PGTB1_RAT
ID PGTB1_RAT Reviewed; 377 AA.
AC P53610;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Geranylgeranyl transferase type-1 subunit beta;
DE EC=2.5.1.59;
DE AltName: Full=Geranylgeranyl transferase type I subunit beta;
DE Short=GGTase-I-beta;
DE AltName: Full=Type I protein geranyl-geranyltransferase subunit beta;
GN Name=Pggt1b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8106351; DOI=10.1016/s0021-9258(17)41845-x;
RA Zhang F.L., Diehl R.E., Kohl N.E., Gibbs J.B., Giros B., Casey P.J.,
RA Omer C.A.;
RT "cDNA cloning and expression of rat and human protein
RT geranylgeranyltransferase type-I.";
RL J. Biol. Chem. 269:3175-3180(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS;
RP SUBSTRATE PEPTIDE AND ISPRENOID ANALOG, SUBUNIT, COFACTOR, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=14609943; DOI=10.1093/emboj/cdg571;
RA Taylor J.S., Reid T.S., Terry K.L., Casey P.J., Beese L.S.;
RT "Structure of mammalian protein geranylgeranyltransferase type-I.";
RL EMBO J. 22:5963-5974(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS AND
RP INHIBITOR, SUBUNIT, AND COFACTOR.
RX PubMed=15248757; DOI=10.1021/bi049280b;
RA Reid T.S., Long S.B., Beese L.S.;
RT "Crystallographic analysis reveals that anticancer clinical candidate L-
RT 778,123 inhibits protein farnesyltransferase and geranylgeranyltransferase-
RT I by different binding modes.";
RL Biochemistry 43:9000-9008(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH FNTA; ZINC IONS AND
RP SUBSTRATES, SUBUNIT, AND COFACTOR.
RX PubMed=15451670; DOI=10.1016/j.jmb.2004.08.056;
RA Reid T.S., Terry K.L., Casey P.J., Beese L.S.;
RT "Crystallographic analysis of CaaX prenyltransferases complexed with
RT substrates defines rules of protein substrate selectivity.";
RL J. Mol. Biol. 343:417-433(2004).
CC -!- FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from
CC geranylgeranyl diphosphate to a cysteine at the fourth position from
CC the C-terminus of proteins with the C-terminal sequence Cys-aliphatic-
CC aliphatic-X. Known substrates include RAC1, RAC2, RAP1A and RAP1B.
CC {ECO:0000269|PubMed:14609943}.
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;
CC Evidence={ECO:0000269|PubMed:14609943};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:14609943, ECO:0000269|PubMed:15248757,
CC ECO:0000269|PubMed:15451670};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:14609943,
CC ECO:0000269|PubMed:15248757, ECO:0000269|PubMed:15451670};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P18898};
CC -!- SUBUNIT: Heterodimer of FNTA and PGGT1B. PGGT1B mediates interaction
CC with substrate peptides. {ECO:0000269|PubMed:14609943,
CC ECO:0000269|PubMed:15248757, ECO:0000269|PubMed:15451670}.
CC -!- INTERACTION:
CC P53610; Q04631: Fnta; NbExp=7; IntAct=EBI-602610, EBI-602447;
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; L24116; AAA17756.1; -; mRNA.
DR PIR; B53044; B53044.
DR RefSeq; NP_112344.1; NM_031082.1.
DR PDB; 1N4P; X-ray; 2.65 A; B/D/F/H/J/L=1-377.
DR PDB; 1N4Q; X-ray; 2.40 A; B/D/F/H/J/L=1-377.
DR PDB; 1N4R; X-ray; 2.80 A; B/D/F/H/J/L=1-377.
DR PDB; 1N4S; X-ray; 2.60 A; B/D/F/H/J/L=1-377.
DR PDB; 1S64; X-ray; 2.55 A; B/D/F/H/J/L=1-377.
DR PDB; 1TNB; X-ray; 2.85 A; B/D/F/H/J/L=1-377.
DR PDB; 1TNO; X-ray; 2.70 A; B/D/F/H/J/L=1-377.
DR PDB; 1TNU; X-ray; 2.70 A; B/D/F/H/J/L=1-377.
DR PDB; 1TNY; X-ray; 2.70 A; B/D/F/H/J/L=1-377.
DR PDB; 1TNZ; X-ray; 2.90 A; B/D/F/H/J/L=1-377.
DR PDBsum; 1N4P; -.
DR PDBsum; 1N4Q; -.
DR PDBsum; 1N4R; -.
DR PDBsum; 1N4S; -.
DR PDBsum; 1S64; -.
DR PDBsum; 1TNB; -.
DR PDBsum; 1TNO; -.
DR PDBsum; 1TNU; -.
DR PDBsum; 1TNY; -.
DR PDBsum; 1TNZ; -.
DR AlphaFoldDB; P53610; -.
DR SMR; P53610; -.
DR CORUM; P53610; -.
DR DIP; DIP-33953N; -.
DR IntAct; P53610; 2.
DR STRING; 10116.ENSRNOP00000004723; -.
DR BindingDB; P53610; -.
DR ChEMBL; CHEMBL2111479; -.
DR PhosphoSitePlus; P53610; -.
DR PaxDb; P53610; -.
DR PRIDE; P53610; -.
DR Ensembl; ENSRNOT00000004723; ENSRNOP00000004723; ENSRNOG00000003541.
DR GeneID; 81746; -.
DR KEGG; rno:81746; -.
DR UCSC; RGD:621754; rat.
DR CTD; 5229; -.
DR RGD; 621754; Pggt1b.
DR eggNOG; KOG0367; Eukaryota.
DR GeneTree; ENSGT00950000183128; -.
DR HOGENOM; CLU_028946_2_2_1; -.
DR InParanoid; P53610; -.
DR OMA; RWCLMRQ; -.
DR OrthoDB; 1042804at2759; -.
DR PhylomeDB; P53610; -.
DR TreeFam; TF105968; -.
DR BRENDA; 2.5.1.59; 5301.
DR EvolutionaryTrace; P53610; -.
DR PRO; PR:P53610; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000003541; Expressed in ileum and 20 other tissues.
DR Genevisible; P53610; RN.
DR GO; GO:0005953; C:CAAX-protein geranylgeranyltransferase complex; IDA:UniProtKB.
DR GO; GO:0004662; F:CAAX-protein geranylgeranyltransferase activity; IDA:UniProtKB.
DR GO; GO:1901363; F:heterocyclic compound binding; IDA:RGD.
DR GO; GO:0004661; F:protein geranylgeranyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0051771; P:negative regulation of nitric-oxide synthase biosynthetic process; IMP:RGD.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0018344; P:protein geranylgeranylation; IDA:UniProtKB.
DR GO; GO:0018342; P:protein prenylation; IBA:GO_Central.
DR GO; GO:0034097; P:response to cytokine; IMP:RGD.
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 3D-structure; Magnesium; Metal-binding; Prenyltransferase;
KW Reference proteome; Repeat; Transferase; Zinc.
FT CHAIN 1..377
FT /note="Geranylgeranyl transferase type-1 subunit beta"
FT /id="PRO_0000119771"
FT REPEAT 144..186
FT /note="PFTB 1"
FT /evidence="ECO:0000255"
FT REPEAT 193..234
FT /note="PFTB 2"
FT /evidence="ECO:0000255"
FT REPEAT 245..284
FT /note="PFTB 3"
FT /evidence="ECO:0000255"
FT REPEAT 291..333
FT /note="PFTB 4"
FT /evidence="ECO:0000255"
FT BINDING 219..221
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000269|PubMed:14609943,
FT ECO:0007744|PDB:1N4P"
FT BINDING 263..266
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000269|PubMed:14609943,
FT ECO:0007744|PDB:1N4P"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:14609943,
FT ECO:0007744|PDB:1N4P"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:14609943,
FT ECO:0007744|PDB:1N4P"
FT BINDING 272..275
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000269|PubMed:14609943,
FT ECO:0007744|PDB:1N4P"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:14609943,
FT ECO:0007744|PDB:1N4P"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:1N4Q"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:1N4Q"
FT HELIX 47..60
FT /evidence="ECO:0007829|PDB:1N4Q"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1N4Q"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:1N4Q"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1N4Q"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1N4Q"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:1N4Q"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:1N4Q"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:1N4S"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:1N4Q"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:1N4Q"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:1N4Q"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:1N4Q"
FT HELIX 220..233
FT /evidence="ECO:0007829|PDB:1N4Q"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:1N4Q"
FT HELIX 242..253
FT /evidence="ECO:0007829|PDB:1N4Q"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:1N4Q"
FT HELIX 272..282
FT /evidence="ECO:0007829|PDB:1N4Q"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:1N4Q"
FT HELIX 291..299
FT /evidence="ECO:0007829|PDB:1N4Q"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:1N4Q"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:1TNO"
FT HELIX 319..331
FT /evidence="ECO:0007829|PDB:1N4Q"
FT TURN 342..345
FT /evidence="ECO:0007829|PDB:1N4Q"
FT HELIX 348..361
FT /evidence="ECO:0007829|PDB:1N4Q"
SQ SEQUENCE 377 AA; 42414 MW; AADEC7301A4A4011 CRC64;
MAATEDDRLA GSGEGERLDF LRDRHVRFFQ RCLQVLPERY SSLETSRLTI AFFALSGLDM
LDSLDVVNKD DIIEWIYSLQ VLPTEDRSNL DRCGFRGSSY LGIPFNPSKN PGTAHPYDSG
HIAMTYTGLS CLIILGDDLS RVDKEACLAG LRALQLEDGS FCAVPEGSEN DMRFVYCASC
ICYMLNNWSG MDMKKAISYI RRSMSYDNGL AQGAGLESHG GSTFCGIASL CLMGKLEEVF
SEKELNRIKR WCIMRQQNGY HGRPNKPVDT CYSFWVGATL KLLKIFQYTN FEKNRNYILS
TQDRLVGGFA KWPDSHPDAL HAYFGICGLS LMEESGICKV HPALNVSTRT SERLRDLHQS
WKTKDSKQCS DNVHISS
