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P00378

- DYR_CHICK

UniProt

P00378 - DYR_CHICK

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Protein

Dihydrofolate reductase

Gene

DHFR

Organism
Gallus gallus (Chicken)
Status
Reviewed - 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

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

PTM / Processingi

Molecule processing

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

Proteomic databases

PaxDbiP00378.

Interactioni

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 binding

Sequence similaritiesi

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

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

        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

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 107 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