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Q9BXS1

- IDI2_HUMAN

UniProt

Q9BXS1 - IDI2_HUMAN

Protein

Isopentenyl-diphosphate delta-isomerase 2

Gene

IDI2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    Isopentenyl diphosphate = dimethylallyl diphosphate.

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Pathwayi

    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

    1. hydrolase activity Source: InterPro
    2. isopentenyl-diphosphate delta-isomerase activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cholesterol biosynthetic process Source: Reactome
    2. dimethylallyl diphosphate biosynthetic process Source: UniProtKB-UniPathway
    3. isopentenyl diphosphate metabolic process Source: MGI
    4. isoprenoid biosynthetic process Source: UniProtKB
    5. small molecule metabolic process Source: Reactome

    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

    BioCyciMetaCyc:HS07522-MONOMER.
    ReactomeiREACT_9405. Cholesterol biosynthesis.
    UniPathwayiUPA00059; UER00104.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isopentenyl-diphosphate delta-isomerase 2 (EC:5.3.3.2)
    Alternative name(s):
    Isopentenyl pyrophosphate isomerase 2
    Short name:
    IPP isomerase 2
    Short name:
    IPPI2
    Gene namesi
    Name:IDI2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:23487. IDI2.

    Subcellular locationi

    Peroxisome 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134935136.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 227227Isopentenyl-diphosphate delta-isomerase 2PRO_0000205228Add
    BLAST

    Proteomic databases

    PaxDbiQ9BXS1.
    PRIDEiQ9BXS1.

    PTM databases

    PhosphoSiteiQ9BXS1.

    Expressioni

    Tissue specificityi

    Detected in skeletal muscle.1 Publication

    Gene expression databases

    BgeeiQ9BXS1.
    CleanExiHS_IDI2.
    GenevestigatoriQ9BXS1.

    Organism-specific databases

    HPAiHPA041254.

    Interactioni

    Protein-protein interaction databases

    BioGridi124870. 2 interactions.
    IntActiQ9BXS1. 1 interaction.
    STRINGi9606.ENSP00000277517.

    Structurei

    Secondary structure

    227
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 44
    Helixi11 – 166
    Beta strandi20 – 245
    Beta strandi30 – 356
    Helixi36 – 394
    Helixi42 – 454
    Turni46 – 483
    Beta strandi51 – 599
    Beta strandi65 – 706
    Beta strandi75 – 773
    Beta strandi84 – 874
    Beta strandi90 – 923
    Helixi93 – 964
    Helixi99 – 1013
    Helixi102 – 11615
    Turni120 – 1223
    Helixi125 – 1273
    Beta strandi128 – 15629
    Turni165 – 1673
    Beta strandi168 – 1747
    Helixi176 – 18813
    Helixi195 – 2039
    Helixi205 – 2084
    Helixi209 – 2113
    Helixi216 – 2183

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PNYX-ray1.81A1-227[»]
    ProteinModelPortaliQ9BXS1.
    SMRiQ9BXS1. Positions 1-227.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BXS1.

    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 signalSequence Analysis

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1443.
    HOGENOMiHOG000274106.
    HOVERGENiHBG002995.
    InParanoidiQ9BXS1.
    KOiK01823.
    OMAiIRYISME.
    OrthoDBiEOG7H4DVK.
    PhylomeDBiQ9BXS1.
    TreeFamiTF300129.

    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.

    Q9BXS1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDINLDWVD RRQLQRLEEM LIVVDENDKV IGADTKRNCH LNENIEKGLL    50
    HRAFSVVLFN TKNRILIQQR SDTKVTFPGY FTDSCSSHPL YNPAELEEKD 100
    AIGVRRAAQR RLQAELGIPG EQISPEDIVF MTIYHHKAKS DRIWGEHEIC 150
    YLLLVRKNVT LNPDPSETKS ILYLSQEELW ELLEREARGE VKVTPWLRTI 200
    AERFLYRWWP HLDDVTPFVE LHKIHRV 227
    Length:227
    Mass (Da):26,753
    Last modified:June 1, 2001 - v1
    Checksum:i2FD79B076D94A7D0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF291755 Genomic DNA. Translation: AAK29358.1.
    AF271729
    , AF271726, AF271727, AF271728 Genomic DNA. Translation: AAK49436.1.
    AF271725 mRNA. Translation: AAK49437.1.
    AK056950 mRNA. Translation: BAB71322.1.
    BC017778 mRNA. Translation: AAH17778.1.
    CCDSiCCDS7055.1.
    RefSeqiNP_150286.1. NM_033261.2.
    UniGeneiHs.591325.
    Hs.9270.

    Genome annotation databases

    EnsembliENST00000277517; ENSP00000277517; ENSG00000148377.
    GeneIDi91734.
    KEGGihsa:91734.
    UCSCiuc001ifv.1. human.

    Polymorphism databases

    DMDMi20978506.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF291755 Genomic DNA. Translation: AAK29358.1 .
    AF271729
    , AF271726 , AF271727 , AF271728 Genomic DNA. Translation: AAK49436.1 .
    AF271725 mRNA. Translation: AAK49437.1 .
    AK056950 mRNA. Translation: BAB71322.1 .
    BC017778 mRNA. Translation: AAH17778.1 .
    CCDSi CCDS7055.1.
    RefSeqi NP_150286.1. NM_033261.2.
    UniGenei Hs.591325.
    Hs.9270.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PNY X-ray 1.81 A 1-227 [» ]
    ProteinModelPortali Q9BXS1.
    SMRi Q9BXS1. Positions 1-227.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124870. 2 interactions.
    IntActi Q9BXS1. 1 interaction.
    STRINGi 9606.ENSP00000277517.

    PTM databases

    PhosphoSitei Q9BXS1.

    Polymorphism databases

    DMDMi 20978506.

    Proteomic databases

    PaxDbi Q9BXS1.
    PRIDEi Q9BXS1.

    Protocols and materials databases

    DNASUi 91734.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000277517 ; ENSP00000277517 ; ENSG00000148377 .
    GeneIDi 91734.
    KEGGi hsa:91734.
    UCSCi uc001ifv.1. human.

    Organism-specific databases

    CTDi 91734.
    GeneCardsi GC10M001064.
    H-InvDB HIX0127248.
    HGNCi HGNC:23487. IDI2.
    HPAi HPA041254.
    MIMi 615389. gene.
    neXtProti NX_Q9BXS1.
    PharmGKBi PA134935136.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1443.
    HOGENOMi HOG000274106.
    HOVERGENi HBG002995.
    InParanoidi Q9BXS1.
    KOi K01823.
    OMAi IRYISME.
    OrthoDBi EOG7H4DVK.
    PhylomeDBi Q9BXS1.
    TreeFami TF300129.

    Enzyme and pathway databases

    UniPathwayi UPA00059 ; UER00104 .
    BioCyci MetaCyc:HS07522-MONOMER.
    Reactomei REACT_9405. Cholesterol biosynthesis.

    Miscellaneous databases

    EvolutionaryTracei Q9BXS1.
    GenomeRNAii 91734.
    NextBioi 77415.
    PROi Q9BXS1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9BXS1.
    CleanExi HS_IDI2.
    Genevestigatori Q9BXS1.

    Family and domain databases

    Gene3Di 3.90.79.10. 1 hit.
    InterProi IPR011876. IsopentenylPP_isomerase_typ1.
    IPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    [Graphical view ]
    PANTHERi PTHR10885. PTHR10885. 1 hit.
    Pfami PF00293. NUDIX. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF018427. Isopntndiph_ism. 1 hit.
    SUPFAMi SSF55811. SSF55811. 1 hit.
    TIGRFAMsi TIGR02150. IPP_isom_1. 1 hit.
    PROSITEi PS51462. NUDIX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "IDI2, a second isopentenyl diphosphate isomerase in mammals."
      Clizbe D.B., Owens M.L., Masuda K.R., Shackelford J.E., Krisans S.K.
      J. Biol. Chem. 282:6668-6676(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skeletal muscle.
    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].
      Tissue: Skeletal muscle.

    Entry informationi

    Entry nameiIDI2_HUMAN
    AccessioniPrimary (citable) accession number: Q9BXS1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 122 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3