ID DXR_THERP Reviewed; 385 AA.
AC B9L006;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 02-NOV-2016, entry version 52.
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};
GN OrderedLocusNames=trd_1005;
OS Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC Bacteria; Chloroflexi; Thermomicrobiales; Thermomicrobiaceae;
OC Thermomicrobium.
OX NCBI_TaxID=309801;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27502 / DSM 5159 / P-2;
RX PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E.,
RA Bryant D.A., Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R.,
RA Ward N.L., Eisen J.A.;
RT "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT Thermomicrobium roseum.";
RL PLoS ONE 4:E4207-E4207(2009).
CC -!- FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction
CC of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol
CC 4-phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00183}.
CC -!- CATALYTIC ACTIVITY: 2-C-methyl-D-erythritol 4-phosphate + NADP(+)
CC = 1-deoxy-D-xylulose 5-phosphate + NADPH. {ECO:0000255|HAMAP-
CC 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
CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC deoxy-D-xylulose 5-phosphate: step 1/6. {ECO:0000255|HAMAP-
CC Rule:MF_00183}.
CC -!- SIMILARITY: Belongs to the DXR family. {ECO:0000255|HAMAP-
CC Rule:MF_00183}.
DR EMBL; CP001275; ACM06158.1; -; Genomic_DNA.
DR RefSeq; WP_015921966.1; NC_011959.1.
DR STRING; 309801.trd_1005; -.
DR PRIDE; B9L006; -.
DR EnsemblBacteria; ACM06158; ACM06158; trd_1005.
DR KEGG; tro:trd_1005; -.
DR PATRIC; 23913182; VBITheRos91376_0948.
DR eggNOG; ENOG4105CEA; Bacteria.
DR eggNOG; COG0743; LUCA.
DR HOGENOM; HOG000007220; -.
DR KO; K00099; -.
DR OMA; GFCPLSE; -.
DR OrthoDB; POG091H0052; -.
DR UniPathway; UPA00056; UER00092.
DR Proteomes; UP000000447; Chromosome.
DR GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
DR Gene3D; 3.40.50.720; -; 1.
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; IPR016040; NAD(P)-bd_dom.
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 Complete proteome; Isoprene biosynthesis; Metal-binding; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1 385 1-deoxy-D-xylulose 5-phosphate
FT reductoisomerase.
FT /FTId=PRO_1000124115.
FT NP_BIND 8 37 NADP. {ECO:0000255|HAMAP-Rule:MF_00183}.
FT METAL 143 143 Divalent metal cation.
FT {ECO:0000255|HAMAP-Rule:MF_00183}.
FT METAL 145 145 Divalent metal cation.
FT {ECO:0000255|HAMAP-Rule:MF_00183}.
FT METAL 215 215 Divalent metal cation.
FT {ECO:0000255|HAMAP-Rule:MF_00183}.
FT BINDING 118 118 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_00183}.
FT BINDING 145 145 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_00183}.
FT BINDING 170 170 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_00183}.
FT BINDING 193 193 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_00183}.
FT BINDING 215 215 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_00183}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 5 377 ihamap:DXP_reductoisom [T]
FT MYHIT 5 125 ipfam:DXP_reductoisom [T]
FT MYHIT 140 223 ipfam:DXP_redisom_C [T]
FT MYHIT 257 372 ipfam:DXPR_C [T]
SQ SEQUENCE 385 AA; 41645 MW; C2DA84EDA86A7CC3 CRC64;
MRLGVSLLGS TGSIGRQTLE VVAAHPDRFR VVALAARSQI DALQEQVRIF RPELVAIAQE
SLGISFPDTR VVSGPGGLVE AATYETADIV VIALSGNSGI EPTLAAAAAG KTIALANKES
VVCAGPLLRD IQSRTGCQVR PVDSEHSALW QLLQLPHRPA EIARVILTAS GGPFRDRPLE
HLNQVTPDEA LAHPTWRMGP KITIDSATLL NKGLELIEAH WLFDLPFERL DVVIHPQSIV
HALLAFVDGT TVAHAAYPDM RLPIQYALFY PERVASTVPP LDLARIGPLE FFPPDTERFP
ALPLAREVGI AGSTYPTVLC AADEIAVEAF LAGQIRFTEI VPLIRSVLDR HQPASEPLTL
EAILAADRWA RSVARELVGR AIRHA
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