Reviewed,
UniProtKB/Swiss-Prot Q8YAS7 (PTC_LISMO)
Last modified
November 3, 2009.
Version 48.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Putrescine carbamoyltransferase Short name=PTCase Short name=PTC EC=2.1.3.6 Alternative name(s): Putrescine transcarbamylase Putrescine transcarbamoylase | ||||
| Gene names |
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| Organism | Listeria monocytogenes [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1639 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria |
Protein attributes
| Sequence length | 341 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the phosphorolysis of N-carbamoylputrescine to form carbamoyl phosphate and putrescine. Is involved in the degradation pathway of the polyamine agmatine By similarity. |
| Catalytic activity | Carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine. HAMAP MF_02102 |
| Pathway | Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from N-carbamoylputrescine (transferase route): step 1/1. HAMAP MF_02102 |
| Subunit structure | Homotrimer By similarity. |
| Subcellular location | Cytoplasm Probable. |
| Sequence similarities | Belongs to the ATCase/OTCase family. PTCase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Polyamine biosynthesis |
| Cellular component | Cytoplasm |
| Molecular function | Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro putrescine biosynthetic process from arginine via N-carbamoylputrescineInferred from electronic annotation. Source: HAMAP |
| Cellular component | ornithine carbamoyltransferase complex Inferred from electronic annotation. Source: InterPro |
| Molecular function | amino acid binding Inferred from electronic annotation. Source: InterPro ornithine carbamoyltransferase activityInferred from electronic annotation. Source: InterPro putrescine 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 – 341 | 341 | Putrescine carbamoyltransferase HAMAP MF_02102 | PRO_0000112946 | |||||
Regions | |||||||||
| Region | 54 – 58 | 5 | Carbamoyl phosphate binding By similarity | ||||||
| Region | 271 – 274 | 4 | Putrescine binding By similarity | ||||||
Sites | |||||||||
| Binding site | 105 | 1 | Carbamoyl phosphate By similarity | ||||||
| Binding site | 132 | 1 | Carbamoyl phosphate By similarity | ||||||
| Site | 29 | 1 | Important for structural integrity By similarity | ||||||
| Site | 145 | 1 | Important for structural integrity By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. Cossart P.Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e / Serovar 1/2a. |
| [2] | "Retrieving sequences of enzymes experimentally characterized but erroneously annotated: the case of the putrescine carbamoyltransferase." Naumoff D.G., Xu Y., Glansdorff N., Labedan B. BMC Genomics 5:52-52(2004) [PubMed: 15287962] [Abstract] Cited for: REANNOTATION AS A PTCASE. |
| [3] | "The difficulty of annotating genes: the case of putrescine carbamoyltransferase." Naumoff D.G., Xu Y., Stalon V., Glansdorff N., Labedan B. Microbiology 150:3908-3911(2004) [PubMed: 15583144] [Abstract] Cited for: GENE NAME. |
Cross-references
Sequence databases | |
|---|---|
| AL591973 Genomic DNA. Translation: CAC98251.1. | |
| PIR | AE1079. |
| RefSeq | NP_463569.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1A1S based on UniProtKB Q51742. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 985152. |
| GenomeReviews | Gene locus lmo0036 in contig AL591824_GR. |
| KEGG | lmo:lmo0036. |
Organism-specific databases | |
| ListiList | LMO00036. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8YAS7. |
| OMA | LGGHAQY. |
Enzyme and pathway databases | |
| BioCyc | LMON169963:LMO0036-MON. |
| BRENDA | 2.1.3.3. 96770. |
Family and domain databases | |
| HAMAP | MF_02102. [Tree] |
| InterPro | IPR006132. Asp/Orn_carbamoyltranf_P_bd. IPR006130. Asp/Orn_carbamoylTrfase. IPR006131. Asp_carbamoyltransf_Asp/Orn_bd. IPR002292. Orn_carbamltrans. [Graphical view] |
| Pfam | PF00185. OTCace. 1 hit. PF02729. OTCace_N. 1 hit. [Graphical view] |
| PRINTS | PR00100. AOTCASE. PR00102. OTCASE. |
| TIGRFAMs | TIGR00658. orni_carb_tr. 1 hit. |
| PROSITE | PS00097. CARBAMOYLTRANSFERASE. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PTC_LISMO | ||||||||
| Accession | Primary (citable) accession number: Q8YAS7 | ||||||||
| 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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