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Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (EC 5.3.3.2) (Isopentenyl diphosphate:dimethylallyl diphosphate isomerase) (Isopentenyl pyrophosphate isomerase) (Type 2 isopentenyl diphosphate isomerase) (IDI-2)

 A0A175RQ67_9RHIZ        Unreviewed;       345 AA.
A0A175RQ67;
07-SEP-2016, integrated into UniProtKB/TrEMBL.
07-SEP-2016, sequence version 1.
25-OCT-2017, entry version 10.
RecName: Full=Isopentenyl-diphosphate delta-isomerase {ECO:0000256|HAMAP-Rule:MF_00354};
Short=IPP isomerase {ECO:0000256|HAMAP-Rule:MF_00354};
EC=5.3.3.2 {ECO:0000256|HAMAP-Rule:MF_00354};
AltName: Full=Isopentenyl diphosphate:dimethylallyl diphosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00354};
AltName: Full=Isopentenyl pyrophosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00354};
AltName: Full=Type 2 isopentenyl diphosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00354};
Short=IDI-2 {ECO:0000256|HAMAP-Rule:MF_00354};
Name=fni {ECO:0000256|HAMAP-Rule:MF_00354};
ORFNames=NS365_09090 {ECO:0000313|EMBL:KTR05945.1};
Aureimonas ureilytica.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
Aurantimonadaceae; Aureimonas.
NCBI_TaxID=401562 {ECO:0000313|EMBL:KTR05945.1, ECO:0000313|Proteomes:UP000078529};
[1] {ECO:0000313|EMBL:KTR05945.1, ECO:0000313|Proteomes:UP000078529}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NS365 {ECO:0000313|EMBL:KTR05945.1,
ECO:0000313|Proteomes:UP000078529};
PubMed=26793183;
Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
Patil P.B.;
"Genomic Resource of Rice Seed Associated Bacteria.";
Front. Microbiol. 6:1551-1551(2016).
-!- FUNCTION: Involved in the biosynthesis of isoprenoids. Catalyzes
the 1,3-allylic rearrangement of the homoallylic substrate
isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate
(DMAPP). {ECO:0000256|HAMAP-Rule:MF_00354}.
-!- CATALYTIC ACTIVITY: Isopentenyl diphosphate = dimethylallyl
diphosphate. {ECO:0000256|HAMAP-Rule:MF_00354}.
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000256|HAMAP-Rule:MF_00354};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00354};
-!- COFACTOR:
Name=NADPH; Xref=ChEBI:CHEBI:57783;
Evidence={ECO:0000256|HAMAP-Rule:MF_00354};
-!- SUBUNIT: Homooctamer. Dimer of tetramers. {ECO:0000256|HAMAP-
Rule:MF_00354}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00354}.
-!- SIMILARITY: Belongs to the IPP isomerase type 2 family.
{ECO:0000256|HAMAP-Rule:MF_00354}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00354}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KTR05945.1}.
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EMBL; LDQA01000021; KTR05945.1; -; Genomic_DNA.
RefSeq; WP_058599966.1; NZ_LDQA01000021.1.
EnsemblBacteria; KTR05945; KTR05945; NS365_09090.
PATRIC; fig|401562.4.peg.1576; -.
Proteomes; UP000078529; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0070402; F:NADPH binding; IEA:UniProtKB-UniRule.
GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-UniRule.
CDD; cd02811; IDI-2_FMN; 1.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_00354; Idi_2; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR000262; FMN-dep_DH.
InterPro; IPR011179; IPdP_isomerase.
PANTHER; PTHR43665; PTHR43665; 1.
Pfam; PF01070; FMN_dh; 2.
PIRSF; PIRSF003314; IPP_isomerase; 1.
TIGRFAMs; TIGR02151; IPP_isom_2; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000078529};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00354};
Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00354};
FMN {ECO:0000256|HAMAP-Rule:MF_00354};
Isomerase {ECO:0000256|HAMAP-Rule:MF_00354,
ECO:0000313|EMBL:KTR05945.1};
Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00354};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00354};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00354};
NADP {ECO:0000256|HAMAP-Rule:MF_00354};
Reference proteome {ECO:0000313|Proteomes:UP000078529}.
DOMAIN 28 99 FMN_dh. {ECO:0000259|Pfam:PF01070}.
DOMAIN 179 338 FMN_dh. {ECO:0000259|Pfam:PF01070}.
NP_BIND 68 70 FMN. {ECO:0000256|HAMAP-Rule:MF_00354}.
NP_BIND 274 276 FMN. {ECO:0000256|HAMAP-Rule:MF_00354}.
NP_BIND 295 296 FMN. {ECO:0000256|HAMAP-Rule:MF_00354}.
REGION 9 10 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00354}.
REGION 98 100 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00354}.
METAL 163 163 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00354}.
BINDING 67 67 FMN. {ECO:0000256|HAMAP-Rule:MF_00354}.
BINDING 98 98 FMN; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00354}.
BINDING 127 127 FMN. {ECO:0000256|HAMAP-Rule:MF_00354}.
BINDING 162 162 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00354}.
BINDING 194 194 FMN. {ECO:0000256|HAMAP-Rule:MF_00354}.
BINDING 224 224 FMN; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00354}.
SEQUENCE 345 AA; 36054 MW; 50469A211206F4C5 CRC64;
MPEADIRSRK GDHLDIVLRP ALVSARVNAG FDAVRFEHAA LPEVDLDEID LSTQFLGRRL
GAPILISSMT GGMERAARIN LRLAEAAQVL GLALAVGSQR IAIEGRGQGG LDGSLRRAAP
DVPILANIGG AQLLAGWGLD EARRAVEMIE ADALIVHLNP LQEAVQPEGD RRWRGLLSAI
EALARDLGRP IVAKEVGNGL SGRLGRRLMD AGVHALDVAG AGGTSWAAIE AERLQDPVAR
ATALLFADWG IPTARAIRDV RAACPEAVVI GSGGVRHGLD VAKAIRLGAD LAGQAAAALP
GADHSAEAVV AHFQEVIQQL RIACFCTGSP DLAALRQAPL LSDEG


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