DXR_VIBVU
ID DXR_VIBVU Reviewed; 402 AA.
AC Q8DBF5;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=VV1_1866;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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; AE016795; AAO10268.1; -; Genomic_DNA.
DR RefSeq; WP_011079768.1; NC_004459.3.
DR PDB; 5KQO; X-ray; 2.35 A; A/B=1-402.
DR PDB; 5KRR; X-ray; 2.50 A; A/B=1-402.
DR PDB; 5KRV; X-ray; 2.30 A; A/B=1-402.
DR PDB; 5KRY; X-ray; 2.30 A; A/B=1-402.
DR PDB; 5KS1; X-ray; 2.40 A; A/B=1-402.
DR PDBsum; 5KQO; -.
DR PDBsum; 5KRR; -.
DR PDBsum; 5KRV; -.
DR PDBsum; 5KRY; -.
DR PDBsum; 5KS1; -.
DR AlphaFoldDB; Q8DBF5; -.
DR SMR; Q8DBF5; -.
DR EnsemblBacteria; AAO10268; AAO10268; VV1_1866.
DR KEGG; vvu:VV1_1866; -.
DR HOGENOM; CLU_035714_4_0_6; -.
DR OMA; PIDSEHF; -.
DR UniPathway; UPA00056; UER00092.
DR Proteomes; UP000002275; Chromosome 1.
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 1: Evidence at protein level;
KW 3D-structure; Isoprene biosynthesis; Metal-binding; NADP; Oxidoreductase.
FT CHAIN 1..402
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT /id="PRO_0000163733"
FT BINDING 7..36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 150
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 152
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 231
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:5KRV"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:5KRV"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:5KRV"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 59..72
FT /evidence="ECO:0007829|PDB:5KRV"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:5KRV"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:5KRV"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 126..142
FT /evidence="ECO:0007829|PDB:5KRV"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:5KRV"
FT TURN 166..170
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:5KRV"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:5KRV"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:5KRV"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:5KRV"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:5KRV"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:5KS1"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 316..327
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 329..347
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 355..368
FT /evidence="ECO:0007829|PDB:5KRV"
FT HELIX 379..400
FT /evidence="ECO:0007829|PDB:5KRV"
SQ SEQUENCE 402 AA; 43352 MW; 13095814BF685BAF CRC64;
MQKLTILGAT GSIGASTLKV IEQNPDKFSV VALAADSNVE KMQQLCQRWQ PEYAVMANKE
AALRLKMALA VLAPNTQVLG GQEALCYVAT LEQVDSVMAA IVGAAGLVPT MAAVKAGKRI
LLANKEALVM SGQLFIDEVE KSGAQLLPVD SEHNAIFQCL PQTVQGNLGR CDLASQGVSH
ILLTGSGGPF RYTDVAELEA VTPEQAIAHP NWSMGPKISV DSATMMNKGL EYIEAKWLFN
ASRDQLKVII HPQSVIHSMV QYLDGSVLAQ MGEPDMATPI ALTLSYPERV KAGVKPLDFT
QVGELTFLQP DFERYPCLAL AIEACYLGQH ATTTLNAANE VAVAAFLARQ IKFTDIARVN
DSVLNQVCKQ SLASGLDSLE SLLELDRMAR TLADEVVRER AQ
