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IDI_ECO7I
ID   IDI_ECO7I               Reviewed;         182 AA.
AC   B7NW30;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Isopentenyl-diphosphate Delta-isomerase {ECO:0000255|HAMAP-Rule:MF_00202};
DE            Short=IPP isomerase {ECO:0000255|HAMAP-Rule:MF_00202};
DE            EC=5.3.3.2 {ECO:0000255|HAMAP-Rule:MF_00202};
DE   AltName: Full=IPP:DMAPP isomerase {ECO:0000255|HAMAP-Rule:MF_00202};
DE   AltName: Full=Isopentenyl pyrophosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00202};
GN   Name=idi {ECO:0000255|HAMAP-Rule:MF_00202}; OrderedLocusNames=ECIAI39_3305;
OS   Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI39 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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:0000255|HAMAP-Rule:MF_00202}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00202};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00202};
CC       Note=Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when
CC       substrate is bound. {ECO:0000255|HAMAP-Rule:MF_00202};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00202};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00202};
CC   -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC       biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate:
CC       step 1/1. {ECO:0000255|HAMAP-Rule:MF_00202}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00202}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00202}.
CC   -!- SIMILARITY: Belongs to the IPP isomerase type 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00202}.
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DR   EMBL; CU928164; CAR19423.1; -; Genomic_DNA.
DR   RefSeq; WP_001192788.1; NC_011750.1.
DR   RefSeq; YP_002409227.1; NC_011750.1.
DR   AlphaFoldDB; B7NW30; -.
DR   SMR; B7NW30; -.
DR   STRING; 585057.ECIAI39_3305; -.
DR   EnsemblBacteria; CAR19423; CAR19423; ECIAI39_3305.
DR   KEGG; ect:ECIAI39_3305; -.
DR   PATRIC; fig|585057.6.peg.3427; -.
DR   HOGENOM; CLU_060552_2_0_6; -.
DR   OMA; FPLRWAN; -.
DR   UniPathway; UPA00059; UER00104.
DR   Proteomes; UP000000749; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02885; IPP_Isomerase; 1.
DR   HAMAP; MF_00202; Idi; 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   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Isoprene biosynthesis; Magnesium; Manganese;
KW   Metal-binding.
FT   CHAIN           1..182
FT                   /note="Isopentenyl-diphosphate Delta-isomerase"
FT                   /id="PRO_1000118724"
FT   DOMAIN          30..164
FT                   /note="Nudix hydrolase"
FT   ACT_SITE        67
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   ACT_SITE        116
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   BINDING         25
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   BINDING         32
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   BINDING         69
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   BINDING         87
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   BINDING         114
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   BINDING         116
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
SQ   SEQUENCE   182 AA;  20446 MW;  A4C8A8B9C48CAA67 CRC64;
     MQTEHVILLN AQGVPTGTLE KYAAHTADTL LHLAFSSWLF NAKGQLLVTR RALSKKAWPG
     VWTNSVCGHP QLGESNEDAV IRRCRFELGV EITAPEPVYP DFRYRATDPN GIVENEVCPV
     FAARTTSALQ INDDEVMDYQ WCDLADVLHG IDATPWAFSP WMVMQATNRE ARKRLSAFTQ
     LK
 
 
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