Skip Header

Contribute Send feedback
Read comments (?) or add your own

P34802 (GGPP1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 1, chloroplastic
Short name=GGPP synthase 1
Short name=GGPS1
Alternative name(s):
(2E,6E)-farnesyl diphosphate synthase 1
Dimethylallyltranstransferase 1
EC=2.5.1.1
Farnesyl diphosphate synthase 1
Farnesyltranstransferase 1
EC=2.5.1.29
Geranyltranstransferase 1
EC=2.5.1.10
Gene names
Name:GGPPS1
Synonyms:GGPPS11, GGPS1
Ordered Locus Names:At4g36810
ORF Names:C7A10.550
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length371 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Heterodimeric geranyl(geranyl)-diphosphate (GPP) synthase large subunit. In vitro, the large subunit catalyzes mainly the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate while the small subunit alone is inactive. Upon association of the two subunits, the product profile changes and the production of gerany-diphosphate is strongly increased. Ref.6

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

Monomer. Part of an heterodimeric geranyl(geranyl)diphosphate synthase. Interacts with GGR. Ref.6

Subcellular location

Plastid › chloroplast Ref.5.

Tissue specificity

Expressed ubiquitously. Ref.5

Sequence similarities

Belongs to the FPP/GGPP synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5656Chloroplast Potential
Chain57 – 371315Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 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 [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]"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E. expand/collapse author list , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
Nature 391:485-488(1998) [PubMed: 9461215] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"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.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"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.
[6]"Heterodimeric geranyl(geranyl)diphosphate synthase from hop (Humulus lupulus) and the evolution of monoterpene biosynthesis."
Wang G., Dixon R.A.
Proc. Natl. Acad. Sci. U.S.A. 106:9914-9919(2009) [PubMed: 19482937] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH GGR.
+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.
CP002687 Genomic DNA. Translation: AEE86705.1.
IPIIPI00516537.
PIRF85434.
RefSeqNP_195399.1. NM_119845.3.
UniGeneAt.304.

3D structure databases

ProteinModelPortalP34802.
SMRP34802. Positions 75-366.
ModBaseSearch...

Protein-protein interaction databases

STRINGP34802.

Proteomic databases

PRIDEP34802.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G36810.1; AT4G36810.1; AT4G36810.
GeneID829834.
GenomeReviewsGene locus AT4G36810 in contig CT486007_GR.
KEGGath:AT4G36810.

Organism-specific databases

TAIRAt4g36810.

Phylogenomic databases

eggNOGKOG0776.
HOGENOMHBG732667.
InParanoidP34802.
OMAIASYQAQ.
PhylomeDBP34802.
ProtClustDBCLSN2915918.

Enzyme and pathway databases

BioCycARA:AT4G36810-MONOMER.
MetaCyc:AT4G36810-MONOMER.
BRENDA2.5.1.29. 399.

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.
KOK13789.
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 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: January 25, 2012
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents