ID   A0A7R7TN08_THETH        Unreviewed;       367 AA.
AC   A0A7R7TN08;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   29-SEP-2021, entry version 2.
DE   RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00183};
DE            Short=DXP reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00183};
DE            EC=1.1.1.267 {ECO:0000256|HAMAP-Rule:MF_00183};
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:BCQ00098.1};
GN   ORFNames=TthHB5002_08700 {ECO:0000313|EMBL:BCP97767.1},
GN   TthHB5008_08680 {ECO:0000313|EMBL:BCQ00098.1};
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274 {ECO:0000313|EMBL:BCQ00098.1};
RN   [1] {ECO:0000313|EMBL:BCQ00098.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HB5002 {ECO:0000313|EMBL:BCP97767.1}, and HB5008
RC   {ECO:0000313|EMBL:BCQ00098.1};
RA   Miyazaki K., Moriya T., Oshima T., Yura K., Bessho Y.;
RT   "Complete genome sequences of twin Thermus thermophilus strains HB5002 and
RT   HB5008 isolated from Mine Onsen hot spring in Japan.";
RL   Submitted (JAN-2021) 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:0000256|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:0000256|ARBA:ARBA00000539, ECO:0000256|HAMAP-
CC         Rule:MF_00183};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|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:0000256|ARBA:ARBA00005094, ECO:0000256|HAMAP-
CC       Rule:MF_00183}.
CC   -!- SIMILARITY: Belongs to the DXR family. {ECO:0000256|ARBA:ARBA00006825,
CC       ECO:0000256|HAMAP-Rule:MF_00183}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00183}.
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DR   EMBL; AP024301; BCP97767.1; -; Genomic_DNA.
DR   EMBL; AP024305; BCQ00098.1; -; Genomic_DNA.
DR   UniPathway; UPA00056; UER00092.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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   Isomerase {ECO:0000313|EMBL:BCQ00098.1};
KW   Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP-
KW   Rule:MF_00183};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00183};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00183};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00183}.
FT   DOMAIN          4..120
FT                   /note="DXP_reductoisom"
FT                   /evidence="ECO:0000259|Pfam:PF02670"
FT   DOMAIN          134..216
FT                   /note="DXP_redisom_C"
FT                   /evidence="ECO:0000259|Pfam:PF08436"
FT   DOMAIN          248..361
FT                   /note="DXPR_C"
FT                   /evidence="ECO:0000259|Pfam:PF13288"
FT   METAL           138
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   METAL           140
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   METAL           208
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         113
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         140
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         164
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         186
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         208
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
SQ   SEQUENCE   367 AA;  40162 MW;  A8F89A83EA9290D6 CRC64;
     MKRVVVLGST GSIGQQALEV CRLRGYEVVG LAAGKNLEAL SRQIALWKPR LVAAEESLHK
     ELKARFPGLR LATAEEVAAL EAEVAVAAIP GLAGLAPTRM AVRTGKRVAL ANKEAMVAAG
     PLLWREAEAH GAEILPVDSE HSALFQALLG ERREDVAELI LTASGGPFLR EPEDLAQVTP
     EMALRHPRWR MGPKVTVDSA TLFNKGLEVL EAKELFRFPL ERIKVLIHPQ AYVHGLVRFV
     DGSLKAQLGP TDMRLFIQYA LTYPERAETP LKDLPIPGVL EFLEPDLKRF PALALAYEAG
     RRGGLAQVAV SAADEVAVEA FLQGKIPFPR IPEILARVLE ATPIEPLTWE SLFAVDAWAR
     EEAKRWA
//