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Protein

Carbonic anhydrase, chloroplastic

Gene
N/A
Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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

Interactioni

Subunit structurei

Homohexamer.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MSTSSINGFS LSSLSPAKTS TKRTTLRPFV SASLNTSSSS SSSTFPSLIQ
60 70 80 90 100
DKPVFASSSP IITPVLREEM GKGYDEAIEE LQKLLREKTE LKATAAEKVE
110 120 130 140 150
QITAQLGTTS SSDGIPKSEA SERIKTGFLH FKKEKYDKNP ALYGELAKGQ
160 170 180 190 200
SPPFMVFACS DSRVCPSHVL DFQPGEAFVV RNVANLVPPY DQAKYAGTGA
210 220 230 240 250
AIEYAVLHLK VSNIVVIGHS ACGGIKGLLS FPFDGTYSTD FIEEWVKIGL
260 270 280 290 300
PAKAKVKAQH GDAPFAELCT HCEKEAVNAS LGNLLTYPFV REGLVNKTLA
310 320
LKGGYYDFVK GSFELWGLEF GLSSTFSV
Length:328
Mass (Da):35,377
Last modified:July 31, 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:
EMBLi
GenBanki
DDBJi
Links Updated
X52558 mRNA. Translation: CAA36792.1.
M63627 mRNA. Translation: AAA33652.1.
PIRiS10200.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52558 mRNA. Translation: CAA36792.1.
M63627 mRNA. Translation: AAA33652.1.
PIRiS10200.

3D structure databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP17067.

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...

Publicationsi

  1. "Nucleotide sequence of pea cDNA encoding chloroplast carbonic anhydrase."
    Roeske C.A., Ogren W.L.
    Nucleic Acids Res. 18:3413-3413(1989) [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(1990) [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(1991) [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(1992) [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(1999) [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: July 31, 1990
Last sequence update: July 31, 1990
Last modified: January 6, 2015
This is version 94 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

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 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.