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Protein

Dihydrofolate reductase

Gene

DHFR

Organism
Heliothis virescens (Tobacco budworm moth)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).By similarity

Catalytic activityi

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

Enzyme regulationi

Activated by dithiothreitol and p-chloromercuribenzoate. Inhibited by trimethoprim, methotrexate, sodium tetrathionate and hydroxymercuribenzoate.1 Publication

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)DescriptionActionsGraphical viewLength
Binding sitei11NADP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei71SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi17 – 23NADPBy similarity7
Nucleotide bindingi55 – 57NADPBy similarity3
Nucleotide bindingi77 – 79NADPBy similarity3
Nucleotide bindingi117 – 124NADPBy similarity8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processOne-carbon metabolism
LigandNADP

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase (EC:1.5.1.3)
Gene namesi
Name:DHFR
OrganismiHeliothis virescens (Tobacco budworm moth)Imported
Taxonomic identifieri7102 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaLepidopteraGlossataDitrysiaNoctuoideaNoctuidaeHeliothinaeHeliothis

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001863711 – 185Dihydrofolate reductaseAdd BLAST185

Proteomic databases

PRIDEiQ9U8B8

Structurei

3D structure databases

ProteinModelPortaliQ9U8B8
SMRiQ9U8B8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 184DHFRPROSITE-ProRule annotationAdd BLAST180

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni31 – 36Substrate bindingBy similarity6

Sequence similaritiesi

Belongs to the dihydrofolate reductase family.Curated

Family and domain databases

CDDicd00209 DHFR, 1 hit
Gene3Di3.40.430.10, 1 hit
InterProiView protein in InterPro
IPR012259 DHFR
IPR024072 DHFR-like_dom_sf
IPR017925 DHFR_CS
IPR001796 DHFR_dom
PANTHERiPTHR22778:SF16 PTHR22778:SF16, 1 hit
PfamiView protein in Pfam
PF00186 DHFR_1, 1 hit
SUPFAMiSSF53597 SSF53597, 1 hit
PROSITEiView protein in PROSITE
PS00075 DHFR_1, 1 hit
PS51330 DHFR_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q9U8B8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQVKLNLIA AACDNMGIGV NGALPWRLKK EMAYFTTMTS KVSEPTKVNA
60 70 80 90 100
VIMGRRTWDC IPDKYRPLQD RVNIVLTHNV DSVKENVPEG VMVFPGLDEA
110 120 130 140 150
IKYIEGREDI ESTWVIGGSS IYRAAMTHPN CGKIYLTEIQ KSFDCDTFFP
160 170 180
NIDKQQFHLV DEEQIPGEKQ VEGNISYYFR VYKKL
Length:185
Mass (Da):21,089
Last modified:May 1, 2000 - v1
Checksum:i9B8C0E50ED175812
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5K → L AA sequence (PubMed:10632709).Curated1
Sequence conflicti7N → D AA sequence (PubMed:10632709).Curated1
Sequence conflicti11 – 13AAC → IFD AA sequence (PubMed:10632709).Curated3
Sequence conflicti15N → D AA sequence (PubMed:10632709).Curated1
Sequence conflicti21N → D AA sequence (PubMed:10632709).Curated1
Sequence conflicti158H → Q AA sequence (PubMed:10632709).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF104106 mRNA Translation: AAF04459.1

Similar proteinsi

Entry informationi

Entry nameiDYR_HELVI
AccessioniPrimary (citable) accession number: Q9U8B8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: May 1, 2000
Last modified: May 23, 2018
This is version 74 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

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

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