GGPPS_SINAL
ID GGPPS_SINAL Reviewed; 366 AA.
AC Q43133;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Geranylgeranyl pyrophosphate synthase, chloroplastic/chromoplastic;
DE Short=GGPP synthase;
DE Short=GGPS;
DE EC=2.5.1.-;
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase;
DE AltName: Full=Dimethylallyltranstransferase;
DE EC=2.5.1.1;
DE AltName: Full=Farnesyl diphosphate synthase;
DE AltName: Full=Farnesyltranstransferase;
DE EC=2.5.1.29;
DE AltName: Full=Geranyltranstransferase;
DE EC=2.5.1.10;
DE Flags: Precursor;
GN Name=GGPS1; Synonyms=GGPS;
OS Sinapis alba (White mustard) (Brassica hirta).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Sinapis.
OX NCBI_TaxID=3728;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=9288918; DOI=10.1111/j.1432-1033.1997.00942.x;
RA Bonk M., Hoffmann B., von Lintig J., Schledz M., Al-Babili S., Hobeika E.,
RA Kleinig H., Beyer P.;
RT "Chloroplast import of four carotenoid biosynthetic enzymes in vitro
RT reveals differential fates prior to membrane binding and oligomeric
RT assembly.";
RL Eur. J. Biochem. 247:942-950(1997).
CC -!- FUNCTION: Catalyzes the trans-addition of the three molecules of IPP
CC onto DMAPP to form geranylgeranyl pyrophosphate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-
CC geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:128769; EC=2.5.1.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-
CC farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769,
CC ChEBI:CHEBI:175763; EC=2.5.1.10;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate =
CC (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate;
CC Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC diphosphate: step 1/1.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC diphosphate: step 1/1.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate
CC biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and
CC isopentenyl diphosphate: step 1/1.
CC -!- SUBUNIT: Dimer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000305|PubMed:9288918}. Plastid, chromoplast
CC {ECO:0000305|PubMed:9288918}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; X98795; CAA67330.1; -; mRNA.
DR PIR; T10452; T10452.
DR PDB; 2J1O; X-ray; 2.00 A; A=74-366.
DR PDB; 2J1P; X-ray; 1.80 A; A/B=74-366.
DR PDBsum; 2J1O; -.
DR PDBsum; 2J1P; -.
DR AlphaFoldDB; Q43133; -.
DR SMR; Q43133; -.
DR PRIDE; Q43133; -.
DR BRENDA; 2.5.1.29; 5734.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR UniPathway; UPA00389; UER00564.
DR EvolutionaryTrace; Q43133; -.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0009509; C:chromoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033386; P:geranylgeranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carotenoid biosynthesis; Chloroplast; Chromoplast;
KW Isoprene biosynthesis; Magnesium; Metal-binding; Plastid; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast and chromoplast"
FT CHAIN ?..366
FT /note="Geranylgeranyl pyrophosphate synthase,
FT chloroplastic/chromoplastic"
FT /id="PRO_0000016474"
FT REGION 44..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT BINDING 115
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT BINDING 144
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT BINDING 151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 162
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT BINDING 251
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250"
FT HELIX 73..90
FT /evidence="ECO:0007829|PDB:2J1P"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:2J1P"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:2J1P"
FT HELIX 130..151
FT /evidence="ECO:0007829|PDB:2J1P"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:2J1P"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2J1P"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:2J1P"
FT HELIX 174..195
FT /evidence="ECO:0007829|PDB:2J1P"
FT HELIX 202..216
FT /evidence="ECO:0007829|PDB:2J1P"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:2J1P"
FT HELIX 221..227
FT /evidence="ECO:0007829|PDB:2J1P"
FT HELIX 236..251
FT /evidence="ECO:0007829|PDB:2J1P"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:2J1P"
FT HELIX 271..298
FT /evidence="ECO:0007829|PDB:2J1P"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:2J1O"
FT HELIX 319..342
FT /evidence="ECO:0007829|PDB:2J1P"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:2J1P"
FT TURN 348..351
FT /evidence="ECO:0007829|PDB:2J1P"
FT HELIX 352..363
FT /evidence="ECO:0007829|PDB:2J1P"
SQ SEQUENCE 366 AA; 39432 MW; 1EADBFD9C4CF4F77 CRC64;
MASSVTPLGS WVLLHHHPST ILTQSRSRSP PSLITLKPIS LTPKRTVSSS SSSSLITKED
NNLKSSSSSF DFMSYIIRKA DSVNKALDSA VPLREPLKIH EAMRYSLLAG GKRVRPVLCI
AACELVGGEE SLAMPARCAV EMIHTMSLIH DDLPCMDNDD LRRGKPTNHK VYGEDVAVLA
GDALLSFAFE HLASATSSEV SPARVVRAVG ELAKAIGTEG LVAGQVVDIS SEGLDLNNVG
LEHLKFIHLH KTAALLEASA VLGGIIGGGS DEEIERLRKF ARCIGLLFQV VDDILDVTKS
SQELGKTAGK DLIADKLTYP KLMGLEKSRE FAEKLNTEAR DQLLGFDSDK VAPLLALANY
IANRQN
