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Mevalonate kinase (MK) (MvK) (EC 2.7.1.36) (Ergosterol biosynthesis protein 12) (Regulation of autonomous replication protein 1)

 KIME_YEAST              Reviewed;         443 AA.
P07277; D6W033;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
25-OCT-2017, entry version 163.
RecName: Full=Mevalonate kinase;
Short=MK;
Short=MvK;
EC=2.7.1.36;
AltName: Full=Ergosterol biosynthesis protein 12;
AltName: Full=Regulation of autonomous replication protein 1;
Name=ERG12; Synonyms=RAR1; OrderedLocusNames=YMR208W;
ORFNames=YM8261.02;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3323847; DOI=10.1007/BF00327205;
Kearsey S.E., Edwards J.;
"Mutations that increase the mitotic stability of minichromosomes in
yeast: characterization of RAR1.";
Mol. Gen. Genet. 210:509-517(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1645230; DOI=10.1007/BF00362081;
Oulmouden A., Karst F.;
"Nucleotide sequence of the ERG12 gene of Saccharomyces cerevisiae
encoding mevalonate kinase.";
Curr. Genet. 19:9-14(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169872;
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome
XIII.";
Nature 387:90-93(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-246.
STRAIN=SP1;
Saito A., Kazuta Y., Kondo H., Tanabe T.;
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
-!- FUNCTION: May contribute to the regulation of the isoprenoid and
sterol pathway in living cells.
-!- FUNCTION: RAR (regulation of autonomous replication) is a protein
whose activity increases the mitotic stability of plasmids.
-!- CATALYTIC ACTIVITY: ATP + (R)-mevalonate = ADP + (R)-5-
phosphomevalonate.
-!- ENZYME REGULATION: Farnesyl pyrophosphate and geranyl
pyrophosphate inhibit mevalonate kinase by binding competitively
at the ATP-binding site.
-!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
biosynthesis via mevalonate pathway; isopentenyl diphosphate from
(R)-mevalonate: step 1/3.
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- MISCELLANEOUS: Present with 3300 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
subfamily. {ECO:0000305}.
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EMBL; X06114; CAA29487.1; -; Genomic_DNA.
EMBL; X55875; CAA39359.1; -; Genomic_DNA.
EMBL; Z49809; CAA89923.1; -; Genomic_DNA.
EMBL; D78165; BAA24409.1; -; Genomic_DNA.
EMBL; BK006946; DAA10107.1; -; Genomic_DNA.
PIR; S05875; BVBYR1.
RefSeq; NP_013935.1; NM_001182715.1.
ProteinModelPortal; P07277; -.
SMR; P07277; -.
BioGrid; 35386; 88.
IntAct; P07277; 3.
MINT; MINT-4498479; -.
STRING; 4932.YMR208W; -.
iPTMnet; P07277; -.
MaxQB; P07277; -.
PRIDE; P07277; -.
EnsemblFungi; YMR208W; YMR208W; YMR208W.
GeneID; 855248; -.
KEGG; sce:YMR208W; -.
EuPathDB; FungiDB:YMR208W; -.
SGD; S000004821; ERG12.
GeneTree; ENSGT00390000011860; -.
HOGENOM; HOG000188935; -.
InParanoid; P07277; -.
KO; K00869; -.
OMA; EGWKFWR; -.
OrthoDB; EOG092C5126; -.
BioCyc; MetaCyc:YMR208W-MONOMER; -.
BioCyc; YEAST:YMR208W-MONOMER; -.
Reactome; R-SCE-191273; Cholesterol biosynthesis.
UniPathway; UPA00057; UER00098.
PRO; PR:P07277; -.
Proteomes; UP000002311; Chromosome XIII.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004496; F:mevalonate kinase activity; IDA:SGD.
GO; GO:0006696; P:ergosterol biosynthetic process; IMP:SGD.
GO; GO:0010142; P:farnesyl diphosphate biosynthetic process, mevalonate pathway; IMP:SGD.
GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IMP:SGD.
Gene3D; 3.30.230.10; -; 1.
Gene3D; 3.30.70.890; -; 1.
InterPro; IPR036554; GHMP_kinase_C_sf.
InterPro; IPR006204; GHMP_kinase_N_dom.
InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
InterPro; IPR006205; Mev_gal_kin.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
Pfam; PF00288; GHMP_kinases_N; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55060; SSF55060; 1.
TIGRFAMs; TIGR00549; mevalon_kin; 1.
PROSITE; PS00627; GHMP_KINASES_ATP; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Cytoplasm; Kinase; Lipid biosynthesis;
Lipid metabolism; Nucleotide-binding; Reference proteome;
Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
Sterol metabolism; Transferase.
CHAIN 1 443 Mevalonate kinase.
/FTId=PRO_0000156662.
NP_BIND 141 151 ATP. {ECO:0000250}.
ACT_SITE 202 202 Proton acceptor. {ECO:0000250}.
BINDING 138 138 ATP. {ECO:0000250}.
SEQUENCE 443 AA; 48460 MW; 8B24052A72C97280 CRC64;
MSLPFLTSAP GKVIIFGEHS AVYNKPAVAA SVSALRTYLL ISESSAPDTI ELDFPDISFN
HKWSINDFNA ITEDQVNSQK LAKAQQATDG LSQELVSLLD PLLAQLSESF HYHAAFCFLY
MFVCLCPHAK NIKFSLKSTL PIGAGLGSSA SISVSLALAM AYLGGLIGSN DLEKLSENDK
HIVNQWAFIG EKCIHGTPSG IDNAVATYGN ALLFEKDSHN GTINTNNFKF LDDFPAIPMI
LTYTRIPRST KDLVARVRVL VTEKFPEVMK PILDAMGECA LQGLEIMTKL SKCKGTDDEA
VETNNELYEQ LLELIRINHG LLVSIGVSHP GLELIKNLSD DLRIGSTKLT GAGGGGCSLT
LLRRDITQEQ IDSFKKKLQD DFSYETFETD LGGTGCCLLS AKNLNKDLKI KSLVFQLFEN
KTTTKQQIDD LLLPGNTNLP WTS


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