B0CHS0 (CARA_BRUSI) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 33.
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: Carbamoyl-phosphate synthase small chain EC=6.3.5.5 Alternative name(s): Carbamoyl-phosphate synthetase glutamine chain | ||||
| Gene names |
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| Organism | Brucella suis (strain ATCC 23445 / NCTC 10510) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 470137 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella |
Protein attributes
| Sequence length | 407 AA. |
| Sequence status | Complete. |
| 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 | Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. HAMAP MF_01209 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 By similarity. |
| Sequence similarities | Belongs to the CarA family. Contains 1 glutamine amidotransferase type-1 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Arginine biosynthesis 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: UniProtKB-KW glutamine metabolic processInferred from electronic annotation. Source: UniProtKB-KW pyrimidine nucleotide biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW carbamoyl-phosphate synthase (glutamine-hydrolyzing) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 407 | 407 | Carbamoyl-phosphate synthase small chain HAMAP MF_01209 | PRO_1000138857 | |||||
Regions | |||||||||
| Domain | 209 – 397 | 189 | Glutamine amidotransferase type-1 | ||||||
| Region | 1 – 205 | 205 | CPSase HAMAP MF_01209 | ||||||
Sites | |||||||||
| Active site | 286 | 1 | Nucleophile By similarity | ||||||
| Active site | 370 | 1 | By similarity | ||||||
| Active site | 372 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "Brucella suis ATCC 23445 whole genome shotgun sequencing project." Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M., Snyder E.E. Brettin T.S.Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 23445 / NCTC 10510. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000911 Genomic DNA. Translation: ABY38571.1. |
| RefSeq | YP_001628141.1. NC_010169.1. |
3D structure databases | |
| ProteinModelPortal | B0CHS0. |
| SMR | B0CHS0. Positions 16-396. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B0CHS0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 5838054. |
| GenomeReviews | Gene locus BSUIS_A1539 in contig CP000911_GR. |
| KEGG | bmt:BSUIS_A1539. |
| PATRIC | 17870668. VBIBruSui83806_3123. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG286341. |
| OMA | FTYPELG. |
| ProtClustDB | PRK12564. |
Enzyme and pathway databases | |
| BioCyc | BSUI470137:BSUIS_A1539-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01209. CPSase_S_chain. [Tree] |
| InterPro | IPR006274. CarbamoylP_synth_ssu. IPR002474. CarbamoylP_synth_ssu_N. IPR017926. GATASE_1. [Graphical view] |
| Gene3D | G3DSA:3.50.30.20. G3DSA:3.50.30.20. 1 hit. |
| KO | K01956. |
| Pfam | PF00988. CPSase_sm_chain. 1 hit. PF00117. GATase. 1 hit. [Graphical view] |
| SMART | SM01097. CPSase_sm_chain. 1 hit. [Graphical view] |
| SUPFAM | SSF52021. CP_synthsmall. 1 hit. |
| TIGRFAMs | TIGR01368. CPSaseIIsmall. 1 hit. |
| PROSITE | PS51273. GATASE_TYPE_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CARA_BRUSI | ||||||||
| Accession | Primary (citable) accession number: B0CHS0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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