F4GCB3 (F4GCB3_ALIDK) Unreviewed, UniProtKB/TrEMBL
Last modified
April 3, 2013.
Version 15.
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: Dihydroorotate dehydrogenase (quinone) HAMAP-Rule MF_00225 EC=1.3.5.2 HAMAP-Rule MF_00225 | ||||
| Gene names |
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| Organism | Alicycliphilus denitrificans (strain DSM 14773 / CIP 107495 / K601) [Complete proteome] [HAMAP] EMBL AEB84772.1 | ||||
| Taxonomic identifier | 596154 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Alicycliphilus › ![]() |
Protein attributes
| Sequence length | 348 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor By similarity. HAMAP-Rule MF_00225 SAAS SAAS012135 |
| Catalytic activity | (S)-dihydroorotate + a quinone = orotate + a quinol. HAMAP-Rule MF_00225 SAAS SAAS012135 |
| Cofactor | Binds 1 FMN per subunit By similarity. HAMAP-Rule MF_00225 SAAS SAAS012135 |
| Pathway | Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. HAMAP-Rule MF_00225 SAAS SAAS012135 |
| Subunit structure | Monomer By similarity. HAMAP-Rule MF_00225 SAAS SAAS012135 |
| Subcellular location | Cell membrane; Peripheral membrane protein By similarity HAMAP-Rule MF_00225. |
| Sequence similarities | Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily. HAMAP-Rule MF_00225 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyrimidine biosynthesis HAMAP-Rule MF_00225 SAAS SAAS012135 |
| Cellular component | Cell membrane HAMAP-Rule MF_00225 Membrane |
| Ligand | FMN HAMAP-Rule MF_00225 SAAS SAAS012135 Flavoprotein HAMAP-Rule MF_00225 SAAS SAAS012135 |
| Molecular function | Oxidoreductase HAMAP-Rule MF_00225 SAAS SAAS012135 EMBL AEB84772.1 |
| 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 |
| Cellular_component | plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | dihydroorotate oxidase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Nucleotide binding | 65 – 69 | 5 | FMN By similarity HAMAP-Rule MF_00225 | ||||||
| Nucleotide binding | 326 – 327 | 2 | FMN By similarity HAMAP-Rule MF_00225 | ||||||
| Region | 114 – 118 | 5 | Substrate binding By similarity HAMAP-Rule MF_00225 | ||||||
| Region | 254 – 255 | 2 | Substrate binding By similarity HAMAP-Rule MF_00225 | ||||||
Sites | |||||||||
| Active site | 183 | 1 | Nucleophile By similarity HAMAP-Rule MF_00225 | ||||||
| Binding site | 69 | 1 | Substrate By similarity HAMAP-Rule MF_00225 | ||||||
| Binding site | 89 | 1 | FMN; via amide nitrogen By similarity HAMAP-Rule MF_00225 | ||||||
| Binding site | 147 | 1 | FMN By similarity HAMAP-Rule MF_00225 | ||||||
| Binding site | 180 | 1 | FMN By similarity HAMAP-Rule MF_00225 | ||||||
| Binding site | 180 | 1 | Substrate By similarity HAMAP-Rule MF_00225 | ||||||
| Binding site | 185 | 1 | Substrate By similarity HAMAP-Rule MF_00225 | ||||||
| Binding site | 225 | 1 | FMN By similarity HAMAP-Rule MF_00225 | ||||||
| Binding site | 253 | 1 | FMN; via carbonyl oxygen By similarity HAMAP-Rule MF_00225 | ||||||
| Binding site | 276 | 1 | FMN; via amide nitrogen By similarity HAMAP-Rule MF_00225 | ||||||
| Binding site | 305 | 1 | FMN; via amide nitrogen By similarity HAMAP-Rule MF_00225 | ||||||
Sequences
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References
| [1] | "Complete sequence of chromosome of Alicycliphilus denitrificans K601." US DOE Joint Genome Institute Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Oosterkamp M. Woyke T.Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 14773 / CIP 107495 / K601. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP002657 Genomic DNA. Translation: AEB84772.1. |
| RefSeq | YP_004388288.1. NC_015422.1. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AEB84772; AEB84772; Alide2_2408. |
| GeneID | 10483455. |
| KEGG | adk:Alide2_2408. |
| PATRIC | 54527494. VBIAliDen79014_2432. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| KO | K00226. |
Enzyme and pathway databases | |
| BioCyc | ADEN596154:GHU6-2528-MONOMER. |
| UniPathway | UPA00070; UER00946. |
Family and domain databases | |
| Gene3D | 3.20.20.70. 1 hit. |
| HAMAP | MF_00225. DHO_dh_type2. |
| InterPro | IPR013785. Aldolase_TIM. IPR012135. Dihydroorotate_DH_1_2. IPR005719. Dihydroorotate_DH_2. IPR001295. Dihydroorotate_DH_CS. [Graphical view] |
| Pfam | PF01180. DHO_dh. 1 hit. [Graphical view] |
| PIRSF | PIRSF000164. DHO_oxidase. 1 hit. |
| TIGRFAMs | TIGR01036. pyrD_sub2. 1 hit. |
| PROSITE | PS00911. DHODEHASE_1. 1 hit. PS00912. DHODEHASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | F4GCB3_ALIDK | ||||||||
| Accession | Primary (citable) accession number: F4GCB3 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
