGEAFVV 

       190        200        210        220        230        240 
RNVANLVPPY DQAKYAGTGA AIEYAVLHLK VSNIVVIGHS ACGGIKGLLS FPFDGTYSTD 

       250        260        270        280        290        300 
FIEEWVKIGL PAKAKVKAQH GDAPFAELCT HCEKEAVNAS LGNLLTYPFV REGLVNKTLA 

       310        320 
LKGGYYDFVK GSFELWGLEF GLSSTFSV

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X52558 mRNA. Translation: CAA36792.1.
M63627 mRNA. Translation: AAA33652.1.
PIRS10200.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EKJX-ray1.93A/B/C/D/E/F/G/H108-328[»]
ProteinModelPortalP17067.
SMRP17067. Positions 109-328.
ModBaseSearch...

Proteomic databases

ProMEXP17067.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. Prok_plnt_COanhd. 1 hit.
PROSITEPS00704. PROK_CO2_ANHYDRASE_1. 1 hit.
PS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP17067.

Entry information

Entry nameCAHC_PEA
AccessionPrimary (citable) accession number: P17067
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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