ID   HPPK_STRPY              Reviewed;         166 AA.
AC   P0C0G2; O33726;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 67.
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;
OS   Streptococcus pyogenes.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G76;
RA   Joensson M., Stroem-Tannergren K., Swedberg G.;
RT   "Enzyme kinetic analysis of two different variants of dihydropteroate
RT   synthase conferring sulfonamide resistance to Streptococcus pyogenes.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-91.
RC   STRAIN=G56;
RX   PubMed=9593127; DOI=10.1128/aac.42.5.1062;
RA   Swedberg G., Ringertz S., Skoeld O.;
RT   "Sulfonamide resistance in Streptococcus pyogenes is associated with
RT   differences in the amino acid sequence of its chromosomal dihydropteroate
RT   synthase.";
RL   Antimicrob. Agents Chemother. 42:1062-1067(1998).
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; AJ312186; CAC39315.1; -; Genomic_DNA.
DR   EMBL; AJ000685; CAA04240.1; -; Genomic_DNA.
DR   RefSeq; WP_002984757.1; NZ_WXZK01000013.1.
DR   AlphaFoldDB; P0C0G2; -.
DR   SMR; P0C0G2; -.
DR   eggNOG; COG0801; Bacteria.
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_0000168259"
SQ   SEQUENCE   166 AA;  18824 MW;  5241A1C55BF70A3A CRC64;
     MTIVYLSLGT NMGDRAAYLQ KALEALADLP QTRLLAQSSI YETTAWGKTG QADFLNMACQ
     LDTQLTAADF LKETQAIEQS LGRVRHEKWG SRTIDIDILL FGEEVYDTKE LKVPHPYMTE
     RAFVLIPLLE LQPDLKLPPN HKFLRDYLAA LDQSDITLFS AQQTEF