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Protein

Geranylgeranylglyceryl phosphate synthase

Gene

MTH_552

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids.UniRule annotation1 Publication

Catalytic activityi

Geranylgeranyl diphosphate + sn-glycerol 1-phosphate = diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate.UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotation

Pathwayi: glycerophospholipid metabolism

This protein is involved in the pathway glycerophospholipid metabolism, which is part of Membrane lipid metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway glycerophospholipid metabolism and in Membrane lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi22 – 221MagnesiumUniRule annotation
Metal bindingi51 – 511MagnesiumUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14508.
MTHE187420:GJNM-552-MONOMER.
UniPathwayiUPA00940.

Names & Taxonomyi

Protein namesi
Recommended name:
Geranylgeranylglyceryl phosphate synthaseUniRule annotation (EC:2.5.1.41UniRule annotation1 Publication)
Short name:
GGGP synthaseUniRule annotation
Short name:
GGGPSUniRule annotation
Short name:
MtGGGPS1 Publication
Alternative name(s):
(S)-3-O-geranylgeranylglyceryl phosphate synthaseUniRule annotation
Phosphoglycerol geranylgeranyltransferaseUniRule annotation
Gene namesi
Ordered Locus Names:MTH_552
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000005223 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi83 – 831V → G: Accepts HepPP as substrate. 1 Publication
Mutagenesisi138 – 1381W → A: Forms homodimers. Shows almost wild-type activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 245245Geranylgeranylglyceryl phosphate synthasePRO_0000138736Add
BLAST

Interactioni

Subunit structurei

Homotetramer (PubMed:21761520). Homohexamer (PubMed:24684232).2 Publications

Protein-protein interaction databases

STRINGi187420.MTH552.

Structurei

Secondary structure

1
245
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 119Combined sources
Beta strandi16 – 216Combined sources
Helixi23 – 253Combined sources
Helixi28 – 4013Combined sources
Beta strandi46 – 494Combined sources
Helixi55 – 6814Combined sources
Beta strandi73 – 764Combined sources
Helixi80 – 823Combined sources
Beta strandi87 – 959Combined sources
Beta strandi98 – 1003Combined sources
Helixi101 – 1044Combined sources
Helixi106 – 11712Combined sources
Beta strandi121 – 13010Combined sources
Helixi134 – 1396Combined sources
Helixi150 – 16213Combined sources
Beta strandi167 – 1715Combined sources
Helixi182 – 19110Combined sources
Beta strandi194 – 2018Combined sources
Helixi205 – 21410Combined sources
Beta strandi217 – 2215Combined sources
Helixi234 – 2418Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MM1X-ray2.80A/B/C/D/E/F1-245[»]
ProteinModelPortaliO26652.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni169 – 1757Glycerol-1-phosphate bindingUniRule annotationCombined sources1 Publication
Regioni200 – 2012Glycerol-1-phosphate bindingUniRule annotationCombined sources1 Publication
Regioni222 – 2232Glycerol-1-phosphate bindingUniRule annotationCombined sources1 Publication

Sequence similaritiesi

Belongs to the GGGP/HepGP synthase family. Group II subfamily.UniRule annotation1 Publication

Phylogenomic databases

eggNOGiarCOG01085. Archaea.
COG1646. LUCA.
KOiK17104.
OMAiEPIPMAY.

Family and domain databases

Gene3Di3.20.20.390. 1 hit.
HAMAPiMF_00112. GGGP_HepGP_synthase.
InterProiIPR008205. GGGP_HepGP_synthase.
IPR010946. GGGP_synth.
[Graphical view]
PfamiPF01884. PcrB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01769. GGGP. 1 hit.
TIGR01768. GGGP-family. 1 hit.

Sequencei

Sequence statusi: Complete.

O26652-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVEDYFHDI LRERKIHLTL IDPEEQTPEE AVEIARAAIR GGTDGIMLGG
60 70 80 90 100
STTDSSELDN TARALRENID VPIILFPGNT TGVSRYADAI FFMSLLNSTN
110 120 130 140 150
PYWIIGAQAL GAATVKKMGI EALPMGYLVV EPGGTVGWVG DTKPVPRNKP
160 170 180 190 200
DIAAAYAMAA EFLGMRLFYL EAGSGAPEHV PEEMIALVKR CTDQILIVGG
210 220 230 240
GIRSGEDAAR VAGAGADVVV TGTVVENSDN VEDKIREIVE GMGSV
Length:245
Mass (Da):26,119
Last modified:September 23, 2008 - v2
Checksum:i7CB5D1AFF72F1C53
GO

Sequence cautioni

The sequence AAB85058.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB85058.1. Different initiation.
PIRiA69173.
RefSeqiWP_048060841.1. NC_000916.1.

Genome annotation databases

EnsemblBacteriaiAAB85058; AAB85058; MTH_552.
GeneIDi1470513.
KEGGimth:MTH_552.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB85058.1. Different initiation.
PIRiA69173.
RefSeqiWP_048060841.1. NC_000916.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MM1X-ray2.80A/B/C/D/E/F1-245[»]
ProteinModelPortaliO26652.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi187420.MTH552.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB85058; AAB85058; MTH_552.
GeneIDi1470513.
KEGGimth:MTH_552.

Phylogenomic databases

eggNOGiarCOG01085. Archaea.
COG1646. LUCA.
KOiK17104.
OMAiEPIPMAY.

Enzyme and pathway databases

UniPathwayiUPA00940.
BioCyciMetaCyc:MONOMER-14508.
MTHE187420:GJNM-552-MONOMER.

Family and domain databases

Gene3Di3.20.20.390. 1 hit.
HAMAPiMF_00112. GGGP_HepGP_synthase.
InterProiIPR008205. GGGP_HepGP_synthase.
IPR010946. GGGP_synth.
[Graphical view]
PfamiPF01884. PcrB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01769. GGGP. 1 hit.
TIGR01768. GGGP-family. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
  2. "Functional assignment of an enzyme that catalyzes the synthesis of an archaea-type ether lipid in bacteria."
    Guldan H., Matysik F.M., Bocola M., Sterner R., Babinger P.
    Angew. Chem. Int. Ed. Engl. 50:8188-8191(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  3. "A comprehensive analysis of the geranylgeranylglyceryl phosphate synthase enzyme family identifies novel members and reveals mechanisms of substrate specificity and quaternary structure organization."
    Peterhoff D., Beer B., Rajendran C., Kumpula E.P., Kapetaniou E., Guldan H., Wierenga R.K., Sterner R., Babinger P.
    Mol. Microbiol. 92:885-899(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH GLYCEROL 1-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF VAL-83 AND TRP-138.

Entry informationi

Entry nameiGGGPS_METTH
AccessioniPrimary (citable) accession number: O26652
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 23, 2008
Last modified: July 6, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.