Q9BXS1 (IDI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

IDI2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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). Ref.1
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	Peroxisome Ref.1.
Tissue specificity	Detected in skeletal muscle. Ref.1
Sequence similarities	Belongs to the IPP isomerase type 1 family. Contains 1 nudix hydrolase domain.

Ontologies

Keywords
Biological process	Cholesterol biosynthesis Isoprene biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Peroxisome
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cholesterol biosynthetic process Traceable author statement. Source: Reactome isoprenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Traceable author statement. Source: Reactome peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	hydrolase activity Inferred from electronic annotation. Source: InterPro isopentenyl-diphosphate delta-isomerase activity Traceable author statement. Source: Reactome metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 227

227

Isopentenyl-diphosphate Delta-isomerase 2

PRO_0000205228

Regions

Domain

49 – 199

151

Nudix hydrolase

Motif

225 – 227

3

Microbody targeting signal Potential

Sites

Active site

86

1

By similarity

Active site

148

1

By similarity

Metal binding

40

1

Magnesium By similarity

Metal binding

51

1

Magnesium By similarity

Metal binding

146

1

Magnesium By similarity

Metal binding

148

1

Magnesium By similarity

Binding site

36

1

Substrate By similarity

Binding site

70

1

Substrate By similarity

Binding site

74

1

Substrate By similarity

Binding site

87

1

Substrate By similarity

Secondary structure

1

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227

Helix Strand Turn

Details...

Helix

1 – 4

4

Helix

11 – 16

6

Beta strand

20 – 24

5

Beta strand

30 – 35

6

Helix

36 – 39

4

Helix

42 – 45

4

Turn

46 – 48

3

Beta strand

51 – 59

9

Beta strand

65 – 70

6

Beta strand

75 – 77

3

Beta strand

84 – 87

4

Beta strand

90 – 92

3

Helix

93 – 96

4

Helix

99 – 101

3

Helix

102 – 116

15

Turn

120 – 122

3

Helix

125 – 127

3

Beta strand

128 – 156

29

Turn

165 – 167

3

Beta strand

168 – 174

7

Helix

176 – 188

13

Helix

195 – 203

9

Helix

205 – 208

4

Helix

209 – 211

3

Helix

216 – 218

3

Sequences

	Sequence		Length	Mass (Da)
	Q9BXS1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 2FD79B076D94A7D0	FASTA	227	26,753
	10 20 30 40 50 60 MSDINLDWVD RRQLQRLEEM LIVVDENDKV IGADTKRNCH LNENIEKGLL HRAFSVVLFN 70 80 90 100 110 120 TKNRILIQQR SDTKVTFPGY FTDSCSSHPL YNPAELEEKD AIGVRRAAQR RLQAELGIPG 130 140 150 160 170 180 EQISPEDIVF MTIYHHKAKS DRIWGEHEIC YLLLVRKNVT LNPDPSETKS ILYLSQEELW 190 200 210 220 ELLEREARGE VKVTPWLRTI AERFLYRWWP HLDDVTPFVE LHKIHRV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 17202134] [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: 14702039] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skeletal muscle.
[4]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00018740.

RefSeq

NP_150286.1. NM_033261.2.

UniGene

Hs.591325.
Hs.9270.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PNY	X-ray	1.81	A	1-227	[»]

ProteinModelPortal

Q9BXS1.

SMR

Q9BXS1. Positions 1-227.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BXS1. 1 interaction.

STRING

Q9BXS1.

Polymorphism databases

DMDM

20978506.

Proteomic databases

PRIDE

Q9BXS1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000277517; ENSP00000277517; ENSG00000148377.

GeneID

91734.

KEGG

hsa:91734.

UCSC

uc001ifv.1. human.

Organism-specific databases

CTD

91734.

GeneCards

GC10M001064.

H-InvDB

HIX0008586.
HIX0127248.

HGNC

HGNC:23487. IDI2.

HPA

HPA041254.

neXtProt

NX_Q9BXS1.

PharmGKB

PA134935136.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13546.

GeneTree

ENSGT00390000008527.

HOGENOM

HBG416977.

HOVERGEN

HBG002995.

InParanoid

Q9BXS1.

OMA

HWDGTVA.

OrthoDB

EOG45757K.

PhylomeDB

Q9BXS1.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000148377-MONOMER.

Reactome

REACT_22258. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

Q9BXS1.

Bgee

Q9BXS1.

CleanEx

HS_IDI2.

Genevestigator

Q9BXS1.

GermOnline

ENSG00000148377. Homo sapiens.

Family and domain databases

InterPro

IPR011876. IsopentenylPP_isomerase_typ1.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]

Gene3D

G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.

KO

K01823.

PANTHER

PTHR10885. IPP_isom_1. 1 hit.

Pfam

PF00293. NUDIX. 1 hit.
[Graphical view]

PIRSF

PIRSF018427. Isopntndiph_ism. 1 hit.

SUPFAM

SSF55811. NUDIX_hydrolase. 1 hit.

TIGRFAMs

TIGR02150. IPP_isom_1. 1 hit.

PROSITE

PS51462. NUDIX. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

77415.

Entry information

Entry name

IDI2_HUMAN

Accession

Primary (citable) accession number: Q9BXS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2002
Last sequence update:	June 1, 2001
Last modified:	January 25, 2012
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.