Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Isopentenyl-diphosphate Delta-isomerase 1

Gene

Idi1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Isopentenyl diphosphate = dimethylallyl diphosphate.

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Pathwayi: dimethylallyl diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes dimethylallyl diphosphate from isopentenyl diphosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. Isopentenyl-diphosphate Delta-isomerase 1 (Idi1), Isopentenyl-diphosphate delta-isomerase 2 (Idi2)
This subpathway is part of the pathway dimethylallyl diphosphate biosynthesis, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes dimethylallyl diphosphate from isopentenyl diphosphate, the pathway dimethylallyl diphosphate biosynthesis and in Isoprenoid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361SubstrateBy similarity
Metal bindingi40 – 401MagnesiumBy similarity
Metal bindingi51 – 511MagnesiumBy similarity
Binding sitei70 – 701SubstrateBy similarity
Binding sitei74 – 741SubstrateBy similarity
Active sitei86 – 861By similarity
Binding sitei87 – 871SubstrateBy similarity
Metal bindingi146 – 1461MagnesiumBy similarity
Active sitei148 – 1481By similarity
Metal bindingi148 – 1481MagnesiumBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Cholesterol biosynthesis, Cholesterol metabolism, Isoprene biosynthesis, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00059; UER00104.

Names & Taxonomyi

Protein namesi
Recommended name:
Isopentenyl-diphosphate Delta-isomerase 1 (EC:5.3.3.2)
Alternative name(s):
Isopentenyl pyrophosphate isomerase 1
Short name:
IPP isomerase 1
Short name:
IPPI1
Gene namesi
Name:Idi1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:2442264. Idi1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
  • peroxisome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 227227Isopentenyl-diphosphate Delta-isomerase 1PRO_0000205225Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei176 – 1761N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP58044.
MaxQBiP58044.
PaxDbiP58044.
PeptideAtlasiP58044.
PRIDEiP58044.

PTM databases

iPTMnetiP58044.
PhosphoSiteiP58044.
SwissPalmiP58044.

Expressioni

Gene expression databases

BgeeiP58044.
CleanExiMM_IDI1.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi235354. 1 interaction.
IntActiP58044. 4 interactions.
MINTiMINT-1854575.
STRINGi10090.ENSMUSP00000132780.

Structurei

3D structure databases

ProteinModelPortaliP58044.
SMRiP58044. Positions 13-227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 199151Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi225 – 2273Microbody targeting signal

Sequence similaritiesi

Belongs to the IPP isomerase type 1 family.Curated
Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0142. Eukaryota.
COG1443. LUCA.
HOGENOMiHOG000274106.
HOVERGENiHBG002995.
InParanoidiP58044.
KOiK01823.
PhylomeDBiP58044.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR011876. IsopentenylPP_isomerase_typ1.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PANTHERiPTHR10885. PTHR10885. 1 hit.
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PIRSFiPIRSF018427. Isopntndiph_ism. 1 hit.
SUPFAMiSSF55811. SSF55811. 1 hit.
TIGRFAMsiTIGR02150. IPP_isom_1. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P58044-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEINTSHLD EKQVQLLAEM CILIDENDNK IGADTKKNCH LNENIDKGLL
60 70 80 90 100
HRAFSVFLFN TENKLLLQQR SDAKITFPGC FTNSCCSHPL SNPGELEENN
110 120 130 140 150
AIGVKRAAKR RLKAELGIPL EEVDLNEMDY LTRIYYKAQS DGIWGEHEVD
160 170 180 190 200
YILFLRKNVT LNPDPNEIKS YCYVSKEEVR EILKKAASGE IKLTPWFKII
210 220
ADTFLFKWWD NLNHLSPFVD HEKIHRL
Length:227
Mass (Da):26,289
Last modified:April 27, 2001 - v1
Checksum:i2B0D1176B9E328D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029302 mRNA. Translation: BAC26382.1.
AK160832 mRNA. Translation: BAE36037.1.
CT010310 mRNA. Translation: CAJ18518.1.
BC004801 mRNA. Translation: AAH04801.1.
BC110313 mRNA. Translation: AAI10314.1.
RefSeqiNP_663335.2. NM_145360.2.
XP_006498576.1. XM_006498513.2.
UniGeneiMm.29847.

Genome annotation databases

GeneIDi102635781.
319554.
KEGGimmu:102635781.
mmu:319554.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029302 mRNA. Translation: BAC26382.1.
AK160832 mRNA. Translation: BAE36037.1.
CT010310 mRNA. Translation: CAJ18518.1.
BC004801 mRNA. Translation: AAH04801.1.
BC110313 mRNA. Translation: AAI10314.1.
RefSeqiNP_663335.2. NM_145360.2.
XP_006498576.1. XM_006498513.2.
UniGeneiMm.29847.

3D structure databases

ProteinModelPortaliP58044.
SMRiP58044. Positions 13-227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi235354. 1 interaction.
IntActiP58044. 4 interactions.
MINTiMINT-1854575.
STRINGi10090.ENSMUSP00000132780.

PTM databases

iPTMnetiP58044.
PhosphoSiteiP58044.
SwissPalmiP58044.

Proteomic databases

EPDiP58044.
MaxQBiP58044.
PaxDbiP58044.
PeptideAtlasiP58044.
PRIDEiP58044.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi102635781.
319554.
KEGGimmu:102635781.
mmu:319554.

Organism-specific databases

CTDi3422.
MGIiMGI:2442264. Idi1.

Phylogenomic databases

eggNOGiKOG0142. Eukaryota.
COG1443. LUCA.
HOGENOMiHOG000274106.
HOVERGENiHBG002995.
InParanoidiP58044.
KOiK01823.
PhylomeDBiP58044.

Enzyme and pathway databases

UniPathwayiUPA00059; UER00104.

Miscellaneous databases

PROiP58044.
SOURCEiSearch...

Gene expression databases

BgeeiP58044.
CleanExiMM_IDI1.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR011876. IsopentenylPP_isomerase_typ1.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PANTHERiPTHR10885. PTHR10885. 1 hit.
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PIRSFiPIRSF018427. Isopntndiph_ism. 1 hit.
SUPFAMiSSF55811. SSF55811. 1 hit.
TIGRFAMsiTIGR02150. IPP_isom_1. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head.
  2. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary tumor.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiIDI1_MOUSE
AccessioniPrimary (citable) accession number: P58044
Secondary accession number(s): Q4FJU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: July 6, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.