PCRB_GEOKA
ID PCRB_GEOKA Reviewed; 239 AA.
AC Q5L3C1;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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, ECO:0000269|PubMed:21761520, ECO:0000269|PubMed:24684232};
DE AltName: Full=Glycerol-1-phosphate heptaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_00112};
GN Name=pcrB {ECO:0000255|HAMAP-Rule:MF_00112}; OrderedLocusNames=GK0274;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=21761520; DOI=10.1002/anie.201101832;
RA Guldan H., Matysik F.M., Bocola M., Sterner R., Babinger P.;
RT "Functional assignment of an enzyme that catalyzes the synthesis of an
RT archaea-type ether lipid in bacteria.";
RL Angew. Chem. Int. Ed. Engl. 50:8188-8191(2011).
RN [3] {ECO:0007744|PDB:4NAE, ECO:0007744|PDB:4NAF}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-228 IN COMPLEX WITH GLYCEROL
RP 1-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=24684232; DOI=10.1111/mmi.12596;
RA Peterhoff D., Beer B., Rajendran C., Kumpula E.P., Kapetaniou E.,
RA Guldan H., Wierenga R.K., Sterner R., Babinger P.;
RT "A comprehensive analysis of the geranylgeranylglyceryl phosphate synthase
RT enzyme family identifies novel members and reveals mechanisms of substrate
RT specificity and quaternary structure organization.";
RL Mol. Microbiol. 92:885-899(2014).
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. To a much lesser extent, is also able to
CC use geranylgeranyl diphosphate (GGPP; C20) as the prenyl donor.
CC {ECO:0000269|PubMed:21761520, ECO:0000269|PubMed:24684232}.
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 ECO:0000269|PubMed:21761520, ECO:0000269|PubMed:24684232};
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 ECO:0000269|PubMed:21761520, ECO:0000269|PubMed:24684232}.
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; BA000043; BAD74559.1; -; Genomic_DNA.
DR RefSeq; WP_011229783.1; NC_006510.1.
DR PDB; 4NAE; X-ray; 2.00 A; A=3-227, B=1-227.
DR PDB; 4NAF; X-ray; 1.90 A; A=3-228, B=2-228.
DR PDBsum; 4NAE; -.
DR PDBsum; 4NAF; -.
DR AlphaFoldDB; Q5L3C1; -.
DR SMR; Q5L3C1; -.
DR STRING; 235909.GK0274; -.
DR EnsemblBacteria; BAD74559; BAD74559; GK0274.
DR KEGG; gka:GK0274; -.
DR eggNOG; COG1646; Bacteria.
DR HOGENOM; CLU_095211_0_0_9; -.
DR OMA; TGAHKEW; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000001172; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002094; F:polyprenyltransferase activity; IGI:UniProtKB.
DR GO; GO:0004659; F:prenyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IGI:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Metal-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..239
FT /note="Heptaprenylglyceryl phosphate synthase"
FT /id="PRO_0000138712"
FT BINDING 12
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112,
FT ECO:0000269|PubMed:24684232, ECO:0007744|PDB:4NAE"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 159..164
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112,
FT ECO:0000269|PubMed:24684232, ECO:0007744|PDB:4NAE"
FT BINDING 189
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112,
FT ECO:0000269|PubMed:24684232, ECO:0007744|PDB:4NAE"
FT BINDING 209..210
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112,
FT ECO:0000269|PubMed:24684232, ECO:0007744|PDB:4NAE"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:4NAF"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:4NAF"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:4NAF"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:4NAF"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:4NAF"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:4NAF"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:4NAF"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:4NAF"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:4NAF"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:4NAF"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:4NAF"
FT TURN 90..94
FT /evidence="ECO:0007829|PDB:4NAF"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:4NAF"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:4NAF"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:4NAF"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:4NAF"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:4NAF"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:4NAF"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:4NAF"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:4NAF"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:4NAF"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:4NAF"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:4NAF"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:4NAF"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:4NAF"
SQ SEQUENCE 239 AA; 26611 MW; 2B4FFB67513DDCAB CRC64;
MEEIRAWRHV FKLDPNKPID DERLERLCES GTDAVIVGGT DGVTIDNVLD LLARIRRFSV
PCALEVTDVE ALTPGFDVYL VPIVLNSRQA EWIIGRHHEA VKQYGDMMNW DEIAAEGYCI
LNPECKAAKL TRADTELDVD DIVAYARLAE HLYKLPIFYL EYSGVYGDPS VVEKVKQALD
QTQLFYGGGI TTPEQAEHMA RYADTVVVGN AIYDAFEQAL ATVAAVKQMA GQRNGDDGK
