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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

GO - Biological processi

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

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi159C → S: 100% loss of activity. 1 Publication1
Mutagenesisi168H → N: Small loss of activity. 1 Publication1
Mutagenesisi203E → A: 100% loss of activity. 1 Publication1
Mutagenesisi208H → N: Small loss of activity. 1 Publication1
Mutagenesisi219H → N: 100% loss of activity. 1 Publication1
Mutagenesisi222C → S: 100% loss of activity. 1 Publication1
Mutagenesisi275E → A: Small loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 70Chloroplast1 PublicationAdd BLAST70
ChainiPRO_000000426971 – 328Carbonic anhydrase, 27 kDa isoformAdd BLAST258
ChainiPRO_0000004270108 – 328Carbonic anhydrase, 25 kDa isoformAdd BLAST221

Proteomic databases

PRIDEiP17067.

Interactioni

Subunit structurei

Homohexamer.

Structurei

Secondary structure

1328
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi120 – 134Combined sources15
Turni135 – 137Combined sources3
Helixi140 – 146Combined sources7
Beta strandi153 – 159Combined sources7
Helixi162 – 164Combined sources3
Helixi166 – 169Combined sources4
Beta strandi176 – 182Combined sources7
Helixi183 – 185Combined sources3
Turni192 – 194Combined sources3
Helixi196 – 207Combined sources12
Beta strandi212 – 221Combined sources10
Helixi223 – 230Combined sources8
Beta strandi239 – 241Combined sources3
Helixi242 – 246Combined sources5
Helixi247 – 249Combined sources3
Helixi250 – 259Combined sources10
Helixi265 – 284Combined sources20
Helixi288 – 295Combined sources8
Beta strandi300 – 307Combined sources8
Turni308 – 311Combined sources4
Beta strandi312 – 318Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EKJX-ray1.93A/B/C/D/E/F/G/H108-328[»]
ProteinModelPortaliP17067.
SMRiP17067.
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:August 1, 1990 - v1
Checksum:iDD26766D96483B2B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti31S → F in AAA33652 (PubMed:16667962).Curated1
Sequence conflicti43S → SS in AAA33652 (PubMed:16667962).Curated1
Sequence conflicti176E → K in AAA33652 (PubMed:16667962).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EKJX-ray1.93A/B/C/D/E/F/G/H108-328[»]
ProteinModelPortaliP17067.
SMRiP17067.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP17067.

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...

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: November 2, 2016
This is version 98 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

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 one 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.