Reviewed,
UniProtKB/Swiss-Prot Q7WF77 (PYRB_BORBR)
Last modified
November 25, 2008.
Version 35.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Aspartate carbamoyltransferase EC=2.1.3.2 Alternative name(s): Aspartate transcarbamylase Short name=ATCase | ||||
| Gene names |
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| Organism | Bordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 518 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella |
Protein attributes
| Sequence length | 317 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate. |
| Pathway | Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 2/6. |
| Sequence similarities | Belongs to the ATCase/OTCase family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Pyrimidine biosynthesis |
| Molecular function | Transferase |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | 'de novo' pyrimidine base biosynthetic process Inferred from electronic annotation. Source: InterPro amino acid metabolic processInferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Molecular function | amino acid binding Inferred from electronic annotation. Source: InterPro aspartate carbamoyltransferase 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 – 317 | 317 | Aspartate carbamoyltransferase | PRO_0000113104 | |||
Sequences
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References
| [1] | "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. Maskell D.J.Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RB50 / ATCC BAA-588 / NCTC 13252. |
Cross-references
Sequence databases | |
|---|---|
| BX640450 Genomic DNA. Translation: CAE34766.1. | |
| RefSeq | NP_890937.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2660325. |
| GenomeReviews | Gene locus BB4403 in contig BX470250_GR. |
| KEGG | bbr:BB4403. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q7WF77. |
Enzyme and pathway databases | |
| BioCyc | BBRO257310:BB4403-MON. |
Family and domain databases | |
| HAMAP | MF_00001. [Tree] |
| InterPro | IPR006130. Asp/Orn_carbamoyltranf. IPR006132. Asp/Orn_carbamoyltranf_P_bd. IPR006131. Asp_carbamoyltransf_Asp/Orn_bd. IPR002082. Aspartate_carbamoyltransf_euk. [Graphical view] |
| Pfam | PF00185. OTCace. 1 hit. PF02729. OTCace_N. 1 hit. [Graphical view] |
| PRINTS | PR00100. AOTCASE. PR00101. ATCASE. |
| TIGRFAMs | TIGR00670. asp_carb_tr. 1 hit. |
| PROSITE | PS00097. CARBAMOYLTRANSFERASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PYRB_BORBR | ||||||||
| Accession | Primary (citable) accession number: Q7WF77 | ||||||||
| 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 |

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