(data stored in ACNUC7421 zone)

SWISSPROT: IDI_RUEPO

ID   IDI_RUEPO               Reviewed;         180 AA.
AC   Q5LWT6;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 95.
DE   RecName: Full=Isopentenyl-diphosphate Delta-isomerase {ECO:0000255|HAMAP-Rule:MF_00202};
DE            Short=IPP isomerase {ECO:0000255|HAMAP-Rule:MF_00202};
DE            EC=5.3.3.2 {ECO:0000255|HAMAP-Rule:MF_00202};
DE   AltName: Full=IPP:DMAPP isomerase {ECO:0000255|HAMAP-Rule:MF_00202};
DE   AltName: Full=Isopentenyl pyrophosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00202};
GN   Name=idi {ECO:0000255|HAMAP-Rule:MF_00202}; OrderedLocusNames=SPO0131;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C.,
RA   Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A.,
RA   Rahe E., Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Catalyzes the 1,3-allylic rearrangement of the
CC       homoallylic substrate isopentenyl (IPP) to its highly
CC       electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_00202};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00202};
CC       Note=Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only
CC       when substrate is bound. {ECO:0000255|HAMAP-Rule:MF_00202};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00202};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00202};
CC   -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC       biosynthesis; dimethylallyl diphosphate from isopentenyl
CC       diphosphate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00202}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00202}.
CC   -!- SIMILARITY: Belongs to the IPP isomerase type 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00202}.
DR   EMBL; CP000031; AAV93459.1; -; Genomic_DNA.
DR   RefSeq; WP_011045902.1; NC_003911.12.
DR   SMR; Q5LWT6; -.
DR   STRING; 246200.SPO0131; -.
DR   EnsemblBacteria; AAV93459; AAV93459; SPO0131.
DR   KEGG; sil:SPO0131; -.
DR   eggNOG; ENOG4108ZEY; Bacteria.
DR   eggNOG; COG1443; LUCA.
DR   HOGENOM; HOG000274107; -.
DR   KO; K01823; -.
DR   OMA; LRLCPWF; -.
DR   OrthoDB; 1345242at2; -.
DR   BioCyc; RPOM246200:G1G48-134-MONOMER; -.
DR   UniPathway; UPA00059; UER00104.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; ISS:TIGR.
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; ISS:TIGR.
DR   CDD; cd02885; IPP_Isomerase; 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   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   3: Inferred from homology;
DR   PRODOM; Q5LWT6.
DR   SWISS-2DPAGE; Q5LWT6.
KW   Complete proteome; Cytoplasm; Isomerase; Isoprene biosynthesis;
KW   Magnesium; Manganese; Metal-binding; Reference proteome.
FT   CHAIN         1    180       Isopentenyl-diphosphate Delta-isomerase.
FT                                /FTId=PRO_0000205267.
FT   DOMAIN       26    160       Nudix hydrolase.
FT   ACT_SITE     62     62       {ECO:0000255|HAMAP-Rule:MF_00202}.
FT   ACT_SITE    110    110       {ECO:0000255|HAMAP-Rule:MF_00202}.
FT   METAL        22     22       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00202}.
FT   METAL        28     28       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00202}.
FT   METAL        62     62       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00202}.
FT   METAL        64     64       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00202}.
FT   METAL        82     82       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00202}.
FT   METAL       108    108       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00202}.
FT   METAL       110    110       Manganese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00202}.
SQ   SEQUENCE   180 AA;  20680 MW;  F057E6F147CF8145 CRC64;
     MGILIPAWVD DRLVPVDKLE AHEKGLKHKA VSVFAVRDMD ILIQRRALGK YHTPGLWANT
     CCTHPDWDES ASTCAVRRLR EELGITGLYP EYRHRLEYHA DVGNGMVENE VVDVFLAHVR
     GPLQVVPNPD EVMEIRWIGY HDLLAEVQRY PERFTPWLKI YLHHHADTIF GPDLIISAKA
//

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