(data stored in ACNUC10043 zone)

SWISSPROT: D1YV21_METPS

ID   D1YV21_METPS            Unreviewed;       211 AA.
AC   D1YV21;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 51.
DE   RecName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase {ECO:0000256|HAMAP-Rule:MF_02131};
DE            Short=HPPK {ECO:0000256|HAMAP-Rule:MF_02131};
DE            EC=2.7.6.3 {ECO:0000256|HAMAP-Rule:MF_02131};
DE   AltName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase {ECO:0000256|HAMAP-Rule:MF_02131};
DE   AltName: Full=6-hydroxymethyl-7,8-dihydropterin diphosphokinase {ECO:0000256|HAMAP-Rule:MF_02131};
DE            Short=6-HMPDK {ECO:0000256|HAMAP-Rule:MF_02131};
DE   AltName: Full=7,8-dihydro-6-hydroxymethylpterin diphosphokinase {ECO:0000256|HAMAP-Rule:MF_02131};
DE   AltName: Full=7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase {ECO:0000256|HAMAP-Rule:MF_02131};
DE            Short=PPPK {ECO:0000256|HAMAP-Rule:MF_02131};
GN   Name=mptE {ECO:0000256|HAMAP-Rule:MF_02131};
GN   OrderedLocusNames=MCP_0221 {ECO:0000313|EMBL:BAI60293.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60293.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
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:0000256|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:0000256|HAMAP-Rule:MF_02131};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02131};
CC   -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02131}.
CC   -!- SIMILARITY: Belongs to the archaeal 6-HMPDK family. {ECO:0000256|HAMAP-
CC       Rule:MF_02131}.
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DR   EMBL; AP011532; BAI60293.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0221; -.
DR   EnsemblBacteria; BAI60293; BAI60293; MCP_0221.
DR   KEGG; mpd:MCP_0221; -.
DR   PATRIC; fig|304371.9.peg.228; -.
DR   eggNOG; arCOG04303; Archaea.
DR   eggNOG; COG1634; LUCA.
DR   HOGENOM; HOG000226046; -.
DR   KO; K07142; -.
DR   OMA; HAHGDNM; -.
DR   UniPathway; UPA00065; -.
DR   Proteomes; UP000001882; 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:2001118; P:tetrahydromethanopterin biosynthetic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
DR   PRODOM; D1YV21.
DR   SWISS-2DPAGE; D1YV21.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02131};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_02131};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_02131};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02131};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02131}.
SQ   SEQUENCE   211 AA;  23480 MW;  42F353276B3D311D CRC64;
     MRYEQWEPYY RAILQDFGWT AEGDEKAAEL LSSMLPEDTP CLARVEELIR GKEVIVCGKA
     PTLQKDMAKV DWWYKYTVIA ADGAVSTLLD QGIVPDIVVS DLDGRHEDLL EADSLGSIIV
     AHAHADNVEA VKSLVPKLRH VVGTTQARPL RNVYNFGGFS DGDRCVFLAK ELGAKSIKII
     GFDLDDTKVT PKKLKKLKWA RRLLGDLGIN I
//

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