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DGGGP_HALSA
ID   DGGGP_HALSA             Reviewed;         276 AA.
AC   Q9HRP0;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 2.
DT   25-MAY-2022, entry version 105.
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=VNG_0610G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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=AAG19118.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE004437; AAG19118.1; ALT_INIT; Genomic_DNA.
DR   PIR; B84219; B84219.
DR   AlphaFoldDB; Q9HRP0; -.
DR   SMR; Q9HRP0; -.
DR   STRING; 64091.VNG_0610G; -.
DR   PaxDb; Q9HRP0; -.
DR   EnsemblBacteria; AAG19118; AAG19118; VNG_0610G.
DR   KEGG; hal:VNG_0610G; -.
DR   PATRIC; fig|64091.14.peg.467; -.
DR   HOGENOM; CLU_073311_1_1_2; -.
DR   InParanoid; Q9HRP0; -.
DR   PhylomeDB; Q9HRP0; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000000554; 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..276
FT                   /note="Digeranylgeranylglyceryl phosphate synthase"
FT                   /id="PRO_0000350693"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        200..220
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"
SQ   SEQUENCE   276 AA;  27621 MW;  486ACC5A79B783E0 CRC64;
     METGRGLVEL ARPVNTLAAG ALTFIGAFVA GGAVGRPAAT GAAVGATWLA TAGGNAINDY
     FDREVDRIND PDRAIPRGAV SPRGALAYSV VLFVGAAALA ATLPVLAVCI AALNLAGLLT
     YTQYLKGRPG AGNALVAYLG GSTFVFGAAA VGSPLAGGVL AALAALSTFA REVIKDVEDL
     AGDRAAGLRT LPVVVGHQRA LAVSAVFVVG AAAASPVPYL VGVFGWWYLV AVCPGVVVMV
     VAAARSYTDP AAGQRLLKRG QLLAAAAFVV GRLVTP
 
 
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