Q54BK1 (GGPPS_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Geranylgeranyl pyrophosphate synthase
Short name=GGPP synthase
Short name=GGPPSase

Alternative name(s):
(2E,6E)-farnesyl diphosphate synthase
Dimethylallyltranstransferase
EC=2.5.1.1
Farnesyl diphosphate synthase
Farnesyltranstransferase
EC=2.5.1.29
Geranylgeranyl diphosphate synthase
Geranyltranstransferase
EC=2.5.1.10

Gene names

Name:	ggps1
ORF Names:	DDB_G0293588

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins By similarity.
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	Homooligomer By similarity.
Subcellular location	Cytoplasm Potential.
Sequence similarities	Belongs to the FPP/GGPP synthase family.

Ontologies

Keywords
Biological process	Isoprene biosynthesis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	isoprenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dimethylallyltranstransferase activity Inferred from electronic annotation. Source: EC farnesyltranstransferase activity Inferred from sequence or structural similarity. Source: dictyBase geranyltranstransferase activity Inferred from sequence or structural similarity. Source: dictyBase metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 303	303	Geranylgeranyl pyrophosphate synthase		PRO_0000327749
Sites
	Metal binding	71	1	Magnesium 1 By similarity
	Metal binding	71	1	Magnesium 2 By similarity
	Metal binding	75	1	Magnesium 1 By similarity
	Metal binding	75	1	Magnesium 2 By similarity
	Metal binding	195	1	Magnesium 3 By similarity
	Binding site	32	1	Isopentenyl diphosphate By similarity
	Binding site	35	1	Isopentenyl diphosphate By similarity
	Binding site	64	1	Isopentenyl diphosphate By similarity
	Binding site	80	1	Dimethylallyl diphosphate By similarity
	Binding site	81	1	Isopentenyl diphosphate By similarity
	Binding site	158	1	Dimethylallyl diphosphate By similarity
	Binding site	159	1	Dimethylallyl diphosphate By similarity
	Binding site	192	1	Dimethylallyl diphosphate By similarity
	Binding site	209	1	Dimethylallyl diphosphate By similarity
	Binding site	219	1	Dimethylallyl diphosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54BK1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: C0DD91100FBC4F88	FASTA	303	34,876
	10 20 30 40 50 60 MENSKIHFSY PLDKSDFKLI EPYTYICESS GKGFRNALIK SFDYWLKVGD EKVQDISKVI 70 80 90 100 110 120 QGLHGASLLI DDIEDNSKLR RGKPVAHSIY GIPQTINSAN FVYFLIMDQC NKLGDPKATT 130 140 150 160 170 180 IFIEELIRLH RGQGYDIFWR DTNTSPSEQE YMNMVNEKTG GLFRLGLRLL QAFSDNNTNY 190 200 210 220 230 240 IDLVEDLGMY YQIRDDLINL VSVDYQQNKS FCEDISEGKF SFPIIHAINA DSNDNRLLRI 250 260 270 280 290 300 LKQKTEDRSV KEHALEYIKS KGSLEYTEKK LNVLKEKIIK QINDLGGNPI LMKLMESLEN SSI

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

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Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000218 Genomic DNA. Translation: EAL60606.1.
RefSeq	XP_629028.1. XM_629026.1.
3D structure databases
HSSP	HSSP built from PDB template 2FVI based on UniProtKB O95749.
ProteinModelPortal	Q54BK1.
SMR	Q54BK1. Positions 18-299.
ModBase	Search...
Protein-protein interaction databases
STRING	Q54BK1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0233098; DDB0233098; DDB_G0293588.
GeneID	8629314.
GenomeReviews	Gene locus ggps1 in contig CM000155_GR.
KEGG	ddi:DDB_G0293588.
Organism-specific databases
dictyBase	DDB_G0293588. ggps1.
Phylogenomic databases
eggNOG	KOG0777.
GeneTree	EPrGT00050000004806.
HOGENOM	HBG397395.
OMA	AVKIFTR.
PhylomeDB	Q54BK1.
ProtClustDB	CLSZ2429239.
Family and domain databases
InterPro	IPR000092. Polyprenyl_synt. IPR017446. Polyprenyl_synth-rel. IPR008949. Terpenoid_synth. [Graphical view]
Gene3D	G3DSA:1.10.600.10. Terpenoid_synth. 1 hit.
KO	K00804.
PANTHER	PTHR12001. Polyprenyl_synt. 1 hit.
Pfam	PF00348. polyprenyl_synt. 1 hit. [Graphical view]
SUPFAM	SSF48576. Terpenoid_synth. 1 hit.
PROSITE	PS00723. POLYPRENYL_SYNTHASE_1. 1 hit. PS00444. POLYPRENYL_SYNTHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GGPPS_DICDI

Accession

Primary (citable) accession number: Q54BK1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	November 16, 2011
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)