Reviewed,
UniProtKB/Swiss-Prot Q9PJ84 (PYRG_CAMJE)
Last modified
June 16, 2009.
Version 49.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: CTP synthase EC=6.3.4.2 Alternative name(s): UTP--ammonia ligase CTP synthetase | ||||
| Gene names |
| ||||
| Organism | Campylobacter jejuni [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 197 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 543 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen By similarity. |
| Catalytic activity | ATP + UTP + NH3 = ADP + phosphate + CTP. HAMAP MF_01227 |
| Enzyme regulation | Allosterically activated by GTP, when glutamine is the substrate. Inhibited by CTP By similarity. |
| Pathway | Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. HAMAP MF_01227 |
| Subunit structure | Homotetramer By similarity. |
| Sequence similarities | Belongs to the CTP synthase family. Contains 1 glutamine amidotransferase type-1 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyrimidine biosynthesis |
| Domain | Glutamine amidotransferase |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW pyrimidine nucleotide biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW CTP synthase activityInferred from electronic annotation. Source: HAMAP protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| flgI | Q9PMJ8 | 1 | EBI-1194588,EBI-1191749 | |
| fliM | Q0PC73 | 1 | EBI-1194588,EBI-1191095 | |
| fliN | O32370 | 1 | EBI-1194588,EBI-1191320 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 543 | 543 | CTP synthase HAMAP MF_01227 | PRO_0000138172 | |||||
Regions | |||||||||
| Domain | 292 – 543 | 252 | Glutamine amidotransferase type-1 | ||||||
| Region | 1 – 254 | 254 | Aminator domain HAMAP MF_01227 | ||||||
Sites | |||||||||
| Active site | 381 | 1 | Nucleophile By similarity | ||||||
| Active site | 516 | 1 | By similarity | ||||||
| Active site | 518 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. Barrell B.G.Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2. |
Cross-references
Sequence databases | |
|---|---|
| AL111168 Genomic DNA. Translation: CAL34208.1. | |
| PIR | F81418. |
| RefSeq | YP_002343499.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9PJ84. 49 interactions. |
Genome annotation databases | |
| GeneID | 904367. |
| GenomeReviews | Gene locus Cj0027 in contig AL111168_GR. |
| KEGG | cje:Cj0027. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | Q9PJ84. CESKSHI. |
Enzyme and pathway databases | |
| BioCyc | CJEJ192222:CJ0027-MON. |
| BRENDA | 6.3.4.2. 255835. |
Family and domain databases | |
| HAMAP | MF_01227. [Tree] |
| InterPro | IPR004468. CTP_synthase. IPR017456. CTP_synthase_N. IPR017926. GATASE_1. IPR000991. GATase_class1_C. [Graphical view] |
| PANTHER | PTHR11550. PyrG_synth. 1 hit. |
| Pfam | PF06418. CTP_synth_N. 1 hit. PF00117. GATase. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00337. PyrG. 1 hit. |
| PROSITE | PS51273. GATASE_TYPE_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PYRG_CAMJE | ||||||||
| Accession | Primary (citable) accession number: Q9PJ84 Secondary accession number(s): Q0PC98 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


