ID   MPTE_PYRFU              Reviewed;         231 AA.
AC   Q8U2A9;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_02131};
DE            Short=HPPK {ECO:0000255|HAMAP-Rule:MF_02131};
DE            EC=2.7.6.3 {ECO:0000255|HAMAP-Rule:MF_02131, ECO:0000269|PubMed:22931285};
DE   AltName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_02131};
DE   AltName: Full=6-hydroxymethyl-7,8-dihydropterin diphosphokinase {ECO:0000255|HAMAP-Rule:MF_02131};
DE            Short=6-HMPDK {ECO:0000255|HAMAP-Rule:MF_02131, ECO:0000303|PubMed:22931285};
DE   AltName: Full=7,8-dihydro-6-hydroxymethylpterin diphosphokinase {ECO:0000255|HAMAP-Rule:MF_02131, ECO:0000303|PubMed:22931285};
DE   AltName: Full=7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_02131};
DE            Short=PPPK {ECO:0000255|HAMAP-Rule:MF_02131};
GN   Name=mptE {ECO:0000255|HAMAP-Rule:MF_02131, ECO:0000303|PubMed:22931285};
GN   OrderedLocusNames=PF0930;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, GENE NAME, AND SUBSTRATE SPECIFICITY.
RX   PubMed=22931285; DOI=10.1021/cb300342u;
RA   Crecy-Lagard V.D., Phillips G., Grochowski L.L., Yacoubi B.E., Jenney F.,
RA   Adams M.W., Murzin A.G., White R.H.;
RT   "Comparative genomics guided discovery of two missing archaeal enzyme
RT   families involved in the biosynthesis of the pterin moiety of
RT   tetrahydromethanopterin and tetrahydrofolate.";
RL   ACS Chem. Biol. 7:1807-1816(2012).
CC   -!- FUNCTION: Catalyzes the transfer of diphosphate from ATP to 6-
CC       hydroxymethyl-7,8-dihydropterin (6-HMD), leading to 6-hydroxymethyl-
CC       7,8-dihydropterin diphosphate (6-HMDP). To a lesser extent, can also
CC       use CTP, UTP, and GTP as the nucleotide triphosphate substrate.
CC       {ECO:0000255|HAMAP-Rule:MF_02131, ECO:0000269|PubMed:22931285}.
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:0000255|HAMAP-Rule:MF_02131,
CC         ECO:0000269|PubMed:22931285};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02131};
CC   -!- SIMILARITY: Belongs to the archaeal 6-HMPDK family. {ECO:0000255|HAMAP-
CC       Rule:MF_02131}.
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DR   EMBL; AE009950; AAL81054.1; -; Genomic_DNA.
DR   RefSeq; WP_011012066.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U2A9; -.
DR   SMR; Q8U2A9; -.
DR   STRING; 186497.PF0930; -.
DR   EnsemblBacteria; AAL81054; AAL81054; PF0930.
DR   GeneID; 41712740; -.
DR   KEGG; pfu:PF0930; -.
DR   PATRIC; fig|186497.12.peg.985; -.
DR   eggNOG; arCOG04303; Archaea.
DR   HOGENOM; CLU_093043_0_0_2; -.
DR   OMA; HAHGDNM; -.
DR   OrthoDB; 105604at2157; -.
DR   PhylomeDB; Q8U2A9; -.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004788; F:thiamine diphosphokinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.10240; -; 1.
DR   HAMAP; MF_02131; HMPDK_arch; 1.
DR   InterPro; IPR027510; HMPDK_MptE.
DR   InterPro; IPR002826; MptE-like.
DR   InterPro; IPR036759; TPK_catalytic_sf.
DR   PANTHER; PTHR39648; PTHR39648; 1.
DR   Pfam; PF01973; MAF_flag10; 1.
DR   SUPFAM; SSF63999; SSF63999; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Magnesium; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..231
FT                   /note="6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase"
FT                   /id="PRO_0000420356"
SQ   SEQUENCE   231 AA;  26262 MW;  568D1258EB655851 CRC64;
     MKWEEWKPFY ERIVKEMGYS IEEDRRAAEL LRDILMENDN YIIKEELNSI IMQKVYVFGA
     GPNLEEALKK GDFKDGTKIA ADGATSALLE YGITPDVVVT DLDGRIRDLL EASRKAVMVV
     HAHGDNMDKL PLVVEFPLVL GTCQTEPLDI VYNFGGFTDG DRAAFLAEEM GAKEIVLVGF
     DFSGIVGKWS KPWLRDHTPA WESKMKKLKF ARELLEWLKN NGRAKIIEFS I