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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)

 B3U4U0_9BACT            Unreviewed;       386 AA.
B3U4U0;
02-SEP-2008, integrated into UniProtKB/TrEMBL.
02-SEP-2008, sequence version 1.
20-JUN-2018, entry version 69.
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,
ECO:0000313|EMBL:ACE75657.1};
ORFNames=NIDE1511 {ECO:0000313|EMBL:CBK41251.1};
Nitrospira defluvii.
Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Nitrospira.
NCBI_TaxID=330214 {ECO:0000313|EMBL:ACE75657.1};
[1] {ECO:0000313|EMBL:ACE75657.1}
NUCLEOTIDE SEQUENCE.
PubMed=18459973; DOI=10.1111/j.1462-2920.2008.01646.x;
Maixner F., Wagner M., Lucker S., Pelletier E., Schmitz-Esser S.,
Hace K., Spieck E., Konrat R., Le Paslier D., Daims H.;
"Environmental genomics reveals a functional chlorite dismutase in the
nitrite-oxidizing bacterium 'Candidatus Nitrospira defluvii'.";
Environ. Microbiol. 10:3043-3056(2008).
[2] {ECO:0000313|EMBL:CBK41251.1, ECO:0000313|Proteomes:UP000001660}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.1003860107;
Lucker S., Wagner M., Maixner F., Pelletier E., Koch H., Vacherie B.,
Rattei T., Sinninghe Damste J., Spieck E., Le Paslier D., Daims H.;
"A Nitrospira metagenome illuminates the physiology and evolution of
globally important nitrite-oxidizing bacteria.";
Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2010).
[3] {ECO:0000313|EMBL:CBK41251.1}
NUCLEOTIDE SEQUENCE.
Genoscope - CEA;
Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
-!- 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; EU559167; ACE75657.1; -; Genomic_DNA.
EMBL; FP929003; CBK41251.1; -; Genomic_DNA.
RefSeq; WP_013248075.1; NC_014355.1.
STRING; 330214.NIDE1511; -.
EnsemblBacteria; CBK41251; CBK41251; NIDE1511.
KEGG; nde:NIDE1511; -.
eggNOG; ENOG4105CEA; Bacteria.
eggNOG; COG0743; LUCA.
HOGENOM; HOG000007221; -.
KO; K00099; -.
OrthoDB; POG091H0052; -.
BioCyc; CNIT330214:NIDE_RS06980-MONOMER; -.
UniPathway; UPA00056; UER00092.
Proteomes; UP000001660; 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;
Complete proteome {ECO:0000313|Proteomes:UP000001660};
Isomerase {ECO:0000313|EMBL:ACE75657.1};
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, ECO:0000313|EMBL:ACE75657.1};
Reference proteome {ECO:0000313|Proteomes:UP000001660}.
DOMAIN 4 130 DXP_reductoisom.
{ECO:0000259|Pfam:PF02670}.
DOMAIN 144 227 DXP_redisom_C.
{ECO:0000259|Pfam:PF08436}.
DOMAIN 259 375 DXPR_C. {ECO:0000259|Pfam:PF13288}.
NP_BIND 7 36 NADP. {ECO:0000256|HAMAP-Rule:MF_00183}.
METAL 148 148 Divalent metal cation.
{ECO:0000256|HAMAP-Rule:MF_00183}.
METAL 150 150 Divalent metal cation.
{ECO:0000256|HAMAP-Rule:MF_00183}.
METAL 219 219 Divalent metal cation.
{ECO:0000256|HAMAP-Rule:MF_00183}.
BINDING 123 123 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00183}.
BINDING 150 150 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00183}.
BINDING 174 174 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00183}.
BINDING 197 197 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00183}.
BINDING 219 219 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00183}.
SEQUENCE 386 AA; 42368 MW; B00E1DD918731F92 CRC64;
MKNIVILGST GSIGTNTLDI VDRFPEEFHV VGLTAGSNDE KLEAQIRKFR PAFAALANEA
AAAKLRDRCA DLPVKILAGN EGVAEVAQSQ DAELVISAIV GGAGLLPTLA AIRAGKQIAL
ANKEPMVMAG ALMQAEAKKH HVRIFPIDSE HSAIFQSLEG HRREDVKRII LTASGGPLWG
FSREQLQDVS PERALQHPNW KMGSKITIDS ATLMNKGLEV IEARWLFDIP ETQIEVLVHR
ESIIHSLVEY TDRSVIAQLG LPDMRTPISY AMRYPERMPL DLPSLDLTEI STLTFFKPDH
ARFPCLQLGY EALRIGGTMP ATMNAANEVA VEAFLQSGIR FLDIPDIIRS TMEAHAPRPI
DGLDDALDAD HWARDKAESL VHALTR


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