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Protein

Dihydrofolate reductase

Gene

dhfR

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed-Annotation score: Annotation score: 5 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 (By similarity).By similarity

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 (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 sitei30SubstrateBy similarity1
Binding sitei61SubstrateBy similarity1
Binding sitei83NADP; via amide nitrogenBy similarity1
Binding sitei119SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi9 – 10NADPBy similarity2
Nucleotide bindingi17 – 22NADPBy similarity6
Nucleotide bindingi46 – 49NADPBy similarity4
Nucleotide bindingi66 – 69NADPBy similarity4
Nucleotide bindingi100 – 105NADPBy similarity6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Antibiotic resistance, One-carbon metabolism, Trimethoprim resistance

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.5.1.3. 1960.
UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase (EC:1.5.1.3)
Gene namesi
Name:dhfR
Synonyms:dfr
Ordered Locus Names:SP_1571
OrganismiStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Taxonomic identifieri170187 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000000585 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001864171 – 168Dihydrofolate reductaseAdd BLAST168

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SP_0371Q97SJ04EBI-6473264,EBI-6473258

Protein-protein interaction databases

IntActiQ54801. 1 interactor.
STRINGi170187.SpneT_02000377.

Chemistry databases

BindingDBiQ54801.

Structurei

Secondary structure

1168
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 11Combined sources7
Beta strandi16 – 19Combined sources4
Helixi28 – 38Combined sources11
Beta strandi41 – 46Combined sources6
Helixi47 – 52Combined sources6
Turni53 – 55Combined sources3
Beta strandi62 – 66Combined sources5
Beta strandi75 – 82Combined sources8
Helixi83 – 91Combined sources9
Beta strandi97 – 101Combined sources5
Helixi103 – 109Combined sources7
Helixi110 – 112Combined sources3
Beta strandi114 – 123Combined sources10
Beta strandi128 – 130Combined sources3
Helixi137 – 139Combined sources3
Beta strandi140 – 148Combined sources9
Beta strandi158 – 165Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IX9X-ray1.95A/B1-168[»]
ProteinModelPortaliQ54801.
SMRiQ54801.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ54801.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 165DHFRPROSITE-ProRule annotationAdd BLAST162

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni8 – 10Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the dihydrofolate reductase family.Curated
Contains 1 DHFR (dihydrofolate reductase) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108YYV. Bacteria.
COG0262. LUCA.
HOGENOMiHOG000040233.
KOiK00287.
OMAiAIARNGV.

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.

Q54801-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKKIVAIWA QDEEGVIGKE NRLPWHLPAE LQHFKETTLN HAILMGRVTF
60 70 80 90 100
DGMGRRLLPK RETLILTRNP EEKIDGVATF QDVQSVLDWY QAQEKNLYII
110 120 130 140 150
GGKQIFQAFE PYLDEVIVTH IHARVEGDTY FPEELDLSLF ETVSSKFYAK
160
DEKNPYDFTI QYRKRKEV
Length:168
Mass (Da):19,703
Last modified:September 26, 2001 - v2
Checksum:i4C3887E290B6303E
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti14E → D in strain: 21. 1
Natural varianti20E → D in strain: 21, 30 and 1/1. 1
Natural varianti60K → Q in strain: 30, 56 and 1/1. 1
Natural varianti65I → V in strain: 92. 1
Natural varianti70P → S in strain: 21, 56 and 1/1. 1
Natural varianti74I → L in strain: 21. 1
Natural varianti77 – 78VA → AV in strain: 30. 2
Natural varianti81Q → H in strain: 21, 56 and 1/1. 1
Natural varianti91Q → H in strain: 21. 1
Natural varianti92A → D in strain: ATCC 49619. 1
Natural varianti94E → D in strain: 21. 1
Natural varianti100I → L in strain: 21, 30, 56 and 1/1. 1
Natural varianti111P → S in strain: 56 and 1/1. 1
Natural varianti135L → F in strain: 21, 30, 56 and 1/1. 1
Natural varianti141E → D in strain: 56. 1
Natural varianti147 – 149FYA → SYT in strain: 21. 3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74777 Genomic DNA. Translation: CAA99035.1.
Z74778 Genomic DNA. Translation: CAA99036.1.
Z84378 Genomic DNA. Translation: CAB06418.1.
Z84379 Genomic DNA. Translation: CAB06419.1.
Z84380 Genomic DNA. Translation: CAB06420.1.
Z84381 Genomic DNA. Translation: CAB06421.1.
AE005672 Genomic DNA. Translation: AAK75658.1.
PIRiA95183.
RefSeqiWP_000162484.1. NZ_AKVY01000001.1.

Genome annotation databases

EnsemblBacteriaiAAK75658; AAK75658; SP_1571.
KEGGispn:SP_1571.
PATRICi19707567. VBIStrPne105772_1626.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74777 Genomic DNA. Translation: CAA99035.1.
Z74778 Genomic DNA. Translation: CAA99036.1.
Z84378 Genomic DNA. Translation: CAB06418.1.
Z84379 Genomic DNA. Translation: CAB06419.1.
Z84380 Genomic DNA. Translation: CAB06420.1.
Z84381 Genomic DNA. Translation: CAB06421.1.
AE005672 Genomic DNA. Translation: AAK75658.1.
PIRiA95183.
RefSeqiWP_000162484.1. NZ_AKVY01000001.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IX9X-ray1.95A/B1-168[»]
ProteinModelPortaliQ54801.
SMRiQ54801.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ54801. 1 interactor.
STRINGi170187.SpneT_02000377.

Chemistry databases

BindingDBiQ54801.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK75658; AAK75658; SP_1571.
KEGGispn:SP_1571.
PATRICi19707567. VBIStrPne105772_1626.

Phylogenomic databases

eggNOGiENOG4108YYV. Bacteria.
COG0262. LUCA.
HOGENOMiHOG000040233.
KOiK00287.
OMAiAIARNGV.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.
BRENDAi1.5.1.3. 1960.

Miscellaneous databases

EvolutionaryTraceiQ54801.

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_STRPN
AccessioniPrimary (citable) accession number: Q54801
Secondary accession number(s): O08440
, O08441, O08442, O08443, Q54973
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 26, 2001
Last modified: November 2, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Strains 1/1, 21, 30, 56 and 92 are trimethoprim resistant.

Keywords - Technical termi

3D-structure, Complete proteome

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.