ID   IDI2_CAMAC              Reviewed;         309 AA.
AC   O48965;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=IPI2;
OS   Camptotheca acuminata (Happy tree).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Cornales; Nyssaceae; Camptotheca.
OX   NCBI_TaxID=16922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Jung K.-H., Christensen D.J., Scott A.I.;
RT   "Isolation and characterization of two genes from Camptotheca acuminata
RT   that encode isopentenyl diphosphate isomerase.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic
CC       substrate isopentenyl (IPP) to its highly electrophilic allylic isomer,
CC       dimethylallyl diphosphate (DMAPP). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=isopentenyl diphosphate = dimethylallyl diphosphate;
CC         Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769;
CC         EC=5.3.3.2;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC       biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate:
CC       step 1/1.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis.
CC   -!- SIMILARITY: Belongs to the IPP isomerase type 1 family. {ECO:0000305}.
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DR   EMBL; AF031080; AAB94133.1; -; mRNA.
DR   AlphaFoldDB; O48965; -.
DR   SMR; O48965; -.
DR   UniPathway; UPA00059; UER00104.
DR   UniPathway; UPA00668; -.
DR   GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   CDD; cd02885; IPP_Isomerase; 1.
DR   InterPro; IPR011876; IsopentenylPP_isomerase_typ1.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   TIGRFAMs; TIGR02150; IPP_isom_1; 1.
DR   PROSITE; PS51462; NUDIX; 1.
PE   2: Evidence at transcript level;
KW   Chlorophyll biosynthesis; Isomerase; Isoprene biosynthesis; Magnesium;
KW   Metal-binding; Photosynthesis.
FT   CHAIN           1..309
FT                   /note="Isopentenyl-diphosphate Delta-isomerase II"
FT                   /id="PRO_0000205235"
FT   DOMAIN          126..278
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   ACT_SITE        163
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        225
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   309 AA;  35205 MW;  BAF51CF8BD2ED0A4 CRC64;
     MSAASHIHSV ACRLSSSFLA SPKLKLHPRL SFFFHSSSFR NHIITRSVFC SSSHLSVRVS
     SYHSSVAAKA TTSAMGDTAT DAGMDAVQRR LMFEDECILV DENDHVVGHD TKYNCHLMEK
     IESDNLLHRA FSVFLFNSKY ELLLQQRSAT KVTFPLVWTN TCCSHPRYRE SELVDENALG
     VRNAAQRKLL DELGIPAEDV PVDQFIPLGR MLYKAPSDGK WGEHELDYLL FIIRDVNVHP
     NPDEVADVKY VNQDQLKDLL RKVDAGEEGL KLSPWFRLVV ENFLFKWWDH VEKGTLQDAT
     DMKTIHKLT