IDI2_ARCFU
ID IDI2_ARCFU Reviewed; 345 AA.
AC O27997;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Isopentenyl-diphosphate delta-isomerase {ECO:0000255|HAMAP-Rule:MF_00354};
DE Short=IPP isomerase {ECO:0000255|HAMAP-Rule:MF_00354};
DE EC=5.3.3.2 {ECO:0000255|HAMAP-Rule:MF_00354};
DE AltName: Full=Isopentenyl diphosphate:dimethylallyl diphosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00354};
DE AltName: Full=Isopentenyl pyrophosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00354};
DE AltName: Full=Type 2 isopentenyl diphosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00354};
DE Short=IDI-2 {ECO:0000255|HAMAP-Rule:MF_00354};
GN Name=fni {ECO:0000255|HAMAP-Rule:MF_00354}; OrderedLocusNames=AF_2287;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
CC -!- FUNCTION: Involved in the biosynthesis of isoprenoids. Catalyzes the
CC 1,3-allylic rearrangement of the homoallylic substrate isopentenyl
CC (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
CC {ECO:0000255|HAMAP-Rule:MF_00354}.
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_00354};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00354};
CC -!- COFACTOR:
CC Name=NADPH; Xref=ChEBI:CHEBI:57783;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00354};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00354};
CC -!- SUBUNIT: Homooctamer. Dimer of tetramers. {ECO:0000255|HAMAP-
CC Rule:MF_00354}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00354}.
CC -!- SIMILARITY: Belongs to the IPP isomerase type 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00354}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB88970.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000782; AAB88970.1; ALT_INIT; Genomic_DNA.
DR PIR; G69535; G69535.
DR RefSeq; WP_048064552.1; NC_000917.1.
DR AlphaFoldDB; O27997; -.
DR SMR; O27997; -.
DR STRING; 224325.AF_2287; -.
DR EnsemblBacteria; AAB88970; AAB88970; AF_2287.
DR GeneID; 1485519; -.
DR KEGG; afu:AF_2287; -.
DR eggNOG; arCOG00613; Archaea.
DR HOGENOM; CLU_065515_1_0_2; -.
DR OMA; WDWGIPT; -.
DR OrthoDB; 42330at2157; -.
DR PhylomeDB; O27997; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070402; F:NADPH binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02811; IDI-2_FMN; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00354; Idi_2; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000262; FMN-dep_DH.
DR InterPro; IPR011179; IPdP_isomerase.
DR PANTHER; PTHR43665; PTHR43665; 1.
DR Pfam; PF01070; FMN_dh; 1.
DR PIRSF; PIRSF003314; IPP_isomerase; 1.
DR TIGRFAMs; TIGR02151; IPP_isom_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Flavoprotein; FMN; Isomerase; Isoprene biosynthesis; Magnesium;
KW Metal-binding; NADP; Reference proteome.
FT CHAIN 1..345
FT /note="Isopentenyl-diphosphate delta-isomerase"
FT /id="PRO_0000134441"
FT BINDING 6..7
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 63..65
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 93..95
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 93
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 122
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 188
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 218
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 265..267
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 286..287
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
SQ SEQUENCE 345 AA; 37421 MW; 87F25B4EA14DF6FE CRC64;
MSTSKRKIDH LKICLEEEVE SGYTGLEDVM LIHKALPEVD YWKIDTEIEF FGKKLSFPLL
IASMTGGHPE TKEINARLGE AVEEAGIGMG VGSQRAAIED ESLADSFTVV REKAPNAFVY
ANIGMPQVIE RGVEIVDRAV EMIDADAVAI HLNYLQEAIQ PEGDLNAEKG LEVLEEVCRS
VKVPVIAKET GAGISREVAV MLKRAGVSAI DVGGKGGTTF SGVEVYRVND EVSKSVGIDF
WDWGLPTAFS IVDCRGILPV IATGGLRSGL DVAKSIAIGA ELGSAALPFL RAAVESAEKV
REEIEYFRRG LKTAMFLTGC KNVEELKGLK VFVSGRLKEW IDFRG
