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Protein

Carbonic anhydrase

Gene
N/A
Organism
Methanosarcina thermophila
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reversible hydration of carbon dioxide. Essential to photosynthetic carbon dioxide fixation.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei96 – 961Proton donor/acceptor
Metal bindingi115 – 1151Zinc2 Publications
Active sitei118 – 1181
Metal bindingi151 – 1511Zinc2 Publications
Metal bindingi156 – 1561Zinc2 Publications
Binding sitei236 – 2361Substrate1 Publication

GO - Molecular functioni

  1. carbonate dehydratase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.2.1.1. 3281.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase (EC:4.2.1.1)
OrganismiMethanosarcina thermophila
Taxonomic identifieri2210 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 34341 PublicationAdd
BLAST
Chaini35 – 247213Carbonic anhydrasePRO_0000004273Add
BLAST

Interactioni

Subunit structurei

Homotrimer.2 Publications

Structurei

Secondary structure

1
247
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 463Combined sources
Beta strandi54 – 563Combined sources
Beta strandi73 – 808Combined sources
Beta strandi91 – 977Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi113 – 1164Combined sources
Beta strandi119 – 1213Combined sources
Turni122 – 1243Combined sources
Helixi128 – 1303Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi137 – 1437Combined sources
Beta strandi154 – 1618Combined sources
Beta strandi172 – 1787Combined sources
Beta strandi189 – 1924Combined sources
Beta strandi199 – 2013Combined sources
Helixi210 – 2145Combined sources
Turni224 – 2274Combined sources
Helixi228 – 24417Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
DisProtiDP00110.
ProteinModelPortaliP40881.
SMRiP40881. Positions 35-247.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40881.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni93 – 953Substrate binding
Regioni109 – 1102Substrate binding

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR001451. Hexapep_transf.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 2 hits.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P40881-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMFNKQIFTI LILSLSLALA GSGCISEGAE DNVAQEITVD EFSNIRENPV
60 70 80 90 100
TPWNPEPSAP VIDPTAYIDP QASVIGEVTI GANVMVSPMA SIRSDEGMPI
110 120 130 140 150
FVGDRSNVQD GVVLHALETI NEEGEPIEDN IVEVDGKEYA VYIGNNVSLA
160 170 180 190 200
HQSQVHGPAA VGDDTFIGMQ AFVFKSKVGN NCVLEPRSAA IGVTIPDGRY
210 220 230 240
IPAGMVVTSQ AEADKLPEVT DDYAYSHTNE AVVYVNVHLA EGYKETS
Length:247
Mass (Da):26,414
Last modified:January 31, 1995 - v1
Checksum:i1256EB566DB9207C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08885 Genomic DNA. Translation: AAA73428.1.
PIRiA57712.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08885 Genomic DNA. Translation: AAA73428.1.
PIRiA57712.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
DisProtiDP00110.
ProteinModelPortaliP40881.
SMRiP40881. Positions 35-247.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP40881.
ChEMBLiCHEMBL3932.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi4.2.1.1. 3281.

Miscellaneous databases

EvolutionaryTraceiP40881.

Family and domain databases

InterProiIPR001451. Hexapep_transf.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 2 hits.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
ProtoNetiSearch...

Publicationsi

  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(1993) [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(1995) [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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEX WITH ZINC AND SUBSTRATE.

Entry informationi

Entry nameiCAH_METTE
AccessioniPrimary (citable) accession number: P40881
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1995
Last sequence update: January 31, 1995
Last modified: November 25, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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.