DGGGP_METTH
ID DGGGP_METTH Reviewed; 281 AA.
AC O27170;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Digeranylgeranylglyceryl phosphate synthase;
DE Short=DGGGP synthase;
DE Short=DGGGPS;
DE EC=2.5.1.42;
DE AltName: Full=(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase;
DE AltName: Full=Geranylgeranylglycerol-phosphate geranylgeranyltransferase;
GN OrderedLocusNames=MTH_1098;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=Marburg / DSM 2133;
RA Zhang D., Poulter C.D.;
RT "Biosynthesis of archaebacterial ether lipids. Formation of ether linkages
RT by prenyltransferases.";
RL J. Am. Chem. Soc. 115:1270-1277(1993).
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:0000269|Ref.2}.
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:0000269|Ref.2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|Ref.2}; Multi-pass
CC membrane protein {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family. DGGGP
CC synthase subfamily. {ECO:0000305}.
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DR EMBL; AE000666; AAB85587.1; -; Genomic_DNA.
DR PIR; H69012; H69012.
DR RefSeq; WP_010876722.1; NC_000916.1.
DR AlphaFoldDB; O27170; -.
DR SMR; O27170; -.
DR STRING; 187420.MTH_1098; -.
DR EnsemblBacteria; AAB85587; AAB85587; MTH_1098.
DR GeneID; 1471506; -.
DR KEGG; mth:MTH_1098; -.
DR PATRIC; fig|187420.15.peg.1076; -.
DR HOGENOM; CLU_073311_1_1_2; -.
DR OMA; DYFDYEI; -.
DR BioCyc; MetaCyc:MON-14509; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000005223; 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 Cell membrane; Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..281
FT /note="Digeranylgeranylglyceryl phosphate synthase"
FT /id="PRO_0000350692"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 281 AA; 30132 MW; E6661FE221C85278 CRC64;
MNPYIEILRP VNAVMAVITV MLMALITGRF DFSVLLASVV VFTATGAGNV INDYFDHEID
AINRPERPIP SGRISRGVAG VYSIILFALA SLMGFYLGLL PGLVVVSSSL LMVYYAWRLK
KRCLVGNITI SFLTGLSFVF GGIVLGEVRA SILLGFYAFL MTMAREIVKD MEDVEGDRAE
GATTLPITHG MRISGVLAAS FMLIASLTSP SLYLLGIFSA LYIPVLLLAV AVFLRAAIMI
LRGQDRATAS RVSRMIKVGM ALTFIAFAAG SGTITALTGL S
