ERG12_GIBZE
ID ERG12_GIBZE Reviewed; 508 AA.
AC I1RPE5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Mevalonate kinase ERG12 {ECO:0000303|PubMed:30874562};
DE Short=MK {ECO:0000305};
DE Short=MvK {ECO:0000305};
DE EC=2.7.1.36 {ECO:0000305|PubMed:30874562};
DE AltName: Full=Ergosterol biosynthesis protein 12 {ECO:0000303|PubMed:30874562};
GN Name=ERG12 {ECO:0000303|PubMed:30874562};
GN ORFNames=FG05912, FGRAMPH1_01T19063;
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.
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: Mevalonate kinase; part of the second module of ergosterol
CC biosynthesis pathway that includes the middle steps of the pathway (By
CC similarity). ERG12 converts mevalonate into 5-phosphomevalonate (By
CC similarity). The second module is carried out in the vacuole and
CC involves the formation of farnesyl diphosphate, which is also an
CC important intermediate in the biosynthesis of ubiquinone, dolichol,
CC heme and prenylated proteins. Activity by the mevalonate kinase ERG12
CC (FG05912) first converts mevalonate into 5-phosphomevalonate. 5-
CC phosphomevalonate is then further converted to 5-diphosphomevalonate by
CC the phosphomevalonate kinase ERG8 (FG09764). The diphosphomevalonate
CC decarboxylase ERG19 (FG10424) then produces isopentenyl diphosphate.
CC The isopentenyl-diphosphate delta-isomerase IDI1 (FG09722) then
CC catalyzes the 1,3-allylic rearrangement of the homoallylic substrate
CC isopentenyl (IPP) to its highly electrophilic allylic isomer,
CC dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate
CC synthase ERG20 (FG06784) catalyzes the sequential condensation of
CC isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then
CC with the resultant geranylpyrophosphate to the ultimate product
CC farnesyl pyrophosphate (Probable). {ECO:0000250|UniProtKB:P07277,
CC ECO:0000305|PubMed:30874562}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+);
CC Xref=Rhea:RHEA:17065, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:36464, ChEBI:CHEBI:58146, ChEBI:CHEBI:456216;
CC EC=2.7.1.36; Evidence={ECO:0000305|PubMed:30874562};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17066;
CC Evidence={ECO:0000305|PubMed:30874562};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P17256};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 1/3. {ECO:0000305|PubMed:30874562}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P17256}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q4WP25}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
CC subfamily. {ECO:0000305}.
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DR EMBL; HG970334; CEF86838.1; -; Genomic_DNA.
DR RefSeq; XP_011324521.1; XM_011326219.1.
DR STRING; 5518.FGSG_05912P0; -.
DR GeneID; 23553064; -.
DR KEGG; fgr:FGSG_05912; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G19063; -.
DR eggNOG; KOG1511; Eukaryota.
DR HOGENOM; CLU_017814_1_0_1; -.
DR InParanoid; I1RPE5; -.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004496; F:mevalonate 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; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR InterPro; IPR006205; Mev_gal_kin.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR43290; PTHR43290; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR00549; mevalon_kin; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Transferase.
FT CHAIN 1..508
FT /note="Mevalonate kinase ERG12"
FT /id="PRO_0000454673"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 267
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q03426"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P17256"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P17256"
FT BINDING 205..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P17256"
FT BINDING 211
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P17256"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P17256"
SQ SEQUENCE 508 AA; 55166 MW; F3A64279D230DC97 CRC64;
MPPSNPAMVN GLNGSHANGN GNGHNHISDS GSETSGESSN GSGRRRMKLN RKMSSPMAPP
FMVSAPGKVI VFGEHSVVHG KAAIAAAISL RSYLHVTTLS KSKRTVSLRF ADIGLVHTWN
IEDLPWEAFQ QPSKKKSYYS LVTELDPDLV AAIQPHIEVV SPNHPEEIRR VHHSSVSAFL
YLFLSLGSPS FPPCLYTLRS TIPIGAGLGS SASVSVCLAS ALLLQLRTLS GPHPDQPADE
ARLQVERINR WAFVSEMCIH GNPSGVDNTV ATQGKAVVFQ RTDYSKPPNV RPLWDFPELP
LLLVDTRQAK STAHEVAKVA KLKQTHPKLV NSILDAMDKV TDAASELIEE TSFDNGSVED
LSKVGELMTI NHGLLVSLGV SHPRLERVRE LVDHEGIGWT KLTGAGGGGC SITLLRPDVP
AEKLQKLEER LETENYAKFE TTLGGDGIGV LWPAVLKNGT EEDEEGGMEI DLEKFLEAEG
TEGVEKLVGV HGDTGEREGW KFWRVESQ
