ID Z9JV57_9MICO Unreviewed; 381 AA.
AC Z9JV57;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=mevalonate kinase {ECO:0000256|ARBA:ARBA00012103};
DE EC=2.7.1.36 {ECO:0000256|ARBA:ARBA00012103};
GN ORFNames=BF93_15925 {ECO:0000313|EMBL:EWS81652.1};
OS Brachybacterium phenoliresistens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=396014 {ECO:0000313|EMBL:EWS81652.1, ECO:0000313|Proteomes:UP000023067};
RN [1] {ECO:0000313|EMBL:EWS81652.1, ECO:0000313|Proteomes:UP000023067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W13A50 {ECO:0000313|EMBL:EWS81652.1,
RC ECO:0000313|Proteomes:UP000023067};
RA Wang X.;
RT "Genome sequence of Brachybacterium phenoliresistens strain W13A50.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EWS81652.1}.
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DR EMBL; JDYK01000006; EWS81652.1; -; Genomic_DNA.
DR RefSeq; WP_051486672.1; NZ_KK069991.1.
DR AlphaFoldDB; Z9JV57; -.
DR STRING; 396014.BF93_15925; -.
DR PATRIC; fig|396014.3.peg.1530; -.
DR eggNOG; COG1577; Bacteria.
DR HOGENOM; CLU_017814_0_0_11; -.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000023067; Unassembled WGS sequence.
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:EWS81652.1};
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:UP000023067};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 154..217
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 286..365
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 381 AA; 37908 MW; 6574406B31A75FCA CRC64;
MPYSPDDAPD RAPRRGGGSE ATRVLATPRR GGGTRTALGS PADPDAQDLA ASATGLHHGS
ALTDGPVDGV GRSHGKAILI GEHAVVYGAA AIALPVPSVE AIAQVELLPA GETSRLTSRL
HSGTFATLPA ELTPVAAAVH AAATAVGLDP DRIHLRIGSQ VPIGRGMGSS AAVAAAVVEA
VADAAGAQLT AEVRHELIQT SERVAHGNPS GLDARTVVSD QPVRFLQRRP QGSVPVARPT
SFVIADSGVS ASTAVAVATV RARREAAPQV VDAVIEELSA LVDPVAAALG SGDMTGLGAG
MTRAHELLRE IGVSSPVLDD LVEGALAAGS PGAKLTGSGG GGCVLALAAS PQAADDLALA
LHAAGAPRTW TMTLAPRKGD A
//
