IDI1_PHARH
ID IDI1_PHARH Reviewed; 251 AA.
AC O42641;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Isopentenyl-diphosphate delta-isomerase {ECO:0000305};
DE EC=5.3.3.2 {ECO:0000269|PubMed:9182699};
DE AltName: Full=Isopentenyl pyrophosphate isomerase {ECO:0000303|PubMed:9182699};
DE Short=IPP isomerase {ECO:0000303|PubMed:9182699};
GN Name=IDI {ECO:0000303|PubMed:9182699};
OS Phaffia rhodozyma (Yeast) (Xanthophyllomyces dendrorhous).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Cystofilobasidiales; Mrakiaceae; Phaffia.
OX NCBI_TaxID=264483;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=9182699; DOI=10.1042/bj3240421;
RA Kajiwara S., Fraser P.D., Kondo K., Misawa N.;
RT "Expression of an exogenous isopentenyl diphosphate isomerase gene enhances
RT isoprenoid biosynthesis in Escherichia coli.";
RL Biochem. J. 324:421-426(1997).
CC -!- FUNCTION: Isopentenyl-diphosphate delta-isomerase; part of the second
CC module of ergosterol biosynthesis pathway that includes the middle
CC steps of the pathway (PubMed:9182699). The second module is carried out
CC in the vacuole and involves the formation of farnesyl diphosphate,
CC which is also an important intermediate in the biosynthesis of
CC ubiquinone, dolichol, heme and prenylated proteins (By similarity).
CC Activity by the mevalonate kinase first converts mevalonate into 5-
CC phosphomevalonate (By similarity). 5-phosphomevalonate is then further
CC converted to 5-diphosphomevalonate by the phosphomevalonate kinase (By
CC similarity). The diphosphomevalonate decarboxylase then produces
CC isopentenyl diphosphate (By similarity). The isopentenyl-diphosphate
CC delta-isomerase then catalyzes the 1,3-allylic rearrangement of the
CC homoallylic substrate isopentenyl (IPP) to its highly electrophilic
CC allylic isomer, dimethylallyl diphosphate (DMAPP) (PubMed:9182699).
CC Finally the farnesyl diphosphate synthase catalyzes the sequential
CC condensation of isopentenyl pyrophosphate with dimethylallyl
CC pyrophosphate, and then with the resultant geranylpyrophosphate to the
CC ultimate product farnesyl pyrophosphate (By similarity).
CC {ECO:0000250|UniProtKB:P15496, ECO:0000269|PubMed:9182699}.
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:0000269|PubMed:9182699};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23285;
CC Evidence={ECO:0000269|PubMed:9182699};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q46822};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q46822};
CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate:
CC step 1/1. {ECO:0000269|PubMed:9182699}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the IPP isomerase type 1 family. {ECO:0000305}.
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DR EMBL; Y15811; CAA75796.1; -; Genomic_DNA.
DR AlphaFoldDB; O42641; -.
DR SMR; O42641; -.
DR UniPathway; UPA00059; UER00104.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IEA:UniProtKB-EC.
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-KW.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02885; IPP_Isomerase; 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 1: Evidence at protein level;
KW Cytoplasm; Isomerase; Isoprene biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Metal-binding; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism.
FT CHAIN 1..251
FT /note="Isopentenyl-diphosphate delta-isomerase"
FT /id="PRO_0000205229"
FT DOMAIN 64..212
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT ACT_SITE 102
FT /evidence="ECO:0000250|UniProtKB:P15496"
FT ACT_SITE 164
FT /evidence="ECO:0000250|UniProtKB:P15496"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13907"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q46822"
FT BINDING 66
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q46822"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13907"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13907"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13907"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q46822"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q46822"
SQ SEQUENCE 251 AA; 28753 MW; 8BB7376AA9329D1E CRC64;
MSMPNIVPPA EVRTEGLSLE EYDEEQVRLM EERCILVNPD DVAYGEASKK TCHLMSNINA
PKDLLHRAFS VFLFRPSDGA LLLQRRADEK ITFPGMWTNT CCSHPLSIKG EVKEENQIGV
RRAASRKLEH ELGVPTSSTP PDSFTYLTRI HYLAPSDGLW GEHEIDYILF STTPTEHTGN
PNEVSDTRYV TKPELQAMFE DESNSFTPWF KLIARDFLFG WWDQLLARRN EKGEVDAKSL
EDLSDNKVWK M
