ID   IDI1_CAMAC              Reviewed;         235 AA.
AC   O48964;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Isopentenyl-diphosphate Delta-isomerase I;
DE            EC=5.3.3.2;
DE   AltName: Full=Isopentenyl pyrophosphate isomerase I;
DE            Short=IPP isomerase I;
GN   Name=IPI1;
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; AF031079; AAB94132.1; -; mRNA.
DR   AlphaFoldDB; O48964; -.
DR   SMR; O48964; -.
DR   PRIDE; O48964; -.
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   PIRSF; PIRSF018427; Isopntndiph_ism; 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..235
FT                   /note="Isopentenyl-diphosphate Delta-isomerase I"
FT                   /id="PRO_0000205234"
FT   DOMAIN          52..204
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   ACT_SITE        89
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        151
FT                   /evidence="ECO:0000250"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   235 AA;  27016 MW;  8E0A5F0706E4B7E7 CRC64;
     MGDAATDAGM DAVQKRLMFE DKCILVDEND NVVGHDTKYN CHLMEKIESE NLLHRAFSVF
     LFNSKYELLL QQRSATKVTF PLVWTNTCCS HPLYRESELI KENALGARNA AQRKLLDELG
     IPAEDVPVDQ FIPLGRILYK APSDGKWGEH ELDYLLFIVR DVNVNPNPDE VADIKYVTRD
     QLKELLRKAD AGEEGLKLSP WFRLVVDNFL FKWWDHVEKG TMHEAADMKS IHKLI