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Reviewed, UniProtKB/Swiss-Prot Q9SLG2 (GGPP4_ARATH)

Last modified February 9, 2010. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Names and origin

Protein namesRecommended name:
    Geranylgeranyl pyrophosphate synthetase 4
      Short name=GGPP synthetase 4
      Short name=GGPS4
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: GGPP4
Ordered Locus Names: At2g18640
ORF Names: F24H14.2
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate.

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

Monomer By similarity.

Subcellular location

Endoplasmic reticulum Ref.4.

Tissue specificity

Faintly expressed in flowers. Ref.4

Sequence similarities

Belongs to the FPP/GGPP synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 372350Geranylgeranyl pyrophosphate synthetase 4
PRO_0000045404

Sites

Metal binding1601Magnesium 1 By similarity
Metal binding1601Magnesium 2 By similarity
Metal binding1661Magnesium 1 By similarity
Metal binding1661Magnesium 2 By similarity
Metal binding2981Magnesium 3 By similarity
Binding site1211Isopentenyl diphosphate By similarity
Binding site1241Isopentenyl diphosphate By similarity
Binding site1531Isopentenyl diphosphate By similarity
Binding site1711Dimethylallyl diphosphate By similarity
Binding site1721Isopentenyl diphosphate By similarity
Binding site2571Dimethylallyl diphosphate By similarity
Binding site2581Dimethylallyl diphosphate By similarity
Binding site2951Dimethylallyl diphosphate By similarity
Binding site3121Dimethylallyl diphosphate By similarity
Binding site3221Dimethylallyl diphosphate By similarity

Experimental info

Sequence conflict1521I → M in AAA96328. Ref.3
Sequence conflict3031E → V in AAA96328. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9SLG2-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: C16F7F798BB7051A

FASTA37240,936
        10         20         30         40         50         60 
MEAQNIFLYL LIVFLSLHFV FTTLKGRLSP ANTRRLIRLL HIPIKSPVAA AIFARKDTRE 

        70         80         90        100        110        120 
FLDSSIKLVN EEDDFGFSFD FKPYMISKAE TINRALDEAI PLIEPLNIHK AMRYAILAGG 

       130        140        150        160        170        180 
KRVRPILCLA ACELVGGEER LAIQAACAVE MIHTMSLIKD DLPCMDNDDL RRGKPTTHKV 

       190        200        210        220        230        240 
FGESVAILSG GALLALAFEH LTEADVSSKK MVRAVKELAK SIGTKGLVAG QAKDLSSEGL 

       250        260        270        280        290        300 
EQNDVGLEDL EYIHVHKTGS LLEASAVIGA VIGGGTEKEI EKVRNFARCI GLLFQVVDDI 

       310        320        330        340        350        360 
LDETKSSEEL GKTAGKDKVA GKLTYPKVIG VEKSKEFVEK LKRDAREHLQ GFDSDKVKPL 

       370 
IALTNFIANR NH 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed: 10617197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations."
Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.
Plant Biotechnol. J. 4:317-324(2006) [PubMed: 17147637] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[3]"Molecular biology of carotenoid biosynthesis in plants."
Bartley G.E., Scolnik P.A., Giuliano G.
Plant Physiol. 45:287-301(1994)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 148-304.
Strain: cv. Wassilewskija.
[4]"Five geranylgeranyl diphosphate synthases expressed in different organs are localized into three subcellular compartments in Arabidopsis."
Okada K., Saito T., Nakagawa T., Kawamukai M., Kamiya Y.
Plant Physiol. 122:1045-1056(2000) [PubMed: 10759500] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC005724 Genomic DNA. Translation: AAD08933.1.
AC006135 Genomic DNA. Translation: AAM15136.1.
DQ446521 mRNA. Translation: ABE65826.1.
L22347 Genomic DNA. Translation: AAA96328.1.
IPIIPI00546039.
PIRG84566.
RefSeqNP_179454.1.
UniGeneAt.66219

3D structure databases

SMRQ9SLG2. Positions 84-367.
ModBaseSearch...

Genome annotation databases

GeneID816379.
KEGGath:AT2G18640.
NMPDRfig|3702.1.peg.8860.

Organism-specific databases

TAIRAt2g18640.

Phylogenomic databases

InParanoidQ9SLG2.
PhylomeDBQ9SLG2.

Enzyme and pathway databases

BioCycMetaCyc:AT2G18640-MONOMER.
BRENDA2.5.1.1. 302.
2.5.1.10. 302.
2.5.1.29. 302.

Gene expression databases

ArrayExpressQ9SLG2.
GenevestigatorQ9SLG2.

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...

Entry information

Entry nameGGPP4_ARATH
AccessionPrimary (citable) accession number: Q9SLG2
Secondary accession number(s): Q1PF45, Q39107
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: May 1, 2000
Last modified: February 9, 2010
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

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