Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Carbonic anhydrase

Gene
N/A
Organism
Coccomyxa sp. PA
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

H2CO3 = CO2 + H2O.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471ZincCombined sources
Metal bindingi103 – 1031Zinc; via tele nitrogenCombined sources
Metal bindingi106 – 1061ZincCombined sources

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

LyaseUniRule annotationImported

Keywords - Ligandi

Metal-bindingCombined sources, ZincCombined sources

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydraseUniRule annotation (EC:4.2.1.1UniRule annotation)
OrganismiCoccomyxa sp. PAImported
Taxonomic identifieri41892 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaTrebouxiophyceaeCoccomyxaceaeCoccomyxa

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UCJX-ray1.85A/B1-227[»]
3UCKX-ray2.50A/B1-227[»]
3UCMX-ray2.51A/B1-227[»]
3UCNX-ray2.25A/B1-227[»]
3UCOX-ray2.50A/B1-227[»]
ProteinModelPortaliQ96554.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the beta-class carbonic anhydrase family.UniRule annotation

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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96554-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAKDTADLS PLLEANRKWA DECAAKDSTY FSKVAGSQAP EYLYIGCADS
60 70 80 90 100
RVSPAQLFNM APGEVFVQRN VGNLVSNKDL NCMSCLEYTV DHLKIKHILV
110 120 130 140 150
CGHYNCGACK AGLVWHPKTA GVTNLWISDV REVRDKNAAK LHGLSADDAW
160 170 180 190 200
DKMVELNVEA QVFNVCASPI VQAAWARGQP LSVHGIVYTP GTGLVKELIK
210 220
PITGMEDAGA LLRADLKQHC FFSESLA
Length:227
Mass (Da):24,696
Last modified:February 1, 1997 - v1
Checksum:i97E3C72EBAB511DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49976 mRNA. Translation: AAC33484.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49976 mRNA. Translation: AAC33484.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UCJX-ray1.85A/B1-227[»]
3UCKX-ray2.50A/B1-227[»]
3UCMX-ray2.51A/B1-227[»]
3UCNX-ray2.25A/B1-227[»]
3UCOX-ray2.50A/B1-227[»]
ProteinModelPortaliQ96554.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Intracellular beta-carbonic anhydrase of the unicellular green alga Coccomyxa. Cloning of the cdna and characterization of the functional enzyme overexpressed in Escherichia coli."
    Hiltonen T., Bjorkbacka H., Forsman C., Clarke A.K., Samuelsson G.
    Plant Physiol. 117:1341-1349(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: PAImported.
  2. "Structural studies of ?-carbonic anhydrase from the green alga Coccomyxa: inhibitor complexes with anions and acetazolamide."
    Huang S., Hainzl T., Grundstrom C., Forsman C., Samuelsson G., Sauer-Eriksson A.E.
    PLoS ONE 6:e28458-e28458(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH ZINC.

Entry informationi

Entry nameiQ96554_9CHLO
AccessioniPrimary (citable) accession number: Q96554
Entry historyi
Integrated into UniProtKB/TrEMBL: February 1, 1997
Last sequence update: February 1, 1997
Last modified: January 7, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.