A7GRK9 (PYRDB_BACCN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 42.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit Short name=DHOD B Short name=DHODase B Short name=DHOdehase B EC=1.3.1.14 Alternative name(s): Dihydrdoorotate oxidase B Orotate reductase (NADH) | ||||
| Gene names |
| ||||
| Organism | Bacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 315749 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 309 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the conversion of dihydroorotate to orotate with NAD+ as electron acceptor By similarity. HAMAP MF_00224 |
| Catalytic activity | (S)-dihydroorotate + NAD+ = orotate + NADH. HAMAP MF_00224 |
| Cofactor | Binds 1 FMN per subunit By similarity. HAMAP MF_00224 |
| Pathway | Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1. HAMAP MF_00224 |
| Subunit structure | Heterotetramer of 2 PyrK and 2 PyrD type B subunits By similarity. |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00224. |
| Sequence similarities | Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyrimidine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | FMN Flavoprotein NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | 'de novo' pyrimidine base biosynthetic process Inferred from electronic annotation. Source: InterPro UMP biosynthetic processInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | dihydroorotate oxidase activity Inferred from electronic annotation. Source: InterPro orotate reductase (NADH) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 309 | 309 | Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit HAMAP MF_00224 | PRO_1000078152 | |||||
Regions | |||||||||
| Nucleotide binding | 45 – 46 | 2 | FMN By similarity | ||||||
| Nucleotide binding | 243 – 244 | 2 | FMN By similarity | ||||||
| Nucleotide binding | 265 – 266 | 2 | FMN By similarity | ||||||
| Region | 69 – 73 | 5 | Substrate binding By similarity | ||||||
| Region | 192 – 193 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 130 | 1 | Nucleophile | ||||||
| Binding site | 21 | 1 | FMN By similarity | ||||||
| Binding site | 45 | 1 | Substrate By similarity | ||||||
| Binding site | 99 | 1 | FMN By similarity | ||||||
| Binding site | 127 | 1 | FMN By similarity | ||||||
| Binding site | 127 | 1 | Substrate By similarity | ||||||
| Binding site | 165 | 1 | FMN By similarity | ||||||
| Binding site | 191 | 1 | FMN; via carbonyl oxygen By similarity | ||||||
| Binding site | 217 | 1 | FMN; via amide nitrogen By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity." Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A. Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NVH 391-98. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000764 Genomic DNA. Translation: ABS22767.1. |
| RefSeq | YP_001375762.1. NC_009674.1. |
3D structure databases | |
| ProteinModelPortal | A7GRK9. |
| SMR | A7GRK9. Positions 2-288. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A7GRK9. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000037183; EBBACP00000036234; EBBACG00000037174. |
| GeneID | 5343666. |
| GenomeReviews | Gene locus Bcer98_2533 in contig CP000764_GR. |
| KEGG | bcy:Bcer98_2533. |
| PATRIC | 18933664. VBIBacCyt128034_2676. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0167. |
| GeneTree | EBGT00050000001544. |
| HOGENOM | HBG472415. |
| OMA | VALRMVW. |
| ProtClustDB | PRK07259. |
Enzyme and pathway databases | |
| BioCyc | BCER315749:BCER98_2533-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00224. DHO_dh_type1. [Tree] |
| InterPro | IPR013785. Aldolase_TIM. IPR005720. Dihydroorotate_DH. IPR024920. Dihydroorotate_DH_1. IPR012135. Dihydroorotate_DH_1_2. IPR001295. Dihydroorotate_DH_CS. [Graphical view] |
| Gene3D | G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. |
| KO | K00226. |
| Pfam | PF01180. DHO_dh. 1 hit. [Graphical view] |
| PIRSF | PIRSF000164. DHO_oxidase. 1 hit. |
| TIGRFAMs | TIGR01037. PyrD_sub1_fam. 1 hit. |
| PROSITE | PS00911. DHODEHASE_1. 1 hit. PS00912. DHODEHASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PYRDB_BACCN | ||||||||
| Accession | Primary (citable) accession number: A7GRK9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with