IDI2_HALSA
ID IDI2_HALSA Reviewed; 360 AA.
AC Q9HHE4; O54623;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
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}; Synonyms=fni1;
GN OrderedLocusNames=VNG_5084G; ORFNames=H0660;
GN and
GN Name=fni2 {ECO:0000255|HAMAP-Rule:MF_00354}; OrderedLocusNames=VNG_5213G;
GN ORFNames=H1696;
GN and
GN Name=fni3 {ECO:0000255|HAMAP-Rule:MF_00354}; OrderedLocusNames=VNG_6081G;
GN and
GN Name=fni4 {ECO:0000255|HAMAP-Rule:MF_00354}; OrderedLocusNames=VNG_6445G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OG Plasmid pNRC100, and Plasmid pNRC200.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1; PLASMID=pNRC100;
RX PubMed=9847077; DOI=10.1101/gr.8.11.1131;
RA Ng W.V., Ciufo S.A., Smith T.M., Bumgarner R.E., Baskin D., Faust J.,
RA Hall B., Loretz C., Seto J., Slagel J., Hood L., DasSarma S.;
RT "Snapshot of a large dynamic replicon in a halophilic archaeon: megaplasmid
RT or minichromosome?";
RL Genome Res. 8:1131-1141(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1; PLASMID=pNRC200;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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=AAC82844.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC82933.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF016485; AAC82844.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF016485; AAC82933.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE004438; AAG20768.1; -; Genomic_DNA.
DR EMBL; AE004438; AAG21040.1; -; Genomic_DNA.
DR RefSeq; WP_010904022.1; NZ_BK010831.1.
DR AlphaFoldDB; Q9HHE4; -.
DR SMR; Q9HHE4; -.
DR EnsemblBacteria; AAC82844; AAC82844; AAC82844.
DR EnsemblBacteria; AAC82933; AAC82933; AAC82933.
DR EnsemblBacteria; AAG20768; AAG20768; VNG_6081G.
DR EnsemblBacteria; AAG21040; AAG21040; VNG_6445G.
DR GeneID; 5955119; -.
DR KEGG; hal:AAC82844.1; -.
DR KEGG; hal:AAC82933.1; -.
DR KEGG; hal:VNG_6081G; -.
DR KEGG; hal:VNG_6445G; -.
DR PATRIC; fig|64091.14.peg.2138; -.
DR HOGENOM; CLU_065515_1_0_2; -.
DR InParanoid; Q9HHE4; -.
DR OrthoDB; 42330at2157; -.
DR PhylomeDB; Q9HHE4; -.
DR Proteomes; UP000000554; Plasmid pNRC100.
DR Proteomes; UP000000554; Plasmid pNRC200.
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; 2.
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; Plasmid; Reference proteome.
FT CHAIN 1..360
FT /note="Isopentenyl-diphosphate delta-isomerase"
FT /id="PRO_0000134442"
FT BINDING 12..13
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 69..71
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 99..101
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 99
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 130
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 196
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 226
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 277..279
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT BINDING 298..299
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
SQ SEQUENCE 360 AA; 38343 MW; 67B14178071D3164 CRC64;
MTAQDSTQTE DRKDDHLQIV QERDVETTGT GFDDVHLVHN ALPELDYDAI DPSIDFLGHD
LSAPIFIESM TGGHHNTTEI NRALARAASE TGIAMGLGSQ RAGLELDDER VLESYTVVRD
AAPDAFIYGN LGAAQLREYD IEMVEQAVEM IDADALAVHL NFLQEATQPE GDVDGRNCVA
AIERVSEALS VPIIVKETGN GISGETAREL TAAGVDALDV AGKGGTTWSG IEAYRAAAAN
APRQKQIGTL FREWGIPTAA STIECVAEHD CVIASGGVRT GLDVAKAIAL GARAGGLAKP
FLKPATDGPD AVIERVGDLI AELRTAMFVT GSGSIDELQQ VEYVLHGKTR EYVEQRTSSE
