MPTE_METJA
ID MPTE_METJA Reviewed; 241 AA.
AC Q59028;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=MJ1634;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, GENE NAME, AND PATHWAY.
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). {ECO:0000255|HAMAP-
CC 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 -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02131,
CC ECO:0000269|PubMed:22931285}.
CC -!- SIMILARITY: Belongs to the archaeal 6-HMPDK family. {ECO:0000255|HAMAP-
CC Rule:MF_02131}.
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DR EMBL; L77117; AAB99656.1; -; Genomic_DNA.
DR PIR; H64503; H64503.
DR RefSeq; WP_010871158.1; NC_000909.1.
DR AlphaFoldDB; Q59028; -.
DR STRING; 243232.MJ_1634; -.
DR EnsemblBacteria; AAB99656; AAB99656; MJ_1634.
DR GeneID; 1452543; -.
DR KEGG; mja:MJ_1634; -.
DR eggNOG; arCOG04303; Archaea.
DR HOGENOM; CLU_093043_0_0_2; -.
DR InParanoid; Q59028; -.
DR OMA; HAHGDNM; -.
DR OrthoDB; 105604at2157; -.
DR PhylomeDB; Q59028; -.
DR BioCyc; MetaCyc:MON-17934; -.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000000805; 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:2001118; P:tetrahydromethanopterin biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:InterPro.
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..241
FT /note="6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase"
FT /id="PRO_0000107449"
SQ SEQUENCE 241 AA; 27581 MW; 7E7F2EBB4AC5DBAA CRC64;
MDMKEWEIFY NKIMEDFGFD KDKDVESAVI LNNILENANT IPVDKLKDII EGREVFIFGA
GPSIKKHINI LKELREINYK NPIIVADGAC KAFLEENIIP DIIVSDLDGD LEALFECNRK
GSIIVVHAHG DNIEKIKKYV PKLKNVVGSC QIPNYKELNL RNVINFGGFT DGDRCCFLAY
HFKAKKLILG GMDFGIYITK YSRPNIKEDI AIGDEIKIKK LEYAKTLINY LKDKIEIEFL
K
