ID DXR_ACIB3 Reviewed; 398 AA.
AC B7H1U5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
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=ABBFA_001475;
OS Acinetobacter baumannii (strain AB307-0294).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=557600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB307-0294;
RX PubMed=18931120; DOI=10.1128/jb.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT baumannii.";
RL J. Bacteriol. 190:8053-8064(2008).
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: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 PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13719;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00183};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00183};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
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; CP001172; ACJ57525.1; -; Genomic_DNA.
DR RefSeq; WP_000194643.1; NZ_CP001172.1.
DR PDB; 4ZN6; X-ray; 2.05 A; A/B=1-398.
DR PDB; 7S04; X-ray; 2.52 A; A=1-398.
DR PDBsum; 4ZN6; -.
DR PDBsum; 7S04; -.
DR AlphaFoldDB; B7H1U5; -.
DR SMR; B7H1U5; -.
DR HOGENOM; CLU_035714_4_0_6; -.
DR UniPathway; UPA00056; UER00092.
DR Proteomes; UP000006924; 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 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 1: Evidence at protein level;
KW 3D-structure; Isoprene biosynthesis; Manganese; Metal-binding; NADP;
KW Oxidoreductase.
FT CHAIN 1..398
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT /id="PRO_1000118488"
FT BINDING 11
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 12
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 13
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 14
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 125
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 126
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 127
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 151
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 152
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 153
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 153
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 186
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 209
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 215
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 222
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 227
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 228
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 231
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 231
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:4ZN6"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:4ZN6"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:4ZN6"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:4ZN6"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:4ZN6"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:4ZN6"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:4ZN6"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:4ZN6"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:4ZN6"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:4ZN6"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 226..238
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:4ZN6"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:4ZN6"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:4ZN6"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:4ZN6"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:4ZN6"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:4ZN6"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 317..327
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 331..347
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 355..366
FT /evidence="ECO:0007829|PDB:4ZN6"
FT HELIX 375..395
FT /evidence="ECO:0007829|PDB:4ZN6"
SQ SEQUENCE 398 AA; 43022 MW; AD5A8F5842524EF6 CRC64;
MTQSVCILGV TGSIGRSTLK ILGQHPDKYS VFAVSAHSRI SELVEICKQF RPKVVVVPEQ
KIAELKTLFA QQNISDIDVL AGQEGLVDIA SHTDVDIVMA AIVGAAGLLP TLAAVKAGKR
VLLANKEALV MSGEIMMQAA RDHQALLLPV DSEHNAIFQS LPHNYLQADR TGQPQLGVSK
ILLTASGGPF LNHSLEQLVH VTPQQACKHP NWSMGQKISV DSATLMNKGL ELIEACHLFS
ISEHFVTVVV HPQSIIHSMV QYVDGSTLAQ MGNPDMCTPI AHALAWPERL QTNVPALDLF
EYSQLNFQAP DTQKFPALNL ARQAMRAGGL APTILNAANE IAVEAFLMER IGFTSIPQVV
EHTLEKLENA AAESIECILD KDKVARSVAQ QYISSIGG
//
