Q9RNU9 (CAPP_STRCO) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 78.
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: Phosphoenolpyruvate carboxylase Short name=PEPC Short name=PEPCase EC=4.1.1.31 | ||||||
| Gene names |
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| Organism | Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 100226 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces › ![]() |
Protein attributes
| Sequence length | 911 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle By similarity. HAMAP-Rule MF_00595 |
| Catalytic activity | Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-. HAMAP-Rule MF_00595 |
| Cofactor | Magnesium By similarity. |
| Sequence similarities | Belongs to the PEPCase type 1 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbon dioxide fixation |
| Ligand | Magnesium |
| Molecular function | Lyase |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | carbon fixation Inferred from electronic annotation. Source: HAMAP oxaloacetate metabolic processInferred from electronic annotation. Source: HAMAP tricarboxylic acid cycleInferred from electronic annotation. Source: InterPro |
| Molecular_function | magnesium ion binding Inferred from electronic annotation. Source: HAMAP phosphoenolpyruvate carboxylase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 911 | 911 | Phosphoenolpyruvate carboxylase HAMAP-Rule MF_00595 | PRO_0000166628 | |||||
Sites | |||||||||
| Active site | 137 | 1 | By similarity | ||||||
| Active site | 569 | 1 | By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Phosphoenolpyruvate carboxylase from Streptomyces coelicolor A3(2): purification of the enzyme, cloning of the ppc gene and over-expression of the protein in a streptomycete." Bramwell H., Nimmo H.G., Hunter I.S., Coggins J.R. Biochem. J. 293:131-136(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: A3(2) / NRRL B-16638. |
| [2] | "The ppc gene of Streptomyces coelicolor A3(2)." Ricketts A.D.J., Hunter I.S. Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: A3(2) / NRRL B-16638. |
| [3] | "Characterization of the phosphoenolpyruvate carboxylase gene from Streptomyces coelicolor A3(2) and a ppc gene disruption mutant." Alves A.M.C.R., te Poele E., White J., Bibb M.J., Dijkhuizen L. Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: A3(2) / NRRL B-16638. |
| [4] | "Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. Hopwood D.A.Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF177946 Genomic DNA. Translation: AAD53311.1. AF160253 Genomic DNA. Translation: AAM54458.1. AL939115 Genomic DNA. Translation: CAB95920.1. |
| RefSeq | NP_627344.1. NC_003888.3. |
3D structure databases | |
| ProteinModelPortal | Q9RNU9. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 100226.SCO3127. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB95920; CAB95920; CAB95920. |
| GeneID | 1098561. |
| KEGG | sco:SCO3127. |
| PATRIC | 23736002. VBIStrCoe124346_3191. |
Phylogenomic databases | |
| eggNOG | COG2352. |
| HOGENOM | HOG000238647. |
| KO | K01595. |
| OMA | AIPWVFG. |
| ProtClustDB | CLSK902480. |
Family and domain databases | |
| HAMAP | MF_00595. PEPcase_type1. |
| InterPro | IPR021135. PEP_COase. IPR018129. PEP_COase_AS. IPR022805. PEP_COase_bac/pln-type. IPR015813. Pyrv/PenolPyrv_Kinase. [Graphical view] |
| Pfam | PF00311. PEPcase. 1 hit. [Graphical view] |
| PRINTS | PR00150. PEPCARBXLASE. |
| SUPFAM | SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit. |
| PROSITE | PS00781. PEPCASE_1. 1 hit. PS00393. PEPCASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CAPP_STRCO | ||||||||
| Accession | Primary (citable) accession number: Q9RNU9 | ||||||||
| 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 |

Clusters with
