GGPPS_GEOAI
ID GGPPS_GEOAI Reviewed; 319 AA.
AC A0A0A7GEY4;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Geranylgeranyl pyrophosphate synthase {ECO:0000303|PubMed:30062607};
DE Short=GGPP synthase {ECO:0000303|PubMed:30062607};
DE Short=GGPPSase {ECO:0000305};
DE EC=2.5.1.- {ECO:0000269|PubMed:30062607};
DE AltName: Full=Dimethylallyltranstransferase {ECO:0000305};
DE EC=2.5.1.1 {ECO:0000269|PubMed:30062607};
DE AltName: Full=Farnesyl diphosphate synthase {ECO:0000305};
DE AltName: Full=Farnesyltranstransferase {ECO:0000305};
DE EC=2.5.1.29 {ECO:0000269|PubMed:30062607};
DE AltName: Full=Geranylgeranyl diphosphate synthase {ECO:0000305};
DE AltName: Full=Geranyltranstransferase {ECO:0000305};
DE EC=2.5.1.10 {ECO:0000269|PubMed:30062607};
GN ORFNames=GACE_1337 {ECO:0000312|EMBL:AIY90378.1};
OS Geoglobus acetivorans.
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Geoglobus.
OX NCBI_TaxID=565033;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21716 / VKM B-2522 / SBH6;
RX PubMed=25416759; DOI=10.1128/aem.02705-14;
RA Mardanov A.V., Slododkina G.B., Slobodkin A.I., Beletsky A.V.,
RA Gavrilov S.N., Kublanov I.V., Bonch-Osmolovskaya E.A., Skryabin K.G.,
RA Ravin N.V.;
RT "The Geoglobus acetivorans genome: Fe(III) reduction, acetate utilization,
RT autotrophic growth, and degradation of aromatic compounds in a
RT hyperthermophilic archaeon.";
RL Appl. Environ. Microbiol. 81:1003-1012(2015).
RN [2] {ECO:0007744|PDB:5JFQ}
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RX PubMed=30062607; DOI=10.1007/s00792-018-1044-5;
RA Petrova T.E., Boyko K.M., Nikolaeva A.Y., Stekhanova T.N., Gruzdev E.V.,
RA Mardanov A.V., Stroilov V.S., Littlechild J.A., Popov V.O.,
RA Bezsudnova E.Y.;
RT "Structural characterization of geranylgeranyl pyrophosphate synthase
RT GACE1337 from the hyperthermophilic archaeon Geoglobus acetivorans.";
RL Extremophiles 22:877-888(2018).
CC -!- FUNCTION: Catalyzes the addition of 3 molecules of isopentenyl
CC diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form
CC geranylgeranyl pyrophosphate (GGPP). Catalyzes the synthesis of
CC geranylgeranyl pyrophosphate as a major product and of farnesyl
CC pyrophosphate in smaller amounts. {ECO:0000269|PubMed:30062607}.
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:30062607};
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:30062607};
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:30062607};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q12051};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051};
CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC diphosphate: step 1/1. {ECO:0000305}.
CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC diphosphate: step 1/1. {ECO:0000305}.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate
CC biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and
CC isopentenyl diphosphate: step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:30062607}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; CP009552; AIY90378.1; -; Genomic_DNA.
DR RefSeq; WP_048092150.1; NZ_CP009552.1.
DR PDB; 5JFQ; X-ray; 2.51 A; A/B=1-319.
DR PDBsum; 5JFQ; -.
DR AlphaFoldDB; A0A0A7GEY4; -.
DR SMR; A0A0A7GEY4; -.
DR STRING; 565033.GACE_1337; -.
DR EnsemblBacteria; AIY90378; AIY90378; GACE_1337.
DR GeneID; 24797917; -.
DR KEGG; gac:GACE_1337; -.
DR eggNOG; arCOG01726; Archaea.
DR HOGENOM; CLU_014015_2_1_2; -.
DR OrthoDB; 55053at2157; -.
DR BRENDA; 2.5.1.29; 17637.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR UniPathway; UPA00389; UER00564.
DR Proteomes; UP000030624; Chromosome.
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: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.
PE 1: Evidence at protein level;
KW 3D-structure; Isoprene biosynthesis; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..319
FT /note="Geranylgeranyl pyrophosphate synthase"
FT /id="PRO_0000448754"
FT BINDING 42
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 45
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 74
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 90
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 91
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 172
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 173
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 210
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 226
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 236
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT HELIX 2..20
FT /evidence="ECO:0007829|PDB:5JFQ"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:5JFQ"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:5JFQ"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:5JFQ"
FT HELIX 64..85
FT /evidence="ECO:0007829|PDB:5JFQ"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:5JFQ"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:5JFQ"
FT HELIX 102..120
FT /evidence="ECO:0007829|PDB:5JFQ"
FT HELIX 127..156
FT /evidence="ECO:0007829|PDB:5JFQ"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:5JFQ"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:5JFQ"
FT HELIX 192..216
FT /evidence="ECO:0007829|PDB:5JFQ"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:5JFQ"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:5JFQ"
FT HELIX 265..273
FT /evidence="ECO:0007829|PDB:5JFQ"
FT HELIX 276..295
FT /evidence="ECO:0007829|PDB:5JFQ"
FT HELIX 302..316
FT /evidence="ECO:0007829|PDB:5JFQ"
SQ SEQUENCE 319 AA; 35918 MW; 54F3878BC3AA31DA CRC64;
MISEIIKDRA KLVNEKIEEL LKEQEPEGLY RAARHYLKAG GKRLRPVITL LSAEALGEDY
RKAIHAAIAI ETVHNFTLVH DDIMDEDEMR RGVKTVHTLF GIPTAILAGD TLYAEAFEIL
SMSDAPPENI VRAVSKLARV CVEICEGQFM DMSFEERDSV GESEYLEMVR KKTGVLIGIS
ASIPAVLFGK DESVEKALWN YGIYSGIGFQ IHDDLLDISG KGKIGKDWGS DILEGKKTLI
VIKAFEEGIE LETFGKGRAS EEELERDIKK LFDCGAVDYA RERAREYIEM AKKNLEVIDE
SPSRNYLVEL ADYLIERDH
