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O27170 (DGGGP_METTH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Digeranylgeranylglyceryl phosphate synthase

Short name=DGGGP synthase
Short name=DGGGPS
EC=2.5.1.42
Alternative name(s):
(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase
Geranylgeranylglycerol-phosphate geranylgeranyltransferase
Gene names
Ordered Locus Names:MTH_1098
OrganismMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) [Reference proteome] [HAMAP]
Taxonomic identifier187420 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length281 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids. Ref.2

Catalytic activity

Geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate = diphosphate + 2,3-bis-O-(geranylgeranyl)glycerol 1-phosphate. Ref.2

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01286

Pathway

Membrane lipid metabolism; glycerophospholipid metabolism. HAMAP-Rule MF_01286

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.2.

Sequence similarities

Belongs to the UbiA prenyltransferase family. DGGGP synthase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 281281Digeranylgeranylglyceryl phosphate synthase HAMAP-Rule MF_01286
PRO_0000350692

Regions

Transmembrane7 – 2721Helical; Potential
Transmembrane32 – 5221Helical; Potential
Transmembrane72 – 9120Helical; Potential
Transmembrane95 – 11723Helical; Potential
Transmembrane128 – 14821Helical; Potential
Transmembrane193 – 21321Helical; Potential
Transmembrane214 – 23421Helical; Potential
Transmembrane258 – 27821Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
O27170 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: E6661FE221C85278

FASTA28130,132
        10         20         30         40         50         60 
MNPYIEILRP VNAVMAVITV MLMALITGRF DFSVLLASVV VFTATGAGNV INDYFDHEID 

        70         80         90        100        110        120 
AINRPERPIP SGRISRGVAG VYSIILFALA SLMGFYLGLL PGLVVVSSSL LMVYYAWRLK 

       130        140        150        160        170        180 
KRCLVGNITI SFLTGLSFVF GGIVLGEVRA SILLGFYAFL MTMAREIVKD MEDVEGDRAE 

       190        200        210        220        230        240 
GATTLPITHG MRISGVLAAS FMLIASLTSP SLYLLGIFSA LYIPVLLLAV AVFLRAAIMI 

       250        260        270        280 
LRGQDRATAS RVSRMIKVGM ALTFIAFAAG SGTITALTGL S 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
[2]"Biosynthesis of archaebacterial ether lipids. Formation of ether linkages by prenyltransferases."
Zhang D., Poulter C.D.
J. Am. Chem. Soc. 115:1270-1277(1993)
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
Strain: Marburg / DSM 2133.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000666 Genomic DNA. Translation: AAB85587.1.
PIRH69012.
RefSeqNP_276226.1. NC_000916.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING187420.MTH1098.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB85587; AAB85587; MTH_1098.
GeneID1471506.
KEGGmth:MTH1098.

Phylogenomic databases

eggNOGCOG0382.
KOK17105.
OMARTYLELM.
ProtClustDBPRK12884.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14509.
MTHE187420:GJNM-1100-MONOMER.
UniPathwayUPA00940.

Family and domain databases

HAMAPMF_01286. DGGGP_synth.
InterProIPR023547. DGGGP_synth.
IPR000537. UbiA_prenyltransferase.
[Graphical view]
PfamPF01040. UbiA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDGGGP_METTH
AccessionPrimary (citable) accession number: O27170
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways