Reviewed, UniProtKB/Swiss-Prot O59703 (GGPPS_SCHPO)

Names and origin

Protein names

Recommended name:
    Geranylgeranyl pyrophosphate synthetase
      Short name=GGPP synthetase
      Short name=GGPPSase
Alternative name(s):
    Geranylgeranyl diphosphate synthase
    Sporulation-specific protein 9
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:	spo9
ORF Names:	SPBC36.06c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the trans-addition of the 3 molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. Required for the membrane attachment of ypt7 and rhb1. May be involved in vesicle trafficking and protein sorting. Required for forespore membrane formation.
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.
Pathway	Isoprenoid biosynthesis; farnesyl-PP biosynthesis; farnesyl-PP from geranyl-PP and isopentenyl-PP: step 1/1. Isoprenoid biosynthesis; geranyl-PP biosynthesis; geranyl-PP from dimethylallyl-PP and isopentenyl-PP: step 1/1. Isoprenoid biosynthesis; geranylgeranyl-PP biosynthesis; geranylgeranyl-PP from farnesyl-PP and isopentenyl-PP: step 1/1.
Subunit structure	Interacts with fps1.
Subcellular location	Cytoplasm. Nucleus.
Sequence similarities	Belongs to the FPP/GGPP synthetase family.

Ontologies

Keywords
Biological process	Carotenoid biosynthesis Isoprene biosynthesis Protein transport Transport
Cellular component	Cytoplasm Nucleus
Molecular function	Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	ascospore formation Ref.3 Inferred from mutant phenotype. Source: GeneDB_SPombe carotenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW protein prenylation Ref.3 Inferred from mutant phenotype. Source: GeneDB_SPombe protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Ref.2 Inferred from direct assay. Source: GeneDB_SPombe nucleus Ref.2 Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	dimethylallyltranstransferase activity Inferred from electronic annotation. Source: EC farnesyltranstransferase activity Inferred from electronic annotation. Source: EC geranyltranstransferase activity Inferred from electronic annotation. Source: EC protein binding Ref.3 Inferred from physical interaction. Source: GeneDB_SPombe protein farnesyltransferase activity Ref.3 Inferred from mutant phenotype. Source: GeneDB_SPombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 351	351	Geranylgeranyl pyrophosphate synthetase		PRO_0000339411
Experimental info
	Mutagenesis	95	1	C → F: No complement of lethality of fps1-delete strain
	Mutagenesis	109	1	R → Q: No GGPP synthetase activity

Sequences

	Sequence		Length	Mass (Da)
	O59703-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: F5DC90A91CC132E7	FASTA	351	40,946
	10 20 30 40 50 60 MVNDFNEKNG IKKRLLDFFP VVLEGIREIL ESMQYFPEET EKLLYSIKRN TLGGKNNRGL 70 80 90 100 110 120 AVLQSLTSLI NRELEEAEFR DAALLGWLIE ILQGCFLMAD DIMDQSIKRR GLDCWYLVVG 130 140 150 160 170 180 VRRAINESQL LEACIPLLIR KYFRNMPYYV DLLDTFREVT FLTELGQQED LLSSRDGEAS 190 200 210 220 230 240 LRSFDLMKYD FIITYKTSFY SFYLPIKCAL LLSRNSNQKA YDTTIKLSKL LGYYFQVQDD 250 260 270 280 290 300 YLDCFGDYTV LGKVGMDIQD NKCTWLVCYA EKFASADQLN LLRAHYGKAG SENIAVIKQL 310 320 330 340 350 YHELQIPELY HKFEDDMVDS ISKEIDLIDE STGLKKCIFT KFFQLIYKRS R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[3]	"Geranylgeranyl diphosphate synthase in fission yeast is a heteromer of farnesyl diphosphate synthase (FPS), Fps1, and an FPS-like protein, Spo9, essential for sporulation." Ye Y., Fujii M., Hirata A., Kawamukai M., Shimoda C., Nakamura T. Mol. Biol. Cell 18:3568-3581(2007) [PubMed: 17596513] [Abstract] Cited for: FUNCTION, INTERACTION WITH FPS1, MUTAGENESIS OF CYS-95 AND ARG-109.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329671 Genomic DNA. Translation: CAA19054.1.
PIR	T40301.
RefSeq	NP_595334.1.
3D structure databases
HSSP	HSSP built from PDB template 1FPS based on UniProtKB P08836.
ModBase	Search...
Genome annotation databases
GeneID	2540933.
KEGG	spo:SPBC36.06c.
NMPDR	fig|4896.1.peg.1200.
Organism-specific databases
GeneDB_Spombe	SPBC36.06c.
Gene expression databases
ArrayExpress	O59703.
Family and domain databases
InterPro	IPR000092. Polyprenyl_synt. IPR008949. Terpenoid_synth. [Graphical view]
Gene3D	G3DSA:1.10.600.10. Terpenoid_synth. 1 hit.
Pfam	PF00348. polyprenyl_synt. 1 hit. [Graphical view]
PROSITE	PS00723. POLYPRENYL_SYNTHET_1. 1 hit. PS00444. POLYPRENYL_SYNTHET_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GGPPS_SCHPO

Accession

Primary (citable) accession number: O59703

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	August 1, 1998
Last modified:	November 25, 2008
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)