DXR_CALS4
ID DXR_CALS4 Reviewed; 382 AA.
AC Q8RA28;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
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}; OrderedLocusNames=TTE1402;
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
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:0000255|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:0000255|HAMAP-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 biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 1/6. {ECO:0000255|HAMAP-Rule:MF_00183}.
CC -!- SIMILARITY: Belongs to the DXR family. {ECO:0000255|HAMAP-
CC Rule:MF_00183}.
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DR EMBL; AE008691; AAM24624.1; -; Genomic_DNA.
DR RefSeq; WP_009611039.1; NC_003869.1.
DR AlphaFoldDB; Q8RA28; -.
DR SMR; Q8RA28; -.
DR STRING; 273068.TTE1402; -.
DR EnsemblBacteria; AAM24624; AAM24624; TTE1402.
DR KEGG; tte:TTE1402; -.
DR eggNOG; COG0743; Bacteria.
DR HOGENOM; CLU_035714_4_0_9; -.
DR OMA; PIDSEHF; -.
DR OrthoDB; 1200722at2; -.
DR UniPathway; UPA00056; UER00092.
DR Proteomes; UP000000555; Chromosome.
DR GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-UniRule.
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-UniRule.
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 Isoprene biosynthesis; Metal-binding; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..382
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT /id="PRO_0000163722"
FT BINDING 7..36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 146
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 148
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 217
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
SQ SEQUENCE 382 AA; 42768 MW; A26FFBA608929038 CRC64;
MKKLIILGST GSIGRQTLDV VRSLKEEFEI VGLTGYNNVS LLSKQIKEFR PKVVAVKDEE
KARKLRENLD EPIEVLTGKE GLKEIVKYEA DMVVVAVEGI AGLIPTVEAI KLGKNIALAN
KEVLVTAGEI VMGLVKEKKI EFLPVDSEHS AILQCLKGNN KREVSNLILT ASGGPFRGKK
KKDLVNVTVE EALKHPNWKM GKKITIDSAT LMNKGFEVIE ARWLFDMPLD KIKVVIHPQS
IIHSMVEYVD GSVIAQLSVP DMRIAIQYAL NYPDRKYVEG VKFLDFYALG QLTFEEPDFE
TFKCLSLAYH AAECGGTMTA VLNAADEVAV SLFLQNKINF LEIAEIIEEA LENHKNIQNP
TLDDIISVDL ETRERIMRKY LR
