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Database: UniProt
Entry: A0A2A3JV81_9RHOB
LinkDB: A0A2A3JV81_9RHOB
Original site: A0A2A3JV81_9RHOB 
ID   A0A2A3JV81_9RHOB        Unreviewed;       389 AA.
AC   A0A2A3JV81;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00183};
DE            Short=DXP reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00183};
DE            EC=1.1.1.267 {ECO:0000256|HAMAP-Rule:MF_00183};
DE   AltName: Full=1-deoxyxylulose-5-phosphate reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00183};
DE   AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00183};
GN   Name=dxr {ECO:0000256|HAMAP-Rule:MF_00183};
GN   ORFNames=CLG85_11535 {ECO:0000313|EMBL:PBD19018.1};
OS   Alloyangia mangrovi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Alloyangia.
OX   NCBI_TaxID=1779329 {ECO:0000313|EMBL:PBD19018.1, ECO:0000313|Proteomes:UP000217448};
RN   [1] {ECO:0000313|EMBL:PBD19018.1, ECO:0000313|Proteomes:UP000217448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAOS 153D {ECO:0000313|EMBL:PBD19018.1,
RC   ECO:0000313|Proteomes:UP000217448};
RA   Verma A., Krishnamurthi S.;
RT   "Yangia sp. SAOS 153D whole genome sequencing.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent rearrangement and reduction of
CC       1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-
CC       phosphate (MEP). {ECO:0000256|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: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|HAMAP-Rule:MF_00183};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|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:0000256|ARBA:ARBA00005094, ECO:0000256|HAMAP-
CC       Rule:MF_00183}.
CC   -!- SIMILARITY: Belongs to the DXR family. {ECO:0000256|ARBA:ARBA00006825,
CC       ECO:0000256|HAMAP-Rule:MF_00183}.
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:PBD19018.1}.
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DR   EMBL; NTHN01000170; PBD19018.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3JV81; -.
DR   OrthoDB; 9806546at2; -.
DR   UniPathway; UPA00056; UER00092.
DR   Proteomes; UP000217448; Unassembled WGS sequence.
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   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   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00243; Dxr; 1.
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   PIRSF; PIRSF006205; Dxp_reductismrs; 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.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP-
KW   Rule:MF_00183}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00183};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00183};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00183};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00183};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00183}.
FT   DOMAIN          4..129
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02670"
FT   DOMAIN          143..226
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08436"
FT   DOMAIN          258..379
FT                   /note="DXP reductoisomerase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13288"
FT   BINDING         10
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         11
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         12
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         13
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         36
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         37
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         38
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         121
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         122
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         123
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         147
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         148
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         149
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         149
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         173
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         196
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         202
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         209
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         214
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         215
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         218
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         218
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
SQ   SEQUENCE   389 AA;  41565 MW;  E66C77E729CB899E CRC64;
     MRRISIFGAT GSIGQNTLDL IARDPESYHV VALTGGKNVA QLAKDARKFG AELAVTADPA
     LLPELRARLA GSSVEAAAGP EAIIEAASRQ ADWVMSAIVG AAGLAPGLRA LEMGATLALA
     NKESMVCAGP LVLHTAQTHG GRVLPVDSEH SAVFQALIGE EMSRVERVII TASGGAFRDW
     PIEKLAEATP EQAATHPNWD MGQRITIDSA SMFNKALEVI ETKEFFDLNP AKIEVVVHPE
     SMIHALVGFC DGALMAHLGP PDMRHAIGFA LNHPQRGALP VERLDLVKLS QLTFRPACET
     RWPALRLARE VMAAGGLSGA VFNAAKEQAL DDFIGNRIGF QDMAGLVEQT LERLSAESAV
     TSAEITLDNV LAADHLARRT ARELMLQYH
//
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