ID   PGTB1_DICDI             Reviewed;         352 AA.
AC   Q55DA3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   10-JUN-2026, entry version 95.
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; ORFNames=DDB_G0269726;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
CC       geranyl-geranyl pyrophosphate to a cysteine at the fourth position from
CC       the C-terminus of proteins having the C-terminal sequence Cys-
CC       aliphatic-aliphatic-X. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] = S-
CC         geranylgeranyl-L-cysteinyl-[protein] + diphosphate;
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P53610};
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:0000250|UniProtKB:P18898};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC       family. {ECO:0000305}.
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DR   EMBL; AAFI02000005; EAL72213.1; -; Genomic_DNA.
DR   RefSeq; XP_646228.1; XM_641136.1.
DR   AlphaFoldDB; Q55DA3; -.
DR   SMR; Q55DA3; -.
DR   FunCoup; Q55DA3; 112.
DR   STRING; 44689.Q55DA3; -.
DR   PaxDb; 44689-Q55DA3; -.
DR   GeneID; 8617182; -.
DR   KEGG; ddi:DDB_G0269726; -.
DR   dictyBase; DDB_G0269726; pggt1b.
DR   VEuPathDB; AmoebaDB:DDB_G0269726; -.
DR   InParanoid; Q55DA3; -.
DR   OMA; RWCLMRQ; -.
DR   PhylomeDB; Q55DA3; -.
DR   Reactome; R-DDI-9953170; GBP-mediated host defense.
DR   PRO; PR:Q55DA3; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005953; C:CAAX-protein geranylgeranyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0004662; F:CAAX-protein geranylgeranyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0004661; F:protein geranylgeranyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0018344; P:protein geranylgeranylation; ISS:UniProtKB.
DR   CDD; cd02895; GGTase-I; 1.
DR   FunFam; 1.50.10.20:FF:000040; Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid; 1.
DR   Gene3D; 1.50.10.20; -; 1.
DR   InterPro; IPR041960; GGTase_I_beta.
DR   InterPro; IPR045089; PGGT1B-like.
DR   InterPro; IPR001330; Prenyltrans.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11774; GERANYLGERANYL TRANSFERASE TYPE BETA SUBUNIT; 1.
DR   PANTHER; PTHR11774:SF4; GERANYLGERANYL TRANSFERASE TYPE-1 SUBUNIT BETA; 1.
DR   Pfam; PF00432; Prenyltrans; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE   2: Evidence at transcript level;
KW   Magnesium; Metal-binding; Prenyltransferase; Reference proteome; Repeat;
KW   Transferase; Zinc.
FT   CHAIN           1..352
FT                   /note="Geranylgeranyl transferase type-1 subunit beta"
FT                   /id="PRO_0000330936"
FT   REPEAT          135..180
FT                   /note="PFTB 1"
FT   REPEAT          187..228
FT                   /note="PFTB 2"
FT   REPEAT          236..276
FT                   /note="PFTB 3"
FT   REPEAT          283..325
FT                   /note="PFTB 4"
FT   BINDING         213..215
FT                   /ligand="geranylgeranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57533"
FT                   /evidence="ECO:0000250|UniProtKB:P53610"
FT   BINDING         255..258
FT                   /ligand="geranylgeranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57533"
FT                   /evidence="ECO:0000250|UniProtKB:P53610"
FT   BINDING         261
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P53610"
FT   BINDING         263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P53610"
FT   BINDING         264..267
FT                   /ligand="geranylgeranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57533"
FT                   /evidence="ECO:0000250|UniProtKB:P53610"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P53610"
SQ   SEQUENCE   352 AA;  39168 MW;  3E8A27894C60C97A CRC64;
     MGSCINEEKL AKFFQRSLNA LPAPYTSGLP NHLSLIFFVV SGLDLLNKTD ILEKEKQDII
     NWVYSRQILP SKDNPEINLE NCGFRGYNFL GQEFCCDKSV HTSENGPLEY DLPSTPNTYC
     ALLILRILGD DFSGVNKKAI IDSLRKRQRE SDGAISGSPN VGDYDLRHLF SACAISFILD
     DWSAINKESA IDYIKSCLSY EFAFGQTPQQ EAHGGPTYCA IASLSLLGRL DVLEPFKEQL
     TFWLVKKQIT GFCGRTNKDP DTCYAFWIGA SLMMIDRYDL IDFASINAFI GSAQHEAIGG
     VAKEPGQLPD VMHSYLSLVG LSFGNIPSIQ QVIPCLNLSK RAAGKDWFEK LI
//