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P83299 (CAH1_CHIHA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 I
Carbonic anhydrase I
Short name=CA-I
Ice-CA
Gene names
Name:ca1
OrganismChionodraco hamatus (Antarctic teleost icefish) (Chaenichthys rhinoceratus hamatus)
Taxonomic identifier36188 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Perciformes › Notothenioidei › Channichthyidae › Chionodraco

Protein attributes

Sequence length259 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reversible hydration of carbon dioxide. Ref.1

Catalytic activity

H2CO3 = CO2 + H2O. Ref.1

Cofactor

Zinc By similarity. UniProtKB P00921

Subcellular location

Cytoplasm Ref.1.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionLyase
   PTMAcetylation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

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

Chain1 – 259259Carbonic anhydrase 1
PRO_0000289146

Regions

Region197 – 1982Substrate binding By similarity

Sites

Active site631Proton acceptor By similarity
Active site1261 By similarity
Metal binding931Zinc; catalytic By similarity UniProtKB P00921
Metal binding951Zinc; catalytic By similarity UniProtKB P00921
Metal binding1181Zinc; catalytic By similarity UniProtKB P00921
Binding site1971Substrate By similarity

Amino acid modifications

Modified residue11N-acetylalanine Ref.1

Sequences

Sequence LengthMass (Da)Tools
P83299 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 65CEBB8ECC61AB67

FASTA25928,343
        10         20         30         40         50         60 
AHAWGYGPTD GPDKWVSNFP IADGPRQSPI DILPGGASYD SGLKPLSLKY DPSNCLEILN 

        70         80         90        100        110        120 
NGHSFQVTFA DDSDSSTLKE GPISGVYRLK QFHFHWGASN DKGSEHTVAG TKYPAELHLV 

       130        140        150        160        170        180 
HWNTKYPSFG EAASKPDGLA VVGVFLKIGD ANASLQKVLD AFNDIRAKGK QTSFADFDPS 

       190        200        210        220        230        240 
TLLPGCLDYW TYDGSLTTPP LLESVTWIVC KEPISVSCEQ MAKFRSLLFS AEGEPECCMV 

       250 
DNYRPPQPLK GRHVRASFQ

« Hide

References

[1]"Biochemical characterization of a S-glutathionylated carbonic anhydrase isolated from gills of the Antarctic icefish Chionodraco hamatus."
Rizzello A., Ciardiello M.A., Acierno R., Carratore V., Verri T., di Prisco G., Storelli C., Maffia M.
Protein J. 26:335-348(2007) [PubMed: 17510781] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACETYLATION AT ALA-1.
Tissue: Gill.

Cross-references

3D structure databases

ProteinModelPortalP83299.
SMRP83299. Positions 1-256.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG002837.

Enzyme and pathway databases

BRENDA4.2.1.1. 7095.

Family and domain databases

InterProIPR001148. a_carbonic_anhydrase.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018440. Carbonic_anhydrase_CA2.
[Graphical view]
Gene3DG3DSA:3.10.200.10. Euk_COanhd. 1 hit.
PANTHERPTHR18952:SF28. Carbonic_anhydrase_CA2. 1 hit.
PTHR18952. Euk_COanhd. 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_CHIHA
AccessionPrimary (citable) accession number: P83299
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: January 25, 2012
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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