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P40881 (CAH_METTE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbonic anhydrase

EC=4.2.1.1
OrganismMethanosarcina thermophila
Taxonomic identifier2210 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length247 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. Essential to photosynthetic carbon dioxide fixation.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc.

Subunit structure

Homotrimer.

Sequence similarities

Belongs to the gamma-class carbonic anhydrase family.

Ontologies

Keywords
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Molecular_functioncarbonate dehydratase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 Ref.1
Chain35 – 247213Carbonic anhydrase
PRO_0000004273

Regions

Region93 – 953Substrate binding
Region109 – 1102Substrate binding

Sites

Active site961Proton donor/acceptor
Active site1181
Metal binding1151Zinc
Metal binding1511Zinc
Metal binding1561Zinc
Binding site2361Substrate

Secondary structure

................................... 247
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P40881 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 1256EB566DB9207C

FASTA24726,414
        10         20         30         40         50         60 
MMFNKQIFTI LILSLSLALA GSGCISEGAE DNVAQEITVD EFSNIRENPV TPWNPEPSAP 

        70         80         90        100        110        120 
VIDPTAYIDP QASVIGEVTI GANVMVSPMA SIRSDEGMPI FVGDRSNVQD GVVLHALETI 

       130        140        150        160        170        180 
NEEGEPIEDN IVEVDGKEYA VYIGNNVSLA HQSQVHGPAA VGDDTFIGMQ AFVFKSKVGN 

       190        200        210        220        230        240 
NCVLEPRSAA IGVTIPDGRY IPAGMVVTSQ AEADKLPEVT DDYAYSHTNE AVVYVNVHLA 


EGYKETS 

« Hide

References

[1]"A carbonic anhydrase from the archaeon Methanosarcina thermophila."
Alber B.E., Ferry J.G.
Proc. Natl. Acad. Sci. U.S.A. 91:6909-6913(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-60.
Strain: DSM 1825 / TM-1.
[2]"A left-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila."
Kisker C., Schindelin H., Alber B.E., Ferry J.G., Rees D.C.
EMBO J. 15:2323-2330(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 35-247 IN COMPLEX WITH ZINC.
[3]"A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila."
Iverson T.M., Alber B.E., Kisker C., Ferry J.G., Rees D.C.
Biochemistry 39:9222-9231(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEX WITH ZINC AND SUBSTRATE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U08885 Genomic DNA. Translation: AAA73428.1.
PIRA57712.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QQ0X-ray1.76A1-247[»]
1QREX-ray1.46A1-247[»]
1QRFX-ray1.55A35-247[»]
1QRGX-ray1.72A35-247[»]
1QRLX-ray1.85A35-247[»]
1QRMX-ray1.95A35-247[»]
1THJX-ray2.80A/B/C35-247[»]
3OTMX-ray1.50A36-247[»]
3OTZX-ray1.60A35-247[»]
3OU9X-ray1.80A35-247[»]
3OUPX-ray1.65A35-247[»]
3OW5X-ray1.80A35-247[»]
DisProtDP00110.
ProteinModelPortalP40881.
SMRP40881. Positions 35-247.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP40881.
ChEMBLCHEMBL3932.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA4.2.1.1. 3281.

Family and domain databases

InterProIPR001451. Hexapep_transf.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF00132. Hexapep. 2 hits.
[Graphical view]
SUPFAMSSF51161. SSF51161. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP40881.

Entry information

Entry nameCAH_METTE
AccessionPrimary (citable) accession number: P40881
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references