DXR_MYCPA
ID DXR_MYCPA Reviewed; 407 AA.
AC Q73VS1;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 104.
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=MAP_2940c;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS05257.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE016958; AAS05257.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_015632592.1; NC_002944.2.
DR AlphaFoldDB; Q73VS1; -.
DR SMR; Q73VS1; -.
DR STRING; 262316.MAP_2940c; -.
DR EnsemblBacteria; AAS05257; AAS05257; MAP_2940c.
DR KEGG; mpa:MAP_2940c; -.
DR eggNOG; COG0743; Bacteria.
DR HOGENOM; CLU_035714_4_0_11; -.
DR OMA; PIDSEHF; -.
DR UniPathway; UPA00056; UER00092.
DR Proteomes; UP000000580; 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;
KW Isoprene biosynthesis; Metal-binding; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..407
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT /id="PRO_0000163677"
FT BINDING 19..48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 152
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 154
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 223
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
SQ SEQUENCE 407 AA; 42315 MW; 7011EEF2B36EECA4 CRC64;
MTNPTSDGQP RGRLRVLVLG STGSIGTQAL QVIAANPDRF EVVGLAAGGA NLDTLLRQRA
ETGVTNVAVA DEHAARRAGD IPFCGPEAAT RLVEETEADV VLNALVGALG LRPTLAALES
GARLALANKE SLIAGGPLVL AAAAPGQIVP VDSEHSALAQ CLRGGTGDEV AKLVLTASGG
PFRGWTAEEL EHVTPEQAGA HPTWSMGPMN TLNSASLVNK GLELIETHLL FGIPYDRIEV
VVHPQSIVHS MVTFVDGSTL AQASPPDMRL PISLALGWPH RVPGAAACCD FSTASSWEFE
PLDNEVFPAV ELARHAGQAG GCMTAIYNAA NEEAAAAFLA GRVSFGAIVE TIADVLHAAD
QWAPKFSETP ANVDDVLDAQ RWARQRAQRA VAQARPATAS AKTPGVV
