ERG8_GIBZE
ID ERG8_GIBZE Reviewed; 443 AA.
AC I1RZD0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Phosphomevalonate kinase ERG8 {ECO:0000303|PubMed:30874562};
DE EC=2.7.4.2 {ECO:0000305|PubMed:30874562};
DE AltName: Full=Ergosterol biosynthesis protein 8 {ECO:0000303|PubMed:30874562};
GN Name=ERG8 {ECO:0000303|PubMed:30874562};
GN ORFNames=FG09764, FGRAMPH1_01T26385;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=30874562; DOI=10.1038/s41467-019-09145-6;
RA Liu Z., Jian Y., Chen Y., Kistler H.C., He P., Ma Z., Yin Y.;
RT "A phosphorylated transcription factor regulates sterol biosynthesis in
RT Fusarium graminearum.";
RL Nat. Commun. 10:1228-1228(2019).
CC -!- FUNCTION: Phosphomevalonate kinase; part of the second module of
CC ergosterol biosynthesis pathway that includes the middle steps of the
CC pathway (By similarity). ERG8 converts 5-phosphomevalonate to 5-
CC diphosphomevalonate (By similarity). The second module is carried out
CC in the vacuole and involves the formation of farnesyl diphosphate,
CC which is also an important intermediate in the biosynthesis of
CC ubiquinone, dolichol, heme and prenylated proteins. Activity by the
CC mevalonate kinase ERG12 (FG05912) first converts mevalonate into 5-
CC phosphomevalonate. 5-phosphomevalonate is then further converted to 5-
CC diphosphomevalonate by the phosphomevalonate kinase ERG8 (FG09764). The
CC diphosphomevalonate decarboxylase ERG19 (FG10424) then produces
CC isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase
CC IDI1 (FG09722) then catalyzes the 1,3-allylic rearrangement of the
CC homoallylic substrate isopentenyl (IPP) to its highly electrophilic
CC allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl
CC diphosphate synthase ERG20 (FG06784) catalyzes the sequential
CC condensation of isopentenyl pyrophosphate with dimethylallyl
CC pyrophosphate, and then with the resultant geranylpyrophosphate to the
CC ultimate product farnesyl pyrophosphate (Probable).
CC {ECO:0000250|UniProtKB:P24521, ECO:0000305|PubMed:30874562}.
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:0000305|PubMed:30874562};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16342;
CC Evidence={ECO:0000305|PubMed:30874562};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 2/3. {ECO:0000305|PubMed:30874562}.
CC -!- INDUCTION: Expression is regulated by the Zn(2)-C6 fungal-type
CC transcription factor FgSR which binds directly to the promoter.
CC {ECO:0000269|PubMed:30874562}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
CC subfamily. {ECO:0000305}.
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DR EMBL; HG970335; CEF85588.1; -; Genomic_DNA.
DR RefSeq; XP_011327956.1; XM_011329654.1.
DR STRING; 5518.FGSG_09764P0; -.
DR GeneID; 23556700; -.
DR KEGG; fgr:FGSG_09764; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G26385; -.
DR eggNOG; KOG4519; Eukaryota.
DR HOGENOM; CLU_022059_1_0_1; -.
DR InParanoid; I1RZD0; -.
DR UniPathway; UPA00057; UER00099.
DR Proteomes; UP000070720; Chromosome 4.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004631; F:phosphomevalonate 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; -; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR31814; PTHR31814; 2.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF017288; PMK_GHMP_euk; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Lipid biosynthesis; Lipid metabolism;
KW Nucleotide-binding; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transferase.
FT CHAIN 1..443
FT /note="Phosphomevalonate kinase ERG8"
FT /id="PRO_0000454674"
FT BINDING 160..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 443 AA; 47639 MW; 1545F3E8A9033C5E CRC64;
MSLKHPTIAV SAPGKVFLAG GYLVLDQEYT AFVFGLNARI NIIAGDIHTT AGVQLTEIVV
DSPQFLDAQW RYGYHLAGEG GGIKVTQLQV GAQINPNPFV ETTLSYALTY IDRVAGHRPS
HSLASARLII LADNDYYSHS ESDTTRSGRF AKFPVTLSNA NKTGLGSSAA LVTSLTASLL
VHYLPEDLFS IDSDKGKRTL HNLAQAAHCA AQGKVGSGFD VATAVYGSCR YRRFSPATLN
KIPEPGVAGF ADALVKLVDG ESEWDVEVLK DAVTMPKGVV LRMCDVDCGS KTVGMVKKVL
AWKSSNPEDS KTLWDELQSR NEQLIATLNA GDVAQLPEKI NAVREKIREM GSASDVPIEP
ESQTELLDAL STVEGVHGGV VPGAGGYDAL ALLMKDDEET KQRVEVFLEK WAAEKGTKVK
LLAVKGEMEG VRSESLDVYA GWV
