ID   HPPK_CAMJE              Reviewed;         157 AA.
AC   Q9PJ54; Q0PC68;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=Cj0065c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL111168; CAL34239.1; -; Genomic_DNA.
DR   PIR; E81422; E81422.
DR   RefSeq; WP_002851803.1; NC_002163.1.
DR   RefSeq; YP_002343529.1; NC_002163.1.
DR   AlphaFoldDB; Q9PJ54; -.
DR   SMR; Q9PJ54; -.
DR   IntAct; Q9PJ54; 1.
DR   STRING; 192222.Cj0065c; -.
DR   PaxDb; Q9PJ54; -.
DR   PRIDE; Q9PJ54; -.
DR   EnsemblBacteria; CAL34239; CAL34239; Cj0065c.
DR   GeneID; 904396; -.
DR   KEGG; cje:Cj0065c; -.
DR   PATRIC; fig|192222.6.peg.64; -.
DR   eggNOG; COG0801; Bacteria.
DR   HOGENOM; CLU_097916_5_0_7; -.
DR   OMA; QVILRQN; -.
DR   UniPathway; UPA00077; UER00155.
DR   Proteomes; UP000000799; Chromosome.
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;
KW   Reference proteome; Transferase.
FT   CHAIN           1..157
FT                   /note="2-amino-4-hydroxy-6-hydroxymethyldihydropteridine
FT                   pyrophosphokinase"
FT                   /id="PRO_0000168248"
SQ   SEQUENCE   157 AA;  18628 MW;  F42BBDE39E0D57E2 CRC64;
     MLKIQGVKHF EKSRFFPFFS QNIRSFKYLA LIGLGSNIEP EKKRFDMLFR VMMDDKRFKI
     LSTSPMLINE AFGFKEQKDF TNAVMLIQTN LHARALLKVL LYYEVKFKRK RTFKNAPRTL
     DLDLLYFSQK VKRDKWCEVP HKGAKERVSV ILPLGMI