DGGGP_METJA
ID DGGGP_METJA Reviewed; 283 AA.
AC Q57727;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 110.
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=MJ0279;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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; L77117; AAB98267.1; -; Genomic_DNA.
DR PIR; H64334; H64334.
DR PDB; 6M31; X-ray; 2.30 A; A/B=1-283.
DR PDB; 6M34; X-ray; 2.90 A; A/B=1-283.
DR PDB; 7BPU; X-ray; 3.32 A; A/B=1-283.
DR PDBsum; 6M31; -.
DR PDBsum; 6M34; -.
DR PDBsum; 7BPU; -.
DR AlphaFoldDB; Q57727; -.
DR SMR; Q57727; -.
DR STRING; 243232.MJ_0279; -.
DR EnsemblBacteria; AAB98267; AAB98267; MJ_0279.
DR KEGG; mja:MJ_0279; -.
DR eggNOG; arCOG00476; Archaea.
DR HOGENOM; CLU_073311_1_1_2; -.
DR InParanoid; Q57727; -.
DR OMA; DYFDYEI; -.
DR PhylomeDB; Q57727; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000000805; 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 3D-structure; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..283
FT /note="Digeranylgeranylglyceryl phosphate synthase"
FT /id="PRO_0000106770"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:6M31"
FT HELIX 17..35
FT /evidence="ECO:0007829|PDB:6M31"
FT HELIX 41..65
FT /evidence="ECO:0007829|PDB:6M31"
FT HELIX 67..72
FT /evidence="ECO:0007829|PDB:6M31"
FT TURN 78..82
FT /evidence="ECO:0007829|PDB:6M31"
FT HELIX 86..104
FT /evidence="ECO:0007829|PDB:6M31"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:6M31"
FT HELIX 109..127
FT /evidence="ECO:0007829|PDB:6M31"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:6M31"
FT HELIX 133..152
FT /evidence="ECO:0007829|PDB:6M31"
FT HELIX 159..182
FT /evidence="ECO:0007829|PDB:6M31"
FT HELIX 184..188
FT /evidence="ECO:0007829|PDB:6M31"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:6M31"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:6M31"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:6M31"
FT HELIX 203..217
FT /evidence="ECO:0007829|PDB:6M31"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:6M31"
FT HELIX 229..251
FT /evidence="ECO:0007829|PDB:6M31"
FT HELIX 255..280
FT /evidence="ECO:0007829|PDB:6M31"
SQ SEQUENCE 283 AA; 31754 MW; 9C98641137661413 CRC64;
MGVFMEKLKT YLELIRVKNC ITASIGGIIG YLISSNFEID ILKSLLVFFV VFFVCAYGNV
INDIFDIEID RINKPSRPLP SGKIKLNEAK KFSAILLILG LVLSLFINIY ALIIAVINAL
FLYLYAKKYK KYKPIGNFII GYLTGSVFLF GGVAGKNVMP VVILFLCSLL SIWGREIVKD
FEDMEGDKKE GVISLPIKYG KKSLYFATFL VVLAVILSPL PYILKIFGIW YLILIAICDI
LFIYAMALLL KEPNKETASK VSKFLKIIMN IVLLAFIVGA IKL
