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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

Zn2+2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei96Proton donor/acceptor1 Publication1
Metal bindingi115Zinc; via pros nitrogen2 Publications1
Active sitei1181 Publication1
Metal bindingi151Zinc; via tele nitrogen2 Publications1
Metal bindingi156Zinc; via tele nitrogen2 Publications1
Binding sitei236Substrate1 Publication1

GO - Molecular functioni

  • carbonate dehydratase activity Source: CACAO
  • 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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3932.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 341 PublicationAdd BLAST34
ChainiPRO_000000427335 – 247Carbonic anhydraseAdd BLAST213

Interactioni

Subunit structurei

Homotrimer.2 Publications

Chemistry databases

BindingDBiP40881.

Structurei

Secondary structure

1247
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi44 – 46Combined sources3
Beta strandi54 – 56Combined sources3
Beta strandi73 – 80Combined sources8
Beta strandi91 – 97Combined sources7
Beta strandi100 – 102Combined sources3
Beta strandi113 – 116Combined sources4
Beta strandi119 – 121Combined sources3
Turni122 – 124Combined sources3
Helixi128 – 130Combined sources3
Beta strandi132 – 134Combined sources3
Beta strandi137 – 143Combined sources7
Beta strandi154 – 161Combined sources8
Beta strandi172 – 178Combined sources7
Beta strandi189 – 192Combined sources4
Beta strandi199 – 201Combined sources3
Helixi210 – 214Combined sources5
Turni224 – 227Combined sources4
Helixi228 – 244Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40881.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni93 – 95Substrate binding1 Publication3
Regioni109 – 110Substrate binding1 Publication2

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR001451. Hexapep.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 2 hits.
PF14602. Hexapep_2. 1 hit.
[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:February 1, 1995 - v1
Checksum:i1256EB566DB9207C
GO

Sequence databases

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

Genome annotation databases

GeneIDi24847494.

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP40881.
ChEMBLiCHEMBL3932.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24847494.

Enzyme and pathway databases

BRENDAi4.2.1.1. 3281.

Miscellaneous databases

EvolutionaryTraceiP40881.

Family and domain databases

InterProiIPR001451. Hexapep.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 2 hits.
PF14602. Hexapep_2. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCAH_METTE
AccessioniPrimary (citable) accession number: P40881
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 30, 2016
This is version 96 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

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.