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Protein

Dihydrofolate reductase

Gene
N/A
Organism
Pneumocystis carinii
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
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 sitei12NADP; via amide nitrogen and carbonyl oxygen5 Publications1
Binding sitei75Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi18 – 24NADP5 Publications7
Nucleotide bindingi59 – 61NADP5 Publications3
Nucleotide bindingi81 – 83NADP5 Publications3
Nucleotide bindingi124 – 131NADP5 Publications8

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. 4924.
SABIO-RKP16184.
UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase (EC:1.5.1.3)
OrganismiPneumocystis carinii
Taxonomic identifieri4754 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaPneumocystidomycetesPneumocystidaceaePneumocystis

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1926.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001863761 – 206Dihydrofolate reductaseAdd BLAST206

Interactioni

Chemistry databases

BindingDBiP16184.

Structurei

Secondary structure

1206
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Beta strandi7 – 14Combined sources8
Beta strandi18 – 21Combined sources4
Helixi30 – 41Combined sources12
Helixi47 – 49Combined sources3
Beta strandi51 – 58Combined sources8
Helixi59 – 64Combined sources6
Helixi67 – 69Combined sources3
Beta strandi75 – 80Combined sources6
Beta strandi89 – 91Combined sources3
Beta strandi93 – 97Combined sources5
Helixi98 – 108Combined sources11
Beta strandi111 – 122Combined sources12
Helixi126 – 134Combined sources9
Beta strandi138 – 146Combined sources9
Beta strandi153 – 155Combined sources3
Helixi163 – 165Combined sources3
Turni166 – 168Combined sources3
Beta strandi169 – 171Combined sources3
Helixi174 – 181Combined sources8
Beta strandi190 – 192Combined sources3
Beta strandi195 – 203Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CD2X-ray2.20A1-206[»]
1DAJX-ray2.30A1-206[»]
1DYRX-ray1.86A1-206[»]
1E26X-ray2.00A1-206[»]
1KLKX-ray2.30A1-206[»]
1LY3X-ray1.90A1-206[»]
1LY4X-ray2.10A1-206[»]
1S3YX-ray2.25A1-206[»]
1VJ3X-ray2.10A2-206[»]
2CD2X-ray1.90A1-206[»]
2FZHX-ray2.10A1-206[»]
2FZIX-ray1.60A1-206[»]
3CD2X-ray2.50A1-206[»]
3NZ6X-ray2.00X1-206[»]
3NZ9X-ray1.80X1-206[»]
3NZAX-ray1.90X1-206[»]
3NZBX-ray1.45X1-206[»]
3NZCX-ray2.00X1-206[»]
3TD8X-ray1.80A1-206[»]
4CD2X-ray2.00A1-206[»]
4G8ZX-ray1.75X3-206[»]
4IXEX-ray1.54D1-206[»]
4IXFX-ray1.70X1-206[»]
4IXGX-ray1.70X1-206[»]
4QJZX-ray1.61D1-206[»]
ProteinModelPortaliP16184.
SMRiP16184.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16184.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 204DHFRPROSITE-ProRule annotationAdd BLAST199

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 37Substrate binding1 Publication6

Sequence similaritiesi

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

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

Sequencei

Sequence statusi: Complete.

P16184-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQQKSLTLI VALTTSYGIG RSNSLPWKLK KEISYFKRVT SFVPTFDSFE
60 70 80 90 100
SMNVVLMGRK TWESIPLQFR PLKGRINVVI TRNESLDLGN GIHSAKSLDH
110 120 130 140 150
ALELLYRTYG SESSVQINRI FVIGGAQLYK AAMDHPKLDR IMATIIYKDI
160 170 180 190 200
HCDVFFPLKF RDKEWSSVWK KEKHSDLESW VGTKVPHGKI NEDGFDYEFE

MWTRDL
Length:206
Mass (Da):23,884
Last modified:April 1, 1990 - v1
Checksum:i6BA64A7019911508
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26495 Genomic DNA. Translation: AAA33787.1.
M26496 mRNA. Translation: AAA33788.1.
PIRiA36177.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26495 Genomic DNA. Translation: AAA33787.1.
M26496 mRNA. Translation: AAA33788.1.
PIRiA36177.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CD2X-ray2.20A1-206[»]
1DAJX-ray2.30A1-206[»]
1DYRX-ray1.86A1-206[»]
1E26X-ray2.00A1-206[»]
1KLKX-ray2.30A1-206[»]
1LY3X-ray1.90A1-206[»]
1LY4X-ray2.10A1-206[»]
1S3YX-ray2.25A1-206[»]
1VJ3X-ray2.10A2-206[»]
2CD2X-ray1.90A1-206[»]
2FZHX-ray2.10A1-206[»]
2FZIX-ray1.60A1-206[»]
3CD2X-ray2.50A1-206[»]
3NZ6X-ray2.00X1-206[»]
3NZ9X-ray1.80X1-206[»]
3NZAX-ray1.90X1-206[»]
3NZBX-ray1.45X1-206[»]
3NZCX-ray2.00X1-206[»]
3TD8X-ray1.80A1-206[»]
4CD2X-ray2.00A1-206[»]
4G8ZX-ray1.75X3-206[»]
4IXEX-ray1.54D1-206[»]
4IXFX-ray1.70X1-206[»]
4IXGX-ray1.70X1-206[»]
4QJZX-ray1.61D1-206[»]
ProteinModelPortaliP16184.
SMRiP16184.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP16184.
ChEMBLiCHEMBL1926.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.
BRENDAi1.5.1.3. 4924.
SABIO-RKP16184.

Miscellaneous databases

EvolutionaryTraceiP16184.

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

Entry informationi

Entry nameiDYR_PNECA
AccessioniPrimary (citable) accession number: P16184
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 2, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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.