P00377 (DYR_PIG) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 68.
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: Dihydrofolate reductase EC=1.5.1.3 | ||
| Gene names |
| ||
| Organism | Sus scrofa (Pig) [Complete proteome] | ||
| Taxonomic identifier | 9823 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Protein attributes
| Sequence length | 186 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFRL1 By similarity. |
| Catalytic activity | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH. |
| Pathway | |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the dihydrofolate reductase family. Contains 1 DHFR (dihydrofolate reductase) domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 186 | 186 | Dihydrofolate reductase | PRO_0000186365 | |||||
Regions | |||||||||
| Domain | 3 – 184 | 182 | DHFR | ||||||
| Nucleotide binding | 15 – 21 | 7 | NADP By similarity | ||||||
| Nucleotide binding | 54 – 56 | 3 | NADP By similarity | ||||||
| Nucleotide binding | 76 – 78 | 3 | NADP By similarity | ||||||
| Nucleotide binding | 116 – 123 | 8 | NADP By similarity | ||||||
| Region | 30 – 35 | 6 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 9 | 1 | NADP; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 70 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 162 | 1 | Cysteine derivative; partial | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Porcine liver dihydrofolate reductase. Purification, properties, and amino acid sequence." Smith S.L., Patrick P., Stone D., Phillips A.W., Burchall J.J. J. Biol. Chem. 254:11475-11484(1979) [PubMed: 500653] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| PIR | RDPGD. A00389. |
3D structure databases | |
| ProteinModelPortal | P00377. |
| SMR | P00377. Positions 1-186. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P00377. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| GeneTree | ENSGT00390000010283. |
| HOVERGEN | HBG000773. |
| OrthoDB | EOG4QJRPF. |
Family and domain databases | |
| InterPro | IPR012259. DHFR. IPR024072. DHFR-like_dom. IPR017925. DHFR_CS. IPR001796. DHFR_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.430.10. G3DSA:3.40.430.10. 1 hit. |
| Pfam | PF00186. DHFR_1. 1 hit. [Graphical view] |
| PRINTS | PR00070. DHFR. |
| SUPFAM | SSF53597. SSF53597. 1 hit. |
| PROSITE | PS00075. DHFR_1. 1 hit. PS51330. DHFR_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DYR_PIG | ||||||||
| Accession | Primary (citable) accession number: P00377 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with