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Entry: A0A0K9F362_9BACI
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ID   A0A0K9F362_9BACI        Unreviewed;       229 AA.
AC   A0A0K9F362;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=ACZ11_22390 {ECO:0000313|EMBL:KMY28513.1};
OS   Lysinibacillus xylanilyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=582475 {ECO:0000313|EMBL:KMY28513.1, ECO:0000313|Proteomes:UP000037326};
RN   [1] {ECO:0000313|Proteomes:UP000037326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23493 {ECO:0000313|Proteomes:UP000037326};
RG   Consortium for Microbial Forensics and Genomics (microFORGE);
RA   Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA   Blagden T., Winegar R.A.;
RL   Submitted (JUL-2015) 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:KMY28513.1}.
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DR   EMBL; LFXJ01000011; KMY28513.1; -; Genomic_DNA.
DR   RefSeq; WP_049668782.1; NZ_LFXJ01000011.1.
DR   AlphaFoldDB; A0A0K9F362; -.
DR   PATRIC; fig|582475.4.peg.5085; -.
DR   OrthoDB; 2381757at2; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000037326; 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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00112}.
FT   BINDING         11
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT   BINDING         39
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT   BINDING         158..163
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT   BINDING         188
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT   BINDING         208..209
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
SQ   SEQUENCE   229 AA;  25472 MW;  61516BA00D74C3BB CRC64;
     MDYLEWRHVF KLDPAKDISD EALEKICESG TDVIIVGGTD GVTLDGVLDL LVRVRRFEVP
     IALEISAIDS VTPGYDYYFI PTVLNSDDPK WIKNLHHEAI KEYGDIMVWD ELVAEGYCIL
     NPDCKVAEVT NAKTDLSIDD VVAYARLAEN FFRLPVFYVE YSGTYGDIEV VSAVKNELKN
     TRLFYGGGIT SAQQAAEMAK YADTVVVGNI IYEDLKAALA TVKAVKNNI
//
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