ID G9MB34_PLAVI Unreviewed; 181 AA.
AC G9MB34;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 32.
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:BAL37262.1};
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:BAL37262.1};
RN [1] {ECO:0000313|EMBL:BAL37262.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HHM {ECO:0000313|EMBL:BAL37262.1};
RA Maghsoodloorad F., Hosseinzade Sardar Abadi N., Nazemalhosseini Mojarad E.,
RA Haghighi A., Gachkar L.;
RT "Plasmodium vivax dhfr and dhps mutations in isolates from Chabahar.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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; AB674519; BAL37262.1; -; Genomic_DNA.
DR AlphaFoldDB; G9MB34; -.
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..181
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAL37262.1"
FT NON_TER 181
FT /evidence="ECO:0000313|EMBL:BAL37262.1"
SQ SEQUENCE 181 AA; 20728 MW; 297087EF54619A13 CRC64;
LQSPTSEGTK NEPFSPRTFR GLGNKGTLPW KCNSVDMKYF RSVTTYVDES KYEKLKWKRE
RYLRMEASQG GGDNTSGGDN THGGDNADKL QNVVVMGRSN WESIPKQYKP LPNKINVVLS
KTLTKEDVKE KVFIIDSIND LLLLLKKLKY YKCFIIGGAQ VYRECLSRNL IKQIYFTRTN
G
//
