DYR_ENCCU
ID DYR_ENCCU Reviewed; 205 AA.
AC O62583;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Dihydrofolate reductase;
DE EC=1.5.1.3;
GN Name=DHFR-1; OrderedLocusNames=ECU01_0170;
GN and
GN Name=DHFR-2; OrderedLocusNames=ECU01_1450;
GN and
GN Name=DHFR-3; OrderedLocusNames=ECU08_0080;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11013707; DOI=10.1089/omi.1.1998.3.1;
RA Duffieux F., Peyret P., Roe B.A., Vivares C.P.;
RT "First report on the systematic sequencing of the small genome of
RT Encephalitozoon cuniculi (Protozoa, Microspora): gene organization of a 4.3
RT kbp region on chromosome I.";
RL Microb. Comp. Genomics 3:1-11(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11157783; DOI=10.1101/gr.164301;
RA Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA Weissenbach J., Saurin W., Vivares C.P.;
RT "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT parasite Encephalitozoon cuniculi (Microspora).";
RL Genome Res. 11:198-207(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
CC -!- FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential
CC reaction for de novo glycine and purine synthesis, and for DNA
CC precursor synthesis (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate +
CC H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.5.1.3; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00660};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-
CC tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
CC -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC {ECO:0000305}.
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DR EMBL; AJ005644; CAA06647.1; -; Genomic_DNA.
DR EMBL; AL391737; CAD24887.1; -; Genomic_DNA.
DR EMBL; AL391737; CAD25017.1; -; Genomic_DNA.
DR EMBL; AL590448; CAD26313.1; -; Genomic_DNA.
DR RefSeq; NP_597137.1; NM_001041746.1.
DR RefSeq; XP_965852.1; XM_960759.1.
DR RefSeq; XP_965982.1; XM_960889.1.
DR AlphaFoldDB; O62583; -.
DR SMR; O62583; -.
DR STRING; 284813.O62583; -.
DR GeneID; 859559; -.
DR GeneID; 860188; -.
DR GeneID; 860189; -.
DR KEGG; ecu:ECU01_0170; -.
DR KEGG; ecu:ECU01_1450; -.
DR KEGG; ecu:ECU08_0080; -.
DR VEuPathDB; MicrosporidiaDB:ECU01_0170; -.
DR VEuPathDB; MicrosporidiaDB:ECU01_1450; -.
DR VEuPathDB; MicrosporidiaDB:ECU08_0080; -.
DR HOGENOM; CLU_043966_2_1_1; -.
DR InParanoid; O62583; -.
DR OMA; NANALPW; -.
DR OrthoDB; 1489621at2759; -.
DR UniPathway; UPA00077; UER00158.
DR Proteomes; UP000000819; Chromosome I.
DR Proteomes; UP000000819; Chromosome VIII.
DR GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00209; DHFR; 1.
DR Gene3D; 3.40.430.10; -; 1.
DR InterPro; IPR012259; DHFR.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR001796; DHFR_dom.
DR PANTHER; PTHR48069; PTHR48069; 1.
DR Pfam; PF00186; DHFR_1; 1.
DR SUPFAM; SSF53597; SSF53597; 1.
DR PROSITE; PS51330; DHFR_2; 1.
PE 3: Inferred from homology;
KW NADP; One-carbon metabolism; Oxidoreductase; Reference proteome.
FT CHAIN 1..205
FT /note="Dihydrofolate reductase"
FT /id="PRO_0000186373"
FT DOMAIN 1..201
FT /note="DHFR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00660"
FT BINDING 7
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 13..19
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 29..34
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 62..64
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 84..86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 118..125
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 205 AA; 22883 MW; 45450EAA534487DD CRC64;
MLALVVALAS HRGIGNANAL PWPRPLAADM AWFRTLSQSI PLISPDRIAL APSASNAVVM
GRRTWDSIPS RFRPLANRIN VVLSRGPARS TENTFFIQTF EALDSLPLPP SSMTFVIGGR
DVYSLALESG RPHLIFATEV FESPECDVFF PHIDWASYEK RDITRDVSRL IDRTLASAFY
SPETATFTEN GTSFKMFLYT KPETR
