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DGGGP_METAC
ID   DGGGP_METAC             Reviewed;         289 AA.
AC   Q8TS44;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=MA_0961;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(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}.
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DR   EMBL; AE010299; AAM04394.1; -; Genomic_DNA.
DR   RefSeq; WP_011020999.1; NC_003552.1.
DR   AlphaFoldDB; Q8TS44; -.
DR   SMR; Q8TS44; -.
DR   STRING; 188937.MA_0961; -.
DR   EnsemblBacteria; AAM04394; AAM04394; MA_0961.
DR   GeneID; 1472851; -.
DR   KEGG; mac:MA_0961; -.
DR   HOGENOM; CLU_073311_1_1_2; -.
DR   InParanoid; Q8TS44; -.
DR   OMA; DYFDYEI; -.
DR   OrthoDB; 104789at2157; -.
DR   PhylomeDB; Q8TS44; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000002487; 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_0000350709"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        44..64
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        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;  31020 MW;  6B8BC9E3655807F2 CRC64;
     MSAGIRTYLE LMRYGNCLMA GFAAVIGTLI AFNILTSGPL SSNFTGPFPF LDAGFVFLVV
     FLVSGAGNAI NDYFDIKIDS INRPERPIPS GRVQAKEALY FSYLLFAAGT LLAFSINSIC
     GLIALFNSLL LILYAKTLKG TPLLGNLSIG YLTGSVFLFG ASVFGLEGLK TLFVLFLLAA
     LAITAREIVK DIEDMEGDRL EDADTLPLRI GAKKAGYLAV LIGLLAVLLS PLPCVMSILG
     LRYLYLVLLA DLGFLAAIVQ LLVKNNPTKS SKMFKIAMFF ALIAFIAGV
 
 
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