PCRB_LISMH
ID PCRB_LISMH Reviewed; 225 AA.
AC B8DFG3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Heptaprenylglyceryl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00112};
DE Short=HepGP synthase {ECO:0000255|HAMAP-Rule:MF_00112};
DE EC=2.5.1.n9 {ECO:0000255|HAMAP-Rule:MF_00112};
DE AltName: Full=Glycerol-1-phosphate heptaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_00112};
GN Name=pcrB {ECO:0000255|HAMAP-Rule:MF_00112}; OrderedLocusNames=LMHCC_0804;
OS Listeria monocytogenes serotype 4a (strain HCC23).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=552536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HCC23;
RX PubMed=21602330; DOI=10.1128/jb.05236-11;
RA Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA Lawrence M.L.;
RT "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL J. Bacteriol. 193:3679-3680(2011).
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:0000255|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:0000255|HAMAP-Rule:MF_00112};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00112};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_00112}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00112}.
CC -!- SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group I
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00112}.
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DR EMBL; CP001175; ACK39156.1; -; Genomic_DNA.
DR RefSeq; WP_003729807.1; NC_011660.1.
DR AlphaFoldDB; B8DFG3; -.
DR SMR; B8DFG3; -.
DR KEGG; lmh:LMHCC_0804; -.
DR HOGENOM; CLU_095211_0_0_9; -.
DR OMA; TGAHKEW; -.
DR UniPathway; UPA00940; -.
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; -; 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 PANTHER; PTHR40029; PTHR40029; 1.
DR Pfam; PF01884; PcrB; 1.
DR TIGRFAMs; TIGR01768; GGGP-family; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Transferase.
FT CHAIN 1..225
FT /note="Heptaprenylglyceryl phosphate synthase"
FT /id="PRO_1000119132"
FT BINDING 6
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 153..158
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 183
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 203..204
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
SQ SEQUENCE 225 AA; 25258 MW; E300D4299DA36C8D CRC64;
MKHLFKLDPA KNLPMNDLTK LVHSGTDGFI IGGTDNVQIE AVQKLYELLG ETDLPIFLEI
SNESMILPEA DHFLIPVVLN TENSKWTHGL HQELIKEMGA FIPWKRVTAE GYVILNKDAK
VAHLTEAKTD LTDEDIVAYA RLAENIFHLP IFYVEYSGMY GDPEVVRKAG AALSNTKFWY
GGGIRSKEQA AEMAKYADTI IVGNIIYEDL EKALETATIF RKKTV