ID   DGGGP_SACS2             Reviewed;         282 AA.
AC   Q9UWY6;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Digeranylgeranylglyceryl phosphate synthase;
DE            Short=DGGGP synthase;
DE            Short=DGGGPS;
DE            EC=2.5.1.42;
DE   AltName: Full=(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase;
DE   AltName: Full=Geranylgeranylglycerol-phosphate geranylgeranyltransferase;
GN   Name=ubiA-2; OrderedLocusNames=SSO0583; ORFNames=C21_016;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=10701121; DOI=10.1139/g99-108;
RA   Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA   Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA   Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA   Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA   Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT   "Gene content and organization of a 281-kbp contig from the genome of the
RT   extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL   Genome 43:116-136(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, PH
RP   DEPENDENCE, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=15356000; DOI=10.1074/jbc.m409207200;
RA   Hemmi H., Shibuya K., Takahashi Y., Nakayama T., Nishino T.;
RT   "(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase from the
RT   thermoacidophilic archaeon Sulfolobus solfataricus. Molecular cloning and
RT   characterization of a membrane-intrinsic prenyltransferase involved in the
RT   biosynthesis of archaeal ether-linked membrane lipids.";
RL   J. Biol. Chem. 279:50197-50203(2004).
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. Cannot use other prenyl donors, i.e. farnesyl
CC       diphosphate (FPP) and phytyl diphosphate. Moreover, 4-hydroxybenzoate,
CC       1,4-dihydroxy 2-naphthoate, homogentisate, and alpha-glycerophosphate
CC       do not function as prenyl acceptor substrates.
CC       {ECO:0000269|PubMed:15356000}.
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;
CC         Evidence={ECO:0000269|PubMed:15356000};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:15356000};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:15356000};
CC       Note=Magnesium. Can also use Ca(2+), but less efficiently.
CC       {ECO:0000269|PubMed:15356000};
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA in vitro.
CC       {ECO:0000269|PubMed:15356000}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|PubMed:15356000};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15356000};
CC       Multi-pass membrane protein {ECO:0000305|PubMed:15356000}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family. DGGGP
CC       synthase subfamily. {ECO:0000305}.
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DR   EMBL; Y18930; CAB57717.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK40896.1; -; Genomic_DNA.
DR   PIR; A99205; A99205.
DR   AlphaFoldDB; Q9UWY6; -.
DR   SMR; Q9UWY6; -.
DR   STRING; 273057.SSO0583; -.
DR   PaxDb; 273057-SSO0583; -.
DR   EnsemblBacteria; AAK40896; AAK40896; SSO0583.
DR   KEGG; sso:SSO0583; -.
DR   PATRIC; fig|273057.12.peg.591; -.
DR   eggNOG; arCOG00476; Archaea.
DR   HOGENOM; CLU_073311_1_1_2; -.
DR   InParanoid; Q9UWY6; -.
DR   PhylomeDB; Q9UWY6; -.
DR   BRENDA; 2.5.1.42; 6163.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000001974; Chromosome.
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   CDD; cd13961; PT_UbiA_DGGGPS; 1.
DR   Gene3D; 1.10.357.140; UbiA prenyltransferase; 1.
DR   Gene3D; 1.20.120.1780; UbiA prenyltransferase; 1.
DR   HAMAP; MF_01286; DGGGP_synth; 1.
DR   InterPro; IPR023547; DGGGP_synth.
DR   InterPro; IPR000537; UbiA_prenyltransferase.
DR   InterPro; IPR044878; UbiA_sf.
DR   PANTHER; PTHR42723; CHLOROPHYLL SYNTHASE; 1.
DR   PANTHER; PTHR42723:SF1; CHLOROPHYLL SYNTHASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01040; UbiA; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..282
FT                   /note="Digeranylgeranylglyceryl phosphate synthase"
FT                   /id="PRO_0000350691"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   282 AA;  30915 MW;  0E98AFDD6590B052 CRC64;
     MSLKSYMQLV RIHNVIGAAL GAIMGFLVSS QWYLELKGIL LSALVVGLIA AGGYVINDVY
     DVEIDKINKP YRPIPSGKIS VNKAKALSIA LFIIGIALSI LLNIYALVIA LVTAIGLIYY
     AKDLKKTGFY GNLLVATTTA LSIFYGGLAF FSDNWLLRII IPTLYAFFLT LIREIVKGIE
     DYNGDSLNNV KTLATTLGIN KSWRIAKILL VLLLIISPLP FFIGFNLIYL ILLILVFIPF
     TILSIIQKET IEGASKARTY LKISAISGII AFLLGSLPFF KG
//