ID F7H2S1_CALJA Unreviewed; 400 AA.
AC F7H2S1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Diphosphomevalonate decarboxylase {ECO:0000256|ARBA:ARBA00019335, ECO:0000256|PIRNR:PIRNR015950};
DE EC=4.1.1.33 {ECO:0000256|ARBA:ARBA00012296, ECO:0000256|PIRNR:PIRNR015950};
GN Name=MVD {ECO:0000313|Ensembl:ENSCJAP00000023667.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000023667.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000023667.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000023667.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the ATP dependent decarboxylation of (R)-5-
CC diphosphomevalonate to form isopentenyl diphosphate (IPP). Functions in
CC the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP),
CC a key precursor for the biosynthesis of isoprenoids and sterol
CC synthesis. {ECO:0000256|ARBA:ARBA00003812,
CC ECO:0000256|RuleBase:RU363086}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-5-diphosphomevalonate + ATP = ADP + CO2 + isopentenyl
CC diphosphate + phosphate; Xref=Rhea:RHEA:23732, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57557,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:456216; EC=4.1.1.33;
CC Evidence={ECO:0000256|ARBA:ARBA00001827,
CC ECO:0000256|PIRNR:PIRNR015950, ECO:0000256|RuleBase:RU363086};
CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004770, ECO:0000256|RuleBase:RU363086}.
CC -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00008831, ECO:0000256|PIRNR:PIRNR015950,
CC ECO:0000256|RuleBase:RU363086}.
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DR AlphaFoldDB; F7H2S1; -.
DR Ensembl; ENSCJAT00000025037.5; ENSCJAP00000023667.3; ENSCJAG00000012897.5.
DR eggNOG; KOG2833; Eukaryota.
DR GeneTree; ENSGT00390000015359; -.
DR HOGENOM; CLU_040369_4_4_1; -.
DR OMA; LTLHAMM; -.
DR OrthoDB; 458712at2759; -.
DR TreeFam; TF105952; -.
DR UniPathway; UPA00063; -.
DR Proteomes; UP000008225; Chromosome 20.
DR Bgee; ENSCJAG00000012897; Expressed in liver and 6 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004163; F:diphosphomevalonate decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 1.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR005935; Mev_decarb.
DR InterPro; IPR029765; Mev_diP_decarb.
DR InterPro; IPR041431; Mvd1_C.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR01240; mevDPdecarb; 1.
DR PANTHER; PTHR10977; DIPHOSPHOMEVALONATE DECARBOXYLASE; 1.
DR PANTHER; PTHR10977:SF3; DIPHOSPHOMEVALONATE DECARBOXYLASE; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR Pfam; PF18376; MDD_C; 1.
DR PIRSF; PIRSF015950; Mev_P_decrbx; 1.
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|PIRNR:PIRNR015950};
KW Cholesterol biosynthesis {ECO:0000256|RuleBase:RU363086};
KW Cholesterol metabolism {ECO:0000256|RuleBase:RU363086};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU363086};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|PIRNR:PIRNR015950};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR015950};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR015950};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955,
KW ECO:0000256|RuleBase:RU363086};
KW Steroid metabolism {ECO:0000256|RuleBase:RU363086};
KW Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011,
KW ECO:0000256|RuleBase:RU363086};
KW Sterol metabolism {ECO:0000256|RuleBase:RU363086}.
FT DOMAIN 111..166
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 197..382
FT /note="Mvd1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18376"
SQ SEQUENCE 400 AA; 43724 MW; 85A5DC5777F2855C CRC64;
MASEKPLAVV TCTAPVNIAV IKYWGKRDEE LVLPINSSLS VTLHQDQLKT TTTAAISKDF
TEDRVWLNGR EEDVGQPRLQ ACLQEIRRLA RKRRNTWDGD LPPSSLNCKV HVASENNFPT
AAGLASSAAG YACLAYTLAR VYGVESDLSE VARRGSGSAC RSLYGGFVEW QMGEQADGKD
SIARQVAPES HWPELRVLIL VVSAEKKLMG STVGMQASVK TSPLLRFRAE SVVPARMAEM
TRCIQERDFR GFAQLTMQDS NQFHATCLDT FPPISYLSHI SWRIIHLVHR FNAHHGDTKV
AYTFDAGPNA VIFTLEDTMA DFVAAVRHTF PPGSNGDTFL RGLQVRPASL PAELKAALAM
EPTPGGVKYI IATQVGPGPQ ILDDPYTHLL GPDGLPKPAA
//
