IDI2_AROAE
ID IDI2_AROAE Reviewed; 189 AA.
AC Q5NWG5;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Isopentenyl-diphosphate Delta-isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00202};
DE Short=IPP isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00202};
DE EC=5.3.3.2 {ECO:0000255|HAMAP-Rule:MF_00202};
DE AltName: Full=IPP:DMAPP isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00202};
DE AltName: Full=Isopentenyl pyrophosphate isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00202};
GN Name=idi2 {ECO:0000255|HAMAP-Rule:MF_00202}; OrderedLocusNames=AZOSEC00720;
GN ORFNames=p2A143;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OG Plasmid pAzo2.
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
CC -!- FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic
CC substrate isopentenyl (IPP) to its highly electrophilic allylic isomer,
CC dimethylallyl diphosphate (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00202}.
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_00202};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00202};
CC Note=Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when
CC substrate is bound. {ECO:0000255|HAMAP-Rule:MF_00202};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00202};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00202};
CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate:
CC step 1/1. {ECO:0000255|HAMAP-Rule:MF_00202}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00202}.
CC -!- SIMILARITY: Belongs to the IPP isomerase type 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_00202}.
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DR EMBL; CR555308; CAI10599.1; -; Genomic_DNA.
DR RefSeq; WP_011255022.1; NC_006824.1.
DR AlphaFoldDB; Q5NWG5; -.
DR SMR; Q5NWG5; -.
DR STRING; 76114.p2A143; -.
DR EnsemblBacteria; CAI10599; CAI10599; p2A143.
DR KEGG; eba:p2A143; -.
DR eggNOG; COG1443; Bacteria.
DR HOGENOM; CLU_060552_2_1_4; -.
DR OMA; VEQEYNH; -.
DR OrthoDB; 1345242at2; -.
DR UniPathway; UPA00059; UER00104.
DR Proteomes; UP000006552; Plasmid pAzo2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02885; IPP_Isomerase; 1.
DR HAMAP; MF_00202; Idi; 1.
DR InterPro; IPR011876; IsopentenylPP_isomerase_typ1.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR PIRSF; PIRSF018427; Isopntndiph_ism; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR TIGRFAMs; TIGR02150; IPP_isom_1; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Isomerase; Isoprene biosynthesis; Magnesium; Manganese;
KW Metal-binding; Plasmid; Reference proteome.
FT CHAIN 1..189
FT /note="Isopentenyl-diphosphate Delta-isomerase 2"
FT /id="PRO_0000205242"
FT DOMAIN 28..160
FT /note="Nudix hydrolase"
FT ACT_SITE 65
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT ACT_SITE 112
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT BINDING 30
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT BINDING 67
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT BINDING 110
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT BINDING 112
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
SQ SEQUENCE 189 AA; 21294 MW; 7AA21A684C2FCE05 CRC64;
MEDQVILVDE HDNKVGFAGK MAAHQRGALH RAISIFVFDS HSRLMLQRRA AGKYHSGGLW
SNTCCSHPRP NEESADAARR RLREEMGVDC ELKKAFSFVY RTKFGSGLIE HEFDHVFFGN
HDGRPVLNPD EADDWKWVDL TELTVDVRKR PETYSFWLAA CLDRVISCRS LNGAGAAAQK
IGSTITLMA
