GGPPS_CAPAN
ID GGPPS_CAPAN Reviewed; 369 AA.
AC P80042;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Geranylgeranyl pyrophosphate synthase, chloroplastic {ECO:0000303|PubMed:1303794};
DE Short=GGPP synthase {ECO:0000303|PubMed:1303794};
DE Short=GGPS {ECO:0000303|PubMed:1303794};
DE EC=2.5.1.- {ECO:0000269|PubMed:1303794};
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase {ECO:0000303|PubMed:1303794};
DE AltName: Full=Dimethylallyltranstransferase {ECO:0000303|PubMed:1303794};
DE EC=2.5.1.1 {ECO:0000269|PubMed:1303794};
DE AltName: Full=Farnesyl diphosphate synthase {ECO:0000303|PubMed:1303794};
DE AltName: Full=Farnesyltranstransferase {ECO:0000303|PubMed:1303794};
DE EC=2.5.1.29 {ECO:0000269|PubMed:1303794};
DE AltName: Full=Geranyltranstransferase {ECO:0000303|PubMed:1303794};
DE EC=2.5.1.10 {ECO:0000269|PubMed:1303794};
DE Flags: Precursor;
GN Name=GGPS1 {ECO:0000305};
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=cv. Lamuyo, and cv. Yolo Wonder; TISSUE=Fruit;
RX PubMed=1303794; DOI=10.1111/j.1365-313x.1992.00025.x;
RA Kuntz M., Roemer S., Suire C., Hugueney P., Weil J.H., Schantz R.,
RA Camara B.;
RT "Identification of a cDNA for the plastid-located geranylgeranyl
RT pyrophosphate synthase from Capsicum annuum: correlative increase in enzyme
RT activity and transcript level during fruit ripening.";
RL Plant J. 2:25-34(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Yolo Wonder;
RX PubMed=7888631; DOI=10.1007/bf00020196;
RA Badillo A., Steppuhn J., Deruere J., Camara B., Kuntz M.;
RT "Structure of a functional geranylgeranyl pyrophosphate synthase gene from
RT Capsicum annuum.";
RL Plant Mol. Biol. 27:425-428(1995).
CC -!- FUNCTION: Catalyzes the trans-addition of the three molecules of IPP
CC onto DMAPP to form geranylgeranyl pyrophosphate.
CC {ECO:0000269|PubMed:1303794}.
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 Evidence={ECO:0000269|PubMed:1303794};
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 Evidence={ECO:0000269|PubMed:1303794};
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 Evidence={ECO:0000269|PubMed:1303794};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P14324};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P14324};
CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC diphosphate: step 1/1. {ECO:0000269|PubMed:1303794}.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC diphosphate: step 1/1. {ECO:0000269|PubMed:1303794}.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate
CC biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and
CC isopentenyl diphosphate: step 1/1. {ECO:0000269|PubMed:1303794}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P34802}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000305|PubMed:1303794}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; X80267; CAA56554.1; -; Genomic_DNA.
DR PIR; S53722; S53722.
DR RefSeq; XP_016568624.1; XM_016713138.1.
DR AlphaFoldDB; P80042; -.
DR SMR; P80042; -.
DR GeneID; 107867046; -.
DR KEGG; cann:107867046; -.
DR OrthoDB; 981769at2759; -.
DR BioCyc; MetaCyc:MON-12171; -.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR UniPathway; UPA00389; UER00564.
DR Proteomes; UP000189700; Chromosome 4.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; IDA:UniProtKB.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IDA:UniProtKB.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IDA:UniProtKB.
DR GO; GO:0004337; F:geranyltranstransferase activity; IDA:UniProtKB.
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 GO; GO:0006720; P:isoprenoid metabolic process; IDA:UniProtKB.
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 Carotenoid biosynthesis; Chloroplast; Isoprene biosynthesis; Magnesium;
KW Metal-binding; Plastid; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000305|PubMed:1303794"
FT CHAIN ?..369
FT /note="Geranylgeranyl pyrophosphate synthase,
FT chloroplastic"
FT /id="PRO_0000016472"
FT BINDING 118
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 121
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 150
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
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 163
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 163
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 168
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 169
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 254
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 255
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 292
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 309
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 319
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 369 AA; 40173 MW; 2D527F5E43A29C6F CRC64;
MRSMNLVDLW AQQACLVFNQ TLSYKSFNGF MKIPLKNSKI NPKLNKKRPF SPLTVSAIAT
TKEDERIEAA QTEEPFNFKI YVTEKAISVN KALDEAIIVK EPHVIHEAMR YSLLAGGKRV
RPMLCLAACE LVGGNQENAM AAACAVEMIH TMSLIHDDLP CMDNDDLRRG KPTNHKIYGE
DVAVLAGDSL LAFAFEHIVN STAGVTPSRI VGAVAELAKS IGTEGLVAGQ VADIKCTGNA
SVSLETLEFI HVHKTAALLE SSVVLGAILG GGTNVEVEKL RRFARCIGLL FQVVDDILDV
TKSSEELGKT AGKDLVVDKT TYPKLLGLEK AKEFAAELNR EAKQQLEGFD SRKAAPLIAL
ADYIAYRDN
