Reviewed,
UniProtKB/Swiss-Prot P25993 (CARA_BACSU)
Last modified
November 3, 2009.
Version 77.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
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 |
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| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1423 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 364 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; (S)-dihydroorotate from bicarbonate: step 1/3. 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. HAMAP MF_01209 |
| 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 – 364 | 364 | Carbamoyl-phosphate synthase pyrimidine-specific small chain HAMAP MF_01209 | PRO_0000112255 | |||||
Regions | |||||||||
| Domain | 171 – 356 | 186 | Glutamine amidotransferase type-1 | ||||||
| Region | 1 – 167 | 167 | CPSase HAMAP MF_01209 | ||||||
Sites | |||||||||
| Active site | 246 | 1 | Nucleophile By similarity | ||||||
| Active site | 329 | 1 | By similarity | ||||||
| Active site | 331 | 1 | By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Functional organization and nucleotide sequence of the Bacillus subtilis pyrimidine biosynthetic operon." Quinn C.L., Stephenson B.T., Switzer R.L. J. Biol. Chem. 266:9113-9127(1991) [PubMed: 1709162] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
Cross-references
Sequence databases | |
|---|---|
| M59757 Genomic DNA. Translation: AAA21269.1. AL009126 Genomic DNA. Translation: CAB13425.1. | |
| PIR | E39845. |
| RefSeq | NP_389434.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1A9X based on UniProtKB P00907. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 937368. |
| GenomeReviews | Gene locus BSU15510 in contig AL009126_GR. |
| KEGG | bsu:BSU15510. |
| NMPDR | fig|224308.1.peg.1553. |
Organism-specific databases | |
| SubtiList | BG10715. pyrAA. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P25993. |
| OMA | LFDGSNC. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU1553-MON. |
| BRENDA | 6.3.5.5. 150. |
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_BACSU | ||||||||
| Accession | Primary (citable) accession number: P25993 | ||||||||
| 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
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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