(data stored in SCRATCH zone)

SWISSPROT: C8U1P1_ECO10

ID   C8U1P1_ECO10            Unreviewed;       398 AA.
AC   C8U1P1;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00183, ECO:0000256|SAAS:SAAS00313822};
DE            Short=DXP reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00183};
DE            EC=1.1.1.267 {ECO:0000256|HAMAP-Rule:MF_00183, ECO:0000256|SAAS:SAAS00340832};
DE   AltName: Full=1-deoxyxylulose-5-phosphate reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00183};
DE   AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00183};
GN   Name=dxr {ECO:0000256|HAMAP-Rule:MF_00183,
GN   ECO:0000313|EMBL:BAI29049.1};
GN   OrderedLocusNames=ECO103_0171 {ECO:0000313|EMBL:BAI29049.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29049.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29049.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction
CC       of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol
CC       4-phosphate (MEP). {ECO:0000256|HAMAP-Rule:MF_00183,
CC       ECO:0000256|SAAS:SAAS00327577}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-
CC         D-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:0000256|HAMAP-Rule:MF_00183,
CC         ECO:0000256|SAAS:SAAS01116073};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00183,
CC         ECO:0000256|SAAS:SAAS00320200};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC       biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC       deoxy-D-xylulose 5-phosphate: step 1/6. {ECO:0000256|HAMAP-
CC       Rule:MF_00183, ECO:0000256|SAAS:SAAS00313810}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00183}.
CC   -!- SIMILARITY: Belongs to the DXR family. {ECO:0000256|HAMAP-
CC       Rule:MF_00183, ECO:0000256|SAAS:SAAS00537059}.
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DR   EMBL; AP010958; BAI29049.1; -; Genomic_DNA.
DR   RefSeq; WP_000811923.1; NC_013353.1.
DR   SMR; C8U1P1; -.
DR   EnsemblBacteria; BAI29049; BAI29049; ECO103_0171.
DR   KEGG; eoh:ECO103_0171; -.
DR   HOGENOM; HOG000007221; -.
DR   KO; K00099; -.
DR   OMA; AHPNWVM; -.
DR   BioCyc; ECOL585395:ECO103_RS00875-MONOMER; -.
DR   UniPathway; UPA00056; UER00092.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; C8U1P1.
DR   SWISS-2DPAGE; C8U1P1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Isomerase {ECO:0000313|EMBL:BAI29049.1};
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00183,
KW   ECO:0000256|SAAS:SAAS00313821};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00183,
KW   ECO:0000256|SAAS:SAAS00313788};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00183, ECO:0000256|SAAS:SAAS00313814};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00183,
KW   ECO:0000256|SAAS:SAAS00313795}.
FT   DOMAIN        4    132       DXP_reductoisom. {ECO:0000259|Pfam:
FT                                PF02670}.
FT   DOMAIN      146    239       DXP_redisom_C. {ECO:0000259|Pfam:
FT                                PF08436}.
FT   DOMAIN      271    387       DXPR_C. {ECO:0000259|Pfam:PF13288}.
FT   NP_BIND       7     36       NADP. {ECO:0000256|HAMAP-Rule:MF_00183}.
FT   METAL       150    150       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00183}.
FT   METAL       152    152       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00183}.
FT   METAL       231    231       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00183}.
FT   BINDING     125    125       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00183}.
FT   BINDING     152    152       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00183}.
FT   BINDING     186    186       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00183}.
FT   BINDING     209    209       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00183}.
FT   BINDING     231    231       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00183}.
SQ   SEQUENCE   398 AA;  43388 MW;  8B532683A4FF1207 CRC64;
     MKQLTILGST GSIGCSTLDV VRHNPEHFRV VALVAGKNVT RMVEQCLEFS PRYAVMDDEA
     SAKLLKTMLQ QQGSRTEVLS GQQAACDMAA LEDVDQVMAA IVGAAGLLPT LAAIRAGKTI
     LLANKESLVT CGRLFMDAVK QSKAQLLPVD SEHNAIFQSL PQPIQHNLGY ADLEQNGVVS
     ILLTGSGGPF RETPLRDLAT MTPDQACRHP NWSMGRKISV DSATMMNKGL EYIEARWLFN
     ASASQMEVLI HPQSVIHSMV RYQDGSVLAQ LGEPDMRTPI AHTMAWPNRV NSGVKPLDFC
     KLSALTFAAP DYDRYPCLKL AMEAFEQGQA ATTALNAANE ITVAAFLAQQ IRFTDIAALN
     LSVLEKMDMR EPQCVDDVLS VDANAREVAR KEVMRLAS
//

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