ID Q8I9L9_PLAVI Unreviewed; 217 AA.
AC Q8I9L9;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 63.
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;
OS Plasmodium vivax (malaria parasite P. vivax).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5855 {ECO:0000313|EMBL:AAO16080.1};
RN [1] {ECO:0000313|EMBL:AAO16080.1}
RP NUCLEOTIDE SEQUENCE.
RA Mallika I., Pukrittayakamee S., Renia L., Letourneur F., Charlieu J.-P.,
RA Learsakulpanich U., Looareesuwan S., White N.J., Snounou G.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAO16080.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12709316; DOI=10.1128/AAC.47.5.1514-1521.2003;
RA Imwong M., Pukrittayakamee S., Renia L., Letourneur F., Charlieu J.P.,
RA Leartsakulpanich U., Looareesuwan S., White N.J., Snounou G.;
RT "Novel point mutations in the dihydrofolate reductase gene of Plasmodium
RT vivax: evidence for sequential selection by drug pressure.";
RL Antimicrob. Agents Chemother. 47:1514-1521(2003).
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; AF525812; AAO16080.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8I9L9; -.
DR HOGENOM; CLU_021669_3_0_1; -.
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..217
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAO16080.1"
FT NON_TER 217
FT /evidence="ECO:0000313|EMBL:AAO16080.1"
SQ SEQUENCE 217 AA; 24797 MW; 11E3D350E1346750 CRC64;
YAICACCKVA PTSEGTKNEP FSPRTFRGLG NKGTLPWKCN SVDMKYFRSV TTYVDESKYE
KLKWKRERYL RMEASQGGGD NTSGGDNTHG GDNADKLQNV VVMGRSNWES IPKQYKPLPN
RINVVLSKTL TKEDVKEKVF IIDSIDDLLL LLKKLKYYKC FIIGGAQVYR ECLSRNLIKQ
IYFTRINGAY PCDVFFPEFD ESQFRVTSVS EVYNSKG
//
