PGTB1_YEAST
ID PGTB1_YEAST Reviewed; 376 AA.
AC P18898; D6VTZ6;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Geranylgeranyl transferase type-1 subunit beta;
DE Short=GGTase-I-beta;
DE EC=2.5.1.59 {ECO:0000269|PubMed:1400380, ECO:0000269|PubMed:7639519, ECO:0000269|PubMed:9109664};
DE AltName: Full=Cell division cycle protein 43;
DE AltName: Full=Geranylgeranyl transferase type I subunit beta;
DE AltName: Full=RAS proteins geranylgeranyltransferase subunit beta;
DE AltName: Full=Type I protein geranyl-geranyltransferase subunit beta;
DE Short=PGGTase I beta;
GN Name=CDC43; Synonyms=CAL1; OrderedLocusNames=YGL155W; ORFNames=G1864;
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 PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2199333; DOI=10.1016/0378-1119(90)90443-u;
RA Johnson D.I., O'Brien J.M., Jacobs C.W.;
RT "Isolation and sequence analysis of CDC43, a gene involved in the control
RT of cell polarity in Saccharomyces cerevisiae.";
RL Gene 90:93-98(1990).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=2013407; DOI=10.1016/0378-1119(91)90119-v;
RA Johnson D.I., O'Brien J.M., Jacobs C.W.;
RT "Isolation and sequence analysis of CDC43, a gene involved in the control
RT of cell polarity in Saccharomyces cerevisiae.";
RL Gene 98:149-150(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A5-8-1A;
RX PubMed=2061313; DOI=10.1016/s0021-9258(18)98904-0;
RA Ohya Y., Goebl M., Goodman L.E., Petersen-Bjoern S., Friesen J.D.,
RA Tamanoi F., Anraku Y.;
RT "Yeast CAL1 is a structural and functional homologue to the DPR1 (RAM) gene
RT involved in ras processing.";
RL J. Biol. Chem. 266:12356-12360(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8585324; DOI=10.1002/yea.320111409;
RA James C.M., Indge K.J., Oliver S.G.;
RT "DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae
RT chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2,
RT PMR1, RCK1, AMS1 and CAL1/CDC43.";
RL Yeast 11:1413-1419(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [6]
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 [7]
RP MUTAGENESIS OF GLY-328.
RX PubMed=6369073; DOI=10.1007/bf00382073;
RA Ohya Y., Ohsumi Y., Anraku Y.;
RT "Genetic study of the role of calcium ions in the cell division cycle of
RT Saccharomyces cerevisiae: a calcium-dependent mutant and its
RT trifluoperazine-dependent pseudorevertants.";
RL Mol. Gen. Genet. 193:389-394(1984).
RN [8]
RP SUBUNIT.
RX PubMed=1918005; DOI=10.1016/s0021-9258(18)55146-2;
RA Kohl N.E., Diehl R.E., Schaber M.D., Rands E., Soderman D.D., He B.,
RA Moores S.L., Pompliano D.L., Ferro-Novick S., Powers S., Thomas K.A.,
RA Gibbs J.B.;
RT "Structural homology among mammalian and Saccharomyces cerevisiae
RT isoprenyl-protein transferases.";
RL J. Biol. Chem. 266:18884-18888(1991).
RN [9]
RP FUNCTION.
RX PubMed=2034682; DOI=10.1073/pnas.88.10.4448;
RA Finegold A.A., Johnson D.I., Farnsworth C.C., Gelb M.H., Judd S.R.,
RA Glomset J.A., Tamanoi F.;
RT "Protein geranylgeranyltransferase of Saccharomyces cerevisiae is specific
RT for Cys-Xaa-Xaa-Leu motif proteins and requires the CDC43 gene product but
RT not the DPR1 gene product.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4448-4452(1991).
RN [10]
RP FUNCTION, SUBUNIT, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1400380; DOI=10.1016/s0021-9258(19)36727-4;
RA Mayer M.L., Caplin B.E., Marshall M.S.;
RT "CDC43 and RAM2 encode the polypeptide subunits of a yeast type I protein
RT geranylgeranyltransferase.";
RL J. Biol. Chem. 267:20589-20593(1992).
RN [11]
RP ERRATUM.
RA Mayer M.L., Caplin B.E., Marshall M.S.;
RL J. Biol. Chem. 268:4568-4568(1993).
RN [12]
RP MUTAGENESIS OF GLY-328.
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 [13]
RP SUBUNIT, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7639519; DOI=10.1006/abbi.1995.1384;
RA Stirtan W.G., Poulter C.D.;
RT "Yeast protein geranylgeranyltransferase type-I: overproduction,
RT purification, and characterization.";
RL Arch. Biochem. Biophys. 321:182-190(1995).
RN [14]
RP MUTAGENESIS OF SER-85; CYS-138; ALA-171 AND ARG-280.
RX PubMed=8804398; DOI=10.1007/bf02173199;
RA Ohya Y., Caplin B.E., Qadota H., Tibbetts M.F., Anraku Y., Pringle J.R.,
RA Marshall M.S.;
RT "Mutational analysis of the beta-subunit of yeast geranylgeranyl
RT transferase I.";
RL Mol. Gen. Genet. 252:1-10(1996).
RN [15]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9109664; DOI=10.1021/bi962579c;
RA Stirtan W.G., Poulter C.D.;
RT "Yeast protein geranylgeranyltransferase type-I: steady-state kinetics and
RT substrate binding.";
RL Biochemistry 36:4552-4557(1997).
RN [16]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-166; HIS-216 AND
RP ASN-282.
RX PubMed=10491163; DOI=10.1046/j.1432-1327.1999.00686.x;
RA Kim H., Yang C.H.;
RT "Active site determination of yeast geranylgeranyl protein transferase type
RT I expressed in Escherichia coli.";
RL Eur. J. Biochem. 265:105-111(1999).
RN [17]
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 [18]
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).
CC -!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
CC geranyl-geranyl diphosphate to proteins having the C-terminal sequence
CC Cys-Ile-Ile-Leu or Cys-Val-Leu-Leu. Acts, among other substrates, on
CC Rho1 and Rho2 and CDC42 proteins. Participates in a RAS-like C-terminal
CC modification of proteins involved in nuclear division and bud growth.
CC It is involved in bud positioning and cell polarity (PubMed:2034682,
CC PubMed:1400380). The beta subunit is responsible for isoprenoid and
CC peptide-binding (PubMed:9109664, PubMed:10491163).
CC {ECO:0000269|PubMed:10491163, ECO:0000269|PubMed:1400380,
CC ECO:0000269|PubMed:2034682, ECO:0000269|PubMed:9109664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] =
CC diphosphate + S-geranylgeranyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533,
CC ChEBI:CHEBI:86021; EC=2.5.1.59; Evidence={ECO:0000269|PubMed:1400380,
CC ECO:0000269|PubMed:7639519, ECO:0000269|PubMed:9109664};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21241;
CC Evidence={ECO:0000269|PubMed:1400380, ECO:0000269|PubMed:7639519,
CC ECO:0000269|PubMed:9109664};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:7639519};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P53610};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:1400380, ECO:0000269|PubMed:7639519};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for geranylgeranyl diphosphate {ECO:0000269|PubMed:7639519};
CC KM=0.86 uM for geranylgeranyl diphosphate
CC {ECO:0000269|PubMed:9109664};
CC KM=0.12 uM for geranylgeranyl diphosphate
CC {ECO:0000269|PubMed:10491163};
CC KM=2.4 uM for dansyl-GCIIL {ECO:0000269|PubMed:7639519};
CC KM=1.6 uM for dansyl-GCIIL {ECO:0000269|PubMed:9109664};
CC KM=0.68 uM for GST-CAIL {ECO:0000269|PubMed:10491163};
CC Vmax=0.2 umol/min/mg enzyme {ECO:0000269|PubMed:7639519};
CC Note=kcat is 0.34 sec(-1) with dansyl-GCIIL as substrate
CC (PubMed:9109664). kcat is 4.8 sec(-1) with GST-CAIL as substrate
CC (PubMed:10491163). {ECO:0000269|PubMed:10491163,
CC ECO:0000269|PubMed:9109664};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:1400380,
CC ECO:0000269|PubMed:7639519};
CC -!- SUBUNIT: Heterodimer of an alpha (RAM2) and a beta (CDC43) subunit.
CC {ECO:0000269|PubMed:1400380, ECO:0000305|PubMed:1918005}.
CC -!- INTERACTION:
CC P18898; P29703: RAM2; NbExp=3; IntAct=EBI-3961, EBI-14814;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3940 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; M31114; AAA34481.1; -; Genomic_DNA.
DR EMBL; M74109; AAA34464.1; -; Genomic_DNA.
DR EMBL; Z48618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z72677; CAA96867.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07957.1; -; Genomic_DNA.
DR PIR; A40875; RGBY43.
DR RefSeq; NP_011360.1; NM_001181020.1.
DR AlphaFoldDB; P18898; -.
DR SMR; P18898; -.
DR BioGRID; 33099; 228.
DR ComplexPortal; CPX-1635; Protein geranylgeranyltransferase type I complex.
DR DIP; DIP-1232N; -.
DR IntAct; P18898; 1.
DR MINT; P18898; -.
DR STRING; 4932.YGL155W; -.
DR MaxQB; P18898; -.
DR PaxDb; P18898; -.
DR PRIDE; P18898; -.
DR EnsemblFungi; YGL155W_mRNA; YGL155W; YGL155W.
DR GeneID; 852722; -.
DR KEGG; sce:YGL155W; -.
DR SGD; S000003123; CDC43.
DR VEuPathDB; FungiDB:YGL155W; -.
DR eggNOG; KOG0367; Eukaryota.
DR GeneTree; ENSGT00950000183128; -.
DR HOGENOM; CLU_028946_2_1_1; -.
DR InParanoid; P18898; -.
DR OMA; RWCLMRQ; -.
DR BioCyc; YEAST:YGL155W-MON; -.
DR PRO; PR:P18898; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P18898; protein.
DR GO; GO:0005953; C:CAAX-protein geranylgeranyltransferase complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004662; F:CAAX-protein geranylgeranyltransferase activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0018344; P:protein geranylgeranylation; IDA:SGD.
DR GO; GO:0018342; P:protein prenylation; IBA:GO_Central.
DR CDD; cd02895; GGTase-I; 1.
DR InterPro; IPR041960; GGTase_I_beta.
DR InterPro; IPR001330; PFTB_repeat.
DR InterPro; IPR045089; PGGT1B-like.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11774; PTHR11774; 1.
DR Pfam; PF00432; Prenyltrans; 4.
DR SUPFAM; SSF48239; SSF48239; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Magnesium; Metal-binding; Prenyltransferase; Reference proteome;
KW Repeat; Transferase; Zinc.
FT CHAIN 1..376
FT /note="Geranylgeranyl transferase type-1 subunit beta"
FT /id="PRO_0000119775"
FT REPEAT 128..179
FT /note="PFTB 1"
FT /evidence="ECO:0000255"
FT REPEAT 192..231
FT /note="PFTB 2"
FT /evidence="ECO:0000255"
FT REPEAT 259..301
FT /note="PFTB 3"
FT /evidence="ECO:0000255"
FT REPEAT 310..353
FT /note="PFTB 4"
FT /evidence="ECO:0000255"
FT BINDING 216..218
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 280..283
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 289..292
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT MUTAGEN 85
FT /note="S->F: In cdc43-2; severely impairs the
FT geranylgeranyl transferase activity."
FT /evidence="ECO:0000269|PubMed:8804398"
FT MUTAGEN 138
FT /note="C->Y: In cdc43-3; severely impairs the
FT geranylgeranyl transferase activity."
FT /evidence="ECO:0000269|PubMed:8804398"
FT MUTAGEN 166
FT /note="R->I: Increases KM for isoprenoid substrate 29-
FT fold."
FT /evidence="ECO:0000269|PubMed:10491163"
FT MUTAGEN 171
FT /note="A->V,T: In cdc43-4,5,6; severely impairs the
FT geranylgeranyl transferase activity."
FT /evidence="ECO:0000269|PubMed:8804398"
FT MUTAGEN 216
FT /note="H->D: Increases KM for peptide substrate 12-fold."
FT /evidence="ECO:0000269|PubMed:10491163"
FT MUTAGEN 280
FT /note="R->C: In cdc43-7; severely impairs the
FT geranylgeranyl transferase activity."
FT /evidence="ECO:0000269|PubMed:8804398"
FT MUTAGEN 282
FT /note="N->A: Decreases catalytic activity 2-fold, but
FT retains substrate binding properties."
FT /evidence="ECO:0000269|PubMed:10491163"
FT MUTAGEN 328
FT /note="G->S: In cal1-1; completely abolishes geranylgeranyl
FT transferase activity. Displays a defect in nuclear division
FT and bud formation."
FT /evidence="ECO:0000269|PubMed:6369073,
FT ECO:0000269|PubMed:8494894, ECO:0000269|PubMed:8804398"
SQ SEQUENCE 376 AA; 42690 MW; B52E56F353B3914E CRC64;
MCQATNGPSR VVTKKHRKFF ERHLQLLPSS HQGHDVNRMA IIFYSISGLS IFDVNVSAKY
GDHLGWMRKH YIKTVLDDTE NTVISGFVGS LVMNIPHATT INLPNTLFAL LSMIMLRDYE
YFETILDKRS LARFVSKCQR PDRGSFVSCL DYKTNCGSSV DSDDLRFCYI AVAILYICGC
RSKEDFDEYI DTEKLLGYIM SQQCYNGAFG AHNEPHSGYT SCALSTLALL SSLEKLSDKF
KEDTITWLLH RQVSSHGCMK FESELNASYD QSDDGGFQGR ENKFADTCYA FWCLNSLHLL
TKDWKMLCQT ELVTNYLLDR TQKTLTGGFS KNDEEDADLY HSCLGSAALA LIEGKFNGEL
CIPQEIFNDF SKRCCF
