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1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXP reductoisomerase) (EC 1.1.1.267) (1-deoxyxylulose-5-phosphate reductoisomerase) (2-C-methyl-D-erythritol 4-phosphate synthase)

 A0A0S2ML80_BIFLN        Unreviewed;       396 AA.
A0A0S2ML80;
17-FEB-2016, integrated into UniProtKB/TrEMBL.
17-FEB-2016, sequence version 1.
20-DEC-2017, entry version 18.
RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00183, ECO:0000256|SAAS:SAAS00671201};
Short=DXP reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00183};
EC=1.1.1.267 {ECO:0000256|HAMAP-Rule:MF_00183, ECO:0000256|SAAS:SAAS00671193};
AltName: Full=1-deoxyxylulose-5-phosphate reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00183};
AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00183};
Name=dxr {ECO:0000256|HAMAP-Rule:MF_00183};
ORFNames=BBL306_1886 {ECO:0000313|EMBL:ALO75415.1};
Bifidobacterium longum subsp. longum.
Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
Bifidobacterium.
NCBI_TaxID=1679 {ECO:0000313|EMBL:ALO75415.1, ECO:0000313|Proteomes:UP000065375};
[1] {ECO:0000313|EMBL:ALO75415.1, ECO:0000313|Proteomes:UP000065375}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CCUG30698 {ECO:0000313|EMBL:ALO75415.1,
ECO:0000313|Proteomes:UP000065375};
PubMed=26489930; DOI=10.1186/s12864-015-1968-4;
O'Callaghan A., Bottacini F., O'Connell Motherway M., van Sinderen D.;
"Pangenome analysis of Bifidobacterium longum and site-directed
mutagenesis through by-pass of restriction-modification systems.";
BMC Genomics 16:832-832(2015).
-!- FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction
of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol
4-phosphate (MEP). {ECO:0000256|HAMAP-Rule:MF_00183,
ECO:0000256|SAAS:SAAS00671194}.
-!- CATALYTIC ACTIVITY: 2-C-methyl-D-erythritol 4-phosphate + NADP(+)
= 1-deoxy-D-xylulose 5-phosphate + NADPH. {ECO:0000256|HAMAP-
Rule:MF_00183, ECO:0000256|SAAS:SAAS00671198}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000256|HAMAP-Rule:MF_00183,
ECO:0000256|SAAS:SAAS00671195};
-!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
deoxy-D-xylulose 5-phosphate: step 1/6. {ECO:0000256|HAMAP-
Rule:MF_00183, ECO:0000256|SAAS:SAAS00671200}.
-!- SIMILARITY: Belongs to the DXR family. {ECO:0000256|HAMAP-
Rule:MF_00183, ECO:0000256|SAAS:SAAS00671197}.
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EMBL; CP011965; ALO75415.1; -; Genomic_DNA.
RefSeq; WP_007053294.1; NZ_MLZK01000013.1.
SMR; A0A0S2ML80; -.
EnsemblBacteria; ALO75415; ALO75415; BBL306_1886.
PATRIC; fig|1679.10.peg.2063; -.
UniPathway; UPA00056; UER00092.
Proteomes; UP000065375; Chromosome.
GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-UniRule.
GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070402; F:NADPH binding; IEA:InterPro.
GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
HAMAP; MF_00183; DXP_reductoisom; 1.
InterPro; IPR003821; DXP_reductoisomerase.
InterPro; IPR013644; DXP_reductoisomerase_C.
InterPro; IPR013512; DXP_reductoisomerase_N.
InterPro; IPR026877; DXPR_C.
InterPro; IPR036169; DXPR_C_sf.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR30525; PTHR30525; 1.
Pfam; PF08436; DXP_redisom_C; 1.
Pfam; PF02670; DXP_reductoisom; 1.
Pfam; PF13288; DXPR_C; 1.
PIRSF; PIRSF006205; Dxp_reductismrs; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF69055; SSF69055; 1.
TIGRFAMs; TIGR00243; Dxr; 1.
3: Inferred from homology;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000065375};
Isomerase {ECO:0000313|EMBL:ALO75415.1};
Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00183,
ECO:0000256|SAAS:SAAS00671199};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00183,
ECO:0000256|SAAS:SAAS00671202};
NADP {ECO:0000256|HAMAP-Rule:MF_00183, ECO:0000256|SAAS:SAAS00671204};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00183,
ECO:0000256|SAAS:SAAS00671203}.
NP_BIND 12 41 NADP. {ECO:0000256|HAMAP-Rule:MF_00183}.
COILED 375 395 {ECO:0000256|SAM:Coils}.
METAL 155 155 Divalent metal cation.
{ECO:0000256|HAMAP-Rule:MF_00183}.
METAL 157 157 Divalent metal cation.
{ECO:0000256|HAMAP-Rule:MF_00183}.
METAL 226 226 Divalent metal cation.
{ECO:0000256|HAMAP-Rule:MF_00183}.
BINDING 131 131 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00183}.
BINDING 157 157 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00183}.
BINDING 181 181 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00183}.
BINDING 204 204 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00183}.
BINDING 226 226 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00183}.
SEQUENCE 396 AA; 42014 MW; 3211E2783BB0C95A CRC64;
MSIASNSTVI ILGSTGSIGT QGLDVISRHP ERFTVTGLAA GGAHIELLAQ QAAQFHVSEV
AVFDETKVPA LQAALAQAGA QGVRVTGGPD SVIAMAGSGA NVVLNGITGS IGLEPSIAAL
KAGSQLALAN KESVVAGGHL LFSAQVRENQ INPVDSEHSA IWQSLRSGTH AEVAKLVVTA
SGGPFRGWKR ADMENITPEQ ALHHPTWNMG PVVTINSSTL MNKGLEVIEA SRLFNVPPER
IDVTVHPQSI VHSMVEFVDG ATICQASPPD MRLPIALGLS APDRMTNVAA ACDWTQAATW
TFEPLDDEAF PAVQLARHCL AASEKHTAVL NAANEQAVHA FLEHRLPYLG IVDTVKAVLD
QMDAELRGNP LFTDVEEMNQ LELEARRRAD DLINKQ


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