Reviewed,
UniProtKB/Swiss-Prot P40137 (CYAA_STIAU)
Last modified
November 24, 2009.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Adenylate cyclase 1 EC=4.6.1.1 Alternative name(s): ATP pyrophosphate-lyase 1 Adenylyl cyclase 1 Short name=AC 1 | ||
| Gene names |
| ||
| Organism | Stigmatella aurantiaca | ||
| Taxonomic identifier | 41 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Cystobacterineae › Cystobacteraceae › Stigmatella |
Protein attributes
| Sequence length | 424 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | ATP = 3',5'-cyclic AMP + diphosphate. |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. |
| Enzyme regulation | Inhibited by adenosine. Activated by GTP. |
| Subcellular location | Cell membrane; Multi-pass membrane protein Potential. |
| Sequence similarities | Belongs to the adenylyl cyclase class-3 family. Contains 1 guanylate cyclase domain. |
| Caution | It is uncertain whether Met-1 or Met-2 is the initiator. |
Ontologies
| Keywords | |
|---|---|
| Biological process | cAMP biosynthesis |
| Cellular component | Cell membrane Membrane |
| Domain | Transmembrane |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Lyase |
| Gene Ontology (GO) | |
| Biological process | cAMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW intracellular signaling cascadeInferred from electronic annotation. Source: InterPro |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate cyclase activityInferred from electronic annotation. Source: EC magnesium 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 – 424 | 424 | Adenylate cyclase 1 | PRO_0000195747 | |||||
Regions | |||||||||
| Transmembrane | 26 – 46 | 21 | Potential | ||||||
| Transmembrane | 57 – 77 | 21 | Potential | ||||||
| Transmembrane | 88 – 108 | 21 | Potential | ||||||
| Transmembrane | 114 – 134 | 21 | Potential | ||||||
| Transmembrane | 163 – 183 | 21 | Potential | ||||||
| Domain | 230 – 363 | 134 | Guanylate cyclase | ||||||
| Region | 1 – 223 | 223 | Ion channel Potential | ||||||
Sites | |||||||||
| Metal binding | 235 | 1 | Magnesium By similarity | ||||||
| Metal binding | 279 | 1 | Magnesium By similarity | ||||||
Sequences
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References
| [1] | "Bifunctional structure of two adenylyl cyclases from the myxobacterium Stigmatella aurantiaca." Coudart-Cavalli M.-P., Sismeiro O., Danchin A. Biochimie 79:757-767(1997) [PubMed: 9523018] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: B17R20. |
| [2] | "Phylogeny of adenylyl cyclases." Danchin A. Adv. Second Messenger Phosphoprotein Res. 27:109-162(1993) [PubMed: 8418825] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 213-424. |
Cross-references
Sequence databases | |
|---|---|
| AJ223796 Genomic DNA. Translation: CAA11549.1. | |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 4.6.1.1. 119283. |
Family and domain databases | |
| InterPro | IPR001054. A/G_cyclase. [Graphical view] |
| Gene3D | G3DSA:3.30.70.1230. A/G_cyclase. 1 hit. |
| Pfam | PF00211. Guanylate_cyc. 1 hit. [Graphical view] |
| SMART | SM00044. CYCc. 1 hit. [Graphical view] |
| PROSITE | PS50125. GUANYLATE_CYCLASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CYAA_STIAU | ||||||||
| Accession | Primary (citable) accession number: P40137 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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