ID A0A1I8N5P9_MUSDO Unreviewed; 393 AA.
AC A0A1I8N5P9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Mevalonate kinase {ECO:0000256|RuleBase:RU363087};
DE Short=MK {ECO:0000256|RuleBase:RU363087};
DE EC=2.7.1.36 {ECO:0000256|RuleBase:RU363087};
GN Name=101901472 {ECO:0000313|EnsemblMetazoa:MDOA011818-PA};
GN Synonyms=LOC101901472 {ECO:0000313|RefSeq:XP_005183768.1};
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370 {ECO:0000313|EnsemblMetazoa:MDOA011818-PA};
RN [1] {ECO:0000313|EnsemblMetazoa:MDOA011818-PA}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA011818-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005183768.1}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|RefSeq:XP_005183768.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|RuleBase:RU363087};
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 ECO:0000256|RuleBase:RU363087}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU363087}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
CC subfamily. {ECO:0000256|RuleBase:RU363087}.
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DR RefSeq; XP_005183768.1; XM_005183711.3.
DR STRING; 7370.A0A1I8N5P9; -.
DR EnsemblMetazoa; MDOA011818-RA; MDOA011818-PA; MDOA011818.
DR GeneID; 101901472; -.
DR KEGG; mde:101901472; -.
DR VEuPathDB; VectorBase:MDOA011818; -.
DR eggNOG; KOG1511; Eukaryota.
DR OrthoDB; 5472812at2759; -.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000095301; Unassembled WGS sequence.
DR Proteomes; UP000694905; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 GO; GO:0016126; P:sterol biosynthetic process; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363087};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU363087};
KW Kinase {ECO:0000256|RuleBase:RU363087, ECO:0000313|RefSeq:XP_005183768.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU363087};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU363087};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363087};
KW Reference proteome {ECO:0000313|Proteomes:UP000694905};
KW Steroid biosynthesis {ECO:0000256|RuleBase:RU363087};
KW Steroid metabolism {ECO:0000256|RuleBase:RU363087};
KW Sterol biosynthesis {ECO:0000256|RuleBase:RU363087};
KW Sterol metabolism {ECO:0000256|RuleBase:RU363087};
KW Transferase {ECO:0000256|RuleBase:RU363087}.
FT DOMAIN 146..220
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 299..370
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
SQ SEQUENCE 393 AA; 43382 MW; E1B18AB340C6C611 CRC64;
MLNFQVKSPG KIILHGEHAV VYHKPALAAV VGVGTTLKFQ NTTEDSSKVS FKLEALNTIF
EIDIASFNAF LKRCRSKFSE YKLDNAVQLL EEVRLELAKQ QDETIDLGSP KKQQTQKAFI
SIYYLLAGAI LSSPVKDLEL QQPFTITIDT ELNIGAGLGS SASYGAALAS AFLAYAQHFD
LTNYKDEENQ QLISLWAFES ERVMHGTPSG IDNTVCTYGG MLRFVKGQGF QPVKILRPLH
ILLVDSKVKR STADIVAKVR HLGETFPEVI NAIWNACEAL VNTAIPLYEN FGTCQDDSEK
FEKLEQLFQI NNDLMKAIGV THPKLEQIFS IAFKRGFFSK ITGAGAGGYA IVLLPENYAS
NEVYWKLKEE LEGAGFGVHA TTAGGEGLRM EPL
//