ID Q8DW87_STRMU Unreviewed; 332 AA.
AC Q8DW87;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE SubName: Full=Mevalonate kinase {ECO:0000313|EMBL:AAN57956.1};
DE EC=2.7.1.36 {ECO:0000313|EMBL:AAN57956.1};
GN OrderedLocusNames=SMU_181 {ECO:0000313|EMBL:AAN57956.1};
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN57956.1, ECO:0000313|Proteomes:UP000002512};
RN [1] {ECO:0000313|EMBL:AAN57956.1, ECO:0000313|Proteomes:UP000002512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512};
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 1/3. {ECO:0000256|ARBA:ARBA00029438}.
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DR EMBL; AE014133; AAN57956.1; -; Genomic_DNA.
DR RefSeq; NP_720650.1; NC_004350.2.
DR RefSeq; WP_002262028.1; NC_004350.2.
DR AlphaFoldDB; Q8DW87; -.
DR STRING; 210007.SMU_181; -.
DR KEGG; smu:SMU_181; -.
DR PATRIC; fig|210007.7.peg.157; -.
DR eggNOG; COG1577; Bacteria.
DR HOGENOM; CLU_017814_0_0_9; -.
DR OrthoDB; 9764892at2; -.
DR PhylomeDB; Q8DW87; -.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004496; F:mevalonate kinase activity; IEA:UniProtKB-EC.
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; GHMP kinase, C-terminal domain; 1.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR006205; Mev_gal_kin.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00549; mevalon_kin; 1.
DR PANTHER; PTHR43290; MEVALONATE KINASE; 1.
DR PANTHER; PTHR43290:SF2; MEVALONATE KINASE; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PRINTS; PR00959; MEVGALKINASE.
DR SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AAN57956.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002512};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAN57956.1}.
FT DOMAIN 103..164
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 241..321
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
SQ SEQUENCE 332 AA; 35761 MW; 757977DBDDD26453 CRC64;
MIDSQLKEKR KVIIEKKIAL GKASGKIILM GEHAVVYGQP AIAIPFSAVE TVAEVKEDGE
ALTVTCEFYD GLVHKMPEIL ESLKHAIRFS LYRIGAPQDP AIHIDIHSTI PAERGMGSSA
AVAVAIARSL FNFYGKVLTD KELWEIVQSS EKIAHGNPSG IDTVTTSGKS PVFFVKDQPI
EQLSINMDAY LIVADTGQTG QTLKAIQSVK ALLSKVTYQI DSLSDPKQAI KELGQLTKLA
KEALLNNYIL ELGEVMNQAH QLLASLTVSN QTLDRLAQAA RQAGALGAKL TGGGRGGCLI
ALAKDKESAE KIARSLLEQG AKQAWCQYLG NL
//
