ID A0A183C6S3_GLOPA Unreviewed; 438 AA.
AC A0A183C6S3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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};
OS Globodera pallida (Potato cyst nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC Globodera.
OX NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_000856900};
RN [1] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Aslett M.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J., Thorpe P.,
RA Tsai I.J., Beasley H., Blok V., Cock P.J.A., Van den Akker S.E.,
RA Holroyd N., Hunt M., Mantelin S., Naghra H., Pain A., Palomares-Rius J.E.,
RA Zarowiecki M., Berriman M., Jones J.T., Urwin P.E.;
RT "The genome and life-stage specific transcriptomes of Globodera pallida
RT elucidate key aspects of plant parasitism by a cyst nematode.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:GPLIN_000856900}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) 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|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; A0A183C6S3; -.
DR WBParaSite; GPLIN_000856900; GPLIN_000856900; GPLIN_000856900.
DR UniPathway; UPA00063; -.
DR Proteomes; UP000050741; Unassembled WGS sequence.
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 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 103..159
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 191..391
FT /note="Mvd1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18376"
FT REGION 336..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 438 AA; 47526 MW; 2A24CE97ED0A7466 CRC64;
MSGFEITIQA PVNIALIKYW GKRNEELVLP LNDSIAITID ELRATTHISI GPNVEANSVT
LNGAAIDIAG SARFRHLFEQ IREYSNRKRK LKGETASKRW HTKIESHTNF PTAAGLASSA
AGFAAIAYGL GKIFRLSERD IIRMARMGSG SACRSIQGGF VHWKAGTQQQ NDSDCFCEKL
VPPSHWTQMR AVIVVVSTEH KKVGSSVGMR NTVRTSELMD TRVQQLVPKR VKQLMSAIRE
RNFATLAEIT MAESNQLHAV CMDTCPPLNY LNATSHALIE FVHDFNTRFG TRLAYTFDAG
PNCCLLLEVD TLALLRRAFA QCFMFNCQFP DDNAGPATEE GEVEAQDDAQ TEMAGPNGSS
TKAAAFPWTT PRAIQIQRIV LSKVGVGPRV LSFTSSAASA SSSATGGSAS SSSSSSNNTN
SSGNSNCSNA TRVDCKML
//
