Reviewed,
UniProtKB/Swiss-Prot Q9K9V8 (CARA_BACHD)
Last modified
June 16, 2009.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Carbamoyl-phosphate synthase pyrimidine-specific small chain EC=6.3.5.5 Alternative name(s): Carbamoyl-phosphate synthetase glutamine chain | ||||
| Gene names |
| ||||
| Organism | Bacillus halodurans [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 86665 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 362 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | 2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. HAMAP MF_01209 |
| Pathway | Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 1/6. HAMAP MF_01209 |
| Subunit structure | Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate By similarity. |
| Sequence similarities | Belongs to the carA 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 | arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP glutamine metabolic processInferred from electronic annotation. Source: UniProtKB-KW pyrimidine nucleotide biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Molecular function | ATP binding Inferred from electronic annotation. Source: HAMAP carbamoyl-phosphate synthase (glutamine-hydrolyzing) 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 – 362 | 362 | Carbamoyl-phosphate synthase pyrimidine-specific small chain HAMAP MF_01209 | PRO_0000112251 | |||||
Regions | |||||||||
| Domain | 171 – 358 | 188 | Glutamine amidotransferase type-1 | ||||||
| Region | 1 – 167 | 167 | CPSase HAMAP MF_01209 | ||||||
Sites | |||||||||
| Active site | 246 | 1 | Nucleophile By similarity | ||||||
| Active site | 331 | 1 | By similarity | ||||||
| Active site | 333 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis." Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K. Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153. |
Cross-references
Sequence databases | |
|---|---|
| BA000004 Genomic DNA. Translation: BAB06256.1. | |
| PIR | A83967. |
| RefSeq | NP_243403.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1JDB based on UniProtKB P00907. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 891501. |
| GenomeReviews | Gene locus BH2537 in contig BA000004_GR. |
| KEGG | bha:BH2537. |
| NMPDR | fig|272558.1.peg.2537. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q9K9V8. |
| OMA | Q9K9V8. LFDGSNC. |
Enzyme and pathway databases | |
| BioCyc | BHAL272558:BH2537-MON. |
| BRENDA | 6.3.5.5. 191865. |
Family and domain databases | |
| HAMAP | MF_01209. [Tree] |
| InterPro | IPR006220. Anth_synthII. IPR001317. CarbamoylP_synth_GATase. IPR006274. CarbamoylP_synth_ssu. IPR002474. CarbamoylP_synth_ssu_N. IPR011702. GATASE. IPR017926. GATASE_1. IPR000991. GATase_class1_C. [Graphical view] |
| PANTHER | PTHR11405:SF4. CarA_synth_small. 1 hit. |
| Pfam | PF00988. CPSase_sm_chain. 1 hit. PF00117. GATase. 1 hit. [Graphical view] |
| PRINTS | PR00097. ANTSNTHASEII. PR00099. CPSGATASE. PR00096. GATASE. |
| TIGRFAMs | TIGR01368. CPSaseIIsmall. 1 hit. |
| PROSITE | PS51273. GATASE_TYPE_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CARA_BACHD | ||||||||
| Accession | Primary (citable) accession number: Q9K9V8 | ||||||||
| 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


