IDI1_ASPFU
ID IDI1_ASPFU Reviewed; 279 AA.
AC Q4WM52;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Isopentenyl-diphosphate delta-isomerase idi1 {ECO:0000305|PubMed:22106303};
DE EC=5.3.3.2 {ECO:0000269|PubMed:16110826};
DE AltName: Full=Ergosterol biosynthesis protein idi1 {ECO:0000303|PubMed:16110826};
DE AltName: Full=Isopentenyl pyrophosphate isomerase idi1 {ECO:0000305|PubMed:22106303};
DE Short=IPP isomerase {ECO:0000305|PubMed:22106303};
GN Name=idi1 {ECO:0000303|PubMed:16110826}; ORFNames=AFUA_6G11160;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=16110826; DOI=10.1080/13693780400029114;
RA Ferreira M.E., Colombo A.L., Paulsen I., Ren Q., Wortman J., Huang J.,
RA Goldman M.H., Goldman G.H.;
RT "The ergosterol biosynthesis pathway, transporter genes, and azole
RT resistance in Aspergillus fumigatus.";
RL Med. Mycol. 43:S313-S319(2005).
RN [3]
RP FUNCTION.
RX PubMed=22106303; DOI=10.1073/pnas.1106399108;
RA Yasmin S., Alcazar-Fuoli L., Gruendlinger M., Puempel T., Cairns T.,
RA Blatzer M., Lopez J.F., Grimalt J.O., Bignell E., Haas H.;
RT "Mevalonate governs interdependency of ergosterol and siderophore
RT biosyntheses in the fungal pathogen Aspergillus fumigatus.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E497-E504(2012).
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 (By similarity). Idi1 catalyzes the 1,3-allylic
CC rearrangement of isopentenyl (IPP) to its highly electrophilic allylic
CC isomer, dimethylallyl diphosphate (DMAPP) (By similarity). The second
CC module is carried out in the vacuole and involves the formation of
CC farnesyl diphosphate, which is also an important intermediate in the
CC biosynthesis of ubiquinone, dolichol, heme and prenylated proteins.
CC Activity by the mevalonate kinase erg12 (AFUA_4G07780) first converts
CC mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then
CC further converted to 5-diphosphomevalonate by the phosphomevalonate
CC kinase erg8 (AFUA_5G10680). The diphosphomevalonate decarboxylase mvd1
CC (AFUA_4G07130) then produces isopentenyl diphosphate. The isopentenyl-
CC diphosphate delta-isomerase idi1 (AFUA_6G11160) then catalyzes the 1,3-
CC allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to
CC its highly electrophilic allylic isomer, dimethylallyl diphosphate
CC (DMAPP). Finally the farnesyl diphosphate synthase erg20 (AFUA_5G02450)
CC catalyzes the sequential condensation of isopentenyl pyrophosphate with
CC dimethylallyl pyrophosphate, and then with the resultant
CC geranylpyrophosphate to the ultimate product farnesyl pyrophosphate
CC (PubMed:16110826, PubMed:22106303) (Probable).
CC {ECO:0000250|UniProtKB:P15496, ECO:0000305|PubMed:16110826,
CC ECO:0000305|PubMed:22106303}.
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:0000305|PubMed:16110826};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23285;
CC Evidence={ECO:0000305|PubMed:16110826};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:16110826};
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:0000305|PubMed:16110826}.
CC -!- SIMILARITY: Belongs to the IPP isomerase type 1 family. {ECO:0000305}.
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DR EMBL; AAHF01000006; EAL88962.1; -; Genomic_DNA.
DR RefSeq; XP_751000.1; XM_745907.1.
DR STRING; 746128.CADAFUBP00007522; -.
DR EnsemblFungi; EAL88962; EAL88962; AFUA_6G11160.
DR GeneID; 3508305; -.
DR KEGG; afm:AFUA_6G11160; -.
DR VEuPathDB; FungiDB:Afu6g11160; -.
DR eggNOG; KOG0142; Eukaryota.
DR HOGENOM; CLU_060552_0_2_1; -.
DR InParanoid; Q4WM52; -.
DR OMA; DNGLTEH; -.
DR OrthoDB; 1281908at2759; -.
DR UniPathway; UPA00059; UER00104.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IBA:GO_Central.
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:0045337; P:farnesyl diphosphate biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0009240; P:isopentenyl diphosphate biosynthetic process; IBA:GO_Central.
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 SUPFAM; SSF55811; SSF55811; 1.
DR TIGRFAMs; TIGR02150; IPP_isom_1; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 3: Inferred from homology;
KW Isomerase; Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Metal-binding; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism.
FT CHAIN 1..279
FT /note="Isopentenyl-diphosphate delta-isomerase idi1"
FT /id="PRO_0000454155"
FT DOMAIN 91..249
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 129..162
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT ACT_SITE 128
FT /evidence="ECO:0000250|UniProtKB:P15496"
FT ACT_SITE 193
FT /evidence="ECO:0000250|UniProtKB:P15496"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13907"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q46822"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q46822"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13907"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13907"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13907"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q46822"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q46822"
SQ SEQUENCE 279 AA; 31591 MW; E69F91B02929A6E5 CRC64;
MTSTATVTVP PRITAENVAT LFPEVDTSLA REVFPSTVEG SAKDSEELAG YDEEQVRLMD
EVCIVLDDDD KPIGSASKKA CHLMTNIDRG LLHRAFSVFL FDSNNRLLLQ QRASEKITFP
DMWTNTCCSH PLGIPGETGA ELDAAVLGVK RAAQRKLDQE LGIKAEQVPL EKFEFFTRIH
YKAPSDGKWG EHETVTDTQI LVDYILFIQA DVDLNVNPNE VRDTKYVSAQ ELKQMFTQPG
LKFTPWFKLI CNSMLFEWWS YLGTADLDKY KGEKEIRRM
