HPPK_STRP8
ID HPPK_STRP8 Reviewed; 166 AA.
AC Q8P151;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase {ECO:0000250|UniProtKB:P26281};
DE EC=2.7.6.3 {ECO:0000250|UniProtKB:P26281};
DE AltName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase {ECO:0000250|UniProtKB:P26281};
DE Short=PPPK {ECO:0000250|UniProtKB:P26281};
DE AltName: Full=7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase {ECO:0000250|UniProtKB:P26281};
DE Short=HPPK {ECO:0000250|UniProtKB:P26281};
GN Name=folK; OrderedLocusNames=spyM18_1062;
OS Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=186103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS8232;
RX PubMed=11917108; DOI=10.1073/pnas.062526099;
RA Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA Veasy L.G., Musser J.M.;
RT "Genome sequence and comparative microarray analysis of serotype M18 group
RT A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
CC -!- FUNCTION: Catalyzes the transfer of pyrophosphate from adenosine
CC triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic
CC step in folate biosynthesis pathway. {ECO:0000250|UniProtKB:P26281}.
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:0000250|UniProtKB:P26281};
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:0000250|UniProtKB:P26281}.
CC -!- SIMILARITY: Belongs to the HPPK family. {ECO:0000305}.
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DR EMBL; AE009949; AAL97686.1; -; Genomic_DNA.
DR RefSeq; WP_002995337.1; NC_003485.1.
DR AlphaFoldDB; Q8P151; -.
DR SMR; Q8P151; -.
DR GeneID; 57852593; -.
DR KEGG; spm:spyM18_1062; -.
DR HOGENOM; CLU_097916_1_2_9; -.
DR OMA; QVILRQN; -.
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: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 CDD; cd00483; HPPK; 1.
DR Gene3D; 3.30.70.560; -; 1.
DR InterPro; IPR000550; Hppk.
DR InterPro; IPR035907; Hppk_sf.
DR Pfam; PF01288; HPPK; 1.
DR SUPFAM; SSF55083; SSF55083; 1.
DR TIGRFAMs; TIGR01498; folK; 1.
DR PROSITE; PS00794; HPPK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Folate biosynthesis; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..166
FT /note="2-amino-4-hydroxy-6-hydroxymethyldihydropteridine
FT pyrophosphokinase"
FT /id="PRO_0000168263"
SQ SEQUENCE 166 AA; 18981 MW; 69533C246F402C55 CRC64;
MTIVYLSLGT NMRDRAAYLQ KALETLADLP QTRLLAQSSI YETAAWGKTD QADFLNMACQ
LDTQLTAADF LKETQAIEQS LGRVRHEKWG SRTIDIDILL FGEEVYDTKE LKVPHPYMTE
RAFVLIPLLE LQPDLKLPPN HKFLRDYLAA LDQSDITLFS AQQTEF
