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Q10132 (IDI1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Isopentenyl-diphosphate Delta-isomerase
EC=5.3.3.2
Alternative name(s):
Isopentenyl pyrophosphate isomerase
Short name=IPP isomerase
Gene names
Name:idi1
ORF Names:SPBC106.15
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).

Catalytic activity

Isopentenyl diphosphate = dimethylallyl diphosphate.

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the IPP isomerase type 1 family.

Contains 1 nudix hydrolase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 227227Isopentenyl-diphosphate Delta-isomerase
PRO_0000205230

Regions

Domain50 – 200151Nudix hydrolase

Sites

Active site871 By similarity
Active site1521 By similarity
Metal binding411Magnesium By similarity
Metal binding521Magnesium By similarity
Metal binding1501Magnesium By similarity
Metal binding1521Magnesium By similarity
Binding site371Substrate By similarity
Binding site711Substrate By similarity
Binding site751Substrate By similarity
Binding site881Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q10132 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: A811B5CA2C9AA834

FASTA22726,864
        10         20         30         40         50         60 
MSSQQEKKDY DEEQLRLMEE VCIVVDENDV PLRYGTKKEC HLMENINKGL LHRAFSMFIF 

        70         80         90        100        110        120 
DEQNRLLLQQ RAEEKITFPS LWTNTCCSHP LDVAGERGNT LPEAVEGVKN AAQRKLFHEL 

       130        140        150        160        170        180 
GIQAKYIPKD KFQFLTRIHY LAPSTGAWGE HEIDYILFFK GKVELDINPN EVQAYKYVTM 

       190        200        210        220 
EELKEMFSDP QYGFTPWFKL ICEHFMFKWW QDVDHASKFQ DTLIHRC

« Hide

References

« Hide 'large scale' references
[1]"Isolation of Schizosaccharomyces pombe isopentenyl diphosphate isomerase cDNA clones by complementation and synthesis of the enzyme in Escherichia coli."
Hahn F.M., Poulter C.D.
J. Biol. Chem. 270:11298-11303(1995) [PubMed: 7744766] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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. expand/collapse author list , 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: 972 / ATCC 24843.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U21154 mRNA. Translation: AAA80596.1.
CU329671 Genomic DNA. Translation: CAB53731.1.
PIRA56442.
RefSeqNP_595164.1. NM_001021073.1.

3D structure databases

ProteinModelPortalQ10132.
SMRQ10132. Positions 14-226.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ10132.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2540174.
GenomeReviewsGene locus idi1 in contig CU329671_GR.
KEGGspo:SPBC106.15.
NMPDRfig|4896.1.peg.1030.

Organism-specific databases

GeneDB_SpombeSPBC106.15.

Phylogenomic databases

eggNOGfuNOG04815.
GeneTreeEFGT00050000006618.
HOGENOMHBG416977.
OMANYELGIP.
OrthoDBEOG4RFQ2V.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-003261-MONOMER.

Gene expression databases

ArrayExpressQ10132.

Family and domain databases

InterProIPR011876. IsopentenylPP_isomerase_typ1.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
Gene3DG3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.
KOK01823.
PfamPF00293. NUDIX. 1 hit.
[Graphical view]
PIRSFPIRSF018427. Isopntndiph_ism. 1 hit.
SUPFAMSSF55811. NUDIX_hydrolase. 1 hit.
TIGRFAMsTIGR02150. IPP_isom_1. 1 hit.
PROSITEPS51462. NUDIX. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIDI1_SCHPO
AccessionPrimary (citable) accession number: Q10132
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: December 14, 2011
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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