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DXR_BURCM
ID   DXR_BURCM               Reviewed;         398 AA.
AC   Q0BE21;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=Bamb_2046;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) 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}.
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DR   EMBL; CP000440; ABI87602.1; -; Genomic_DNA.
DR   RefSeq; WP_011657283.1; NZ_CP009798.1.
DR   AlphaFoldDB; Q0BE21; -.
DR   SMR; Q0BE21; -.
DR   STRING; 339670.Bamb_2046; -.
DR   EnsemblBacteria; ABI87602; ABI87602; Bamb_2046.
DR   GeneID; 44692705; -.
DR   KEGG; bam:Bamb_2046; -.
DR   PATRIC; fig|339670.21.peg.2897; -.
DR   eggNOG; COG0743; Bacteria.
DR   OMA; PIDSEHF; -.
DR   UniPathway; UPA00056; UER00092.
DR   Proteomes; UP000000662; Chromosome 1.
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;
KW   Isoprene biosynthesis; Metal-binding; NADP; Oxidoreductase.
FT   CHAIN           1..398
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT                   /id="PRO_1000020225"
FT   BINDING         8..37
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         151
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         153
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         224
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
SQ   SEQUENCE   398 AA;  42199 MW;  6948AC58295C840E CRC64;
     MQKRLTLLGS TGSIGDSTLD VVARHPERFS VYALTAHRNG DKLVEQCLRF APEVAVVGDA
     NTAAHVEAKL RAAGSKTIVL YGPQALVDVS KSDGCDTVVA AIVGAAGLAP SLAAARAGKR
     ILLANKESLV MSGAIFMDAV RDHGAILLPV DSEHNAIFQC MPRDENEHGG ISKIILTASG
     GPFRTREPAT LADVTPDEAC KHPNWVMGRK ISVDSATMMN KGLEVIEAHW IFGLAGDRID
     VLIHPQSVIH SLVSYRDGSV LAQLGNPDMR TPIAHALAFP ERVDAGVDQL DLAQIVQLSF
     EKPDYTRFPC LALALKALEE GGIASAALNA ANEIAVEAFL ERRIGFMAIA ATVDAVLNAL
     PNRSPNGLDD VLAADAEARR LAAEIIAKAP APRVERTV
 
 
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