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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)

 U4KRX2_ACHPJ            Unreviewed;       315 AA.
U4KRX2;
11-DEC-2013, integrated into UniProtKB/TrEMBL.
11-DEC-2013, sequence version 1.
25-OCT-2017, entry version 23.
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=idi {ECO:0000313|EMBL:CCV64521.1};
Synonyms=fni {ECO:0000256|HAMAP-Rule:MF_00354};
ORFNames=BN85409440 {ECO:0000313|EMBL:CCV64521.1};
Acholeplasma palmae (strain ATCC 49389 / J233).
Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
Acholeplasmataceae; Acholeplasma.
NCBI_TaxID=1318466 {ECO:0000313|EMBL:CCV64521.1, ECO:0000313|Proteomes:UP000032740};
[1] {ECO:0000313|EMBL:CCV64521.1, ECO:0000313|Proteomes:UP000032740}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=J233 {ECO:0000313|EMBL:CCV64521.1,
ECO:0000313|Proteomes:UP000032740};
PubMed=24158107; DOI=10.1159/000354322;
Kube M., Siewert C., Migdoll A.M., Duduk B., Holz S., Rabus R.,
Seemuller E., Mitrovic J., Muller I., Buttner C., Reinhardt R.;
"Analysis of the Complete Genomes of Acholeplasma brassicae , A.
palmae and A. laidlawii and Their Comparison to the Obligate Parasites
from ' Candidatus Phytoplasma'.";
J. Mol. Microbiol. Biotechnol. 24:19-36(2013).
-!- 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}.
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EMBL; FO681347; CCV64521.1; -; Genomic_DNA.
EnsemblBacteria; CCV64521; CCV64521; BN85409440.
KEGG; apal:BN85409440; -.
KO; K01823; -.
Proteomes; UP000032740; Chromosome Acholeplasma palmae.
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; 1.
PIRSF; PIRSF003314; IPP_isomerase; 1.
TIGRFAMs; TIGR02151; IPP_isom_2; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000032740};
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:CCV64521.1};
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:UP000032740}.
DOMAIN 147 309 FMN_dh. {ECO:0000259|Pfam:PF01070}.
NP_BIND 51 53 FMN. {ECO:0000256|HAMAP-Rule:MF_00354}.
NP_BIND 247 249 FMN. {ECO:0000256|HAMAP-Rule:MF_00354}.
NP_BIND 268 269 FMN. {ECO:0000256|HAMAP-Rule:MF_00354}.
REGION 81 83 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00354}.
METAL 141 141 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00354}.
BINDING 81 81 FMN; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00354}.
BINDING 110 110 FMN. {ECO:0000256|HAMAP-Rule:MF_00354}.
BINDING 140 140 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00354}.
BINDING 172 172 FMN. {ECO:0000256|HAMAP-Rule:MF_00354}.
BINDING 197 197 FMN. {ECO:0000256|HAMAP-Rule:MF_00354}.
BINDING 202 202 FMN; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00354}.
SEQUENCE 315 AA; 35291 MW; 061476764BCE3434 CRC64;
MALALTQKTG TNDFDQIHFE HMSLPKYDFN DINLESCYFN RQFKYPFYIN AMTGGTQKTK
EANEKLAKLA KHYGLAMAVG SQKIALENKS VQDTFSVIHD IYPDGFFIGN LSANATYEDV
LKASQMIHAQ AFQIHLNPVQ ELAMQEGDRN FKHWKNNIAL IAKEIKIPLI VKEVGFGMNE
KTIASLINLG VSNIDVSGNG GTNFAKIENA RVNRNDGFLE GFGISTVKSL KYSQKYQEKA
NFIASGGIRS ALDIVKSLVL GACAVGLSKF FLETIQLAWD EQIKKVDELI SDIKKVMILL
NVNNIKDLRN VQYFD


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