ID K4RGL4_STRDJ Unreviewed; 335 AA.
AC K4RGL4;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=mevalonate kinase {ECO:0000256|ARBA:ARBA00012103};
DE EC=2.7.1.36 {ECO:0000256|ARBA:ARBA00012103};
GN ORFNames=BN159_7950 {ECO:0000313|EMBL:CCK32329.1};
OS Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK32329.1, ECO:0000313|Proteomes:UP000008043};
RN [1] {ECO:0000313|EMBL:CCK32329.1, ECO:0000313|Proteomes:UP000008043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101723 / JCM 4913 / KCC S-0913 / 768
RC {ECO:0000313|Proteomes:UP000008043};
RX PubMed=23043000; DOI=10.1128/JB.01592-12;
RA Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R., Blom J.,
RA Pelzer S., Kalinowski J., Mack M.;
RT "Genome sequence of the bacterium Streptomyces davawensis JCM 4913 and
RT heterologous production of the unique antibiotic roseoflavin.";
RL J. Bacteriol. 194:6818-6827(2012).
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 1/3. {ECO:0000256|ARBA:ARBA00029438}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
CC subfamily. {ECO:0000256|ARBA:ARBA00006495}.
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DR EMBL; HE971709; CCK32329.1; -; Genomic_DNA.
DR AlphaFoldDB; K4RGL4; -.
DR STRING; 1214101.BN159_7950; -.
DR KEGG; sdv:BN159_7950; -.
DR PATRIC; fig|1214101.3.peg.8046; -.
DR eggNOG; COG1577; Bacteria.
DR HOGENOM; CLU_017814_0_0_11; -.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000008043; 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; IPR006203; GHMP_knse_ATP-bd_CS.
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.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCK32329.1};
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:UP000008043};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 109..171
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 242..318
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
SQ SEQUENCE 335 AA; 34739 MW; 2E843D105866A377 CRC64;
MALSTSAEGV SADRRARSVG VGRAHAKAVL LGEHAVVYGA PALAVPVPQL TVTASVHSPR
HGGDGPGEVS FTMTGSPSRP MVAQATDGLR RLIGEFTATM GLADSPRLEV TIDGGIPHGR
GLGSSAACAR AVVHALAELY DREVTERETF DLVQTAENLA HGRSSGVDAR AVGALAPLLF
QRGEVQELSI GCYDVLVLAD SGVVGRTKDA VELLREGFQR HTGAQERFVD RAAGLTEQAR
LALADGRPED LGARLTDYHD LLRAAGLSTN AIDTLVEAAL TAGSLGAKIT GGGLGGCVLA
LTRREQAAEV TRELHAAGAV RCWTVPLKGP DEHAC
//
