DGGGP_PYRHO
ID DGGGP_PYRHO Reviewed; 277 AA.
AC O57753;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Digeranylgeranylglyceryl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01286};
DE Short=DGGGP synthase {ECO:0000255|HAMAP-Rule:MF_01286};
DE Short=DGGGPS {ECO:0000255|HAMAP-Rule:MF_01286};
DE EC=2.5.1.42 {ECO:0000255|HAMAP-Rule:MF_01286};
DE AltName: Full=(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01286};
DE AltName: Full=Geranylgeranylglycerol-phosphate geranylgeranyltransferase {ECO:0000255|HAMAP-Rule:MF_01286};
GN OrderedLocusNames=PH0027;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
CC -!- FUNCTION: Prenyltransferase that catalyzes the transfer of the
CC geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2
CC hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This
CC reaction is the second ether-bond-formation step in the biosynthesis of
CC archaeal membrane lipids. {ECO:0000255|HAMAP-Rule:MF_01286}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-
CC (geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-
CC glycerol 1-phosphate + diphosphate; Xref=Rhea:RHEA:18109,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57677, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:58837; EC=2.5.1.42; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01286};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01286};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_01286}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01286};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01286}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family. DGGGP
CC synthase subfamily. {ECO:0000255|HAMAP-Rule:MF_01286}.
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DR EMBL; BA000001; BAA29095.1; -; Genomic_DNA.
DR PIR; H71220; H71220.
DR RefSeq; WP_010884148.1; NC_000961.1.
DR AlphaFoldDB; O57753; -.
DR SMR; O57753; -.
DR STRING; 70601.3256412; -.
DR EnsemblBacteria; BAA29095; BAA29095; BAA29095.
DR GeneID; 1443930; -.
DR KEGG; pho:PH0027; -.
DR eggNOG; arCOG00476; Archaea.
DR OMA; DYFDYEI; -.
DR OrthoDB; 104789at2157; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047295; F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.357.140; -; 1.
DR HAMAP; MF_01286; DGGGP_synth; 1.
DR InterPro; IPR023547; DGGGP_synth.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR044878; UbiA_sf.
DR Pfam; PF01040; UbiA; 1.
PE 3: Inferred from homology;
KW Cell membrane; Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..277
FT /note="Digeranylgeranylglyceryl phosphate synthase"
FT /id="PRO_0000350717"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 199..218
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 222..244
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
SQ SEQUENCE 277 AA; 30123 MW; 29E6B56C697FF9E9 CRC64;
MEPKAFVEIM RPHNCILAGI VGILGSLVAY EGIPPVQKLI LIFLVVYFGC SAGNTINDYF
DVEIDKINRP NRPIPRGAIT RKAAFYYGVL QYFIGLIIAL LLGWSAFLFA LGAYFLTFVY
AWKLKPLPFI GNVTVALLTA ATPIYGAVGV GRIDLAGYLA ICAFLVNVSR EIMKDIEDFE
GDKRLGARTL PIMIGKKKSG IIASIFGFLT IISSFLPVKV GIGLGYLPII IVDIMIAKAS
IDVLVNPEKA GKGQKILKFA TFIAVISFLL GALTREV
