ID B5H4M7_STRE2 Unreviewed; 197 AA.
AC B5H4M7;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=SSDG_00103 {ECO:0000313|EMBL:EDY61788.1};
OS Streptomyces pristinaespiralis (strain ATCC 25486 / DSM 40338 / CBS 914.69
OS / JCM 4507 / NBRC 13074 / NRRL 2958 / 5647).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=457429 {ECO:0000313|EMBL:EDY61788.1, ECO:0000313|Proteomes:UP000002805};
RN [1] {ECO:0000313|Proteomes:UP000002805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25486 / DSM 40338 / CBS 914.69 / JCM 4507 / NBRC 13074 /
RC NRRL 2958 / 5647 {ECO:0000313|Proteomes:UP000002805};
RG The Broad Institute Genome Sequencing Platform;
RA Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Straight P., Clardy J.,
RA Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., Lander E.,
RA Galagan J., Nusbaum C., Birren B.;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25486 / DSM 40338 / CBS 914.69 / JCM 4507 / NBRC 13074 /
RC NRRL 2958 / 5647 {ECO:0000313|Proteomes:UP000002805};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Streptomyces pristinaespiralis strain ATCC 25486.";
RL Submitted (OCT-2009) 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}.
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DR EMBL; CM000950; EDY61788.1; -; Genomic_DNA.
DR RefSeq; WP_005308932.1; NZ_CM000950.1.
DR AlphaFoldDB; B5H4M7; -.
DR eggNOG; COG1443; Bacteria.
DR HOGENOM; CLU_060552_2_1_11; -.
DR UniPathway; UPA00059; UER00104.
DR Proteomes; UP000002805; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002805}.
FT DOMAIN 46..183
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT ACT_SITE 83
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00202,
FT ECO:0000256|PIRSR:PIRSR018427-1"
FT ACT_SITE 132
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00202,
FT ECO:0000256|PIRSR:PIRSR018427-1"
FT BINDING 41
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00202"
FT BINDING 48
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00202"
FT BINDING 85
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00202"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00202"
FT BINDING 130
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00202"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00202"
SQ SEQUENCE 197 AA; 21195 MW; 30411BA69803E0EF CRC64;
MPITPATAAT SSSNGTSPAI LLELVDEEGN TIGTAEKLAA HQAPGQLHRA FSVFLFDEQG
RLLLQRRALG KYHSPSVWSN TCCGHPYPGE APFAAAARRT YEELGVSPSL LAEAGTVRYN
HPDPESGLVE QEYNHLFVGM VQAPLLPDPE EIGETAFVTP DELTELHGRA TFSAWFMTVL
DAARPAIREL TGPAGGW
//
