Reviewed,
UniProtKB/Swiss-Prot Q81WF1 (CARA_BACAN)
Last modified
November 3, 2009.
Version 52.
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 small chain EC=6.3.5.5 Alternative name(s): Carbamoyl-phosphate synthetase glutamine chain | ||||
| Gene names |
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| Organism | Bacillus anthracis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1392 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 365 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 | 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: 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 – 365 | 365 | Carbamoyl-phosphate synthase small chain HAMAP MF_01209 | PRO_0000112246 | |||||
Regions | |||||||||
| Domain | 170 – 357 | 188 | Glutamine amidotransferase type-1 | ||||||
| Region | 1 – 166 | 166 | CPSase HAMAP MF_01209 | ||||||
Sites | |||||||||
| Active site | 245 | 1 | Nucleophile By similarity | ||||||
| Active site | 330 | 1 | By similarity | ||||||
| Active site | 332 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. Fraser C.M.Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton. |
| [2] | "Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor. |
| [3] | "Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne. |
Cross-references
Sequence databases | |
|---|---|
| AE016879 Genomic DNA. Translation: AAP27753.1. AE017334 Genomic DNA. Translation: AAT33143.1. AE017225 Genomic DNA. Translation: AAT56040.1. | |
| RefSeq | NP_846267.1. YP_020668.1. YP_029989.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1JDB based on UniProtKB P00907. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1086653. 2819581. 2852140. |
| GenomeReviews | Gene locus BA_4026 in contig AE016879_GR. Gene locus BAS3738 in contig AE017225_GR. Gene locus GBAA_4026 in contig AE017334_GR. |
| KEGG | ban:BA4026. bar:GBAA4026. bat:BAS3738. |
| TIGR | BA_4026. GBAA_4026. |
Phylogenomic databases | |
| HOGENOM | Q81WF1. |
| OMA | LFDGSNC. |
Enzyme and pathway databases | |
| BioCyc | BANT260799:BAS3738-MON. BANT261594:GBAA4026-MON. |
| BRENDA | 6.3.5.5. 267517. |
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_BACAN | ||||||||
| Accession | Primary (citable) accession number: Q81WF1 Secondary accession number(s): Q6HUJ9, Q6KNT4 | ||||||||
| 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


