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P24322 (GGPPS_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Geranylgeranyl pyrophosphate synthase
Short name=GGPP synthase
Short name=GGPPSase
Alternative name(s):
(2E,6E)-farnesyl diphosphate synthase
Albino-3 protein
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:al-3
ORF Names:B8P8.010, NCU01427
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

Protein attributes

Sequence length433 AA.
Sequence statusComplete.
Protein existenceEvidence 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 + (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.

Subcellular location

Cytoplasm.

Induction

By blue light.

Sequence similarities

Belongs to the FPP/GGPP synthase family.

Caution

It is uncertain whether Met-1 or Met-6 is the initiator.

Sequence caution

The sequence AAC13867.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAD70868.1 differs from that shown. Reason: Erroneous initiation.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 433433Geranylgeranyl pyrophosphate synthase
PRO_0000123966

Sites

Metal binding1861Magnesium 1 By similarity
Metal binding1861Magnesium 2 By similarity
Metal binding1901Magnesium 1 By similarity
Metal binding1901Magnesium 2 By similarity
Metal binding3101Magnesium 3 By similarity
Binding site1471Isopentenyl diphosphate By similarity
Binding site1501Isopentenyl diphosphate By similarity
Binding site1791Isopentenyl diphosphate By similarity
Binding site1951Dimethylallyl diphosphate By similarity
Binding site1961Isopentenyl diphosphate By similarity
Binding site2731Dimethylallyl diphosphate By similarity
Binding site2741Dimethylallyl diphosphate By similarity
Binding site3071Dimethylallyl diphosphate By similarity
Binding site3241Dimethylallyl diphosphate By similarity
Binding site3341Dimethylallyl diphosphate By similarity
Site2181Important for determining product chain length By similarity

Natural variations

Alternative sequence1 – 9898Missing in isoform 3.
VSP_029973
Alternative sequence1 – 8888Missing in isoform 2.
VSP_029974

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: BE6BB03A938BDFA5

FASTA43348,485
        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

« Hide

Isoform 2 [UniParc].

Checksum: B30B9441DDEA584C
Show »

FASTA34539,317
Isoform 3 [UniParc].

Checksum: D2264B56379A1B88
Show »

FASTA33538,191

References

« Hide '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. expand/collapse author list , 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

EMBL
GenBank
DDBJ		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.
PIRS15662.
RefSeqXP_960695.2. XM_955602.2.

3D structure databases

ProteinModelPortalP24322.
SMRP24322. Positions 128-407.
ModBaseSearch...

Protein-protein interaction databases

STRINGP24322.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000004018; EFNCRP00000004018; EFNCRG00000004013.
GeneID3876842.
KEGGncr:NCU01427.
NMPDRfig|5141.1.peg.4853.

Phylogenomic databases

eggNOGfuNOG04319.
GeneTreeEFGT00050000002292.
OMAIHSIRSN.
OrthoDBEOG4QVGMM.

Enzyme and pathway databases

BioCycNCRA-XX3-01:NCRA-XX3-01-005137-MONOMER.

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.
KOK00804.
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 nameGGPPS_NEUCR
AccessionPrimary (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: November 16, 2011
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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