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Protein

Dihydrofolate reductase type 8

Gene

dhfrVIII

Organism
Shigella sonnei
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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

Miscellaneous

Confers high-level trimethoprim resistance.

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 (dfrA12), Dihydrofolate reductase (CI641_25660), Dihydrofolate reductase (CI641_06920), Dihydrofolate reductase (folA), Dihydrofolate reductase type 8 (dhfrVIII)
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.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processAntibiotic resistance, Methotrexate resistance, One-carbon metabolism, Trimethoprim resistance
LigandNADP

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase type 8 (EC:1.5.1.3)
Alternative name(s):
DHFR type IIIC
Dihydrofolate reductase type VIII
Gene namesi
Name:dhfrVIII
Synonyms:dhfrIIIc
Encoded oniPlasmid pBH7000 Publication
OrganismiShigella sonnei
Taxonomic identifieri624 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001864261 – 169Dihydrofolate reductase type 8Add BLAST169

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP0ABQ8
SMRiP0ABQ8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 169DHFRPROSITE-ProRule annotationAdd BLAST167

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.

P0ABQ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIELHAILAA TANGCIGKDN ALPWPPLKGD LARFKKLTMG KVVIMGRKTY
60 70 80 90 100
ESLPVKLEGR TCIVMTRQAL ELPGVRDANG AIFVNNVSDA MRFAQEESVG
110 120 130 140 150
DVAYVIGGAE IFKRLALMIT QIELTFVKRL YEGDTYVDLA EMVKDYEQNG
160
MEEHDLHTYF TYRKKELTE
Length:169
Mass (Da):19,021
Last modified:November 8, 2005 - v1
Checksum:i76E1ABA0C0DE30CC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09273 Genomic DNA Translation: AAA79232.1
RefSeqiWP_000571065.1, NZ_LXVF01000360.1

Entry informationi

Entry nameiDYR8_SHISO
AccessioniPrimary (citable) accession number: P0ABQ8
Secondary accession number(s): Q57452
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: March 28, 2018
This is version 52 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Plasmid

Documents

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

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