ID S3CCS6_OPHP1 Unreviewed; 445 AA.
AC S3CCS6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Phosphomevalonate kinase {ECO:0000256|ARBA:ARBA00012958, ECO:0000256|PIRNR:PIRNR017288};
DE EC=2.7.4.2 {ECO:0000256|ARBA:ARBA00012958, ECO:0000256|PIRNR:PIRNR017288};
GN ORFNames=F503_05807 {ECO:0000313|EMBL:EPE10712.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE10712.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE10712.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE10712.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-5-phosphomevalonate + ATP = (R)-5-diphosphomevalonate +
CC ADP; Xref=Rhea:RHEA:16341, ChEBI:CHEBI:30616, ChEBI:CHEBI:57557,
CC ChEBI:CHEBI:58146, ChEBI:CHEBI:456216; EC=2.7.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00029326};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16342;
CC Evidence={ECO:0000256|ARBA:ARBA00029326};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 2/3. {ECO:0000256|ARBA:ARBA00005017,
CC ECO:0000256|PIRNR:PIRNR017288}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
CC subfamily. {ECO:0000256|ARBA:ARBA00006495,
CC ECO:0000256|PIRNR:PIRNR017288}.
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DR EMBL; KE148146; EPE10712.1; -; Genomic_DNA.
DR AlphaFoldDB; S3CCS6; -.
DR STRING; 1262450.S3CCS6; -.
DR VEuPathDB; FungiDB:F503_05807; -.
DR eggNOG; KOG4519; Eukaryota.
DR HOGENOM; CLU_022059_1_0_1; -.
DR OMA; LVIHRTM; -.
DR OrthoDB; 991613at2759; -.
DR UniPathway; UPA00057; UER00099.
DR Proteomes; UP000016923; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004631; F:phosphomevalonate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniRule.
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; IPR016005; Erg8.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR035102; Phosphomevalonate_kinase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR PANTHER; PTHR31814; -; 1.
DR PANTHER; PTHR31814:SF2; PHOSPHOMEVALONATE KINASE; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF017288; PMK_GHMP_euk; 2.
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};
KW Kinase {ECO:0000256|PIRNR:PIRNR017288, ECO:0000313|EMBL:EPE10712.1};
KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR017288};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR017288};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016923};
KW Steroid biosynthesis {ECO:0000256|PIRNR:PIRNR017288};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221,
KW ECO:0000256|PIRNR:PIRNR017288};
KW Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW Transferase {ECO:0000256|PIRNR:PIRNR017288}.
FT DOMAIN 164..229
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
SQ SEQUENCE 445 AA; 46740 MW; 22D4D9AED238F6F9 CRC64;
MSAGPTDTTA ISAPGKVLLA GGYLVLDRAY TGLVFGLSAR INVIARAIET SPGVQLSEIV
VDSPQFQDAK WTYGYHLADE DGGIQVTQLQ TGTTANANPF VETTLSYALT YVSSLAKLSP
AHSITASRLT ILADNDYYSQ PDNVSSTPSQ RFTRFPTTLS GANKTGLGSS AALVTSLTAA
VLSHYLPTTL FDIYTAAGKD TLHNLAQAAH CAAQGKVGSG FDVAAAVYGS CTYQRFSPSV
LEGIPEPGQP GFSTTLQNVI SGSGWDTEIA KGSVALPAGV AVRMCDVDCG SQTVSMVKKV
LAWRSSAPED SKLLWDTLQE RNGKLATVLR DGAVDELPAA IGSIRELVRK MGTESGVPIE
PESQTELLDA VSTVEGVYGG VVPGAGGFDA VSLLIKDDEA TASRLEAFLA KWSQDKGGRV
RLLKVKGEME GARKEDTSIY GGWIN
//