ID V6L4F1_9ACTN Unreviewed; 307 AA.
AC V6L4F1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=1-deoxy-D-xylulose-5-phosphate reductoisomerase {ECO:0000256|ARBA:ARBA00012366};
DE EC=1.1.1.267 {ECO:0000256|ARBA:ARBA00012366};
DE Flags: Fragment;
GN ORFNames=N566_03675 {ECO:0000313|EMBL:EST39128.1};
OS Streptomycetaceae bacterium MP113-05.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae.
OX NCBI_TaxID=1380770 {ECO:0000313|EMBL:EST39128.1, ECO:0000313|Proteomes:UP000017915};
RN [1] {ECO:0000313|EMBL:EST39128.1, ECO:0000313|Proteomes:UP000017915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP113-05 {ECO:0000313|EMBL:EST39128.1,
RC ECO:0000313|Proteomes:UP000017915};
RA Valde M., Degnes K.F., Sletta H., Ruckert C., Kalinowski J., Zotchev S.B.;
RT "Streptomyces bacterium from a marine sponge: physiological
RT characterization and genome-based analysis of secondary metabolite
RT biosynthesis potential.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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:ARBA00034272};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13719;
CC Evidence={ECO:0000256|ARBA:ARBA00034272};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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}.
CC -!- SIMILARITY: Belongs to the DXR family. {ECO:0000256|ARBA:ARBA00006825}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EST39128.1}.
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DR EMBL; AWQV01000125; EST39128.1; -; Genomic_DNA.
DR AlphaFoldDB; V6L4F1; -.
DR STRING; 1380770.N566_03675; -.
DR PATRIC; fig|1380770.3.peg.623; -.
DR HOGENOM; CLU_766186_0_0_11; -.
DR UniPathway; UPA00056; UER00092.
DR Proteomes; UP000017915; Unassembled WGS sequence.
DR GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-EC.
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 Gene3D; 1.10.1740.10; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR036169; DXPR_C_sf.
DR PANTHER; PTHR30525; 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE; 1.
DR PANTHER; PTHR30525:SF0; 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, CHLOROPLASTIC; 1.
DR Pfam; PF08436; DXP_redisom_C; 1.
DR Pfam; PF02670; DXP_reductoisom; 1.
DR Pfam; PF13288; DXPR_C; 1.
DR SUPFAM; SSF69055; 1-deoxy-D-xylulose-5-phosphate reductoisomerase, C-terminal domain; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000017915}.
FT DOMAIN 3..44
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02670"
FT DOMAIN 56..139
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08436"
FT DOMAIN 172..292
FT /note="DXP reductoisomerase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13288"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EST39128.1"
SQ SEQUENCE 307 AA; 32119 MW; A0E611C4D2DD28F2 CRC64;
LAASECHTVL NGITGSIGLA PTLAALKAGR VLALANKESL IVGGPLVKAL ARPGQIIPVD
SEHSALFQAL MGGARREVRK LLVTASGGPF RGRSRAELAD VTPKDALAHP TWAMGPVITV
NSATLVNKGL EVIEAHLLYD IPFDRIQVVV HPQSAVHSMV EFTDGSTLAQ CGPPDMRLPI
ALGIGWPERV PDAGPVFDWT KPMSWDFLPL DTDAFPSVPL ACHVGALGGT APAVYNAANE
ECVEAFLADR LPFTGIADTV ASVVEEHTGA GPSGGTDLTL NGVLEAESWA RTRARELAAR
AVVEARA
//
