P0ABF0 (CYNT_ECO57) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 39.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Carbonic anhydrase 1 EC=4.2.1.1 Alternative name(s): Carbonate dehydratase 1 | ||||
| Gene names |
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| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 219 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Reversible hydration of carbon dioxide. Carbon dioxide formed in the bicarbonate-dependent decomposition of cyanate by cyanase (CynS) diffuses out of the cell faster than it would be hydrated to bicarbonate, so the apparent function of this enzyme is to catalyze the hydration of carbon dioxide and thus prevent depletion of cellular bicarbonate By similarity. |
| Catalytic activity | H2CO3 = CO2 + H2O. |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Subunit structure | Oligomer By similarity. |
| Sequence similarities | Belongs to the beta-class carbonic anhydrase family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Metal-binding Zinc |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | carbon utilization Inferred from electronic annotation. Source: InterPro |
| Molecular function | carbonate dehydratase activity Inferred from electronic annotation. Source: EC zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 219 | 219 | Carbonic anhydrase 1 | PRO_0000077460 | |||||
Sites | |||||||||
| Metal binding | 39 | 1 | Zinc By similarity | ||||||
| Metal binding | 41 | 1 | Zinc By similarity | ||||||
| Metal binding | 98 | 1 | Zinc By similarity | ||||||
| Metal binding | 101 | 1 | Zinc By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 59 | 1 | V → G in BAB33815. Ref.2 | ||||||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG54688.1. BA000007 Genomic DNA. Translation: BAB33815.1. |
| PIR | D85528. H90677. |
| RefSeq | NP_286080.1. NC_002655.2. NP_308419.1. NC_002695.1. |
3D structure databases | |
| ProteinModelPortal | P0ABF0. |
| SMR | P0ABF0. Positions 1-202. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000027255; EBESCP00000026148; EBESCG00000026307. EBESCT00000058004; EBESCP00000055832; EBESCG00000057052. |
| GeneID | 914494. 957265. |
| GenomeReviews | Gene locus Z0435 in contig AE005174_GR. Gene locus ECs0392 in contig BA000007_GR. |
| KEGG | ece:Z0435. ecs:ECs0392. |
| PATRIC | 18349731. VBIEscCol44059_0386. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000009995. |
| HOGENOM | HBG711150. |
| OMA | WHYVIED. |
| ProtClustDB | CLSK866979. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS0392-MONOMER. |
Family and domain databases | |
| InterPro | IPR001765. Carbonic_anhydrase. IPR015892. Carbonic_anhydrase_CS. [Graphical view] |
| Gene3D | G3DSA:3.40.1050.10. CO_anhd_prok_pln. 1 hit. |
| KO | K01673. |
| PANTHER | PTHR11002. Carbonic_anhydrase. 1 hit. |
| Pfam | PF00484. Pro_CA. 1 hit. [Graphical view] |
| SMART | SM00947. Pro_CA. 1 hit. [Graphical view] |
| SUPFAM | SSF53056. Prok_plnt_COanhd. 1 hit. |
| PROSITE | PS00704. PROK_CO2_ANHYDRASE_1. 1 hit. PS00705. PROK_CO2_ANHYDRASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CYNT_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P0ABF0 Secondary accession number(s): P17582, P78278 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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