Reviewed, UniProtKB/Swiss-Prot P24322 (GGPPS_NEUCR)

Names and origin

Protein names

Recommended name:
    Geranylgeranyl pyrophosphate synthetase
      Short name=GGPP synthetase
      Short name=GGPPSase
Alternative name(s):
    Geranylgeranyl diphosphate synthase
    Albino-3 protein
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:	al-3
ORF Names:	B8P8.010, NCU01427

Organism

Neurospora crassa [Complete proteome]

Taxonomic identifier

5141 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
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.
Subcellular location	Cytoplasm.
Induction	By blue light.
Sequence similarities	Belongs to the FPP/GGPP synthetase family.
Caution	It is uncertain whether Met-1 or Met-6 is the initiator.

Ontologies

Keywords
Biological process	Carotenoid biosynthesis Isoprene biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative initiation
Molecular function	Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	carotenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fraction Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	dimethylallyltranstransferase activity Inferred from electronic annotation. Source: EC farnesyltranstransferase activity Inferred from sequence or structural similarity. Source: UniProtKB geranyltranstransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative initiation. [Align] [Select]

Isoform 1 (identifier: P24322-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Main product.

Isoform 2 (identifier: P24322-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-88: Missing.

Isoform 3 (identifier: P24322-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-98: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 433	433	Geranylgeranyl pyrophosphate synthetase		PRO_0000123966
Sites
	Active site	273	1	By similarity
Natural variations
	Alternative sequence	1 – 98	98	Missing in isoform 3.		VSP_029973
	Alternative sequence	1 – 88	88	Missing in isoform 2.		VSP_029974

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 15, 2008. Version 2. Checksum: BE6BB03A938BDFA5	FASTA	433	48,485
	10 20 30 40 50 60 MEHVTMAVTS SSPGPAPLSL LSNNDDFIAP FNINTKFPSA IVPPRTSSNQ PISVAIPSNR 70 80 90 100 110 120 ISSAGLAATQ QAQTRKRKAS VAQISLPSML PTSFSPYTMA PQPPQPPPNP DRFATEDFFS 130 140 150 160 170 180 PSRRTWSEEK EKVLTGPYDY LNGHPGKDIR SQMVKAFDAW LDVPSESLEV ITKVISMLHT 190 200 210 220 230 240 ASLLVDDVED NSVLRRGFPV AHSIFGIPQT INTSNYVYFY ALQELQKLKN PKAVSIFSEE 250 260 270 280 290 300 LLNLHRGQGM DLFWRDTLTC PTEDDYLEMV SNKTGGLFRL GIKLMQAESR SPVDCVPLVN 310 320 330 340 350 360 IIGLIFQIAD DYHNLWNREY TANKGMCEDL TEGKFSFPVI HSIRSNPSNM QLLNILKQKT 370 380 390 400 410 420 GDEEVKRYAV AYMESTGSFE YTRKVIKVLV DRARQMTEDI DDGRGKSGGI HKILDRIMLH 430 QEENVAQKNG KKE
	Isoform 2. Checksum: B30B9441DDEA584C	FASTA	345	39,317
	10 20 30 40 50 60 MLPTSFSPYT MAPQPPQPPP NPDRFATEDF FSPSRRTWSE EKEKVLTGPY DYLNGHPGKD 70 80 90 100 110 120 IRSQMVKAFD AWLDVPSESL EVITKVISML HTASLLVDDV EDNSVLRRGF PVAHSIFGIP 130 140 150 160 170 180 QTINTSNYVY FYALQELQKL KNPKAVSIFS EELLNLHRGQ GMDLFWRDTL TCPTEDDYLE 190 200 210 220 230 240 MVSNKTGGLF RLGIKLMQAE SRSPVDCVPL VNIIGLIFQI ADDYHNLWNR EYTANKGMCE 250 260 270 280 290 300 DLTEGKFSFP VIHSIRSNPS NMQLLNILKQ KTGDEEVKRY AVAYMESTGS FEYTRKVIKV 310 320 330 340 LVDRARQMTE DIDDGRGKSG GIHKILDRIM LHQEENVAQK NGKKE
	Isoform 3. Checksum: D2264B56379A1B88	FASTA	335	38,191
	10 20 30 40 50 60 MAPQPPQPPP NPDRFATEDF FSPSRRTWSE EKEKVLTGPY DYLNGHPGKD IRSQMVKAFD 70 80 90 100 110 120 AWLDVPSESL EVITKVISML HTASLLVDDV EDNSVLRRGF PVAHSIFGIP QTINTSNYVY 130 140 150 160 170 180 FYALQELQKL KNPKAVSIFS EELLNLHRGQ GMDLFWRDTL TCPTEDDYLE MVSNKTGGLF 190 200 210 220 230 240 RLGIKLMQAE SRSPVDCVPL VNIIGLIFQI ADDYHNLWNR EYTANKGMCE DLTEGKFSFP 250 260 270 280 290 300 VIHSIRSNPS NMQLLNILKQ KTGDEEVKRY AVAYMESTGS FEYTRKVIKV LVDRARQMTE 310 320 330 DIDDGRGKSG GIHKILDRIM LHQEENVAQK NGKKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Neurospora crassa carotenoid biosynthetic gene (albino 3) reveals highly conserved regions among prenyltransferases." Carattoli A., Romano N., Ballario P., Morelli G., Macino G. J. Biol. Chem. 266:5854-5859(1991) [PubMed: 1826006] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[2]	"What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence." Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U. Nucleic Acids Res. 31:1944-1954(2003) [PubMed: 12655011] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[3]	"The genome sequence of the filamentous fungus Neurospora crassa." Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W. Nature 422:859-868(2003) [PubMed: 12712197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[4]	"Internal translational initiation in the mRNA from the Neurospora crassa albino-3 gene." Vittorioso P., Carattoli A., Londei P., Macino G. J. Biol. Chem. 269:26650-26654(1994) [PubMed: 7929398] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-134, ALTERNATIVE INITIATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U20940 Genomic DNA. Translation: AAC13867.1. Different initiation. BX294018 Genomic DNA. Translation: CAD70868.1. Different initiation. AABX02000014 Genomic DNA. Translation: EAA31459.2. S74011 Genomic DNA. Translation: AAP21085.1.
PIR	S15662.
RefSeq	XP_960695.2.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3876842.
KEGG	ncr:NCU01427.
NMPDR	fig|5141.1.peg.4853.
Enzyme and pathway databases
BioCyc	NCRA-XX3-01:NCRA-XX3-01-005137-MON.
BRENDA	2.5.1.1. 266. 2.5.1.10. 266. 2.5.1.29. 266.
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.
PANTHER	PTHR12001. Polyprenyl_synt. 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_NEUCR

Accession

Primary (citable) accession number: P24322
Secondary accession number(s): Q7RVC0, Q86ZV1

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	January 15, 2008
Last modified:	June 16, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)