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P56966 (GGPPS_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Geranylgeranyl pyrophosphate synthase
Short name=GGPP synthase
Short name=GGPPSase
Alternative name(s):
(2E,6E)-farnesyl diphosphate synthase
Dimethylallyltranstransferase
EC=2.5.1.1
Farnesyl diphosphate synthase
Farnesyltranstransferase
EC=2.5.1.29
Geranylgeranyl diphosphate synthase
Geranyltranstransferase
EC=2.5.1.10
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

Protein attributes

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

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 + (2E,6E)-farnesyl diphosphate.

(2E,6E)-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 synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 300300Geranylgeranyl pyrophosphate synthase
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

Sequences

Sequence LengthMass (Da)Tools
P56966 [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

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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC120313 mRNA. Translation: AAI20314.1.
IPIIPI00690042.
RefSeqNP_001073269.1. NM_001079801.1.
UniGeneBt.71777.

3D structure databases

ProteinModelPortalP56966.
SMRP56966. Positions 6-295.
ModBaseSearch...

Protein-protein interaction databases

STRINGP56966.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000017376; ENSBTAP00000017376; ENSBTAG00000013068.
GeneID780882.
KEGGbta:780882.

Organism-specific databases

CTD9453.

Phylogenomic databases

eggNOGmaNOG04590.
GeneTreeENSGT00390000010417.
HOVERGENHBG051729.
InParanoidP56966.
OMAAVKIFTR.
OrthoDBEOG4CG08P.
PhylomeDBP56966.

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.
KOK00804.
PANTHERPTHR12001. Polyprenyl_synt. 1 hit.
PfamPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMSSF48576. Terpenoid_synth. 1 hit.
PROSITEPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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: November 16, 2011
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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