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P00380

- DYR_ENTFC

UniProt

P00380 - DYR_ENTFC

Protein

Dihydrofolate reductase

Gene

folA

Organism
Enterococcus faecium (Streptococcus faecium)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. 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

    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

    MFISMWAQDK NGLIGKDGLL PWRLPNDMRF FREHTMDKIL VMGRKTYEGM    50
    GKLSLPYRHI IVLTTQKDFK VEKNAEVLHS IDELLAYAKD IPEDIYVSGG 100
    SRIFQALLPE TKIIWRTLID AEFEGDTFIG EIDFTSFELV EEHEGIVNQE 150
    NQYPHRFQKW QKMSKVV 167
    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