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P00380

- DYR_ENTFC

UniProt

P00380 - DYR_ENTFC

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Protein

Dihydrofolate reductase

Gene

folA

Organism
Enterococcus faecium (Streptococcus faecium)
Status
Reviewed - Annotation score: 3 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei7 – 71NADP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei27 – 271SubstrateBy similarity
Binding sitei58 – 581SubstrateBy similarity
Binding sitei117 – 1171SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 197NADPBy similarity
Nucleotide bindingi45 – 462NADPBy similarity
Nucleotide bindingi64 – 652NADPBy similarity
Nucleotide bindingi99 – 1068NADPBy similarity

GO - Molecular functioni

  1. dihydrofolate reductase activity Source: UniProtKB-EC
  2. NADP binding Source: InterPro

GO - Biological processi

  1. glycine biosynthetic process Source: InterPro
  2. nucleotide biosynthetic process Source: InterPro
  3. one-carbon metabolic process Source: UniProtKB-KW
  4. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00077; UER00158.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrofolate reductase (EC:1.5.1.3)
Gene namesi
Name:folA
OrganismiEnterococcus faecium (Streptococcus faecium)
Taxonomic identifieri1352 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 167167Dihydrofolate reductasePRO_0000186390Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP00380.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 162162DHFRPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Family and domain databases

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.

P00380-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFISMWAQDK NGLIGKDGLL PWRLPNDMRF FREHTMDKIL VMGRKTYEGM
60 70 80 90 100
GKLSLPYRHI IVLTTQKDFK VEKNAEVLHS IDELLAYAKD IPEDIYVSGG
110 120 130 140 150
SRIFQALLPE TKIIWRTLID AEFEGDTFIG EIDFTSFELV EEHEGIVNQE
160
NQYPHRFQKW QKMSKVV
Length:167
Mass (Da):19,583
Last modified:July 21, 1986 - v1
Checksum:iE00C2CF3BC420585
GO

Sequence databases

PIRiA00392. RDSODF.

Cross-referencesi

Sequence databases

PIRi A00392. RDSODF.

3D structure databases

ProteinModelPortali P00380.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00077 ; UER00158 .

Family and domain databases

Gene3Di 3.40.430.10. 1 hit.
InterProi IPR012259. DHFR.
IPR024072. DHFR-like_dom.
IPR017925. DHFR_CS.
IPR001796. DHFR_dom.
[Graphical view ]
Pfami PF00186. DHFR_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000194. DHFR. 1 hit.
PRINTSi PR00070. DHFR.
SUPFAMi SSF53597. SSF53597. 1 hit.
PROSITEi PS00075. DHFR_1. 1 hit.
PS51330. DHFR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The structure of the mutant dihydrofolate reductase from Streptococcus faecium. Amino acid sequence of peptide CNBr 7 and complete sequence of the protein."
    Peterson D.L., Gleisner J.M., Blakley R.L.
    J. Biol. Chem. 250:4945-4954(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: A / var. Durans.

Entry informationi

Entry nameiDYR_ENTFC
AccessioniPrimary (citable) accession number: P00380
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 1, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3