Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dihydrofolate reductase

Gene

DHFR

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91NADP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei70 – 701SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 217NADPBy similarity
Nucleotide bindingi54 – 563NADPBy similarity
Nucleotide bindingi76 – 783NADPBy similarity
Nucleotide bindingi116 – 1238NADPBy similarity

GO - Molecular functioni

  1. dihydrofolate reductase activity Source: UniProtKB
  2. drug binding Source: UniProtKB
  3. mRNA binding Source: UniProtKB
  4. NADP binding Source: InterPro

GO - Biological processi

  1. glycine biosynthetic process Source: InterPro
  2. nucleotide biosynthetic process Source: InterPro
  3. one-carbon metabolic process Source: UniProtKB-KW
  4. response to methotrexate Source: UniProtKB-KW
  5. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
  6. tetrahydrofolate metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Methotrexate resistance, One-carbon metabolism

Keywords - Ligandi

NADP, RNA-binding

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase (EC:1.5.1.3)
Gene namesi
Name:DHFR
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 186186Dihydrofolate reductasePRO_0000186365Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321N6-acetyllysine; alternateBy similarity
Modified residuei32 – 321N6-succinyllysine; alternateBy similarity
Modified residuei162 – 1621Cysteine derivative; partial

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP00377.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000015020.

Structurei

3D structure databases

ProteinModelPortaliP00377.
SMRiP00377. Positions 1-186.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 184182DHFRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 356Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the dihydrofolate reductase family.Curated
Contains 1 DHFR (dihydrofolate reductase) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0262.
HOGENOMiHOG000040235.
HOVERGENiHBG000773.
InParanoidiP00377.

Family and domain databases

Gene3Di3.40.430.10. 1 hit.
InterProiIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamiPF00186. DHFR_1. 1 hit.
[Graphical view]
PRINTSiPR00070. DHFR.
SUPFAMiSSF53597. SSF53597. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00377-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
VRPLNCIVAV SQNMGIGKNG DLPWPPLRNE YKYFQRMTTT SSVEGKQNLV
60 70 80 90 100
IMGRKTWFSI PEKNRPLKDR INIVLSRELK EPPQGAHFLA KSLDDALKLT
110 120 130 140 150
EQPELKDKVD MVWIVGGSSV YKEAMNKPGH IRLFVTRIMK EFESDTFFPE
160 170 180
IDLEKYKLLS ECSGVPSDVQ EEKGIKYKFE VYEKNN
Length:186
Mass (Da):21,455
Last modified:July 21, 1986 - v1
Checksum:iD05DB526FE5C12CE
GO

Sequence databases

PIRiA00389. RDPGD.

Cross-referencesi

Sequence databases

PIRiA00389. RDPGD.

3D structure databases

ProteinModelPortaliP00377.
SMRiP00377. Positions 1-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000015020.

Proteomic databases

PaxDbiP00377.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG0262.
HOGENOMiHOG000040235.
HOVERGENiHBG000773.
InParanoidiP00377.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.

Family and domain databases

Gene3Di3.40.430.10. 1 hit.
InterProiIPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view]
PfamiPF00186. DHFR_1. 1 hit.
[Graphical view]
PRINTSiPR00070. DHFR.
SUPFAMiSSF53597. SSF53597. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Liver.

Entry informationi

Entry nameiDYR_PIG
AccessioniPrimary (citable) accession number: P00377
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 4, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.