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P20507 (CAH1_CHLRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Carbonic anhydrase 1
EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase 1
Short name=CA1

Cleaved into the following 2 chains:

  1. Carbonic anhydrase 1 large chain
  2. Carbonic anhydrase 1 small chain
Gene names
Name:CAH1
OrganismChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

Protein attributes

Sequence length377 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.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc.

Subunit structure

Tetramer of two large and two small subunits linked by two disulfide bonds.

Subcellular location

Periplasm.

Induction

Requires light in addition to a decrease in CO2 concentration during growth.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionLyase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processone-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncarbonate dehydratase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.4
Chain21 – 377357Carbonic anhydrase 1
PRO_0000004257
Chain21 – 305285Carbonic anhydrase 1 large chain
PRO_0000004258
Chain341 – 37737Carbonic anhydrase 1 small chain
PRO_0000004259

Regions

Region260 – 2612Substrate binding By similarity
Compositional bias307 – 32014His-rich

Sites

Active site1121Proton acceptor By similarity
Metal binding1631Zinc; catalytic By similarity
Metal binding1651Zinc; catalytic By similarity
Metal binding1821Zinc; catalytic By similarity
Binding site2601Substrate By similarity

Amino acid modifications

Glycosylation1011N-linked (GlcNAc...) Ref.5
Glycosylation1351N-linked (GlcNAc...) Ref.5
Glycosylation2971N-linked (GlcNAc...) Ref.5
Disulfide bond21Interchain Ref.5
Disulfide bond61 ↔ 264 Ref.5
Disulfide bond194 ↔ 198 Ref.5
Disulfide bond296 ↔ 351Interchain (between large and small chains) Ref.5

Secondary structure

1 ....................................................... 377
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20507 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 26500D573313EB3D

FASTA37741,628
        10         20         30         40         50         60 
MARTGALLLV ALALAGCAQA CIYKFGTSPD SKATVSGDHW DHGLNGENWE GKDGAGNAWV 

        70         80         90        100        110        120 
CKTGRKQSPI NVPQYQVLDG KGSKIANGLQ TQWSYPDLMS NGTSVQVINN GHTIQVQWTY 

       130        140        150        160        170        180 
NYAGHATIAI PAMHNQTNRI VDVLEMRPND AADRVTAVPT QFHFHSTSEH LLAGKIYPLE 

       190        200        210        220        230        240 
LHIVHQVTEK LEACKGGCFS VTGILFQLDN GPDNELLEPI FANMPSREGT FSNLPAGTTI 

       250        260        270        280        290        300 
KLGELLPSDR DYVTYEGSLT TPPCSEGLLW HVMTQPQRIS FGQWNRYRLA VGLKECNSTE 

       310        320        330        340        350        360 
TAADAGHHHH HRRLLHNHAH LEEVPAATSE PKHYFRRVML AESANPDAYT CKAVAFGQNF 

       370 
RNPQYANGRT IKLARYH

« Hide

References

[1]"cDNA cloning, sequence, and expression of carbonic anhydrase in Chlamydomonas reinhardtii: regulation by environmental CO2 concentration."
Fukuzawa H., Fujiwara S., Yamamoto Y., Dionisio-Sese M.L., Miyachi S.
Proc. Natl. Acad. Sci. U.S.A. 87:4383-4387(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"Structure and differential expression of two genes encoding carbonic anhydrase in Chlamydomonas reinhardtii."
Fujiwara S., Fukuzawa H., Tachiki A., Miyachi S.
Proc. Natl. Acad. Sci. U.S.A. 87:9779-9783(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Nucleotide sequences of two genes CAH1 and CAH2 which encode carbonic anhydrase polypeptides in Chlamydomonas reinhardtii."
Fukuzawa H., Fujiwara S., Tachiki A., Miyachi S.
Nucleic Acids Res. 18:6441-6442(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: IAM C-9.
[4]"Subunit constitution of carbonic anhydrase from Chlamydomonas reinhardtii."
Kamo T., Shimogawara K., Fukuzawa H., Muto S., Miyachi S.
Eur. J. Biochem. 192:557-562(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-37 AND 341-377.
[5]"Structural analysis of periplasmic carbonic anhydrase 1 of Chlamydomonas reinhardtii."
Ishida S., Muto S., Miyachi S.
Eur. J. Biochem. 214:9-16(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-101; ASN-135 AND ASN-297.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D90206 Genomic DNA. Translation: BAA14232.2.
PIRA35795. S14187.
RefSeqXP_001692291.1. XM_001692239.1.
UniGeneCre.3137.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3B1BX-ray1.88A/B1-377[»]
ProteinModelPortalP20507.
ModBaseSearch...

Proteomic databases

PRIDEP20507.
ProMEXP20507.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5717875.
KEGGcre:CHLREDRAFT_24120.

Phylogenomic databases

eggNOGCOG3338.
OMATEKLEAC.
ProtClustDBCLSN2702778.

Enzyme and pathway databases

BioCycCHLAMY:CHLREDRAFT_24120-MONOMER.

Family and domain databases

Gene3D3.10.200.10. 2 hits.
InterProIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERPTHR18952. PTHR18952. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMSSF51069. Euk_COanhd. 1 hit.
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAH1_CHLRE
AccessionPrimary (citable) accession number: P20507
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 3, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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