DGGGP_METMA
ID DGGGP_METMA Reviewed; 289 AA.
AC Q8PV96;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 25-MAY-2022, entry version 114.
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=MM_2075;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM31771.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008384; AAM31771.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_015412297.1; NC_003901.1.
DR AlphaFoldDB; Q8PV96; -.
DR SMR; Q8PV96; -.
DR STRING; 192952.MM_2075; -.
DR EnsemblBacteria; AAM31771; AAM31771; MM_2075.
DR GeneID; 44088296; -.
DR KEGG; mma:MM_2075; -.
DR PATRIC; fig|192952.21.peg.2382; -.
DR eggNOG; arCOG00476; Archaea.
DR HOGENOM; CLU_073311_1_1_2; -.
DR OMA; DYFDYEI; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000000595; 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; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..289
FT /note="Digeranylgeranylglyceryl phosphate synthase"
FT /id="PRO_0000350711"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 120..140
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 218..238
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; 30992 MW; 5C074E25B2637870 CRC64;
MSAGIRTYLE LMRYKNCLMA GFAAAIGTLI AFNILISGTS TPNFEDAFPF LDAGLVFLVV
FLVSGAGNAI NDYFDIKIDS INRPERPIPS GRVKAKEAFY FSYLLFALGT LIAFSINSIC
GSIALFNSLL LILYAKTLKG TPLLGNLSIG YLTGSVFLFG ASIFGFGGIK ALSVLFLLAA
LAITAREIVK DIEDMEGDSL EGADTLPLRI GAKKAGYLAV LTGLLAVILS PLPYFMSVLG
LRYIYLVSLA DLGFLAAIIQ LLVRNNPTKS SKLFKIAMFF ALIAFIAGV
