PGTB1_SCHPO
ID PGTB1_SCHPO Reviewed; 355 AA.
AC P32434;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Geranylgeranyl transferase type-1 subunit beta;
DE EC=2.5.1.59 {ECO:0000269|PubMed:9781874};
DE AltName: Full=Geranylgeranyl transferase type I subunit beta;
DE Short=GGTase-I-beta;
DE AltName: Full=Type I protein geranyl-geranyltransferase subunit beta;
DE Short=PGGT;
GN Name=cwg2; ORFNames=SPAC2E1P5.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=8262067; DOI=10.1002/j.1460-2075.1993.tb06220.x;
RA Diaz M., Sanchez Y., Bennett T., Dun C.R., Godoy C., Tamanoi F., Duran A.,
RA Perez P.;
RT "The Schizosaccharomyces pombe cwg2+ gene codes for the beta subunit of a
RT geranylgeranyltransferase type I required for beta-glucan synthesis.";
RL EMBO J. 12:5245-5254(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=9781874; DOI=10.1046/j.1365-2958.1998.01009.x;
RA Arellano M., Coll P.M., Yang W., Duran A., Tamanoi F., Perez P.;
RT "Characterization of the geranylgeranyl transferase type I from
RT Schizosaccharomyces pombe.";
RL Mol. Microbiol. 29:1357-1367(1998).
CC -!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
CC geranyl-geranyl pyrophosphate to proteins having the C-terminal C-A-A-L
CC where A is an aliphatic amino acid (PubMed:8262067, PubMed:9781874). In
CC particular it modifies the GTP-binding component of the 1,3-beta-D-
CC glucan synthase (PubMed:8262067). {ECO:0000269|PubMed:8262067,
CC ECO:0000269|PubMed:9781874}.
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:9781874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21241;
CC Evidence={ECO:0000269|PubMed:9781874};
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(cwp1) and a beta(cwg2) subunit.
CC {ECO:0000269|PubMed:9781874}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; Z12155; CAA78143.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB86347.1; -; Genomic_DNA.
DR PIR; S41686; S41686.
DR RefSeq; NP_594142.1; NM_001019566.1.
DR AlphaFoldDB; P32434; -.
DR SMR; P32434; -.
DR BioGRID; 278015; 4.
DR STRING; 4896.SPAC2E1P5.04c.1; -.
DR MaxQB; P32434; -.
DR PaxDb; P32434; -.
DR EnsemblFungi; SPAC2E1P5.04c.1; SPAC2E1P5.04c.1:pep; SPAC2E1P5.04c.
DR GeneID; 2541514; -.
DR KEGG; spo:SPAC2E1P5.04c; -.
DR PomBase; SPAC2E1P5.04c; cwg2.
DR VEuPathDB; FungiDB:SPAC2E1P5.04c; -.
DR eggNOG; KOG0367; Eukaryota.
DR HOGENOM; CLU_028946_2_1_1; -.
DR InParanoid; P32434; -.
DR OMA; RWCLMRQ; -.
DR PhylomeDB; P32434; -.
DR PRO; PR:P32434; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005953; C:CAAX-protein geranylgeranyltransferase complex; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004662; F:CAAX-protein geranylgeranyltransferase activity; IMP:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0061951; P:establishment of protein localization to plasma membrane; IC:PomBase.
DR GO; GO:0018344; P:protein geranylgeranylation; IDA:PomBase.
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 Magnesium; Metal-binding; Prenyltransferase; Reference proteome; Repeat;
KW Transferase; Zinc.
FT CHAIN 1..355
FT /note="Geranylgeranyl transferase type-1 subunit beta"
FT /id="PRO_0000119778"
FT REPEAT 119..163
FT /note="PFTB 1"
FT REPEAT 169..210
FT /note="PFTB 2"
FT REPEAT 234..275
FT /note="PFTB 3"
FT REPEAT 282..324
FT /note="PFTB 4"
FT BINDING 195..197
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 254..257
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 263..266
FT /ligand="geranylgeranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57533"
FT /evidence="ECO:0000250|UniProtKB:P53610"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P53610"
SQ SEQUENCE 355 AA; 40023 MW; 811A3CBFF0067071 CRC64;
MELTRAKHIA FFKRHLILFP TPYEEHDCER TVLAFFCLLG LDLLNALNTI DDDDKKSWIE
WIYKNYVTKE SKGIKYSGFQ AYRTGIQPIS FEQEPQLAGT VFSICCLLFL GDNLSRIDRD
LIKNFVELCK TSQGHFRSIA VPSCSDQDMR QLYMATTIAS LLDFSLSDPL CSIQYIKSCQ
RYEGGFSLLP YGEAHAGATF CALASWSLIL KMIPNSSLNT SNQSYNLMDC VPKVERLIRW
LASRQLSSGG LNGRTNKDVD TCYAYWVLSS LKLLDALPFI DGGELEKYLL LHAQHALGGF
SKTPGEFPDV LHSALGLYAM AYQDDKSFPK VNADIHMTSK YINICRDCIQ AAKGK
