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Reviewed, UniProtKB/Swiss-Prot P34802 (GGPP1_ARATH)

Last modified February 9, 2010. Version 81. 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 1, chloroplastic
      Short name=GGPP synthetase 1
      Short name=GGPS1
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
Ordered Locus Names: At4g36810
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length371 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.

Subcellular location

Plastidchloroplast Ref.3.

Tissue specificity

Expressed ubiquitously. Ref.3

Sequence similarities

Belongs to the FPP/GGPP synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5656Chloroplast Potential
Chain57 – 371315Geranylgeranyl pyrophosphate synthetase 1, chloroplastic
PRO_0000016471

Regions

Compositional bias21 – 5838Ser-rich

Sites

Metal binding1551Magnesium 1 By similarity
Metal binding1551Magnesium 2 By similarity
Metal binding1611Magnesium 1 By similarity
Metal binding1611Magnesium 2 By similarity
Metal binding2971Magnesium 3 By similarity
Binding site1161Isopentenyl diphosphate By similarity
Binding site1191Isopentenyl diphosphate By similarity
Binding site1481Isopentenyl diphosphate By similarity
Binding site1661Dimethylallyl diphosphate By similarity
Binding site1671Isopentenyl diphosphate By similarity
Binding site2561Dimethylallyl diphosphate By similarity
Binding site2571Dimethylallyl diphosphate By similarity
Binding site2941Dimethylallyl diphosphate By similarity
Binding site3111Dimethylallyl diphosphate By similarity
Binding site3211Dimethylallyl diphosphate By similarity

Experimental info

Sequence conflict1081R → S in AAA32797. Ref.1
Sequence conflict1411A → R in AAA32797. Ref.1
Sequence conflict1921A → S in AAA32797. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P34802-1 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: EFA8088A75B6A005

FASTA37140,174
        10         20         30         40         50         60 
MASVTLGSWI VVHHHNHHHP SSILTKSRSR SCPITLTKPI SFRSKRTVSS SSSIVSSSVV 

        70         80         90        100        110        120 
TKEDNLRQSE PSSFDFMSYI ITKAELVNKA LDSAVPLREP LKIHEAMRYS LLAGGKRVRP 

       130        140        150        160        170        180 
VLCIAACELV GGEESTAMPA ACAVEMIHTM SLIHDDLPCM DNDDLRRGKP TNHKVFGEDV 

       190        200        210        220        230        240 
AVLAGDALLS FAFEHLASAT SSDVVSPVRV VRAVGELAKA IGTEGLVAGQ VVDISSEGLD 

       250        260        270        280        290        300 
LNDVGLEHLE FIHLHKTAAL LEASAVLGAI VGGGSDDEIE RLRKFARCIG LLFQVVDDIL 

       310        320        330        340        350        360 
DVTKSSKELG KTAGKDLIAD KLTYPKIMGL EKSREFAEKL NREARDQLLG FDSDKVAPLL 

       370 
ALANYIAYRQ N 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of an Arabidopsis cDNA for geranylgeranyl pyrophosphate synthase."
Scolnik P.A., Bartley G.E.
Plant Physiol. 104:1469-1470(1994) [PubMed: 8016276] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed: 10617198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"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
L25813 mRNA. Translation: AAA32797.1.
Z99708 Genomic DNA. Translation: CAB16803.1.
AL161590 Genomic DNA. Translation: CAB80347.1.
IPIIPI00516537.
PIRF85434.
RefSeqNP_195399.1.
UniGeneAt.304

3D structure databases

SMRP34802. Positions 75-366.
ModBaseSearch...

Proteomic databases

PRIDEP34802.

Genome annotation databases

GeneID829834.
GenomeReviewsGene locus AT4G36810 in contig CT486007_GR.
KEGGath:AT4G36810.

Organism-specific databases

TAIRAt4g36810.

Phylogenomic databases

eggNOGKOG0776.
HOGENOMHBG732667.
InParanoidP34802.
OMAKPTCHVV.
PhylomeDBP34802.

Enzyme and pathway databases

BioCycMetaCyc:AT4G36810-MONOMER.
BRENDA2.5.1.1. 302.
2.5.1.10. 302.
2.5.1.29. 302.

Gene expression databases

ArrayExpressP34802.
GenevestigatorP34802.
GermOnlineAT4G36810. Arabidopsis thaliana.

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 nameGGPP1_ARATH
AccessionPrimary (citable) accession number: P34802
Secondary accession number(s): O23201
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: April 27, 2001
Last modified: February 9, 2010
This is version 81 of the entry and version 2 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