Reviewed,
UniProtKB/Swiss-Prot Q1LTN7 (PYRG_BAUCH)
Last modified
June 16, 2009.
Version 25.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
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 | Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 374463 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia |
Protein attributes
| Sequence length | 543 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
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 |
| Complete GO annotation... | |
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_0000266067 | |||||
Regions | |||||||||
| Domain | 291 – 538 | 248 | Glutamine amidotransferase type-1 | ||||||
| Region | 1 – 253 | 253 | Aminator domain HAMAP MF_01227 | ||||||
Sites | |||||||||
| Active site | 379 | 1 | Nucleophile By similarity | ||||||
| Active site | 511 | 1 | By similarity | ||||||
| Active site | 513 | 1 | By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000238 Genomic DNA. Translation: ABF13830.1. | |
| RefSeq | YP_588677.1. |
3D structure databases | |
| SMR | Q1LTN7. Positions 1-539. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 4056160. |
| GenomeReviews | Gene locus BCI_0222 in contig CP000238_GR. |
| KEGG | bci:BCI_0222. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q1LTN7. |
| OMA | Q1LTN7. EFNNAYR. |
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_BAUCH | ||||||||
| Accession | Primary (citable) accession number: Q1LTN7 | ||||||||
| Entry history |
| ||||||||
| 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


