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Reviewed, UniProtKB/Swiss-Prot P56966 (GGPPS_BOVIN)

Last modified January 19, 2010. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Geranylgeranyl pyrophosphate synthetase
      Short name=GGPP synthetase
      Short name=GGPPSase
Alternative name(s):
    Geranylgeranyl diphosphate synthase
Including the following 3 domains:
    1- Recommended name:
            Dimethylallyltranstransferase
              EC=2.5.1.1
    2- Recommended name:
            Geranyltranstransferase
              EC=2.5.1.10
    3- Recommended name:
            Farnesyltranstransferase
              EC=2.5.1.29
Gene names
Name: GGPS1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length300 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins.

Catalytic activity

Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate.

Geranyl diphosphate + isopentenyl diphosphate = diphosphate + trans,trans-farnesyl diphosphate.

Trans,trans-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + geranylgeranyl diphosphate.

Cofactor

Binds 3 magnesium ions per subunit By similarity.

Pathway

Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.

Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.

Isoprenoid biosynthesis; geranylgeranyl diphosphate biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and isopentenyl diphosphate: step 1/1.

Subunit structure

Homohexamer; trimer of homodimers By similarity.

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the FPP/GGPP synthetase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 300300Geranylgeranyl pyrophosphate synthetase
PRO_0000123961

Sites

Metal binding641Magnesium 1 By similarity
Metal binding641Magnesium 2 By similarity
Metal binding681Magnesium 1 By similarity
Metal binding681Magnesium 2 By similarity
Metal binding1881Magnesium 3 By similarity
Binding site251Isopentenyl diphosphate By similarity
Binding site281Isopentenyl diphosphate By similarity
Binding site571Isopentenyl diphosphate By similarity
Binding site731Dimethylallyl diphosphate By similarity
Binding site741Isopentenyl diphosphate By similarity
Binding site1511Dimethylallyl diphosphate By similarity
Binding site1521Dimethylallyl diphosphate By similarity
Binding site1851Dimethylallyl diphosphate By similarity
Binding site2021Dimethylallyl diphosphate By similarity
Binding site2121Dimethylallyl diphosphate By similarity

Amino acid modifications

Modified residue251N6-acetyllysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
P56966-1 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: FF6606F42CB9AE81

FASTA30034,900
        10         20         30         40         50         60 
MEKTQETVQR ILLEPYKYLL QLPGKQVRTK LSQAFNHWLK VPEDKLQIII EVTEMLHNAS 

        70         80         90        100        110        120 
LLIDDIEDNS KLRRGFPVAH SIYGIPSVIN SANYVYFLGL EKVLTLNHPD AVKLFTRQLL 

       130        140        150        160        170        180 
ELHQGQGLDI YWRDNYTCPT EEEYKAMVLQ KTGGLFGLAV GLMQLFSDYK EDLKPLLDTL 

       190        200        210        220        230        240 
GLFFQIRDDY ANLHSKEYSE NKSFCEDLTE GKFSFPTIHA IWSRPESTQV QNILRQRTEN 

       250        260        270        280        290        300 
IDIKKYCVHY LENVGSFEYT RNTLKELESK AYKQIDARGG NPELVALIKH LSKMFKEENE

« Hide

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References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Brain cortex.
[2]"Human geranylgeranyl diphosphate synthase. cDNA cloning and expression."
Kuzuguchi T., Morita Y., Sagami I., Sagami H., Ogura K.
J. Biol. Chem. 274:5888-5894(1999) [PubMed: 10026212] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-296, PROTEIN SEQUENCE OF 3-16 AND 289-296.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC120313 mRNA. Translation: AAI20314.1.
IPIIPI00690042.
RefSeqNP_001073269.1.

3D structure databases

SMRP56966. Positions 6-295.
ModBaseSearch...

Protein-protein interaction databases

STRINGP56966.

Genome annotation databases

EnsemblENSBTAT00000017376; ENSBTAP00000017376; ENSBTAG00000013068; Bos taurus. [Genome view]
GeneID780882.
KEGGbta:780882.

Organism-specific databases

CTD780882.

Phylogenomic databases

eggNOGmaNOG04590.
HOVERGENP56966.
InParanoidP56966.
OMADIEDNSI.
OrthoDBEOG9G7FJM.
PhylomeDBP56966.

Enzyme and pathway databases

BRENDA2.5.1.1. 251.
2.5.1.10. 251.
2.5.1.29. 251.

Family and domain databases

InterProIPR000092. Polyprenyl_synt.
IPR017446. Polyprenyl_synth-rel.
IPR008949. Terpenoid_synth.
[Graphical view]
Gene3DG3DSA:1.10.600.10. Terpenoid_synth. 1 hit.
PANTHERPTHR12001. Polyprenyl_synt. 1 hit.
PfamPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
PROSITEPS00723. POLYPRENYL_SYNTHET_1. 1 hit.
PS00444. POLYPRENYL_SYNTHET_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameGGPPS_BOVIN
AccessionPrimary (citable) accession number: P56966
Secondary accession number(s): Q0VC78
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: April 3, 2007
Last modified: January 19, 2010
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents