ID A0A1J1HAN4_PLARL Unreviewed; 653 AA.
AC A0A1J1HAN4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Dihydropteroate synthetase, putative {ECO:0000313|EMBL:CRH02537.1};
DE EC=2.5.1.15 {ECO:0000313|EMBL:CRH02537.1};
GN Name=DHPS {ECO:0000313|EMBL:CRH02537.1};
GN ORFNames=PRELSG_1426800 {ECO:0000313|EMBL:CRH02537.1};
OS Plasmodium relictum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Haemamoeba).
OX NCBI_TaxID=85471 {ECO:0000313|EMBL:CRH02537.1, ECO:0000313|Proteomes:UP000220158};
RN [1] {ECO:0000313|EMBL:CRH02537.1, ECO:0000313|Proteomes:UP000220158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGS1 {ECO:0000313|EMBL:CRH02537.1,
RC ECO:0000313|Proteomes:UP000220158};
RG Pathogen Informatics;
RL Submitted (APR-2015) 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; LN835309; CRH02537.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1HAN4; -.
DR VEuPathDB; PlasmoDB:PRELSG_1426800; -.
DR OMA; FAKKHDQ; -.
DR OrthoDB; 5411at2759; -.
DR UniPathway; UPA00077; UER00155.
DR Proteomes; UP000220158; Chromosome 14.
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};
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 Reference proteome {ECO:0000313|Proteomes:UP000220158};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CRH02537.1}.
FT DOMAIN 340..645
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 653 AA; 77276 MW; 4EEAAAAB871FFCEB CRC64;
MVFIKKIMNS TDSNKRNIAV LNIGTNDKNN SVTILETAFY LIEKYIGKII NTSYLYETVP
EYIILDEIKS IENVTNEICE DYEINDINWL KDIVKALECS RYEENYDLIH ECYEYDKFLK
NEKLNESTIE EVAADDYELE SKNLIKKNDE IMKENLEKYK NKYYTKYFYN VVVVVRSFVE
DPLSMLIILK YIEQLMKRKN IKKRLKFENR LLDIDILFFN NYTIFKKKIE LEKSDIYKVF
LKYINIEKDK NKIYEIIETL KDEIQFLCIP HLYTRFRYSI LLCLNDVIPQ YKHPVLKEKI
STLYNNCVKN FEEKYKINIK ENNKKIYVLK DQLLYLKEKT QIVGILNVNY DSFSDGGLFA
DPSKAVDRIF EMINEGANVI DIGGESSAPF VVPNPKISER DLVMPVLRLF HQEWDKLESE
LKKDIIKPVI SIDTVHYDIF KECVEENFVD VLNDISACTN NPEIIKLLKK ENKYLSVVLM
HKRGNPHTMD KLTDYNNIVY DIKNYLVDRL NFLVLNGIPR YRIILDVGLG FAKKHDQSIK
LLKDIHVYDD YPLFIGYSRK RFIAHCMNEN SIINRKKEAF GDEKSENENK KKGWIFKMNN
VRQDKDQLLY QKNICGGLAI ASYLFYKKVD LIRVHDVLET KAVLDVLTKI HKL
//
