GGGPS_METTM
ID GGGPS_METTM Reviewed; 245 AA.
AC P0C882; D9PWD8;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 65.
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:11732904, ECO:0000269|Ref.3};
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=MTBMA_c09410;
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
RN [2]
RP PROTEIN SEQUENCE OF 1-35; 93-113; 125-150 AND 158-183, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=11732904; DOI=10.1021/bi0111799;
RA Soderberg T., Chen A., Poulter C.D.;
RT "Geranylgeranylglyceryl phosphate synthase. Characterization of the
RT recombinant enzyme from Methanobacterium thermoautotrophicum.";
RL Biochemistry 40:14847-14854(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, AND ACTIVITY
RP REGULATION.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RA Zhang D., Poulter C.D.;
RT "Biosynthesis of archaebacterial ether lipids. Formation of ether linkages
RT by prenyltransferases.";
RL J. Am. Chem. Soc. 115:1270-1277(1993).
RN [4]
RP FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=8408023; DOI=10.1016/s0021-9258(20)80598-5;
RA Chen A., Zhang D., Poulter C.D.;
RT "(S)-geranylgeranylglyceryl phosphate synthase. Purification and
RT characterization of the first pathway-specific enzyme in archaebacterial
RT membrane lipid biosynthesis.";
RL J. Biol. Chem. 268:21701-21705(1993).
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). This reaction is the first
CC ether-bond-formation step in the biosynthesis of archaeal membrane
CC lipids. Cannot use sn-glycerol-3-phosphate (G3P) or
CC dihydroxyacetonephosphate (DHAP) as substrate.
CC {ECO:0000269|PubMed:11732904, ECO:0000269|PubMed:8408023,
CC ECO:0000269|Ref.3}.
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:11732904, ECO:0000269|Ref.3};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00112,
CC ECO:0000269|PubMed:8408023, ECO:0000269|Ref.3};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA in vitro. {ECO:0000269|Ref.3}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.5 uM for G1P (at 55 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:11732904};
CC KM=506 nM for GGPP (at 55 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:11732904};
CC Vmax=4.0 umol/min/mg enzyme (at 55 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:11732904};
CC pH dependence:
CC Optimum pH is 6.0-9.0. {ECO:0000269|PubMed:11732904};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius at pH 8.0.
CC {ECO:0000269|PubMed:11732904};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_00112}.
CC -!- SUBUNIT: Homopentamer. {ECO:0000269|PubMed:11732904}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00112,
CC ECO:0000269|PubMed:8408023}.
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; CP001710; ADL58536.1; -; Genomic_DNA.
DR RefSeq; WP_013295760.1; NC_014408.1.
DR AlphaFoldDB; P0C882; -.
DR SMR; P0C882; -.
DR STRING; 79929.MTBMA_c09410; -.
DR EnsemblBacteria; ADL58536; ADL58536; MTBMA_c09410.
DR GeneID; 9704649; -.
DR KEGG; mmg:MTBMA_c09410; -.
DR PATRIC; fig|79929.8.peg.920; -.
DR HOGENOM; CLU_068610_0_0_2; -.
DR OMA; ADAIFFM; -.
DR OrthoDB; 94629at2157; -.
DR SABIO-RK; P0C882; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000000345; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 Cytoplasm; Direct protein sequencing; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Metal-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Transferase.
FT CHAIN 1..245
FT /note="Geranylgeranylglyceryl phosphate synthase"
FT /id="PRO_0000350773"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 51
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 169..175
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 200..201
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 222..223
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT CONFLICT 149
FT /note="K -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 25818 MW; 407E79BB41A9800A CRC64;
MKVEDYFHDI LGERKIHLTL IDPEEQTPEE AVEIAEAAIR GGTDGIMLGG STTDSSELDA
TAGALRENID VPIILFPGNT TGVSRHADAI FFMSLLNSNN PYWIIGAQAL GAPAVKKMGI
EALPMGYLVV EPGGTVGWVG DTKPVPRNKP DIAAAYAMAA EFLGMRLFYL EAGSGAPQHV
PEEMISLVKR CTDQILIVGG GIRTGADAAR VAGAGADIIV TGTVVENSSN VEDKIREIVE
GMGSL
