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MVK_METTH
ID   MVK_METTH               Reviewed;         303 AA.
AC   Q50559; O26152;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Mevalonate kinase {ECO:0000255|HAMAP-Rule:MF_00217};
DE            Short=MK {ECO:0000255|HAMAP-Rule:MF_00217};
DE            Short=MVK {ECO:0000255|HAMAP-Rule:MF_00217};
DE            EC=2.7.1.36 {ECO:0000255|HAMAP-Rule:MF_00217};
GN   Name=mvk {ECO:0000255|HAMAP-Rule:MF_00217}; OrderedLocusNames=MTH_46;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RA   Sharma S., Reeve J.N.;
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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 phosphorylation of (R)-mevalonate (MVA) to (R)-
CC       mevalonate 5-phosphate (MVAP). Functions in the mevalonate (MVA)
CC       pathway leading to isopentenyl diphosphate (IPP), a key precursor for
CC       the biosynthesis of isoprenoid compounds such as archaeal membrane
CC       lipids. {ECO:0000255|HAMAP-Rule:MF_00217}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+);
CC         Xref=Rhea:RHEA:17065, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:36464, ChEBI:CHEBI:58146, ChEBI:CHEBI:456216;
CC         EC=2.7.1.36; Evidence={ECO:0000255|HAMAP-Rule:MF_00217};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00217};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC       step 1/3. {ECO:0000255|HAMAP-Rule:MF_00217}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00217}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00217}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00217}.
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DR   EMBL; U47134; AAA87051.1; -; Genomic_DNA.
DR   EMBL; AE000666; AAB84553.1; -; Genomic_DNA.
DR   PIR; B69160; B69160.
DR   AlphaFoldDB; Q50559; -.
DR   SMR; Q50559; -.
DR   STRING; 187420.MTH_46; -.
DR   EnsemblBacteria; AAB84553; AAB84553; MTH_46.
DR   KEGG; mth:MTH_46; -.
DR   PATRIC; fig|187420.15.peg.44; -.
DR   HOGENOM; CLU_017814_0_0_2; -.
DR   OMA; NTVCTYG; -.
DR   UniPathway; UPA00057; UER00098.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004496; F:mevalonate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.890; -; 1.
DR   HAMAP; MF_00217; Mevalonate_kinase; 1.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR   InterPro; IPR006205; Mev_gal_kin.
DR   InterPro; IPR022937; Mevalonate_kinase_arc.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR43290; PTHR43290; 1.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55060; SSF55060; 1.
DR   TIGRFAMs; TIGR00549; mevalon_kin; 1.
DR   PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Isoprene biosynthesis; Kinase; Lipid biosynthesis;
KW   Lipid metabolism; Magnesium; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..303
FT                   /note="Mevalonate kinase"
FT                   /id="PRO_0000156666"
FT   ACT_SITE        141
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00217"
FT   BINDING         90..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00217"
FT   CONFLICT        108
FT                   /note="A -> P (in Ref. 2; AAB84553)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   303 AA;  32225 MW;  599CAC09B6164276 CRC64;
     MKSSASAPAK AILFGEHAVV YSKPAIAAAI DRRVTVTVSE SSSTHVTIPS LGIRHSSERP
     SGGILDYIGR CLELYHDASP LDIRVEMEIP AGSGLGSSAA LTVALIGALD RYHGRDHGPG
     ETAARAHRVE VDVQGAASPL DTAISTYGGL VYLDSQRRVR QFEADLGDLV IAHLDYSGET
     ARMVAGVAER FRRFPDIMGR IMDTVESITN TAYRELLRNN TEPLGELMNL NQGLLDSMGV
     STRELSMMVY EARNAGAAGS KITGAGGGGS IIAHCPGCVD DVVTALNRNW KAMRAEFSVK
     GLI
 
 
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