MPTE_METTH
ID MPTE_METTH Reviewed; 232 AA.
AC O27637;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 102.
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};
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};
DE AltName: Full=7,8-dihydro-6-hydroxymethylpterin diphosphokinase {ECO:0000255|HAMAP-Rule:MF_02131};
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}; OrderedLocusNames=MTH_1600;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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}.
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 -!- 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 -!- SIMILARITY: Belongs to the archaeal 6-HMPDK family. {ECO:0000255|HAMAP-
CC Rule:MF_02131}.
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DR EMBL; AE000666; AAB86073.1; -; Genomic_DNA.
DR PIR; G69080; G69080.
DR RefSeq; WP_010877208.1; NC_000916.1.
DR AlphaFoldDB; O27637; -.
DR SMR; O27637; -.
DR STRING; 187420.MTH_1600; -.
DR EnsemblBacteria; AAB86073; AAB86073; MTH_1600.
DR GeneID; 1471869; -.
DR KEGG; mth:MTH_1600; -.
DR PATRIC; fig|187420.15.peg.1564; -.
DR HOGENOM; CLU_093043_0_0_2; -.
DR OMA; HAHGDNM; -.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000005223; 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 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..232
FT /note="6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase"
FT /id="PRO_0000107450"
SQ SEQUENCE 232 AA; 25950 MW; 0CFDDD4BF58578EB CRC64;
MEVQVWLRWY TRILDDFGFD RRADEESASY LDAFLREHGC LRVDDIDVPS SDFIVFGAGP
SLRSHLKRFR ALDEPMTVIS ADGATTALLE EDVLPDIIVT DLDGKMEDII EANRQGAVVV
VHAHGNNLPA LRRYLPLLQN IIGTTQSIPH GCLHNFGGFT DGDRAVFLAA ALGAGRIVLA
GMDFGEVVTR YSRPDMDSEL GPADPVKRLK LEYASRLIDW LERNGDVRIE RW
