FNTB_YEAST
ID FNTB_YEAST Reviewed; 431 AA.
AC P22007; D6VRQ8; E9P902; Q12422;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Protein farnesyltransferase subunit beta;
DE Short=FTase-beta;
DE Short=PFTase beta;
DE EC=2.5.1.58 {ECO:0000269|PubMed:17142567, ECO:0000269|PubMed:8424764};
DE AltName: Full=CAAX farnesyltransferase subunit beta;
DE AltName: Full=Ras proteins prenyltransferase subunit beta;
GN Name=RAM1 {ECO:0000303|PubMed:3533274}; Synonyms=DPR1, SCG2, STE16;
GN OrderedLocusNames=YDL090C; ORFNames=D2412;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3064491; DOI=10.1002/yea.320040405;
RA Goodman L.E., Perou C.M., Fujiyama A., Tamanoi F.;
RT "Structure and expression of yeast DPR1, a gene essential for the
RT processing and intracellular localization of ras proteins.";
RL Yeast 4:271-281(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8923743;
RX DOI=10.1002/(sici)1097-0061(199610)12:13%3c1377::aid-yea35%3e3.0.co;2-r;
RA Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G.,
RA Jimenez A., Remacha M.A.;
RT "The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome
RT IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open
RT reading frames.";
RL Yeast 12:1377-1384(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF ASP-209.
RX PubMed=3533274; DOI=10.1016/0092-8674(86)90598-2;
RA Powers S., Michaelis S., Broek D., Santa Anna S., Field J., Herskowitz I.,
RA Wigler M.;
RT "RAM, a gene of yeast required for a functional modification of RAS
RT proteins and for production of mating pheromone a-factor.";
RL Cell 47:413-422(1986).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF GLY-259.
RX PubMed=2124698; DOI=10.1073/pnas.87.24.9665;
RA Goodman L.E., Judd S.R., Farnsworth C.C., Powers S., Gelb M.H.,
RA Glomset J.A., Tamanoi F.;
RT "Mutants of Saccharomyces cerevisiae defective in the farnesylation of Ras
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9665-9669(1990).
RN [8]
RP FUNCTION.
RX PubMed=1860864; DOI=10.1016/s0021-9258(18)98729-6;
RA Moores S.L., Schaber M.D., Mosser S.D., Rands E., O'Hara M.B., Garsky V.M.,
RA Marshall M.S., Pompliano D.L., Gibbs J.B.;
RT "Sequence dependence of protein isoprenylation.";
RL J. Biol. Chem. 266:14603-14610(1991).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=1763050; DOI=10.1073/pnas.88.24.11373;
RA He B., Chen P., Chen S.-Y., Vancura K.L., Michaelis S., Powers S.;
RT "RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide
RT components of the farnesyltransferase that prenylates a-factor and Ras
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:11373-11377(1991).
RN [10]
RP MUTAGENESIS OF ASP-209 AND GLY-259.
RX PubMed=8494894; DOI=10.1021/bi00070a028;
RA Omer C.A., Kral A.M., Diehl R.E., Prendergast G.C., Powers S., Allen C.M.,
RA Gibbs J.B., Kohl N.E.;
RT "Characterization of recombinant human farnesyl-protein transferase:
RT cloning, expression, farnesyl diphosphate binding, and functional homology
RT with yeast prenyl-protein transferases.";
RL Biochemistry 32:5167-5176(1993).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8424764; DOI=10.1042/bj2890025;
RA Gomez R., Goodman L.E., Tripathy S.K., O'Rourke E., Manne V., Tamanoi F.;
RT "Purified yeast protein farnesyltransferase is structurally and
RT functionally similar to its mammalian counterpart.";
RL Biochem. J. 289:25-31(1993).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8527442; DOI=10.1021/bi00051a017;
RA Dolence J.M., Cassidy P.B., Mathis J.R., Poulter C.D.;
RT "Yeast protein farnesyltransferase: steady-state kinetic studies of
RT substrate binding.";
RL Biochemistry 34:16687-16694(1995).
RN [13]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7651159; DOI=10.1016/0076-6879(95)50060-x;
RA Cassidy P.B., Dolence J.M., Poulter C.D.;
RT "Continuous fluorescence assay for protein prenyltransferases.";
RL Methods Enzymol. 250:30-43(1995).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF SER-159.
RX PubMed=7878044; DOI=10.1073/pnas.92.5.1704;
RA Mitsuzawa H., Esson K., Tamanoi F.;
RT "Mutant farnesyltransferase beta subunit of Saccharomyces cerevisiae that
RT can substitute for geranylgeranyltransferase type I beta subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:1704-1708(1995).
RN [15]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9174352; DOI=10.1021/bi9629182;
RA Mathis J.R., Poulter C.D.;
RT "Yeast protein farnesyltransferase: a pre-steady-state kinetic analysis.";
RL Biochemistry 36:6367-6376(1997).
RN [16]
RP MUTAGENESIS OF SER-159; TYR-362 AND TYR-366.
RX PubMed=8995312; DOI=10.1074/jbc.272.1.680;
RA Del Villar K., Mitsuzawa H., Yang W., Sattler I., Tamanoi F.;
RT "Amino acid substitutions that convert the protein substrate specificity of
RT farnesyltransferase to that of geranylgeranyltransferase type I.";
RL J. Biol. Chem. 272:680-687(1997).
RN [17]
RP MUTAGENESIS OF GLY-149.
RX PubMed=9380709; DOI=10.1073/pnas.94.20.10774;
RA Trueblood C.E., Boyartchuk V.L., Rine J.;
RT "Substrate specificity determinants in the farnesyltransferase beta-
RT subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:10774-10779(1997).
RN [18]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP 57-ARG--VAL-64; ILE-74; 206-GLY--GLY-212; GLY-308 AND 351-LEU--LYS-354.
RX PubMed=9545274; DOI=10.1074/jbc.273.16.9472;
RA Caplin B.E., Ohya Y., Marshall M.S.;
RT "Amino acid residues that define both the isoprenoid and CAAX preferences
RT of the Saccharomyces cerevisiae protein farnesyltransferase. Creating the
RT perfect farnesyltransferase.";
RL J. Biol. Chem. 273:9472-9479(1998).
RN [19]
RP COFACTOR, AND MUTAGENESIS OF TYR-310.
RX PubMed=10529185; DOI=10.1021/bi990794y;
RA Rozema D.B., Poulter C.D.;
RT "Yeast protein farnesyltransferase. pKas of peptide substrates bound as
RT zinc thiolates.";
RL Biochemistry 38:13138-13146(1999).
RN [20]
RP REACTION MECHANISM, AND COFACTOR.
RX PubMed=12173942; DOI=10.1021/bi020349u;
RA Harris C.M., Derdowski A.M., Poulter C.D.;
RT "Modulation of the zinc(II) center in protein farnesyltransferase by
RT mutagenesis of the zinc(II) ligands.";
RL Biochemistry 41:10554-10562(2002).
RN [21]
RP SUBSTRATE SPECIFICITY.
RX PubMed=12667062; DOI=10.1021/bi0266838;
RA Turek-Etienne T.C., Strickland C.L., Distefano M.D.;
RT "Biochemical and structural studies with prenyl diphosphate analogues
RT provide insights into isoprenoid recognition by protein farnesyl
RT transferase.";
RL Biochemistry 42:3716-3724(2003).
RN [22]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [23]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [24]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17142567; DOI=10.1128/ec.00203-06;
RA Grabinska K.A., Magnelli P., Robbins P.W.;
RT "Prenylation of Saccharomyces cerevisiae Chs4p Affects Chitin Synthase III
RT activity and chitin chain length.";
RL Eukaryot. Cell 6:328-336(2007).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Catalyzes the transfer of a farnesyl moiety from farnesyl
CC diphosphate to a cysteine at the fourth position from the C-terminus of
CC several proteins having the C-terminal sequence Cys-aliphatic-
CC aliphatic-X where X is Ser, Ala, Met, Cys, or Gln. Required for the
CC membrane localization of proteins such as a-factor, Ras proteins and
CC other membrane proteins containing the C-terminal CAAX motif
CC (PubMed:3533274, PubMed:2124698, PubMed:1860864, PubMed:1763050,
CC PubMed:8424764, PubMed:8527442, PubMed:17142567). The beta subunit is
CC responsible for isoprenoid and peptide-binding (PubMed:7878044,
CC PubMed:8995312, PubMed:9380709, PubMed:9545274, PubMed:12667062).
CC {ECO:0000269|PubMed:12667062, ECO:0000269|PubMed:17142567,
CC ECO:0000269|PubMed:1763050, ECO:0000269|PubMed:1860864,
CC ECO:0000269|PubMed:2124698, ECO:0000269|PubMed:3533274,
CC ECO:0000269|PubMed:7878044, ECO:0000269|PubMed:8424764,
CC ECO:0000269|PubMed:8527442, ECO:0000269|PubMed:8995312,
CC ECO:0000269|PubMed:9380709, ECO:0000269|PubMed:9545274}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] =
CC diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:13345, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11535,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:86019,
CC ChEBI:CHEBI:175763; EC=2.5.1.58;
CC Evidence={ECO:0000269|PubMed:17142567, ECO:0000269|PubMed:8424764,
CC ECO:0000269|PubMed:8527442, ECO:0000269|PubMed:9174352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13346;
CC Evidence={ECO:0000269|PubMed:17142567, ECO:0000269|PubMed:8424764,
CC ECO:0000269|PubMed:8527442, ECO:0000269|PubMed:9174352};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:10529185, ECO:0000269|PubMed:12173942};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:12173942};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.1 uM for farnesyl diphosphate {ECO:0000269|PubMed:8424764};
CC KM=0.16 uM for farnesyl diphosphate {ECO:0000269|PubMed:9545274};
CC KM=0.9 uM for dansyl-GCVIA {ECO:0000269|PubMed:8527442};
CC KM=3.59 uM for geranylgeranyl diphosphate
CC {ECO:0000269|PubMed:9545274};
CC KM=0.46 uM for Ras-CIIS {ECO:0000269|PubMed:9545274};
CC KM=4.12 uM for Ras-CIIM (for farnesyl transferase reaction)
CC {ECO:0000269|PubMed:9545274};
CC KM=0.28 uM for Ras-CIIM (for geranyl-geranyl transferase reaction)
CC {ECO:0000269|PubMed:9545274};
CC KM=10.2 uM for Ras-CIIL {ECO:0000269|PubMed:9545274};
CC Vmax=3.4 umol/min/mg enzyme {ECO:0000269|PubMed:8527442};
CC Note=kcat is 4.5 sec(-1) with dansyl-GCVIA as substrate.
CC {ECO:0000269|PubMed:8527442};
CC pH dependence:
CC Optimum pH is 7.8. {ECO:0000269|PubMed:8424764};
CC -!- SUBUNIT: Heterodimer of an alpha (RAM2) and a beta (RAM1) subunit.
CC {ECO:0000269|PubMed:1763050, ECO:0000269|PubMed:8424764}.
CC -!- INTERACTION:
CC P22007; P29703: RAM2; NbExp=3; IntAct=EBI-14806, EBI-14814;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Decreases SKT5 farnesylation.
CC {ECO:0000269|PubMed:17142567}.
CC -!- MISCELLANEOUS: Present with 3910 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; M22753; AAA34579.1; -; Genomic_DNA.
DR EMBL; X95644; CAA64921.1; -; Genomic_DNA.
DR EMBL; Z74138; CAA98656.1; -; Genomic_DNA.
DR EMBL; AY692971; AAT92990.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11768.1; -; Genomic_DNA.
DR PIR; S67626; BVBYDP.
DR RefSeq; NP_010193.1; NM_001180149.1.
DR AlphaFoldDB; P22007; -.
DR SMR; P22007; -.
DR BioGRID; 31970; 246.
DR ComplexPortal; CPX-1634; Protein farnesyltransferase complex.
DR DIP; DIP-1556N; -.
DR IntAct; P22007; 10.
DR MINT; P22007; -.
DR STRING; 4932.YDL090C; -.
DR BindingDB; P22007; -.
DR ChEMBL; CHEMBL2111393; -.
DR iPTMnet; P22007; -.
DR MaxQB; P22007; -.
DR PaxDb; P22007; -.
DR PRIDE; P22007; -.
DR EnsemblFungi; YDL090C_mRNA; YDL090C; YDL090C.
DR GeneID; 851468; -.
DR KEGG; sce:YDL090C; -.
DR SGD; S000002248; RAM1.
DR VEuPathDB; FungiDB:YDL090C; -.
DR eggNOG; KOG0365; Eukaryota.
DR GeneTree; ENSGT00950000183128; -.
DR HOGENOM; CLU_028946_0_2_1; -.
DR InParanoid; P22007; -.
DR OMA; GADYYHT; -.
DR BioCyc; YEAST:MON3O-269; -.
DR BRENDA; 2.5.1.58; 984.
DR Reactome; R-SCE-9648002; RAS processing.
DR PRO; PR:P22007; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P22007; protein.
DR GO; GO:0005965; C:protein farnesyltransferase complex; IDA:SGD.
DR GO; GO:0004660; F:protein farnesyltransferase activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0018343; P:protein farnesylation; IDA:UniProtKB.
DR GO; GO:0018342; P:protein prenylation; IBA:GO_Central.
DR CDD; cd02893; FTase; 1.
DR InterPro; IPR026872; FTB.
DR InterPro; IPR001330; PFTB_repeat.
DR InterPro; IPR045089; PGGT1B-like.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11774; PTHR11774; 1.
DR PANTHER; PTHR11774:SF6; PTHR11774:SF6; 1.
DR Pfam; PF00432; Prenyltrans; 5.
DR SUPFAM; SSF48239; SSF48239; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Prenyltransferase; Reference proteome; Repeat;
KW Transferase; Zinc.
FT CHAIN 1..431
FT /note="Protein farnesyltransferase subunit beta"
FT /id="PRO_0000119768"
FT REPEAT 130..171
FT /note="PFTB 1"
FT /evidence="ECO:0000255"
FT REPEAT 182..224
FT /note="PFTB 2"
FT /evidence="ECO:0000255"
FT REPEAT 231..273
FT /note="PFTB 3"
FT /evidence="ECO:0000255"
FT REPEAT 280..322
FT /note="PFTB 4"
FT /evidence="ECO:0000255"
FT REPEAT 332..375
FT /note="PFTB 5"
FT /evidence="ECO:0000255"
FT BINDING 258..261
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 301..304
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P49356,
FT ECO:0000305|PubMed:10529185, ECO:0000305|PubMed:12173942"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P49356,
FT ECO:0000305|PubMed:10529185, ECO:0000305|PubMed:12173942"
FT BINDING 310..313
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P49356,
FT ECO:0000305|PubMed:10529185, ECO:0000305|PubMed:12173942"
FT SITE 108
FT /note="Important for selectivity against geranylgeranyl
FT diphosphate"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT MUTAGEN 57..64
FT /note="RYKVLQSV->HYKFFQRH: Impairs isoprenyl transferase
FT activity."
FT /evidence="ECO:0000269|PubMed:9545274"
FT MUTAGEN 74
FT /note="I->D: Farnesylates only Ras-CIIS and not Ras-
FT CII(M,L), and it geranylgeranylates all three substrates as
FT well or better than wild type."
FT /evidence="ECO:0000269|PubMed:9545274"
FT MUTAGEN 149
FT /note="G->D,E: Alters protein substrate specificity. Able
FT to farnesylate Ras2 variants with positively charged C-
FT terminal amino acids (CIIR and CIIK)."
FT /evidence="ECO:0000269|PubMed:9380709"
FT MUTAGEN 149
FT /note="G->R,K: Alters protein substrate specificity. Able
FT to farnesylate Ras2 variants with a negatively charged C-
FT terminal aspartate (CIID)."
FT /evidence="ECO:0000269|PubMed:9380709"
FT MUTAGEN 159
FT /note="S->D,N: Can substitute for PGGT-I beta subunit
FT (CDC43) in vivo. Has increased activity to farnesylate a
FT substrate for PGGT-I. On the other hand, the ability to
FT farnesylate its own substrate is reduced, due to its
FT increased affinity for PGGT-I protein substrates. Increases
FT the kcat/Km value for PGGTase-I substrates about 20-fold."
FT /evidence="ECO:0000269|PubMed:7878044,
FT ECO:0000269|PubMed:8995312"
FT MUTAGEN 206..212
FT /note="GEVDTRG->DEDDLRF: Farnesylates Ras-CII(S,M,L) at
FT wild type levels but can no longer geranylgeranylate the
FT RasCII(M,L) substrates."
FT /evidence="ECO:0000269|PubMed:9545274"
FT MUTAGEN 209
FT /note="D->N: In ram1-1; causes a defect in a-factor
FT production."
FT /evidence="ECO:0000269|PubMed:2124698,
FT ECO:0000269|PubMed:8494894"
FT MUTAGEN 259
FT /note="G->V: In ram1-2; abolishes farnesyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:1860864,
FT ECO:0000269|PubMed:8494894"
FT MUTAGEN 308
FT /note="G->T: Impairs isoprenyl transferase activity."
FT /evidence="ECO:0000269|PubMed:9545274"
FT MUTAGEN 310
FT /note="Y->K: Impairs isoprenyl transferase activity."
FT /evidence="ECO:0000269|PubMed:10529185"
FT MUTAGEN 351..354
FT /note="LRDK->FSKN: Farnesylates Ras-CIIS and Ras-CIIM but
FT not Ras-CIIL, and is not capable of geranylgeranylating the
FT Ras-CII(M,L) substrates."
FT /evidence="ECO:0000269|PubMed:9545274"
FT MUTAGEN 362
FT /note="Y->H: Can substitute for PGGT-I beta subunit, by
FT modulating the substrate specificity for the peptide
FT substrate."
FT /evidence="ECO:0000269|PubMed:8995312"
FT MUTAGEN 362
FT /note="Y->L,M,I: Can substitute for PGGT-I beta subunit, by
FT modulating the substrate specificity for the peptide
FT substrate. Increases the kcat/Km value for PGGTase-I
FT substrates about 20-fold."
FT /evidence="ECO:0000269|PubMed:8995312"
FT MUTAGEN 366
FT /note="Y->N: Can substitute for PGGT-I beta subunit, by
FT modulating the substrate specificity for the peptide
FT substrate."
FT /evidence="ECO:0000269|PubMed:8995312"
FT CONFLICT 47
FT /note="K -> R (in Ref. 5; AAT92990)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 48190 MW; 2E3B64F30D2FF13A CRC64;
MRQRVGRSIA RAKFINTALL GRKRPVMERV VDIAHVDSSK AIQPLMKELE TDTTEARYKV
LQSVLEIYDD EKNIEPALTK EFHKMYLDVA FEISLPPQMT ALDASQPWML YWIANSLKVM
DRDWLSDDTK RKIVDKLFTI SPSGGPFGGG PGQLSHLAST YAAINALSLC DNIDGCWDRI
DRKGIYQWLI SLKEPNGGFK TCLEVGEVDT RGIYCALSIA TLLNILTEEL TEGVLNYLKN
CQNYEGGFGS CPHVDEAHGG YTFCATASLA ILRSMDQINV EKLLEWSSAR QLQEERGFCG
RSNKLVDGCY SFWVGGSAAI LEAFGYGQCF NKHALRDYIL YCCQEKEQPG LRDKPGAHSD
FYHTNYCLLG LAVAESSYSC TPNDSPHNIK CTPDRLIGSS KLTDVNPVYG LPIENVRKII
HYFKSNLSSP S
