ID   IDI2_ARATH              Reviewed;         284 AA.
AC   Q42553;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 67.
DE   RecName: Full=Isopentenyl-diphosphate Delta-isomerase II;
DE            EC=5.3.3.2;
DE   AltName: Full=Isopentenyl pyrophosphate isomerase II;
DE            Short=IPP isomerase II;
GN   Name=IPP2; OrderedLocusNames=At3g02780; ORFNames=F13E7.28;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98145438; PubMed=9484444; DOI=10.1023/A:1005935516274;
RA   Campbell M., Hahn F.M., Poulter C.D., Leustek T.;
RT   "Analysis of the isopentenyl diphosphate isomerase gene family from
RT   Arabidopsis thaliana.";
RL   Plant Mol. Biol. 36:323-328(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: Catalyzes the 1,3-allylic rearrangement of the
CC       homoallylic substrate isopentenyl (IPP) to its highly
CC       electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP)
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Isopentenyl diphosphate = dimethylallyl
CC       diphosphate.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl-PP biosynthesis;
CC       dimethylallyl-PP from isopentenyl-PP: step 1/1.
CC   -!- PATHWAY: Porphyrin biosynthesis; chlorophyll biosynthesis.
CC   -!- SIMILARITY: Belongs to the IPP isomerase type 1 family.
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DR   EMBL; U49259; AAC49920.1; -; mRNA.
DR   EMBL; AC018363; AAF26982.1; -; Genomic_DNA.
DR   EMBL; AF428343; AAL16273.1; -; mRNA.
DR   EMBL; AY127023; AAM83247.1; -; mRNA.
DR   EMBL; AY143845; AAN28784.1; -; mRNA.
DR   IPI; IPI00516444; -.
DR   PIR; S71370; S71370.
DR   RefSeq; NP_186927.1; -.
DR   UniGene; At.10819; -.
DR   HSSP; Q46822; 1NFZ.
DR   PRIDE; Q42553; -.
DR   GeneID; 820960; -.
DR   GenomeReviews; BA000014_GR; AT3G02780.
DR   KEGG; ath:AT3G02780; -.
DR   NMPDR; fig|3702.1.peg.12225; -.
DR   TAIR; At3g02780; -.
DR   OMA; Q42553; NENEVAE.
DR   BioCyc; MetaCyc:AT3G02780-MON; -.
DR   BRENDA; 5.3.3.2; 302.
DR   ArrayExpress; Q42553; -.
DR   GermOnline; AT3G02780; Arabidopsis thaliana.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase act...; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009908; P:flower development; IMP:TAIR.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   InterPro; IPR011876; IsopentenylPP_isomerase_typ1.
DR   InterPro; IPR000086; NUDIX_hydrolase_core.
DR   Gene3D; G3DSA:3.90.79.10; NUDIX_hydrolase; 1.
DR   PANTHER; PTHR10885; IPP_isom_1; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   PIRSF; PIRSF018427; Isopntndiph_ism; 1.
DR   ProDom; PD004109; IPP_isomerase; 1.
DR   TIGRFAMs; TIGR02150; IPP_isom_1; 1.
PE   2: Evidence at transcript level;
KW   Chlorophyll biosynthesis; Complete proteome; Isomerase;
KW   Isoprene biosynthesis; Magnesium; Metal-binding; Photosynthesis.
FT   CHAIN         1    284       Isopentenyl-diphosphate Delta-isomerase
FT                                II.
FT                                /FTId=PRO_0000205233.
FT   ACT_SITE    139    139       By similarity.
FT   ACT_SITE    201    201       By similarity.
FT   METAL        92     92       Magnesium (By similarity).
FT   METAL       104    104       Magnesium (By similarity).
FT   METAL       199    199       Magnesium (By similarity).
FT   METAL       201    201       Magnesium (By similarity).
FT   BINDING      88     88       Substrate (By similarity).
FT   BINDING     123    123       Substrate (By similarity).
FT   BINDING     127    127       Substrate (By similarity).
FT   BINDING     140    140       Substrate (By similarity).
SQ   SEQUENCE   284 AA;  32607 MW;  614D02F354E242FF CRC64;
     MSASSLFNLP LIRLRSLALS SSFSSFRFAH RPLSSISPRK LPNFRAFSGT AMTDTKDAGM
     DAVQRRLMFE DECILVDETD RVVGHDSKYN CHLMENIEAK NLLHRAFSVF LFNSKYELLL
     QQRSNTKVTF PLVWTNTCCS HPLYRESELI QDNALGVRNA AQRKLLDELG IVAEDVPVDE
     FTPLGRMLYK APSDGKWGEH ELDYLLFIVR DVKVQPNPDE VAEIKYVSRE ELKELVKKAD
     AGEEGLKLSP WFRLVVDNFL MKWWDHVEKG TLVEAIDMKT IHKL
//