ID A0A1B0AAW7_GLOPL Unreviewed; 393 AA.
AC A0A1B0AAW7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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};
OS Glossina pallidipes (Tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7398 {ECO:0000313|EnsemblMetazoa:GPAI039724-PA, ECO:0000313|Proteomes:UP000092445};
RN [1] {ECO:0000313|Proteomes:UP000092445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000092445};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GPAI039724-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPAI039724-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 AlphaFoldDB; A0A1B0AAW7; -.
DR STRING; 7398.A0A1B0AAW7; -.
DR EnsemblMetazoa; GPAI039724-RA; GPAI039724-PA; GPAI039724.
DR VEuPathDB; VectorBase:GPAI039724; -.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000092445; Unassembled WGS sequence.
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};
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 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 145..220
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 300..371
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
SQ SEQUENCE 393 AA; 43539 MW; 179D7F7370AA93D0 CRC64;
MFDFQVRAPG KIILHGEHAV VYHKPALAAV VGLATTLRFS MDQTQPIISV QLEALNNNFS
VEVKAFNEFL SKFRTKYPTE KSDSTVQLLE EVRVELAKQQ EEQLENNSSS KKQKNQKSFM
SIYYLLAGAV LSSPVKDFKI TNGFRLHIDT ELNIGSGLGS SASYGVALAA AFLLYARHFD
VSSYQDPQNL ALISNWAFES ERIVHGTPSG VDNTICSYGG MLRFVKGQGF QTINIVRPLN
ILLVDSKVKR STADIVAKVR HLSETFPEVI NAIWDALEAL VTEAIPLYEI FGNSQDDSEK
FEKLERLFQI NNDLLKAIGV SHPKLEQIFS IAYKRGFFSK VTGAGAGGYV IVLLPDNYAK
NEVYWKLKEE LEAAGFGVHS TTAGGDGLSI EKL
//
