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Protein

Geranylgeranylglyceryl phosphate synthase

Gene

AF_0403

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
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. To a much lesser extent, is also able to use heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) as the prenyl donor.3 Publications

Catalytic activityi

Geranylgeranyl diphosphate + sn-glycerol 1-phosphate = diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate.3 Publications

Cofactori

Mg2+By similarity

Pathwayi: glycerophospholipid metabolism

This protein is involved in the pathway glycerophospholipid metabolism, which is part of Membrane lipid metabolism.1 Publication
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
Binding sitei11 – 111Glycerol-1-phosphate
Metal bindingi13 – 131MagnesiumSequence analysis
Metal bindingi39 – 391MagnesiumSequence analysis
Binding sitei170 – 1701Glycerol-1-phosphate; via amide nitrogen
Binding sitei195 – 1951Glycerol-1-phosphate; via amide nitrogen
Binding sitei216 – 2161Glycerol-1-phosphate

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

BioCyciAFUL224325:GJBC-413-MONOMER.
UniPathwayiUPA00940.

Names & Taxonomyi

Protein namesi
Recommended name:
Geranylgeranylglyceryl phosphate synthaseCurated (EC:2.5.1.413 Publications)
Short name:
AfGGGPSCurated
Short name:
GGGP synthase1 Publication
Short name:
GGGPSCurated
Alternative name(s):
(S)-3-O-geranylgeranylglyceryl phosphate synthaseCurated
Phosphoglycerol geranylgeranyltransferaseCurated
Gene namesi
Ordered Locus Names:AF_0403
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
Proteomesi
  • UP000002199 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi99 – 991W → A: Increased efficiency with HepPP as substrate, wich becomes similar to that of B.subtilis PcrB. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 231231Geranylgeranylglyceryl phosphate synthasePRO_0000138728Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi224325.AF0403.

Structurei

Secondary structure

1
231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Beta strandi8 – 125Combined sources
Helixi20 – 278Combined sources
Turni28 – 303Combined sources
Beta strandi32 – 365Combined sources
Helixi44 – 5411Combined sources
Beta strandi61 – 633Combined sources
Beta strandi75 – 839Combined sources
Beta strandi86 – 883Combined sources
Turni89 – 935Combined sources
Helixi94 – 1018Combined sources
Helixi102 – 1065Combined sources
Helixi107 – 1159Combined sources
Beta strandi119 – 1268Combined sources
Helixi132 – 1365Combined sources
Helixi145 – 15713Combined sources
Beta strandi162 – 1676Combined sources
Helixi175 – 18410Combined sources
Beta strandi186 – 1949Combined sources
Helixi199 – 20810Combined sources
Beta strandi209 – 2146Combined sources
Helixi216 – 2216Combined sources
Helixi223 – 2275Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F6UX-ray1.55A/B1-231[»]
2F6XX-ray2.00A/B1-231[»]
ProteinModelPortaliO29844.
SMRiO29844. Positions 1-231.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO29844.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni165 – 1673Glycerol-1-phosphate binding

Sequence similaritiesi

Belongs to the GGGP synthase family.Curated

Phylogenomic databases

eggNOGiarCOG01085. Archaea.
COG1646. LUCA.
KOiK17104.
OMAiIVYIEYS.

Family and domain databases

Gene3Di3.20.20.390. 1 hit.
HAMAPiMF_00112. GGGP_HepGP_synthase.
InterProiIPR008205. GGGP_HepGP_synthase.
IPR026438. GGGP_synthase_archaea.
[Graphical view]
PfamiPF01884. PcrB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01768. GGGP-family. 1 hit.
TIGR04146. GGGPS_Afulg. 1 hit.

Sequencei

Sequence statusi: Complete.

O29844-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRWRKWRHIT KLDPDRTNTD EIIKAVADSG TDAVMISGTQ NVTYEKARTL
60 70 80 90 100
IEKVSQYGLP IVVEPSDPSN VVYDVDYLFV PTVLNSADGD WITGKHAQWV
110 120 130 140 150
RMHYENLQKF TEIIESEFIQ IEGYIVLNPD SAVARVTKAL CNIDKELAAS
160 170 180 190 200
YALVGEKLFN LPIIYIEYSG TYGNPELVAE VKKVLDKARL FYGGGIDSRE
210 220 230
KAREMLRYAD TIIVGNVIYE KGIDAFLETL P
Length:231
Mass (Da):26,144
Last modified:January 1, 1998 - v1
Checksum:i935D2D657550ABDD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB90827.1.
PIRiC69300.
RefSeqiWP_010877910.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB90827; AAB90827; AF_0403.
GeneIDi24793941.
KEGGiafu:AF_0403.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB90827.1.
PIRiC69300.
RefSeqiWP_010877910.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F6UX-ray1.55A/B1-231[»]
2F6XX-ray2.00A/B1-231[»]
ProteinModelPortaliO29844.
SMRiO29844. Positions 1-231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224325.AF0403.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB90827; AAB90827; AF_0403.
GeneIDi24793941.
KEGGiafu:AF_0403.

Phylogenomic databases

eggNOGiarCOG01085. Archaea.
COG1646. LUCA.
KOiK17104.
OMAiIVYIEYS.

Enzyme and pathway databases

UniPathwayiUPA00940.
BioCyciAFUL224325:GJBC-413-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO29844.

Family and domain databases

Gene3Di3.20.20.390. 1 hit.
HAMAPiMF_00112. GGGP_HepGP_synthase.
InterProiIPR008205. GGGP_HepGP_synthase.
IPR026438. GGGP_synthase_archaea.
[Graphical view]
PfamiPF01884. PcrB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01768. GGGP-family. 1 hit.
TIGR04146. GGGPS_Afulg. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
    Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
    , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
    Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
  2. "Reconstruction of the archaeal isoprenoid ether lipid biosynthesis pathway in Escherichia coli through digeranylgeranylglyceryl phosphate."
    Lai D., Lluncor B., Schroeder I., Gunsalus R.P., Liao J.C., Monbouquette H.G.
    Metab. Eng. 11:184-191(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
  3. "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: FUNCTION, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF TRP-99.
  4. "The crystal structure of (S)-3-O-geranylgeranylglyceryl phosphate synthase reveals an ancient fold for an ancient enzyme."
    Payandeh J., Fujihashi M., Gillon W., Pai E.F.
    J. Biol. Chem. 281:6070-6078(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH G1P, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

Entry informationi

Entry nameiGGGPS_ARCFU
AccessioniPrimary (citable) accession number: O29844
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: January 20, 2016
This is version 106 of the entry and version 1 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.