ID Q9BLN5_PLACH Unreviewed; 673 AA.
AC Q9BLN5;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase {ECO:0000256|ARBA:ARBA00013253};
DE EC=2.7.6.3 {ECO:0000256|ARBA:ARBA00013253};
DE Flags: Fragment;
GN Name=pppk-dhps {ECO:0000313|EMBL:CAC24559.1};
OS Plasmodium chabaudi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5825 {ECO:0000313|EMBL:CAC24559.1};
RN [1] {ECO:0000313|EMBL:CAC24559.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AS {ECO:0000313|EMBL:CAC24559.1};
RA Hayton K.;
RL Thesis (2000), Department of Institute of Cell, Animal and Population
RL Biology, University of Edinburgh, Edinburgh, United Kingdom.
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}.
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DR EMBL; AJ302077; CAC24559.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9BLN5; -.
DR VEuPathDB; PlasmoDB:PCHAS_1428500; -.
DR HOGENOM; CLU_391048_0_0_1; -.
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: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; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
DR InterPro; IPR000489; Pterin-binding_dom.
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; 2.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAC24559.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 331..664
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT COILED 414..441
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAC24559.1"
SQ SEQUENCE 673 AA; 79147 MW; 82C0287501AEE33A CRC64;
ENNKGNIVVL NFGTTDKTNA VTILETALYL TEKYIGKIIN TSYMYETVPE YIVLDKSNIP
NNIIGEDDPY DVSSLNELVN GLENSKYENV FQEDESLVSQ CEEYEIFLNN KDLFENKIKQ
ISVEEYKTEA SNIIKENDEI MKINLEKHKN KYYTNYFYNL AVVFKSFIDD PLHLLVILKY
IEHLMKRKNS KEVEKFENRL IDIDILFFNN YTIFEKNINL TKDSLYAIMC KYINIECDDN
CNKRLKDIEQ IKDNIKFLSI PHVYTKHRYS ILLCLNDIIP NYKHNTLKET INNLYEEFIT
NFSKLYNTCI KKYNKRLYVL KNEVLYLKEK TNIVGILNTN YNSFSDGGLF VKPDIAVRRI
FQMINEGVDI IDIGGESSAP FVSHNPEIKE RDLVIPVLEL FEQEWNKMLQ ICKNEKIDKE
EKGIEKQNDK LNQNNLSLQT KTSTIYKPPI SIDTMNYDLF KECVDKNLVD ILNDISACTN
DPQIIKLLKK KNKYYSVVLM HKRGDPHTMD MLTQYEDVVY DIKKYLEERL NFLTLNGIPR
YRIILDIGLG FAKKHDQSIK LLQNIHVYDD YPLFIGYSRK RFISHTLAQT CVEICPNTIA
QNENIQNDES DKNGFTVRNI RKDKDQYLYQ KNILGGLAIA SYCFEKKVEM IRVHDVFETR
CVLDMMKKLH QNE
//
