ID W9IVA0_FUSOX Unreviewed; 443 AA.
AC W9IVA0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=FOYG_05130 {ECO:0000313|EMBL:EWY96416.1};
OS Fusarium oxysporum NRRL 32931.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY96416.1, ECO:0000313|Proteomes:UP000030753};
RN [1] {ECO:0000313|EMBL:EWY96416.1, ECO:0000313|Proteomes:UP000030753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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; JH717841; EWY96416.1; -; Genomic_DNA.
DR AlphaFoldDB; W9IVA0; -.
DR HOGENOM; CLU_022059_1_0_1; -.
DR OrthoDB; 991613at2759; -.
DR UniPathway; UPA00057; UER00099.
DR Proteomes; UP000030753; 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; IPR013750; GHMP_kinase_C_dom.
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; PF08544; GHMP_kinases_C; 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:EWY96416.1};
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:UP000030753};
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 162..227
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 339..408
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
SQ SEQUENCE 443 AA; 47937 MW; 5781913795DF6084 CRC64;
MTLHHPTIAV SAPGKVFLAG GYLVLDQEYT AFVFGLDARI NIIAGDIHTT AGVQLTEIVV
DSPQFLEAQW RYGYHLAGEG GGIKVTQLQV GAQINPNPFV ETTLSYALTY IDRVAKQRPS
HSMASARLII LADNDYYSHS ESESTRQGRF AKFPVTLGDA NKTGLGSSAA LVTSLTAALL
AHYLPEDLFN IQSDRGKRTL HNLAQAAHCA AQGKVGSGFD VATAVYGSCR YRRFSPETLS
SIPEPGAAGF ADALVKLVDG ESAWDVEVLK DAVIMPKGVV LRMCDVDCGS KTVGMVKKVL
KWRSSNPEES KKLWDELQKR NEQLIATLNA GDVENLPGKI TAVREMIRQM GSASDVPIEP
ESQTELLDAL STVEGVYGGV VPGAGGYDAL ALLMKDDEET KQRVEEFLDK WAKEKGTKVK
LLGVKGEMEG VRSESLDVYA GWI
//
