(data stored in ACNUC9435 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   11-DEC-2019, entry version 97.
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) (Silicibacter
OS   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., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   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 homoallylic
CC       substrate isopentenyl (IPP) to its highly electrophilic allylic isomer,
CC       dimethylallyl diphosphate (DMAPP). {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 when
CC       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-Rule:MF_00202};
CC   -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC       biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate:
CC       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; DNGLTEH; -.
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   Cytoplasm; Isomerase; Isoprene biosynthesis; Magnesium; Manganese;
KW   Metal-binding; Reference proteome.
FT   CHAIN           1..180
FT                   /note="Isopentenyl-diphosphate Delta-isomerase"
FT                   /id="PRO_0000205267"
FT   DOMAIN          26..160
FT                   /note="Nudix hydrolase"
FT   ACT_SITE        62
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   ACT_SITE        110
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   METAL           22
FT                   /note="Manganese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   METAL           28
FT                   /note="Manganese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   METAL           62
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   METAL           64
FT                   /note="Manganese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   METAL           82
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   METAL           108
FT                   /note="Manganese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00202"
FT   METAL           110
FT                   /note="Manganese"
FT                   /evidence="ECO:0000255|HAMAP-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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