GGGPS_CHIPD
ID GGGPS_CHIPD Reviewed; 252 AA.
AC C7PEQ0;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Geranylgeranylglyceryl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00112};
DE Short=GGGP synthase {ECO:0000255|HAMAP-Rule:MF_00112};
DE Short=GGGPS {ECO:0000255|HAMAP-Rule:MF_00112};
DE EC=2.5.1.41 {ECO:0000255|HAMAP-Rule:MF_00112, ECO:0000269|PubMed:24684232};
DE AltName: Full=(S)-3-O-geranylgeranylglyceryl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00112};
DE AltName: Full=Phosphoglycerol geranylgeranyltransferase {ECO:0000255|HAMAP-Rule:MF_00112};
GN OrderedLocusNames=Cpin_0373 {ECO:0000312|EMBL:ACU57872.1};
OS Chitinophaga pinensis (strain ATCC 43595 / DSM 2588 / LMG 13176 / NBRC
OS 15968 / NCIMB 11800 / UQM 2034).
OC Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=485918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43595 / DSM 2588 / LMG 13176 / NBRC 15968 / NCIMB 11800 / UQM
RC 2034;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Sims D., Meinche L., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Chitinophaga pinensis DSM 2588.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF TYR-143.
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 the transfer of the
CC geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3
CC hydroxyl of sn-glycerol-1-phosphate (G1P). {ECO:0000255|HAMAP-
CC Rule:MF_00112, ECO:0000269|PubMed:24684232}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + sn-glycerol 1-
CC phosphate = diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-
CC phosphate; Xref=Rhea:RHEA:23404, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57677, ChEBI:CHEBI:57685, ChEBI:CHEBI:58756; EC=2.5.1.41;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00112,
CC ECO:0000269|PubMed:24684232};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00112};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:24684232}.
CC -!- SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group II
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00112}.
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DR EMBL; CP001699; ACU57872.1; -; Genomic_DNA.
DR RefSeq; WP_012788048.1; NC_013132.1.
DR AlphaFoldDB; C7PEQ0; -.
DR SMR; C7PEQ0; -.
DR STRING; 485918.Cpin_0373; -.
DR EnsemblBacteria; ACU57872; ACU57872; Cpin_0373.
DR KEGG; cpi:Cpin_0373; -.
DR eggNOG; COG1646; Bacteria.
DR HOGENOM; CLU_068610_0_0_10; -.
DR OMA; ADAIFFM; -.
DR OrthoDB; 1560657at2; -.
DR Proteomes; UP000002215; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0047294; F:phosphoglycerol geranylgeranyltransferase 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; IPR038597; GGGP/HepGP_synthase_sf.
DR InterPro; IPR008205; GGGP_HepGP_synthase.
DR InterPro; IPR010946; GGGP_synth.
DR Pfam; PF01884; PcrB; 1.
DR TIGRFAMs; TIGR01769; GGGP; 1.
DR TIGRFAMs; TIGR01768; GGGP-family; 1.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Transferase.
FT CHAIN 1..252
FT /note="Geranylgeranylglyceryl phosphate synthase"
FT /id="PRO_0000436907"
FT BINDING 25
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 174..180
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 205..206
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 227..228
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT MUTAGEN 143
FT /note="Y->A: Forms homodimers. Strong decrease in
FT activity."
FT /evidence="ECO:0000269|PubMed:24684232"
SQ SEQUENCE 252 AA; 26552 MW; 739A0680ADBFBC6F CRC64;
MHNKIYNSFI DRKAKGIKSF AVLIDPDKVN PADIADLAAK CTAAKVDYIF LGGSLVITNH
LDECVQQFKT LCDIPVVLFP GSPSQVSRYA DALLYLSVIS GRNPELLIGQ HVLSAPAVKK
SGLEVISTGY VLIDGGAPTT VSYISNTTPI PSDKDDIAMC TAMAGEMLGM KVVFMDAGSG
ARKPITESMI SRVASQVSAP IIVGGGIRDA EKAYLNCKAG ADIIVVGNAI EKETSLIKEM
ADAVHAAAPV LK
