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Database: UniProt
Entry: Q9GNB0_PLAFA
LinkDB: Q9GNB0_PLAFA
Original site: Q9GNB0_PLAFA 
ID   Q9GNB0_PLAFA            Unreviewed;       220 AA.
AC   Q9GNB0;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=Bifunctional dihydrofolate reductase-thymidylate synthase {ECO:0000256|ARBA:ARBA00019798};
DE            EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
DE            EC=2.1.1.45 {ECO:0000256|ARBA:ARBA00011947};
DE   Flags: Fragment;
GN   Name=dhfr-ts {ECO:0000313|EMBL:AAG10123.1};
OS   Plasmodium falciparum (malaria parasite P. falciparum).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5833 {ECO:0000313|EMBL:AAG10123.1};
RN   [1] {ECO:0000313|EMBL:AAG10123.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=10915101; DOI=10.1086/315731;
RA   Basco L.K., Tahar R., Keundjian A., Ringwald P.;
RT   "Sequence variations in the genes encoding dihydropteroate synthase and
RT   dihydrofolate reductase and clinical response to sulfadoxine-pyrimethamine
RT   in patients with acute uncomplicated falciparum malaria.";
RL   J. Infect. Dis. 182:624-628(2000).
CC   -!- FUNCTION: Bifunctional enzyme. Involved in de novo dTMP biosynthesis.
CC       Key enzyme in folate metabolism. Catalyzes an essential reaction for de
CC       novo glycine and purine synthesis, DNA precursor synthesis, and for the
CC       conversion of dUMP to dTMP. {ECO:0000256|ARBA:ARBA00025154}.
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-
CC       tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004903}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the dihydrofolate reductase family.
CC       {ECO:0000256|RuleBase:RU004474}.
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DR   EMBL; AF248519; AAG10122.1; -; Genomic_DNA.
DR   EMBL; AF248520; AAG10123.1; -; Genomic_DNA.
DR   UniPathway; UPA00077; UER00158.
DR   GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-EC.
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; Dihydrofolate Reductase, subunit A; 1.
DR   InterPro; IPR012259; DHFR.
DR   InterPro; IPR024072; DHFR-like_dom_sf.
DR   InterPro; IPR017925; DHFR_CS.
DR   InterPro; IPR001796; DHFR_dom.
DR   PANTHER; PTHR48069; DIHYDROFOLATE REDUCTASE; 1.
DR   PANTHER; PTHR48069:SF3; DIHYDROFOLATE REDUCTASE; 1.
DR   Pfam; PF00186; DHFR_1; 1.
DR   PRINTS; PR00070; DHFR.
DR   SUPFAM; SSF53597; Dihydrofolate reductase-like; 1.
DR   PROSITE; PS00075; DHFR_1; 1.
DR   PROSITE; PS51330; DHFR_2; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          1..215
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAG10123.1"
FT   NON_TER         220
FT                   /evidence="ECO:0000313|EMBL:AAG10123.1"
SQ   SEQUENCE   220 AA;  25894 MW;  862D9125565B0AE0 CRC64;
     ICACCKVESK NEGKKNEVFN NYTFRGLGNK GVLPWKCNSL DMKYFXAVTT YVNESKYEKL
     KYKRCKYLNK ETVDNVNDMP NSKKLQNVVV MGRTXWESIP KKFKPLSNRI NVILSRTLKK
     EDFDEDVYII NKVEDLIVLL GKLNYYKCFI IGGSVVYQEF LEKKLIKKIY FTRINSTYEC
     DVFFPEINEN EYQIISVSDV YTSNNTTLDF IIYKKTNNKM
//
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