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Protein

Dihydrofolate reductase

Gene

folA

Organism
Staphylococcus aureus
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.

Miscellaneous

There are two DhfR isozymes in S.aureus, this one is chromosomal and is sensitive to trimethoprim.

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 (dfrA), Dihydrofolate reductase (dhfrXII), Dihydrofolate reductase (dfrK), Dihydrofolate reductase (dfrA), Dihydrofolate reductase type 1 from Tn4003 (dfrA), Dihydrofolate reductase (dfrA), Dihydrofolate reductase (dfrA), Dihydrofolate reductase (dfrK), Dihydrofolate reductase (folA), Dihydrofolate reductase (BSZ10_04505), Dihydrofolate reductase (dfrK), Dihydrofolate reductase (dfrK), Dihydrofolate reductase (dfrA_1), Dihydrofolate reductase (dfrA), Dihydrofolate reductase (dfrA), Dihydrofolate reductase (dfrA), Dihydrofolate reductase (dfrG)
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 sitei28Substrate1 Publication1
Binding sitei50Substrate1 Publication1
Binding sitei58Substrate1 Publication1
Binding sitei93Substrate; via carbonyl oxygen1 Publication1
Binding sitei101NADP1 Publication1
Binding sitei122NADP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi7 – 8NADP1 Publication2
Nucleotide bindingi15 – 20NADP1 Publication6
Nucleotide bindingi44 – 47NADP1 Publication4
Nucleotide bindingi63 – 66NADP1 Publication4
Nucleotide bindingi93 – 98NADP1 Publication6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processOne-carbon metabolism
LigandNADP

Enzyme and pathway databases

BRENDAi1.5.1.3 3352
UniPathwayiUPA00077; UER00158

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase (EC:1.5.1.3)
Short name:
DHFR
Gene namesi
Name:folA
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1681620

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001864112 – 159Dihydrofolate reductaseAdd BLAST158

Interactioni

Chemistry databases

BindingDBiP0A017

Structurei

Secondary structure

1159
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 10Combined sources8
Beta strandi14 – 17Combined sources4
Helixi26 – 36Combined sources11
Beta strandi39 – 44Combined sources6
Helixi45 – 51Combined sources7
Beta strandi58 – 63Combined sources6
Beta strandi75 – 77Combined sources3
Helixi80 – 85Combined sources6
Beta strandi90 – 94Combined sources5
Helixi96 – 102Combined sources7
Turni103 – 105Combined sources3
Beta strandi107 – 114Combined sources8
Beta strandi121 – 123Combined sources3
Turni129 – 131Combined sources3
Beta strandi132 – 139Combined sources8
Beta strandi150 – 157Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2W9GX-ray1.95A1-159[»]
2W9HX-ray1.48A1-159[»]
3FRAX-ray2.35X2-159[»]
3FRBX-ray2.00X2-159[»]
3FRDX-ray2.10X2-159[»]
3FREX-ray2.20X2-159[»]
3FRFX-ray2.20X2-159[»]
3FY8X-ray2.20X2-159[»]
3FY9X-ray2.25X2-159[»]
3FYVX-ray2.20X2-159[»]
3FYWX-ray2.10X2-159[»]
3I8AX-ray2.41X2-158[»]
3LG4X-ray3.15A/B1-158[»]
3M08X-ray2.01A2-158[»]
3M09X-ray2.01A2-158[»]
3SGYX-ray2.60A/B2-158[»]
3SH2X-ray3.00A/B2-158[»]
3SQYX-ray1.50X1-159[»]
3SR5X-ray1.68X2-159[»]
3SRQX-ray1.69X1-159[»]
3SRRX-ray1.70X1-159[»]
3SRSX-ray1.70X1-159[»]
3SRUX-ray1.70X1-159[»]
3SRWX-ray1.70X1-159[»]
4FGGX-ray2.30A1-159[»]
4FGHX-ray2.50A1-159[»]
4LAEX-ray1.69X1-159[»]
4LAGX-ray1.70X1-159[»]
4LAHX-ray1.88X1-159[»]
4LEKX-ray1.70X1-159[»]
4XE6X-ray2.69X1-157[»]
4XECX-ray2.69X2-158[»]
5HF0X-ray2.25X2-158[»]
5HF2X-ray1.81X2-158[»]
5ISPX-ray1.84X2-158[»]
5ISQX-ray1.90X2-158[»]
5ISTX-ray1.72X2-158[»]
5JG0X-ray1.88X2-158[»]
ProteinModelPortaliP0A017
SMRiP0A017
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A017

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 157DHFRPROSITE-ProRule annotationAdd BLAST156

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni6 – 7Substrate binding1 Publication2

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A017-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLSILVAHD LQRVIGFENQ LPWHLPNDLK HVKKLSTGHT LVMGRKTFES
60 70 80 90 100
IGKPLPNRRN VVLTSDTSFN VEGVDVIHSI EDIYQLPGHV FIFGGQTLFE
110 120 130 140 150
EMIDKVDDMY ITVIEGKFRG DTFFPPYTFE DWEVASSVEG KLDEKNTIPH

TFLHLIRKK
Length:159
Mass (Da):18,251
Last modified:January 23, 2007 - v2
Checksum:i811898409FEAFAAB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z16422 Genomic DNA Translation: CAA78910.1
PIRiS32014
RefSeqiWP_000175746.1, NZ_PQWV01000003.1

Similar proteinsi

Entry informationi

Entry nameiDYR_STAAU
AccessioniPrimary (citable) accession number: P0A017
Secondary accession number(s): P10167
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 89 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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

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