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Protein

Dihydrofolate reductase

Gene

folA

Organism
Neisseria gonorrhoeae
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

Miscellaneous

Strain T47/F62 is trimethoprim resistant by overproduction of DHFR.

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 (folA), Dihydrofolate reductase (folA), Dihydrofolate reductase (folA), Dihydrofolate reductase (folA), Dihydrofolate reductase (folA), Dihydrofolate reductase (folA)
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 sitei29SubstrateBy similarity1
Binding sitei60SubstrateBy similarity1
Binding sitei117SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi8 – 9NADPBy similarity2
Nucleotide bindingi16 – 21NADPBy similarity6
Nucleotide bindingi45 – 48NADPBy similarity4
Nucleotide bindingi65 – 68NADPBy similarity4
Nucleotide bindingi98 – 103NADPBy similarity6

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase (EC:1.5.1.3)
Gene namesi
Name:folA
OrganismiNeisseria gonorrhoeae
Taxonomic identifieri485 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3565

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001864011 – 162Dihydrofolate reductaseAdd BLAST162

Interactioni

Chemistry databases

BindingDBiP04174

Structurei

3D structure databases

ProteinModelPortaliP04174
SMRiP04174
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 161DHFRPROSITE-ProRule annotationAdd BLAST159

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni7 – 9Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the dihydrofolate reductase family.Curated

Phylogenomic databases

eggNOGiENOG4108YYV Bacteria
COG0262 LUCA

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
PIRSFiPIRSF000194 DHFR, 1 hit
SUPFAMiSSF53597 SSF53597, 1 hit
PROSITEiView protein in PROSITE
PS00075 DHFR_1, 1 hit
PS51330 DHFR_2, 1 hit

Sequencei

Sequence statusi: Complete.

P04174-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKITIIAAC AENLCIGAGN AMPWHIPEDF AFFKVYTLGK PVIMGRKTWE
60 70 80 90 100
SLPVKPLPGR RNIVISRQAD YCAAGAETVA SLEVALALCA GAEEAVIMGG
110 120 130 140 150
AQIYGQAMPL ATDLRITEVD LSVEGDAFFP EIDRTHWREA ERTERRVSSK
160
GVAYTFVHYL GK
Length:162
Mass (Da):17,731
Last modified:March 20, 1987 - v1
Checksum:iA23BA94E6764E564
GO

Sequence databases

PIRiA00393 RDNHD

Similar proteinsi

Entry informationi

Entry nameiDYR_NEIGO
AccessioniPrimary (citable) accession number: P04174
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: March 28, 2018
This is version 82 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

Direct protein sequencing
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Main funding by: National Institutes of Health