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Database: UniProt
Entry: D3KYV3_PLAVI
LinkDB: D3KYV3_PLAVI
Original site: D3KYV3_PLAVI 
ID   D3KYV3_PLAVI            Unreviewed;       208 AA.
AC   D3KYV3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, 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;
GN   Name=DHFR {ECO:0000313|EMBL:BAI79253.1};
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:BAI79253.1};
RN   [1] {ECO:0000313|EMBL:BAI79253.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ShH {ECO:0000313|EMBL:BAI79253.1};
RA   Matuschek M., Wallwey C., Li S.-M.;
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAI79253.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ShH {ECO:0000313|EMBL:BAI79253.1};
RX   PubMed=27007559; DOI=10.1590/S1678-9946201658016;
RA   Sharifi-Sarasiabi K., Haghighi A., Kazemi B., Taghipour N., Mojarad E.N.,
RA   Gachkar L.;
RT   "MOLECULAR SURVEILLANCE OF Plasmodium vivax AND Plasmodium falciparum DHFR
RT   MUTATIONS IN ISOLATES FROM SOUTHERN IRAN.";
RL   Rev. Inst. Med. Trop. Sao Paulo 58:e16-e16(2016).
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; AB547456; BAI79253.1; -; Genomic_DNA.
DR   EMBL; AB547457; BAI79254.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3KYV3; -.
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          9..208
FT                   /note="DHFR"
FT                   /evidence="ECO:0000259|PROSITE:PS51330"
FT   REGION          85..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         208
FT                   /evidence="ECO:0000313|EMBL:BAI79253.1"
SQ   SEQUENCE   208 AA;  23552 MW;  C9D80BB8C8F120F4 CRC64;
     MEDLSDVFDI YAICACCKVA PTSEGTKNEP FSPRTFRGLG NKGTLPWKCN SVDMKYFSSV
     TTYVDESKYE KLKWKRERYL RMEASQGGGD NTSGGDNTHG GDNTHGGDNA DKLQNVVVMG
     RSSWESIPKQ YKPLPNRINV VLSKTLTKED VKEKVFIIDS IDDLLLLLKK LKYYKCFIIG
     GAQVYRECLS RNLIKQIYFT RINGAYPC
//
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