(data stored in ACNUC7421 zone)

SWISSPROT: B7UIL8_ECO27

ID   B7UIL8_ECO27            Unreviewed;       398 AA.
AC   B7UIL8;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-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:CAS07726.1};
GN   OrderedLocusNames=E2348C_0178 {ECO:0000313|EMBL:CAS07726.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07726.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07726.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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; FM180568; CAS07726.1; -; Genomic_DNA.
DR   RefSeq; WP_000811915.1; NC_011601.1.
DR   EnsemblBacteria; CAS07726; CAS07726; E2348C_0178.
DR   KEGG; ecg:E2348C_0178; -.
DR   HOGENOM; HOG000007221; -.
DR   KO; K00099; -.
DR   OMA; AHPNWVM; -.
DR   BioCyc; ECOL574521:E2348C_RS00920-MONOMER; -.
DR   UniPathway; UPA00056; UER00092.
DR   Proteomes; UP000008205; 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; B7UIL8.
DR   SWISS-2DPAGE; B7UIL8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Isomerase {ECO:0000313|EMBL:CAS07726.1};
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;  43386 MW;  031413CE900AEF6D CRC64;
     MKQLTILGST GSIGCSTLDV VRHNPEHFRV VALVAGKNVT RMVEQCLEFS PRYAVMDDEA
     SAKLLKTILQ QQGSRTEVLS GQQAACDMAA LEDVDQVMAA IVGAAGLLPT LAAIRAGKTI
     LLANKESLVT CGRLFMDAVK QSKAQLLPVD SEHNAIFQSL PQPIQHNLGY ADLEQNGVVS
     ILLTGSGGPF RETPLRDLAT MTPDQACRHP NWSMGRKISV DSATMMNKGL EYIEARWLFN
     ACASQMEVLI HPQSVIHSMV RYQDGSVLAQ LGEPDMRTPI AHTMAWPNRV NSGVKPLDFC
     KLSALTFAAP DYDRYPCLKL AMEAFEQGQA ATTALNAANE ITVAAFLAQQ IRFTDIAALN
     LSVLEKMDMR EPQCVDDVLS VDANAREVAR KEVMRLAS
//

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