ID A0A1Q9NBE1_9ARCH Unreviewed; 279 AA.
AC A0A1Q9NBE1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Geranylgeranylglyceryl phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00112};
DE Short=GGGP synthase {ECO:0000256|HAMAP-Rule:MF_00112};
DE Short=GGGPS {ECO:0000256|HAMAP-Rule:MF_00112};
DE EC=2.5.1.41 {ECO:0000256|HAMAP-Rule:MF_00112};
DE AltName: Full=(S)-3-O-geranylgeranylglyceryl phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00112};
DE AltName: Full=Phosphoglycerol geranylgeranyltransferase {ECO:0000256|HAMAP-Rule:MF_00112};
GN ORFNames=HeimC3_45860 {ECO:0000313|EMBL:OLS19377.1};
OS Candidatus Heimdallarchaeota archaeon LC_3.
OC Archaea; Asgard group; Candidatus Heimdallarchaeota.
OX NCBI_TaxID=1841598 {ECO:0000313|EMBL:OLS19377.1, ECO:0000313|Proteomes:UP000186063};
RN [1] {ECO:0000313|EMBL:OLS19377.1, ECO:0000313|Proteomes:UP000186063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC_3 {ECO:0000313|EMBL:OLS19377.1};
RX PubMed=28077874; DOI=10.1038/nature21031;
RA Zaremba-Niedzwiedzka K., Caceres E.F., Saw J.H., Backstrom D.,
RA Juzokaite L., Vancaester E., Seitz K.W., Anantharaman K., Starnawski P.,
RA Kjeldsen K.U., Scott M.B., Nunoura T., Banfield J.F., Schramm A.,
RA Baker B.J., Spang A., Ettema T.J.G.;
RT "Asgard archaea illuminate the origin of eukaryotic cellular complexity.";
RL Nature 541:353-358(2017).
CC -!- FUNCTION: Prenyltransferase that catalyzes the transfer of the
CC geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3
CC hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first
CC ether-bond-formation step in the biosynthesis of archaeal membrane
CC lipids. {ECO:0000256|HAMAP-Rule:MF_00112}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + sn-glycerol 1-
CC phosphate = diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-
CC phosphate; Xref=Rhea:RHEA:23404, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57677, ChEBI:CHEBI:57685, ChEBI:CHEBI:58756; EC=2.5.1.41;
CC Evidence={ECO:0000256|ARBA:ARBA00000742, ECO:0000256|HAMAP-
CC Rule:MF_00112};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00112};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000256|HAMAP-Rule:MF_00112}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00112}.
CC -!- SIMILARITY: Belongs to the GGGP/HepGP synthase family.
CC {ECO:0000256|HAMAP-Rule:MF_00112}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00112}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLS19377.1}.
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DR EMBL; MDVS01000119; OLS19377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9NBE1; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000186063; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0047294; F:phosphoglycerol geranylgeranyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0002094; F:polyprenyltransferase activity; IEA:UniProt.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.390; FMN-linked oxidoreductases; 1.
DR HAMAP; MF_00112; GGGP_HepGP_synthase; 1.
DR InterPro; IPR039074; GGGP/HepGP_synthase_I.
DR InterPro; IPR038597; GGGP/HepGP_synthase_sf.
DR InterPro; IPR008205; GGGP_HepGP_synthase.
DR InterPro; IPR010946; GGGP_synth.
DR NCBIfam; TIGR01769; GGGP; 1.
DR NCBIfam; TIGR01768; GGGP-family; 1.
DR PANTHER; PTHR40029; -; 1.
DR PANTHER; PTHR40029:SF2; HEPTAPRENYLGLYCERYL PHOSPHATE SYNTHASE; 1.
DR Pfam; PF01884; PcrB; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00112};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00112};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00112};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00112};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00112};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_00112};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_00112};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00112}.
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
SQ SEQUENCE 279 AA; 30713 MW; DBF6D42E2A894DAA CRC64;
MIIILNNTTN LLNKTKTDES EQNMFPRLPA RPLRDIIYQK IQKHPLQSTL FDPENDLQIL
AHKAELAVEQ GTDILLIGGS SHVQPIKFFE SIAAIKAVSK DVPVIIYNAN FEMISNDADG
ILYGSVLNSK DMYYVINNSA NAAPLFKKLN VEPLATAFLI FEPGMTVGYV LNCHLLPQNN
LKIPAAYSLT AENLGYSFVY LEAGSKAPYT VSPDVIKAVR STINIPIIVG GGVVSEDKAR
EVVEAGADIV VIGTHFENVE DMSNIIDVIH STKRFKPEK
//
