Reviewed,
UniProtKB/Swiss-Prot O93937 (PYR1_EMENI)
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June 16, 2009.
Version 58.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Protein pyrABCN Including the following 2 domains: 1- Recommended name: Glutamine-dependent carbamoyl-phosphate EC=6.3.5.5 2- Recommended name: Aspartate carbamoyltransferase EC=2.1.3.2 | ||||
| Gene names |
| ||||
| Organism | Emericella nidulans (Aspergillus nidulans) | ||||
| Taxonomic identifier | 162425 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella |
Protein attributes
| Sequence length | 2275 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | This protein is a "fusion" protein encoding three enzymatic activities of the pyrimidine pathway (GATase, CPSase, and ATCase) By similarity. UniProtKB P07259 |
| Catalytic activity | 2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate. |
| Pathway | Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 1/6. Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 2/6. |
| Domain | The DHOase domain is defective. |
| Miscellaneous | GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) form together the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5). In eukaryotes EC 6.3.5.5 is synthesized by two pathway-specific (arginine and pyrimidine) genes under separate control. |
| Sequence similarities | In the central section; belongs to the DHOase family. Contains 2 ATP-grasp domains. Contains 1 glutamine amidotransferase type-1 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyrimidine biosynthesis |
| Domain | Repeat |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase Transferase |
| Technical term | Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | 'de novo' pyrimidine base biosynthetic process Ref.1 Traceable author statement. Source: UniProtKB glutamine metabolic processInferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW amino acid bindingInferred from electronic annotation. Source: InterPro aspartate carbamoyltransferase activity Ref.1Traceable author statement. Source: UniProtKB carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Ref.1Traceable author statement. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2275 | 2275 | Protein pyrABCN | PRO_0000199509 | |||||
Regions | |||||||||
| Domain | 265 – 453 | 189 | Glutamine amidotransferase type-1 | ||||||
| Domain | 604 – 796 | 193 | ATP-grasp 1 | ||||||
| Domain | 1139 – 1330 | 192 | ATP-grasp 2 | ||||||
| Region | 1 – 440 | 440 | GATase (Glutamine amidotransferase) By similarity UniProtKB P07259 | ||||||
| Region | 441 – 482 | 42 | Linker By similarity UniProtKB P07259 | ||||||
| Region | 483 – 1522 | 1040 | CPSase (Carbamoyl-phosphate synthase) By similarity UniProtKB P07259 | ||||||
| Region | 1523 – 1532 | 10 | Linker By similarity UniProtKB P07259 | ||||||
| Region | 1533 – 1862 | 330 | Defective DHOase domain By similarity UniProtKB P07259 | ||||||
| Region | 1863 – 1953 | 91 | Linker By similarity UniProtKB P07259 | ||||||
| Region | 1954 – 2258 | 305 | ATCase (Aspartate transcarbamylase) By similarity UniProtKB P07259 | ||||||
Sites | |||||||||
| Active site | 342 | 1 | For GATase activity By similarity UniProtKB P07259 | ||||||
| Active site | 426 | 1 | For GATase activity By similarity UniProtKB P07259 | ||||||
| Active site | 428 | 1 | For GATase activity By similarity UniProtKB P07259 | ||||||
Experimental info | |||||||||
| Sequence conflict | 19 | 1 | G → R in AAD09129. Ref.1 | ||||||
| Sequence conflict | 169 – 170 | 2 | WL → CV in AAD09129. Ref.1 | ||||||
| Sequence conflict | 403 | 1 | V → D in AAD09129. Ref.1 | ||||||
| Sequence conflict | 454 | 1 | P → A in AAD09129. Ref.1 | ||||||
| Sequence conflict | 909 – 910 | 2 | SV → RL in AAD09129. Ref.1 | ||||||
| Sequence conflict | 1007 | 1 | T → A in AAD09129. Ref.1 | ||||||
| Sequence conflict | 1741 | 1 | A → R in AAD09129. Ref.1 | ||||||
| Sequence conflict | 2013 | 1 | A → V in AAD09129. Ref.1 | ||||||
| Sequence conflict | 2238 | 1 | Q → L in AAD09129. Ref.1 | ||||||
| Sequence conflict | 2269 – 2270 | 2 | LA → IE in AAD09129. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Structural and transcriptional analysis of the pyrABCN, pyrD and pyrF genes in Aspergillus nidulans and the evolutionary origin of fungal dihydroorotases." Aleksenko A., Liu W., Gojkovic Z., Nielsen J., Piskur J. Mol. Microbiol. 33:599-611(1999) [PubMed: 10417650] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: FGSC 4. |
| [2] | "Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H.  Birren B.W.Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4. |
Cross-references
Sequence databases | |
|---|---|
| AF112473 Genomic DNA. Translation: AAD09129.1. AACD01000007 Genomic DNA. Translation: EAA66664.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1M6V based on UniProtKB P00968. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 2.1.3.2. 3859. 6.3.5.5. 3859. |
Family and domain databases | |
| PROSITE | PS50975. ATP_GRASP. 2 hits. PS00097. CARBAMOYLTRANSFERASE. 1 hit. PS00866. CPSASE_1. 2 hits. PS00867. CPSASE_2. 2 hits. PS51273. GATASE_TYPE_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PYR1_EMENI | ||||||||
| Accession | Primary (citable) accession number: O93937 Secondary accession number(s): Q5BFW5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |
