Reviewed,
UniProtKB/Swiss-Prot P83299 (CAH1_CHIHA)
Last modified
September 22, 2009.
Version 18.
History...
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90%,
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Carbonic anhydrase 1 EC=4.2.1.1 Alternative name(s): Carbonic anhydrase I Short name=CA-I Carbonate dehydratase I Ice-CA | ||
| Gene names |
| ||
| Organism | Chionodraco hamatus (Antarctic teleost icefish) | ||
| Taxonomic identifier | 36188 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Perciformes › Notothenioidei › Channichthyidae › Chionodraco |
Protein attributes
| Sequence length | 259 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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 | |
| Sequence similarities | Belongs to the alpha-carbonic anhydrase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Metal-binding Zinc |
| Molecular function | Lyase |
| PTM | Acetylation |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | one-carbon metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | carbonate dehydratase activity Inferred from electronic annotation. Source: EC zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 259 | 259 | Carbonic anhydrase 1 | PRO_0000289146 | |||||
Sites | |||||||||
| Metal binding | 93 | 1 | Zinc; catalytic By similarity UniProtKB P00921 | ||||||
| Metal binding | 95 | 1 | Zinc; catalytic By similarity UniProtKB P00921 | ||||||
| Metal binding | 118 | 1 | Zinc; catalytic By similarity UniProtKB P00921 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylalanine Ref.1 | ||||||
Sequences
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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 | |
|---|---|
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 4.2.1.1. 275374. |
Family and domain databases | |
| InterPro | IPR001148. Carbonic_anhydrase_a-class_cat. IPR018338. Carbonic_anhydrase_a-class_CS. IPR018440. Carbonic_anhydrase_CA2. [Graphical view] |
| Gene3D | G3DSA:3.10.200.10. Euk_COanhd. 1 hit. |
| PANTHER | PTHR18952:SF28. Carbonic_anhydrase_CA2. 1 hit. PTHR18952. Euk_COanhd. 1 hit. |
| Pfam | PF00194. Carb_anhydrase. 1 hit. [Graphical view] |
| ProDom | PD000865. Euk_COanhd. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS00162. ALPHA_CA_1. 1 hit. PS51144. ALPHA_CA_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CAH1_CHIHA | ||||||||
| Accession | Primary (citable) accession number: P83299 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

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