DGGGP_SACS2
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 25-MAY-2022, entry version 118.
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; Crenarchaeota; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 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 OMA; DYFDYEI; -.
DR PhylomeDB; Q9UWY6; -.
DR BRENDA; 2.5.1.42; 6163.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000001974; 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 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
