C6D525 (C6D525_PAESJ) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 32.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200 EC=4.1.1.23 HAMAP-Rule MF_01200 Alternative name(s): OMP decarboxylase HAMAP-Rule MF_01200 | ||||
| Gene names |
| ||||
| Organism | Paenibacillus sp. (strain JDR-2) [Complete proteome] [HAMAP] EMBL ACT02490.1 | ||||
| Taxonomic identifier | 324057 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Paenibacillaceae › Paenibacillus![]() |
Protein attributes
| Sequence length | 241 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP) By similarity. HAMAP-Rule MF_01200 SAAS SAAS014732 |
| Catalytic activity | Orotidine 5'-phosphate = UMP + CO2. HAMAP-Rule MF_01200 |
| Pathway | Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. HAMAP-Rule MF_01200 |
| Subunit structure | Homodimer By similarity. HAMAP-Rule MF_01200 SAAS SAAS014732 |
| Sequence similarities | Belongs to the OMP decarboxylase family. Type 1 subfamily. HAMAP-Rule MF_01200 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyrimidine biosynthesis HAMAP-Rule MF_01200 |
| Molecular function | Decarboxylase HAMAP-Rule MF_01200 Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | 'de novo' UMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 'de novo' pyrimidine nucleobase biosynthetic processInferred from electronic annotation. Source: InterPro |
| Molecular_function | orotidine-5'-phosphate decarboxylase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Region | 66 – 75 | 10 | Substrate binding By similarity HAMAP-Rule MF_01200 | ||||||
Sites | |||||||||
| Active site | 68 | 1 | Proton donor By similarity HAMAP-Rule MF_01200 | ||||||
| Binding site | 17 | 1 | Substrate By similarity HAMAP-Rule MF_01200 | ||||||
| Binding site | 39 | 1 | Substrate By similarity HAMAP-Rule MF_01200 | ||||||
| Binding site | 129 | 1 | Substrate By similarity HAMAP-Rule MF_01200 | ||||||
| Binding site | 191 | 1 | Substrate By similarity HAMAP-Rule MF_01200 | ||||||
| Binding site | 200 | 1 | Substrate By similarity HAMAP-Rule MF_01200 | ||||||
| Binding site | 220 | 1 | Substrate; via amide nitrogen By similarity HAMAP-Rule MF_01200 | ||||||
| Binding site | 221 | 1 | Substrate By similarity HAMAP-Rule MF_01200 | ||||||
Sequences
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References
| [1] | "Complete genome sequence of Paenibacillus sp. strain JDR-2." Chow V., Nong G., St John F.J., Rice J.D., Dickstein E., Chertkov O., Bruce D., Detter C., Brettin T., Han J., Woyke T., Pitluck S., Nolan M., Pati A., Martin J., Copeland A., Land M.L., Goodwin L. Preston J.F.Stand. Genomic Sci. 6:1-10(2012) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JDR-2. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001656 Genomic DNA. Translation: ACT02490.1. |
| RefSeq | YP_003012576.1. NC_012914.1. |
3D structure databases | |
| ProteinModelPortal | C6D525. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 324057.Pjdr2_3860. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ACT02490; ACT02490; Pjdr2_3860. |
| GeneID | 8126385. |
| KEGG | pjd:Pjdr2_3860. |
| PATRIC | 22838255. VBIPaeSp118865_3841. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0284. |
| HOGENOM | HOG000226071. |
| KO | K01591. |
| OMA | NFKIFLD. |
| ProtClustDB | CLSK2551236. |
Enzyme and pathway databases | |
| BioCyc | PSP324057:GH5H-3953-MONOMER. |
| UniPathway | UPA00070; UER00120. |
Family and domain databases | |
| Gene3D | 3.20.20.70. 1 hit. |
| HAMAP | MF_01200_B. OMPdecase_type1_B. |
| InterPro | IPR013785. Aldolase_TIM. IPR014732. OMPdecase. IPR018089. OMPdecase_AS. IPR001754. OMPdeCOase_dom. IPR011060. RibuloseP-bd_barrel. [Graphical view] |
| Pfam | PF00215. OMPdecase. 1 hit. [Graphical view] |
| SMART | SM00934. OMPdecase. 1 hit. [Graphical view] |
| SUPFAM | SSF51366. RibP_bind_barrel. 1 hit. |
| TIGRFAMs | TIGR01740. pyrF. 1 hit. |
| PROSITE | PS00156. OMPDECASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | C6D525_PAESJ | ||||||||
| Accession | Primary (citable) accession number: C6D525 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
