(data stored in ACNUC7421 zone)

SWISSPROT: DXR_DESOH

ID   DXR_DESOH               Reviewed;         383 AA.
AC   A8ZTM6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   11-DEC-2019, entry version 73.
DE   RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183};
DE            Short=DXP reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183};
DE            EC=1.1.1.267 {ECO:0000255|HAMAP-Rule:MF_00183};
DE   AltName: Full=1-deoxyxylulose-5-phosphate reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183};
DE   AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00183};
GN   Name=dxr {ECO:0000255|HAMAP-Rule:MF_00183}; OrderedLocusNames=Dole_0480;
OS   Desulfococcus oleovorans (strain DSM 6200 / Hxd3).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfococcus.
OX   NCBI_TaxID=96561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6200 / Hxd3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA   Richardson P.;
RT   "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of
CC       1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-
CC       phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00183}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-
CC         xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792,
CC         ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00183};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00183};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 1/6. {ECO:0000255|HAMAP-Rule:MF_00183}.
CC   -!- SIMILARITY: Belongs to the DXR family. {ECO:0000255|HAMAP-
CC       Rule:MF_00183}.
DR   EMBL; CP000859; ABW66290.1; -; Genomic_DNA.
DR   RefSeq; WP_012173909.1; NC_009943.1.
DR   SMR; A8ZTM6; -.
DR   STRING; 96561.Dole_0480; -.
DR   EnsemblBacteria; ABW66290; ABW66290; Dole_0480.
DR   KEGG; dol:Dole_0480; -.
DR   eggNOG; ENOG4105CEA; Bacteria.
DR   eggNOG; COG0743; LUCA.
DR   HOGENOM; HOG000007221; -.
DR   KO; K00099; -.
DR   OMA; AANEECV; -.
DR   OrthoDB; 1200722at2; -.
DR   BioCyc; DOLE96561:G1GAC-494-MONOMER; -.
DR   UniPathway; UPA00056; UER00092.
DR   Proteomes; UP000008561; Chromosome.
DR   GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070402; F:NADPH binding; IEA:InterPro.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00183; DXP_reductoisom; 1.
DR   InterPro; IPR003821; DXP_reductoisomerase.
DR   InterPro; IPR013644; DXP_reductoisomerase_C.
DR   InterPro; IPR013512; DXP_reductoisomerase_N.
DR   InterPro; IPR026877; DXPR_C.
DR   InterPro; IPR036169; DXPR_C_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR30525; PTHR30525; 1.
DR   Pfam; PF08436; DXP_redisom_C; 1.
DR   Pfam; PF02670; DXP_reductoisom; 1.
DR   Pfam; PF13288; DXPR_C; 1.
DR   PIRSF; PIRSF006205; Dxp_reductismrs; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF69055; SSF69055; 1.
DR   TIGRFAMs; TIGR00243; Dxr; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8ZTM6.
DR   SWISS-2DPAGE; A8ZTM6.
KW   Isoprene biosynthesis; Metal-binding; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..383
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT                   /id="PRO_1000098492"
FT   NP_BIND         7..36
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   METAL           149
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   METAL           151
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   METAL           220
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         124
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         151
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         175
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         198
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         220
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
SQ   SEQUENCE   383 AA;  40863 MW;  32156A39AD999190 CRC64;
     MKRLTLLGST GSIGVNTLKV VSRFCDRFSV EALCARGSVD TLAEQVQRFS PSLAVVIDAP
     TAQALKERLP AGSRTEVLFG EAGYCHAVSL PGVDMVVSAM VGAAGLGPTI AAIKAGKAVA
     LANKEVLVMA GETVMALAAQ KGVPLLPIDS EHSAIFQCLQ GNDKTFLSKI HLTASGGPFL
     NKTRQEIETA TPEQALAHPT WTMGKKISID SATLMNKGLE VIEARFLFDV PADCIEVVVH
     PQSIIHSMVS YIDGSMMAQL SVPDMKGAIA YALSYPERLD LNQPAPDLAA LEQLTFFSPD
     LDRFPCLGLA FEACRRKKTF PAVLNAANEV AVDAFLREAI PFGRIPRVIE QVLAEHTGVT
     DPSLSDIKDA DAWARQRAGA LLP
//

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