ID A0A1V4EJP5_9ACTN Unreviewed; 198 AA.
AC A0A1V4EJP5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Isopentenyl-diphosphate Delta-isomerase {ECO:0000256|ARBA:ARBA00012057, ECO:0000256|HAMAP-Rule:MF_00202};
DE Short=IPP isomerase {ECO:0000256|HAMAP-Rule:MF_00202};
DE EC=5.3.3.2 {ECO:0000256|ARBA:ARBA00012057, ECO:0000256|HAMAP-Rule:MF_00202};
DE AltName: Full=IPP:DMAPP isomerase {ECO:0000256|HAMAP-Rule:MF_00202};
DE AltName: Full=Isopentenyl pyrophosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00202};
GN Name=idi {ECO:0000256|HAMAP-Rule:MF_00202};
GN ORFNames=B1L11_10180 {ECO:0000313|EMBL:OPG13139.1};
OS Microbispora sp. GKU 823.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=1652100 {ECO:0000313|EMBL:OPG13139.1, ECO:0000313|Proteomes:UP000190255};
RN [1] {ECO:0000313|EMBL:OPG13139.1, ECO:0000313|Proteomes:UP000190255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GKU 823 {ECO:0000313|EMBL:OPG13139.1,
RC ECO:0000313|Proteomes:UP000190255};
RA Kruasuwan W.;
RT "Draft genome sequence of sugarcane root-associated plant growth promoting
RT Microbispora sp. GKU 823.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00202};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00202};
CC Note=Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when
CC substrate is bound. {ECO:0000256|HAMAP-Rule:MF_00202};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00202};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00202};
CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate:
CC step 1/1. {ECO:0000256|ARBA:ARBA00004826, ECO:0000256|HAMAP-
CC Rule:MF_00202}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00202}.
CC -!- SIMILARITY: Belongs to the IPP isomerase type 1 family.
CC {ECO:0000256|ARBA:ARBA00007579, ECO:0000256|HAMAP-Rule:MF_00202}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC {ECO:0000256|ARBA:ARBA00005582}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPG13139.1}.
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DR EMBL; MWJN01000013; OPG13139.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4EJP5; -.
DR OrthoDB; 9809458at2; -.
DR UniPathway; UPA00059; UER00104.
DR Proteomes; UP000190255; Unassembled WGS sequence.
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 Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 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 NCBIfam; TIGR02150; IPP_isom_1; 1.
DR PANTHER; PTHR10885; ISOPENTENYL-DIPHOSPHATE DELTA-ISOMERASE; 1.
DR PANTHER; PTHR10885:SF20; NUDIX HYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00293; NUDIX; 1.
DR PIRSF; PIRSF018427; Isopntndiph_ism; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00202};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00202};
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP-
KW Rule:MF_00202}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00202};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_00202};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00202}.
FT DOMAIN 31..165
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT ACT_SITE 68
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00202,
FT ECO:0000256|PIRSR:PIRSR018427-1"
FT ACT_SITE 117
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00202,
FT ECO:0000256|PIRSR:PIRSR018427-1"
FT BINDING 26
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00202"
FT BINDING 33
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00202"
FT BINDING 70
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00202"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00202"
FT BINDING 115
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00202"
FT BINDING 117
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00202"
SQ SEQUENCE 198 AA; 21384 MW; E7A4ED6C770B8C10 CRC64;
MTSQEHVVLV DGEGNPIGTA PKSTVHGAET PLHLAFSSYV FDHRGRVLLS RRAGSKLTWP
DAWTNSCCGH PLPGEPLSSA VIRRLGFELG LAVESVDLIL PGFSYRAVMD NGTVENELCP
VYRAVVTEEA APNAEEVGEV RWEPWTRFAA EVMSGELDIS PWAREQVPQL VALGPDPLAW
PVADAAALPP AARPLSNR
//
