Reviewed,
UniProtKB/Swiss-Prot Q6HES5 (PYRB_BACHK)
Last modified
February 9, 2010.
Version 47.
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 |
| ||||
| Organism | Bacillus thuringiensis subsp. konkukian [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 180856 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 304 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate. HAMAP MF_00001 |
| Pathway | Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. HAMAP MF_00001 |
| 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 cellular 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 – 304 | 304 | Aspartate carbamoyltransferase HAMAP MF_00001 | PRO_0000113096 | |||
Sequences
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References
| [1] | "Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. Gilna P.J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 97-27. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017355 Genomic DNA. Translation: AAT60636.1. |
| RefSeq | YP_037951.1. |
3D structure databases | |
| SMR | Q6HES5. Positions 2-291. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2855677. |
| GenomeReviews | Gene locus BT9727_3631 in contig AE017355_GR. |
| KEGG | btk:BT9727_3631. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG579429. |
| OMA | VMMLRVQ. |
Enzyme and pathway databases | |
| BioCyc | BTHU281309:BT9727_3631-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00001. Asp_carb_tr. [Tree] |
| InterPro | IPR006132. Asp/Orn_carbamoyltranf_P_bd. IPR006130. Asp/Orn_carbamoylTrfase. IPR006131. Asp_carbamoyltransf_Asp/Orn_bd. IPR002082. Asp_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_BACHK | ||||||||
| Accession | Primary (citable) accession number: Q6HES5 | ||||||||
| 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


