ID   HPPK_MYCBO              Reviewed;         188 AA.
AC   P64144; A0A1R3Y4N8; O06276; X2BNQ7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=BQ2027_MB3636C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU02264.1; -; Genomic_DNA.
DR   RefSeq; NP_857275.1; NC_002945.3.
DR   RefSeq; WP_003419536.1; NC_002945.4.
DR   AlphaFoldDB; P64144; -.
DR   SMR; P64144; -.
DR   EnsemblBacteria; SIU02264; SIU02264; BQ2027_MB3636C.
DR   GeneID; 45427592; -.
DR   PATRIC; fig|233413.5.peg.3982; -.
DR   OMA; QVILRQN; -.
DR   UniPathway; UPA00077; UER00155.
DR   Proteomes; UP000001419; 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; Transferase.
FT   CHAIN           1..188
FT                   /note="2-amino-4-hydroxy-6-hydroxymethyldihydropteridine
FT                   pyrophosphokinase"
FT                   /id="PRO_0000168256"
SQ   SEQUENCE   188 AA;  20732 MW;  D14AE440760CDCF4 CRC64;
     MTRVVLSVGS NLGDRLARLR SVADGLGDAL IAASPIYEAD PWGGVEQGQF LNAVLIADDP
     TCEPREWLRR AQEFERAAGR VRGQRWGPRN LDVDLIACYQ TSATEALVEV TARENHLTLP
     HPLAHLRAFV LIPWIAVDPT AQLTVAGCPR PVTRLLAELE PADRDSVRLF RPSFDLNSRH
     PVSRAPES