ID A0A1L3MVX5_9BACI Unreviewed; 227 AA.
AC A0A1L3MVX5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=A9C19_18050 {ECO:0000313|EMBL:APH06483.1};
OS Bacillus weihaiensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1547283 {ECO:0000313|EMBL:APH06483.1, ECO:0000313|Proteomes:UP000181936};
RN [1] {ECO:0000313|EMBL:APH06483.1, ECO:0000313|Proteomes:UP000181936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alg07 {ECO:0000313|EMBL:APH06483.1,
RC ECO:0000313|Proteomes:UP000181936};
RX PubMed=27901120; DOI=10.1038/srep38248;
RA Zhu Y., Chen P., Bao Y., Men Y., Zeng Y., Yang J., Sun J., Sun Y.;
RT "Complete genome sequence and transcriptomic analysis of a novel marine
RT strain Bacillus weihaiensis reveals the mechanism of brown algae
RT degradation.";
RL Sci. Rep. 6:38248-38248(2016).
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}.
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DR EMBL; CP016020; APH06483.1; -; Genomic_DNA.
DR RefSeq; WP_072581283.1; NZ_CP016020.1.
DR AlphaFoldDB; A0A1L3MVX5; -.
DR STRING; 1547283.A9C19_18050; -.
DR KEGG; bwh:A9C19_18050; -.
DR OrthoDB; 2381757at2; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000181936; Chromosome.
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:UP000181936};
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 227 AA; 25265 MW; 9A5B8A9D4D8DA1DD CRC64;
MYDINEWKHV FKLDPDKDIS DEDLEKVCES GTDAILIGGS DNVTEDNVLN LMARVRRYLI
PCVLEVSSAE SIVPGFDLYF IPSVMNSKGT KWLIDLQHEA VKEYGEIMNW EEILVEGYCI
LNPDCKAAAL TGANTELSIE DVKAYARVAE NMFHLPIFYL EYSGKLGDIE VVKETKSVLN
ETKLFYGGGI SSAEEAKQFA EFADVVVVGN SLYTDLKAAL KTVDAVK
//
