P40881 (CAH_METTE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Carbonic anhydrase EC=4.2.1.1
Organism	Methanosarcina thermophila
Taxonomic identifier	2210 [NCBI]
Taxonomic lineage	cellular organisms › Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	247 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular_function	carbonate dehydratase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW transferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 34

34

Ref.1

Chain

35 – 247

213

Carbonic anhydrase

PRO_0000004273

Regions

Region

93 – 95

3

Substrate binding

Region

109 – 110

2

Substrate binding

Sites

Active site

96

1

Proton donor/acceptor

Active site

118

1

Metal binding

115

1

Zinc

Metal binding

151

1

Zinc

Metal binding

156

1

Zinc

Binding site

236

1

Substrate

Secondary structure

1

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247

Helix Strand Turn

Details...

Beta strand

44 – 46

3

Beta strand

54 – 56

3

Beta strand

73 – 80

8

Beta strand

91 – 97

7

Beta strand

100 – 102

3

Beta strand

113 – 116

4

Beta strand

119 – 121

3

Turn

122 – 124

3

Helix

128 – 130

3

Beta strand

132 – 134

3

Beta strand

137 – 143

7

Beta strand

154 – 161

8

Beta strand

172 – 178

7

Beta strand

189 – 192

4

Beta strand

199 – 201

3

Helix

210 – 214

5

Turn

224 – 227

4

Helix

228 – 244

17

Sequences

	Sequence		Length	Mass (Da)
	P40881 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 1256EB566DB9207C	FASTA	247	26,414
	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

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.

PIR

A57712.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QQ0	X-ray	1.76	A	1-247	[»]
1QRE	X-ray	1.46	A	1-247	[»]
1QRF	X-ray	1.55	A	35-247	[»]
1QRG	X-ray	1.72	A	35-247	[»]
1QRL	X-ray	1.85	A	35-247	[»]
1QRM	X-ray	1.95	A	35-247	[»]
1THJ	X-ray	2.80	A/B/C	35-247	[»]
3OTM	X-ray	1.50	A	36-247	[»]
3OTZ	X-ray	1.60	A	35-247	[»]
3OU9	X-ray	1.80	A	35-247	[»]
3OUP	X-ray	1.65	A	35-247	[»]
3OW5	X-ray	1.80	A	35-247	[»]

DisProt

DP00110.

ProteinModelPortal

P40881.

SMR

P40881. Positions 35-247.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

4.2.1.1. 3281.

Family and domain databases

InterPro

IPR001451. Hexapep_transf.
IPR011004. Trimer_LpxA-like.
[Graphical view]

Pfam

PF00132. Hexapep. 2 hits.
[Graphical view]

SUPFAM

SSF51161. Trimer_LpxA_like. 1 hit.

ProtoNet

Search...

Other

BindingDB

P40881.

ChEMBL

CHEMBL3932.

EvolutionaryTrace

P40881.

Entry information

Entry name

CAH_METTE

Accession

Primary (citable) accession number: P40881

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	April 3, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program