位置:首页 > 蛋白库 > IDI2_LEGPL
IDI2_LEGPL
ID   IDI2_LEGPL              Reviewed;         342 AA.
AC   Q5WUY8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Isopentenyl-diphosphate delta-isomerase {ECO:0000255|HAMAP-Rule:MF_00354};
DE            Short=IPP isomerase {ECO:0000255|HAMAP-Rule:MF_00354};
DE            EC=5.3.3.2 {ECO:0000255|HAMAP-Rule:MF_00354};
DE   AltName: Full=Isopentenyl diphosphate:dimethylallyl diphosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00354};
DE   AltName: Full=Isopentenyl pyrophosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00354};
DE   AltName: Full=Type 2 isopentenyl diphosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00354};
DE            Short=IDI-2 {ECO:0000255|HAMAP-Rule:MF_00354};
GN   Name=fni {ECO:0000255|HAMAP-Rule:MF_00354}; OrderedLocusNames=lpl2029;
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lens;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
CC   -!- FUNCTION: Involved in the biosynthesis of isoprenoids. Catalyzes the
CC       1,3-allylic rearrangement of the homoallylic substrate isopentenyl
CC       (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
CC       {ECO:0000255|HAMAP-Rule:MF_00354}.
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_00354};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00354};
CC   -!- COFACTOR:
CC       Name=NADPH; Xref=ChEBI:CHEBI:57783;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00354};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00354};
CC   -!- SUBUNIT: Homooctamer. Dimer of tetramers. {ECO:0000255|HAMAP-
CC       Rule:MF_00354}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00354}.
CC   -!- SIMILARITY: Belongs to the IPP isomerase type 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00354}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR628337; CAH16269.1; -; Genomic_DNA.
DR   RefSeq; WP_011216009.1; NC_006369.1.
DR   AlphaFoldDB; Q5WUY8; -.
DR   SMR; Q5WUY8; -.
DR   EnsemblBacteria; CAH16269; CAH16269; lpl2029.
DR   KEGG; lpf:lpl2029; -.
DR   LegioList; lpl2029; -.
DR   HOGENOM; CLU_065515_1_0_6; -.
DR   OMA; WDWGIPT; -.
DR   Proteomes; UP000002517; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070402; F:NADPH binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02811; IDI-2_FMN; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00354; Idi_2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000262; FMN-dep_DH.
DR   InterPro; IPR011179; IPdP_isomerase.
DR   PANTHER; PTHR43665; PTHR43665; 1.
DR   Pfam; PF01070; FMN_dh; 1.
DR   PIRSF; PIRSF003314; IPP_isomerase; 1.
DR   TIGRFAMs; TIGR02151; IPP_isom_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Flavoprotein; FMN; Isomerase; Isoprene biosynthesis; Magnesium;
KW   Metal-binding; NADP.
FT   CHAIN           1..342
FT                   /note="Isopentenyl-diphosphate delta-isomerase"
FT                   /id="PRO_1000048444"
FT   BINDING         11..12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         68
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         69..71
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         99..101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         99
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         128
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         163
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         194
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         219
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         224
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         275..277
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
FT   BINDING         296..297
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00354"
SQ   SEQUENCE   342 AA;  37964 MW;  115867C91A1D6CFB CRC64;
     MQNEYSQFEQ RKRDHIELAL MPANQSSELN PFDHFSLVHE ALPDLDFKDI SIQSIRFNKP
     VEKPFIISSM TAGHSNAIEI NYRLMEACSK TKWAMGVGSQ RRELTDKQAA FEWEPLRRDF
     PMVSLFSNLG IAQLIDTPIS AIQRLIDTLH AEALIIHCNP LQECIQPEGT TNFHGCWAAL
     EALVKKINSP VIVKETGCGF SKNTLLRLNN IGVAAVDVSG VGGTHWGRIE GHRADKDPIR
     HRTADTFRNW GIDTLQSTHN AISLNPSFEI WGSGGVRNGL DAAKLFALGA TTVGFAKPML
     EAALDSTDQV LTQMNTIEYE LKTAMFCTGS LVLDDLKEKA CP
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024