ID Q25866_PLAFA Unreviewed; 706 AA.
AC Q25866;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Dihydropterin pyrophosphokinase and Dihydropteroate synthetase {ECO:0000313|EMBL:CAA83456.1};
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:CAA83456.1};
RN [1] {ECO:0000313|EMBL:CAA83456.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=K1 {ECO:0000313|EMBL:CAA83456.1};
RX PubMed=7925353; DOI=10.1111/j.1432-1033.1994.00397.x;
RA Brooks D.R., Wang P., Read M., Watkins W.M., Sims P.F., Hyde J.E.;
RT "Sequence variation of the hydroxymethyldihydropterin pyrophosphokinase:
RT dihydropteroate synthase gene in lines of the human malaria parasite,
RT Plasmodium falciparum, with differing resistance to sulfadoxine.";
RL Eur. J. Biochem. 224:397-405(1994).
RN [2] {ECO:0000313|EMBL:CAA83456.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=K1 {ECO:0000313|EMBL:CAA83456.1};
RA Sims P.F.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate =
CC 7,8-dihydropteroate + diphosphate; Xref=Rhea:RHEA:19949,
CC ChEBI:CHEBI:17836, ChEBI:CHEBI:17839, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:72950; EC=2.5.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00000012};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-
CC 6-yl)methyl diphosphate + AMP + H(+); Xref=Rhea:RHEA:11412,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:44841,
CC ChEBI:CHEBI:72950, ChEBI:CHEBI:456215; EC=2.7.6.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000198};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-
CC 4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-
CC dihydroneopterin triphosphate: step 4/4.
CC {ECO:0000256|ARBA:ARBA00005051}.
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-
CC dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
CC dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00004763}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the DHPS family.
CC {ECO:0000256|ARBA:ARBA00009951}.
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DR EMBL; Z31584; CAA83456.1; -; Genomic_DNA.
DR AlphaFoldDB; Q25866; -.
DR VEuPathDB; PlasmoDB:PF3D7_0810800; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000226100; -.
DR VEuPathDB; PlasmoDB:Pf7G8_080015800; -.
DR VEuPathDB; PlasmoDB:PfCD01_080016300; -.
DR VEuPathDB; PlasmoDB:PfDd2_080015900; -.
DR VEuPathDB; PlasmoDB:PfGA01_080014400; -.
DR VEuPathDB; PlasmoDB:PfGB4_080015500; -.
DR VEuPathDB; PlasmoDB:PfGN01_080016400; -.
DR VEuPathDB; PlasmoDB:PfHB3_080016200; -.
DR VEuPathDB; PlasmoDB:PfIT_080015700; -.
DR VEuPathDB; PlasmoDB:PfKE01_080016300; -.
DR VEuPathDB; PlasmoDB:PfKH01_080015800; -.
DR VEuPathDB; PlasmoDB:PfKH02_080016300; -.
DR VEuPathDB; PlasmoDB:PfML01_080016400; -.
DR VEuPathDB; PlasmoDB:PfNF135_000017400; -.
DR VEuPathDB; PlasmoDB:PfNF166_080014600; -.
DR VEuPathDB; PlasmoDB:PfNF54_080014600; -.
DR VEuPathDB; PlasmoDB:PfSD01_080016100; -.
DR VEuPathDB; PlasmoDB:PfSN01_080015300; -.
DR VEuPathDB; PlasmoDB:PfTG01_080016600; -.
DR UniPathway; UPA00077; UER00155.
DR GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.70.560; 7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK; 1.
DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR InterPro; IPR045031; DHP_synth-like.
DR InterPro; IPR006390; DHP_synth_dom.
DR InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
DR InterPro; IPR000489; Pterin-binding_dom.
DR NCBIfam; TIGR01496; DHPS; 1.
DR PANTHER; PTHR20941; FOLATE SYNTHESIS PROTEINS; 1.
DR PANTHER; PTHR20941:SF1; FOLIC ACID SYNTHESIS PROTEIN FOL1; 1.
DR Pfam; PF01288; HPPK; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF55083; 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR PROSITE; PS00793; DHPS_2; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAA83456.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 389..698
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 706 AA; 83388 MW; E1D557468C9D315D CRC64;
METIQELILS EENKTNIAVL NLGTNDRRNA VLILETALHL VEKYLGKIIN TSYLYETVPE
YIVLDKKESC EKINKDCRIY DVNYINELMQ NLEESKYEEN KELIDKCEEY ETFLKNGKVD
NSILKEVNVE NYLLECNNII VKNDEIMKNN LSKYKDKYYT SYFYNLTVVV KTFVNDPLSM
LVVIKYIEEL MKRENVKEKE KFENRIIDID ILFFNDFTIF MKNIKLEKNM IYKILSKYIH
LERDIRNGND NMSKVNMDKD INLNNNNNIK KKNNNDIDCD CVDQKMNNHV NNKNYINSFR
DPQEIINNMV DNIEFLSIPH VYTTHRYSIL LCLNDMIPEY KHNVLNNTIR CLYNKYVSRM
KEQYNINIKE NNKRIYVLKD RISYLKEKTN IVGILNVNYD SFSDGGIFVE PKRAVQRMFE
MINEGASVID IGGESSGPFV IPNPKISERD LVVPVLQLFQ KEWNDIKNKI VKCDAKPIIS
IDTINYNVFK ECVDNDLVDI LNDISACTNN PEIIKLLKKK NKFYSVVLMH KRGNPHTMDK
LTNYDNLVYD IKNYLEQRLN FLVLNGIPRY RILFDIGLGF GKKHDQSIKL LQNIHVYDEY
PLFIGYSRKR FIAHCMNDQN VVINTQQKLH DEQQNENKNI VDKSHNWMFQ MNYMRKDKDQ
LLYQKNICGG LAIASYSYYK KVDLIRVHDV LETKSVLDVL TKIDQV
//
