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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)

 A9NGD2_ACHLI            Unreviewed;       323 AA.
A9NGD2;
05-FEB-2008, integrated into UniProtKB/TrEMBL.
05-FEB-2008, sequence version 1.
25-OCT-2017, entry version 66.
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:ABX81412.1};
Synonyms=fni {ECO:0000256|HAMAP-Rule:MF_00354};
OrderedLocusNames=ACL_0797 {ECO:0000313|EMBL:ABX81412.1};
Acholeplasma laidlawii (strain PG-8A).
Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
Acholeplasmataceae; Acholeplasma.
NCBI_TaxID=441768 {ECO:0000313|EMBL:ABX81412.1, ECO:0000313|Proteomes:UP000008558};
[1] {ECO:0000313|EMBL:ABX81412.1, ECO:0000313|Proteomes:UP000008558}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PG-8A {ECO:0000313|EMBL:ABX81412.1,
ECO:0000313|Proteomes:UP000008558};
PubMed=21784942; DOI=10.1128/JB.05059-11;
Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M.,
Akopian T.A., Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y.,
Kazanov M.D., Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S.,
Demina I.A., Serebryakova M.V., Galyamina M.A., Vtyurin N.N.,
Rogov S.I., Alexeev D.G., Ladygina V.G., Govorun V.M.;
"Complete genome and proteome of Acholeplasma laidlawii.";
J. Bacteriol. 193:4943-4953(2011).
-!- 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; CP000896; ABX81412.1; -; Genomic_DNA.
RefSeq; WP_012242743.1; NC_010163.1.
ProteinModelPortal; A9NGD2; -.
STRING; 441768.ACL_0797; -.
EnsemblBacteria; ABX81412; ABX81412; ACL_0797.
KEGG; acl:ACL_0797; -.
eggNOG; ENOG4106UJV; Bacteria.
eggNOG; COG1304; LUCA.
HOGENOM; HOG000072127; -.
KO; K01823; -.
OMA; VGSQRAM; -.
OrthoDB; POG091H07K8; -.
Proteomes; UP000008558; Chromosome.
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:UP000008558};
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:ABX81412.1};
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:UP000008558}.
DOMAIN 161 317 FMN_dh. {ECO:0000259|Pfam:PF01070}.
NP_BIND 60 62 FMN. {ECO:0000256|HAMAP-Rule:MF_00354}.
NP_BIND 254 256 FMN. {ECO:0000256|HAMAP-Rule:MF_00354}.
NP_BIND 275 276 FMN. {ECO:0000256|HAMAP-Rule:MF_00354}.
REGION 5 6 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00354}.
METAL 149 149 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00354}.
BINDING 90 90 FMN; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00354}.
BINDING 118 118 FMN. {ECO:0000256|HAMAP-Rule:MF_00354}.
BINDING 148 148 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00354}.
BINDING 180 180 FMN. {ECO:0000256|HAMAP-Rule:MF_00354}.
BINDING 205 205 FMN. {ECO:0000256|HAMAP-Rule:MF_00354}.
BINDING 210 210 FMN; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00354}.
SEQUENCE 323 AA; 35979 MW; 12C26E3619CAC33D CRC64;
MSKNRKDDHI NIAKSFKKKS NMFDKILLEG TDLPDLSMDD IDLSTEFLGM KVPYPFYINA
MTGGSEKAHK INEFLSKIAD HFNLPMVTGS QSIMFKDPSS IDSFKVIRNN HKGIIVGNIN
PNMTLEQAQV AVSTIQANAL SIHLNVIQEL VMNEGDRDFR LWSNHIESVV KHLNKPVIVK
QVGLGLSLKT IQKIKTLGVK YIDVSGSGGT SFIDIESTRS AKDYSYLNDF SIDTAQALIN
LKNEKDLEIY ASGGIRHPLD VIKSLILGAK ACGLSKWFLD LTDLEFAAAV KKVEEFIEDL
KKIMLILGVS SLKDLKQVTY NIV


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