ID A0A093F1J2_TAUER Unreviewed; 306 AA.
AC A0A093F1J2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Mevalonate kinase {ECO:0000256|ARBA:ARBA00012103, ECO:0000256|RuleBase:RU363087};
DE Short=MK {ECO:0000256|RuleBase:RU363087};
DE EC=2.7.1.36 {ECO:0000256|ARBA:ARBA00012103, ECO:0000256|RuleBase:RU363087};
DE Flags: Fragment;
GN ORFNames=N340_08846 {ECO:0000313|EMBL:KFV20546.1};
OS Tauraco erythrolophus (Red-crested turaco).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Musophagiformes; Musophagidae; Tauraco.
OX NCBI_TaxID=121530 {ECO:0000313|EMBL:KFV20546.1, ECO:0000313|Proteomes:UP000053661};
RN [1] {ECO:0000313|EMBL:KFV20546.1, ECO:0000313|Proteomes:UP000053661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV20546.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of mevalonate to mevalonate 5-
CC phosphate, a key step in isoprenoid and cholesterol biosynthesis.
CC {ECO:0000256|RuleBase:RU363087}.
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 Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
CC subfamily. {ECO:0000256|ARBA:ARBA00006495,
CC ECO:0000256|RuleBase:RU363087}.
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DR EMBL; KL475775; KFV20546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093F1J2; -.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000053661; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
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, ECO:0000256|RuleBase:RU363087};
KW Cholesterol biosynthesis {ECO:0000256|RuleBase:RU363087};
KW Cholesterol metabolism {ECO:0000256|RuleBase:RU363087};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU363087};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU363087};
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:UP000053661};
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|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363087}.
FT DOMAIN 40..122
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 208..266
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV20546.1"
FT NON_TER 306
FT /evidence="ECO:0000313|EMBL:KFV20546.1"
SQ SEQUENCE 306 AA; 32176 MW; 104EA3F92EF60E44 CRC64;
LKEFAGITAE ASAPESLATL AFLYMCLAVS AKYGDLPSMD ILVWSELPTG AGLGSSAAYA
VCLAGALLTA CGAISCPLKE GESTARWTEE ELTLINSWAF QGERVIHGNP SGVDNAVGTW
GGALRYQSGK ITPLKRVPML RILLTNTKVP RSTKVLVAGV KEKILKFPAI MNPVLDSIDA
ISQECQSVLE AMPANPSPEY YPVLEELFDI NQHHLNVIGV GHPSLDRLCR VTASHGLHSK
LTGAGGGGCG ITLLRPDTSP LAVEAAKRDL CACGFECWET NIGAPGVTLH SPSSLSAAVL
HALSES
//
