DGGGP_METBF
ID DGGGP_METBF Reviewed; 289 AA.
AC Q46BD9;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 102.
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=Mbar_A1863;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ70803.1; -; Genomic_DNA.
DR RefSeq; WP_011306849.1; NC_007355.1.
DR AlphaFoldDB; Q46BD9; -.
DR SMR; Q46BD9; -.
DR STRING; 269797.Mbar_A1863; -.
DR EnsemblBacteria; AAZ70803; AAZ70803; Mbar_A1863.
DR GeneID; 3624565; -.
DR KEGG; mba:Mbar_A1863; -.
DR eggNOG; arCOG00476; Archaea.
DR HOGENOM; CLU_073311_1_1_2; -.
DR OMA; DYFDYEI; -.
DR OrthoDB; 104789at2157; -.
DR UniPathway; UPA00940; -.
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..289
FT /note="Digeranylgeranylglyceryl phosphate synthase"
FT /id="PRO_0000350710"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
SQ SEQUENCE 289 AA; 31348 MW; 978F829A9EEABE68 CRC64;
MSASVRTYLE IMRYENCLMA GFAAIIGTLI AFNILTSNAP SSYSPGEFPL FSSVLIFLAV
FLVAGAGNAI NDYFDVRIDS INRPDRPIPS GRMKLKEALY FSYTLFALGT LLAFSINPIC
GVIALFNSLV LIFYAKTLKG TPLLGNLSIG YLTGSSFLFG ASVFGLEGLK ALFVLFLLAA
LAITAREIVK DIEDMEGDKM EGADTLPLRV GAKKASYLAA LIGFLAVIFS PLPYHLSMLG
LRYLYLVLLA DLGFLAAIYQ LLARNNPTKS SKMFKIAMFF ALIAFIAGV
