Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dihydrofolate reductase

Gene

folA

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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.

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 (dfrA), Dihydrofolate reductase type 1 from Tn4003 (dfrA), Dihydrofolate reductase (dfrA), Dihydrofolate reductase (dfrA), Dihydrofolate reductase (dfrA), Dihydrofolate reductase (dfrK), Dihydrofolate reductase (RK97_06330), Dihydrofolate reductase (folA), Dihydrofolate reductase (dfrA), Dihydrofolate reductase (dfrK), Dihydrofolate reductase (dfrA), Dihydrofolate reductase (dfrK), 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

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NADP

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

Protein-protein interaction databases

STRINGi93062.SACOL1461.

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[»]
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
Contains 1 DHFR (dihydrofolate reductase) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108YYV. Bacteria.
COG0262. LUCA.

Family and domain databases

CDDicd00209. DHFR. 1 hit.
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]
PIRSFiPIRSF000194. DHFR. 1 hit.
PRINTSiPR00070. DHFR.
SUPFAMiSSF53597. SSF53597. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]

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_MCFM01000014.1.

Genome annotation databases

GeneIDi28380994.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z16422 Genomic DNA. Translation: CAA78910.1.
PIRiS32014.
RefSeqiWP_000175746.1. NZ_MCFM01000014.1.

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[»]
ProteinModelPortaliP0A017.
SMRiP0A017.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL1461.

Chemistry databases

BindingDBiP0A017.
ChEMBLiCHEMBL1681620.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi28380994.

Phylogenomic databases

eggNOGiENOG4108YYV. Bacteria.
COG0262. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.
BRENDAi1.5.1.3. 3352.

Miscellaneous databases

EvolutionaryTraceiP0A017.
PROiP0A017.

Family and domain databases

CDDicd00209. DHFR. 1 hit.
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]
PIRSFiPIRSF000194. DHFR. 1 hit.
PRINTSiPR00070. DHFR.
SUPFAMiSSF53597. SSF53597. 1 hit.
PROSITEiPS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDYR_STAAU
AccessioniPrimary (citable) accession number: P0A017
Secondary accession number(s): P10167
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.