GenomeNet

Database: UniProt
Entry: A3KCU6_PLAFA
LinkDB: A3KCU6_PLAFA
Original site: A3KCU6_PLAFA 
ID   A3KCU6_PLAFA            Unreviewed;       184 AA.
AC   A3KCU6;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 52.
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:BAF47694.1};
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:BAF47694.1};
RN   [1] {ECO:0000313|EMBL:BAF47694.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17210777; DOI=10.1128/AAC.01186-06;
RA   Mita T., Tanabe K., Takahashi N., Tsukahara T., Eto H., Dysoley L.,
RA   Ohmae H., Kita K., Krudsood S., Looareesuwan S., Kaneko A., Bjorkman A.,
RA   Kobayakawa T.;
RT   "Independent evolution of pyrimethamine resistance in Plasmodium falciparum
RT   isolates in Melanesia.";
RL   Antimicrob. Agents Chemother. 51:1071-1077(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB271908; BAF47694.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3KCU6; -.
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          10..184
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
FT   NON_TER         184
FT                   /evidence="ECO:0000313|EMBL:BAF47694.1"
SQ   SEQUENCE   184 AA;  21658 MW;  0A737E2372F59F02 CRC64;
     MMEQVCDVFD IYAICACCKV ESKNEGKKNE VFNNYTFRGL GNKGVLPWKC HSLDMKYFCA
     VTTYVNESKY EKLKYKRCKY LNKETVDNVN DMPNSKKLQN VVVMGRTNWE SIPKKFKPLS
     NRINVILSRT LKKEDFDEDV YIINKVEDLI VLLGKLNYYK CFIIGGSVVY QEFLEKKLIK
     KIYF
//
DBGET integrated database retrieval system