SubmitCancel

Skip Header

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

P00378

- DYR_CHICK

UniProt

P00378 - DYR_CHICK

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Dihydrofolate reductase
Gene
DHFR
Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 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.

Pathwayi

Sites

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

Regions

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

GO - Molecular functioni

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

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
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 189189Dihydrofolate reductase
PRO_0000186367Add
BLAST

Proteomic databases

PaxDbiP00378.

Interactioni

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP00378.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 184182DHFR
Add
BLAST

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0262.
HOVERGENiHBG000773.
InParanoidiP00378.

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.

P00378-1 [UniParc]FASTAAdd to Basket

« Hide

VRSLNSIVAV CQNMGIGKDG NLPWPPLRNE YKYFQRMTST SHVEGKQNAV    50
IMGKKTWFSI PEKNRPLKDR INIVLSRELK EAPKGAHYLS KSLDDALALL 100
DSPELKSKVD MVWIVGGTAV YKAAMEKPIN HRLFVTRILH EFESDTFFPE 150
IDYKDFKLLT EYPGVPADIQ EEDGIQYKFE VYQKSVLAQ 189
Length:189
Mass (Da):21,650
Last modified:July 21, 1986 - v1
Checksum:iBC5F50C94BCA3EDA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411E → Q AA sequence 1 Publication

Sequence databases

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

Cross-referencesi

Sequence databases

PIRi A00390. RDCHD.
UniGenei Gga.2883.
Gga.48831.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DR1 X-ray 2.20 A 1-189 [» ]
1DR2 X-ray 2.30 A 1-189 [» ]
1DR3 X-ray 2.30 A 1-189 [» ]
1DR4 X-ray 2.40 A 1-189 [» ]
1DR5 X-ray 2.40 A 1-189 [» ]
1DR6 X-ray 2.40 A 1-189 [» ]
1DR7 X-ray 2.40 A 1-189 [» ]
8DFR X-ray 1.70 A 1-189 [» ]
ProteinModelPortali P00378.
SMRi P00378. Positions 1-186.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P00378.
ChEMBLi CHEMBL2575.

Proteomic databases

PaxDbi P00378.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0262.
HOVERGENi HBG000773.
InParanoidi P00378.

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00158 .

Miscellaneous databases

EvolutionaryTracei P00378.
PROi P00378.

Family and domain databases

Gene3Di 3.40.430.10. 1 hit.
InterProi IPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view ]
Pfami PF00186. DHFR_1. 1 hit.
[Graphical view ]
PRINTSi PR00070. DHFR.
SUPFAMi SSF53597. SSF53597. 1 hit.
PROSITEi PS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Primary structure of chicken liver dihydrofolate reductase."
    Kumar A.A., Blankenship D.T., Kaufman B.T., Freisheim J.H.
    Biochemistry 19:667-678(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "Activation of chicken liver dihydrofolate reductase by urea and guanidine hydrochloride is accompanied by conformational change at the active site."
    Fan Y.X., Ju M., Zhou J.M., Tsou C.L.
    Biochem. J. 315:97-102(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-22; 138-141 AND 158-161.
  3. "Crystal structure of chicken liver dihydrofolate reductase complexed with NADP+ and biopterin."
    McTigue M.A., Davies J.F. II, Kaufman B.T., Kraut J.
    Biochemistry 31:7264-7273(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH NADPH AND DIHYDROBIOPTERIN.

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: January 22, 2014
This is version 105 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

External Data

Dasty 3

Similar proteinsi