ID A0A3D8GRA6_9BACI Unreviewed; 230 AA.
AC A0A3D8GRA6;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Heptaprenylglyceryl phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00112};
DE Short=HepGP synthase {ECO:0000256|HAMAP-Rule:MF_00112};
DE EC=2.5.1.n9 {ECO:0000256|HAMAP-Rule:MF_00112};
DE AltName: Full=Glycerol-1-phosphate heptaprenyltransferase {ECO:0000256|HAMAP-Rule:MF_00112};
GN Name=pcrB {ECO:0000256|HAMAP-Rule:MF_00112};
GN ORFNames=DRW41_11125 {ECO:0000313|EMBL:RDU36606.1};
OS Neobacillus piezotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=2259171 {ECO:0000313|EMBL:RDU36606.1, ECO:0000313|Proteomes:UP000257144};
RN [1] {ECO:0000313|EMBL:RDU36606.1, ECO:0000313|Proteomes:UP000257144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-04 {ECO:0000313|EMBL:RDU36606.1,
RC ECO:0000313|Proteomes:UP000257144};
RA Yu L., Tang X.;
RT "Bacillus sp. YLB-04 draft genome sequence.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Prenyltransferase that catalyzes in vivo the transfer of the
CC heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon
CC atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing
CC heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-
CC formation step in the biosynthesis of archaea-type G1P-based membrane
CC lipids found in Bacillales. {ECO:0000256|HAMAP-Rule:MF_00112}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-heptaprenyl diphosphate + sn-glycerol 1-phosphate =
CC 3-heptaprenyl-sn-glycero-1-phosphate + diphosphate;
CC Xref=Rhea:RHEA:33495, ChEBI:CHEBI:33019, ChEBI:CHEBI:57685,
CC ChEBI:CHEBI:58206, ChEBI:CHEBI:64781; EC=2.5.1.n9;
CC Evidence={ECO:0000256|ARBA:ARBA00001875, 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 -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00112}.
CC -!- SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group I
CC subfamily. {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:RDU36606.1}.
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DR EMBL; QNQT01000004; RDU36606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8GRA6; -.
DR OrthoDB; 2381757at2; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000257144; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002094; F:polyprenyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02812; PcrB_like; 1.
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 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000257144};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00112}.
FT BINDING 12
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT BINDING 159..164
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT BINDING 189
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT BINDING 209..210
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
SQ SEQUENCE 230 AA; 25691 MW; 7042854B6E157F62 CRC64;
MYDFREWRHV FKLDPAREIA DSDLEAICES GTDAVIVGGT DGVTLEGVLD LMARVRRFTV
PCVLEVSNLE SVTPGFDLYF VPSILNSKDP KWINGLHFEA VKEYGDIMDW DEFAMEAYVI
LNEECKAAKL TQAETRLSEE DIKAYAMMAE KMFGMPIFYL EYSGAFGNPE MVSAAKKGLE
KAVLFYGGGI KTKEQAAEMA RHADVIVVGN SIYEDIDKAL ETVKAVKVEK
//
