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UniProtKB/Swiss-Prot entry P34802


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GGPP1_ARATH
Primary accession number P34802
Secondary accession number O23201
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on April 27, 2001 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 69)
Name and origin of the protein
Protein name Geranylgeranyl pyrophosphate synthetase 1, chloroplastic [Precursor]
Synonyms GGPP synthetase 1
GGPS1
Includes Dimethylallyltranstransferase
     (EC 2.5.1.1)
Geranyltranstransferase
     (EC 2.5.1.10)
Farnesyltranstransferase
     (EC 2.5.1.29)
Gene name
Name: GGPS1
OrderedLocusNames: At4g36810
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1104/pp.104.4.1469; PubMed=8016276 [NCBI, ExPASy, EBI, Israel, Japan]
Scolnik P.A., Bartley G.E.;
"Nucleotide sequence of an Arabidopsis cDNA for geranylgeranyl pyrophosphate synthase.";
Plant Physiol. 104:1469-1470(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[3]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1104/pp.122.4.1045; PubMed=10759500 [NCBI, ExPASy, EBI, Israel, Japan]
Okada K., Saito T., Nakagawa T., Kawamukai M., Kamiya Y.;
"Five geranylgeranyl diphosphate synthases expressed in different organs are localized into three subcellular compartments in Arabidopsis.";
Plant Physiol. 122:1045-1056(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L25813; AAA32797.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99708; CAB16803.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161590; CAB80347.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR F85434; F85434.
RefSeq NP_195399.1; -.
UniGene At.304
3D structure databases
SMR P34802; 75-366.
ModBase P34802.
Enzyme and pathway databases
BioCyc MetaCyc:AT4G36810-MON; -.
Organism-specific databases
TAIR At4g36810; -.
Gene expression databases
ArrayExpress P34802; -.
GermOnline AT4G36810; Arabidopsis thaliana.
Ontologies
GO
GO:0009507; Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0004161; Molecular function: dimethylallyltranstransferase activity (inferred from electronic annotation from EC).
GO:0004311; Molecular function: farnesyltranstransferase activity (inferred from electronic annotation from EC).
GO:0004337; Molecular function: geranyltranstransferase activity (inferred from electronic annotation from EC).
GO:0016117; Biological process: carotenoid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000092; Polyprenyl_synt.
IPR017446; Polyprenyl_synth-rel.
IPR008949; Terpenoid_synth.
Graphical view of domain structure.
Gene3D G3DSA:1.10.600.10; Terpenoid_synth; 1.
PANTHER PTHR12001; Polyprenyl_synt; 1.
Pfam PF00348; polyprenyl_synt; 1.
Pfam graphical view of domain structure.
PROSITE PS00723; POLYPRENYL_SYNTHET_1; 1.
PS00444; POLYPRENYL_SYNTHET_2; 1.
BLOCKS P34802.
ProtoNet P34802.
Genome annotation databases
GeneID 829834; -.
GenomeReviews CT486007_GR; AT4G36810.
KEGG ath:AT4G36810; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Carotenoid biosynthesis; Chloroplast; Complete proteome; Isoprene biosynthesis; Multifunctional enzyme; Plastid; Transferase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    56  56     Chloroplast (Potential). 
CHAIN   57   371  315     Geranylgeranyl pyrophosphate synthetase 1, chloroplastic. PRO_0000016471
COMPBIAS   21    58  38     Ser-rich. 
CONFLICT   108   108        R -> S (in Ref. 1; AAA32797). 
CONFLICT   141   141        A -> R (in Ref. 1; AAA32797). 
CONFLICT   192   192        A -> S (in Ref. 1; AAA32797). 
Sequence information
Length: 371 AA [This is the length of the unprocessed precursor] Molecular weight: 40174 Da [This is the MW of the unprocessed precursor] CRC64: EFA8088A75B6A005 [This is a checksum on the sequence]
        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 

P34802 in FASTA format

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