GenomeNet

Database: UniProt
Entry: A8C544_PLAMA
LinkDB: A8C544_PLAMA
Original site: A8C544_PLAMA 
ID   A8C544_PLAMA            Unreviewed;       226 AA.
AC   A8C544;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   24-JAN-2024, entry version 40.
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 malariae.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=5858 {ECO:0000313|EMBL:ABQ23921.1};
RN   [1] {ECO:0000313|EMBL:ABQ23921.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Af16 {ECO:0000313|EMBL:ABQ23926.1}, Au237
RC   {ECO:0000313|EMBL:ABQ23933.1}, Av427 {ECO:0000313|EMBL:ABQ23921.1},
RC   and Vp64 {ECO:0000313|EMBL:ABQ23932.1};
RX   PubMed=17682097; DOI=10.1128/AAC.00234-07;
RA   Tanomsing N., Imwong M., Pukrittayakamee S., Chotivanich K.,
RA   Looareesuwan S., Mayxay M., Dolecek C., Hien T.T., do Rosario V.E.,
RA   Arez A.P., Michon P., Snounou G., White N.J., Day N.P.;
RT   "Genetic analysis of the dihydrofolate reductase-thymidylate synthase gene
RT   from geographically diverse isolates of Plasmodium malariae.";
RL   Antimicrob. Agents Chemother. 51:3523-3530(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; EF206328; ABQ23921.1; -; Genomic_DNA.
DR   EMBL; EF206333; ABQ23926.1; -; Genomic_DNA.
DR   EMBL; EF206339; ABQ23932.1; -; Genomic_DNA.
DR   EMBL; EF206340; ABQ23933.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8C544; -.
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..226
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABQ23921.1"
FT   NON_TER         226
FT                   /evidence="ECO:0000313|EMBL:ABQ23921.1"
SQ   SEQUENCE   226 AA;  26247 MW;  E52FB9F9BDF66FFA CRC64;
     DIYAICACCK VPNHGEGKKN EIFSTKTFRG LGNKGCLPWK SNSLDMKYFS SVTTYVNEMK
     YKKLKYKREK YLEKEISNEN SSTVFENISL LSSSKLQNVV VMGRSSWVSI PKQYKPLPNR
     INVVLSRTLK KEDVKEDIFI INNMDQLVLL LKKLNYYKCF IIGGAIVYKE CLERNLIKQI
     YFTRINNVYE CDVFFPEIDE NVFQITSVSD VYTSNCTSLD FVIFSK
//
DBGET integrated database retrieval system