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Protein

Dihydrofolate reductase

Gene

DHFR

Organism
Gallus gallus (Chicken)
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. May bind to mRNA.

Catalytic activityi

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

Pathwayi: tetrahydrofolate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate.
Proteins known to be involved in this subpathway in this organism are:
  1. Dihydrofolate reductase (DHFR)
This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91NADP; via amide nitrogen and carbonyl oxygenCombined sources1 Publication
Binding sitei64 – 641SubstrateBy similarity
Binding sitei70 – 701Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 217NADP1 Publication
Nucleotide bindingi54 – 563NADPCombined sources1 Publication
Nucleotide bindingi76 – 783NADPCombined sources1 Publication
Nucleotide bindingi116 – 1238NADP1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Methotrexate resistance, One-carbon metabolism

Keywords - Ligandi

NADP, RNA-binding

Enzyme and pathway databases

BRENDAi1.5.1.3. 1306.
SABIO-RKP00378.
UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase (EC:1.5.1.3)
Gene namesi
Name:DHFR
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2575.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 189189Dihydrofolate reductasePRO_0000186367Add
BLAST

Proteomic databases

PaxDbiP00378.

Interactioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000025076.

Chemistry

BindingDBiP00378.

Structurei

Secondary structure

1
189
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Beta strandi15 – 184Combined sources
Beta strandi23 – 253Combined sources
Helixi28 – 3912Combined sources
Beta strandi47 – 537Combined sources
Helixi54 – 596Combined sources
Helixi62 – 643Combined sources
Beta strandi70 – 756Combined sources
Beta strandi87 – 926Combined sources
Helixi93 – 1019Combined sources
Helixi103 – 1064Combined sources
Beta strandi109 – 1146Combined sources
Helixi118 – 1269Combined sources
Beta strandi127 – 14014Combined sources
Beta strandi145 – 1473Combined sources
Turni153 – 1553Combined sources
Beta strandi156 – 1583Combined sources
Beta strandi170 – 1723Combined sources
Beta strandi175 – 18410Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DR1X-ray2.20A1-189[»]
1DR2X-ray2.30A1-189[»]
1DR3X-ray2.30A1-189[»]
1DR4X-ray2.40A1-189[»]
1DR5X-ray2.40A1-189[»]
1DR6X-ray2.40A1-189[»]
1DR7X-ray2.40A1-189[»]
8DFRX-ray1.70A1-189[»]
ProteinModelPortaliP00378.
SMRiP00378. Positions 1-186.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00378.

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 binding1 Publication

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1324. Eukaryota.
COG0262. LUCA.
HOVERGENiHBG000773.
InParanoidiP00378.

Family and domain databases

CDDicd00209. DHFR. 1 hit.
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.

P00378-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
VRSLNSIVAV CQNMGIGKDG NLPWPPLRNE YKYFQRMTST SHVEGKQNAV
60 70 80 90 100
IMGKKTWFSI PEKNRPLKDR INIVLSRELK EAPKGAHYLS KSLDDALALL
110 120 130 140 150
DSPELKSKVD MVWIVGGTAV YKAAMEKPIN HRLFVTRILH EFESDTFFPE
160 170 180
IDYKDFKLLT EYPGVPADIQ EEDGIQYKFE VYQKSVLAQ
Length:189
Mass (Da):21,650
Last modified:July 21, 1986 - v1
Checksum:iBC5F50C94BCA3EDA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411E → Q AA sequence (PubMed:8670138).Curated

Sequence databases

PIRiA00390. RDCHD.
UniGeneiGga.2883.
Gga.48831.

Cross-referencesi

Sequence databases

PIRiA00390. RDCHD.
UniGeneiGga.2883.
Gga.48831.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DR1X-ray2.20A1-189[»]
1DR2X-ray2.30A1-189[»]
1DR3X-ray2.30A1-189[»]
1DR4X-ray2.40A1-189[»]
1DR5X-ray2.40A1-189[»]
1DR6X-ray2.40A1-189[»]
1DR7X-ray2.40A1-189[»]
8DFRX-ray1.70A1-189[»]
ProteinModelPortaliP00378.
SMRiP00378. Positions 1-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000025076.

Chemistry

BindingDBiP00378.
ChEMBLiCHEMBL2575.

Proteomic databases

PaxDbiP00378.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1324. Eukaryota.
COG0262. LUCA.
HOVERGENiHBG000773.
InParanoidiP00378.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.
BRENDAi1.5.1.3. 1306.
SABIO-RKP00378.

Miscellaneous databases

EvolutionaryTraceiP00378.
PROiP00378.

Family and domain databases

CDDicd00209. DHFR. 1 hit.
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...

Entry informationi

Entry nameiDYR_CHICK
AccessioniPrimary (citable) accession number: P00378
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 7, 2016
This is version 118 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.