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Database: UniProt
Entry: A0A329ZA14_9HELI
LinkDB: A0A329ZA14_9HELI
Original site: A0A329ZA14_9HELI 
ID   A0A329ZA14_9HELI        Unreviewed;       363 AA.
AC   A0A329ZA14;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=CCY99_08555 {ECO:0000313|EMBL:RAX51714.1};
OS   Helicobacter sp. 16-1353.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=2004996 {ECO:0000313|EMBL:RAX51714.1, ECO:0000313|Proteomes:UP000251728};
RN   [1] {ECO:0000313|EMBL:RAX51714.1, ECO:0000313|Proteomes:UP000251728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16-1353 {ECO:0000313|EMBL:RAX51714.1,
RC   ECO:0000313|Proteomes:UP000251728};
RX   PubMed=29225701; DOI=10.1186/s13099-017-0220-y;
RA   Feng Y., Mannion A., Madden C.M., Swennes A.G., Townes C., Byrd C.,
RA   Marini R.P., Fox J.G.;
RT   "Cytotoxic Escherichia coli strains encoding colibactin and cytotoxic
RT   necrotizing factor (CNF) colonize laboratory macaques.";
RL   Gut Pathog. 9:71-71(2017).
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:RAX51714.1}.
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DR   EMBL; NHYM01000016; RAX51714.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A329ZA14; -.
DR   OrthoDB; 9806546at2; -.
DR   UniPathway; UPA00056; UER00092.
DR   Proteomes; UP000251728; Unassembled WGS sequence.
DR   GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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   Isomerase {ECO:0000313|EMBL:RAX51714.1};
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          1..122
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02670"
FT   DOMAIN          130..211
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08436"
FT   DOMAIN          241..358
FT                   /note="DXP reductoisomerase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13288"
FT   BINDING         7
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         8
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         9
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         10
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         31
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         33
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         114
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         115
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         116
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         134
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         135
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         136
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         136
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         158
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         181
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         187
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         194
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         199
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         200
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         203
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
FT   BINDING         203
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00183"
SQ   SEQUENCE   363 AA;  40349 MW;  B4A519D591139397 CRC64;
     MIILGSTGSI GINAIDIAIK NHKKIEMLSV GDNIDLLNKQ IQMTNPTFIV IKDKKNANKV
     RYSNKQKLFF GESGILEALN LSKSKIVINA IVGFSGLKPS LEVIKLNKKL ALANKESLVV
     GGKLLDSTNI IPVDSEHFAL KELIGSKKNI KKMIITASGG ALRDCKTKDL YYQTPQNALN
     HPNWAMGKKI TIDSATMINK LFEILEAKWL FKTNNIDALI ERNSIIHALI QTNDNAFYAH
     LGSNDMKLPI SYAILGKKAK NIDSIKEIDL TNYTFNLKAI DTKHYPLWNL KDSLLQTPQL
     GIILNAANEI LVSKFLDGKI PFGKISDGIF SAIARFSNDI KNIDNISDIQ NIDNQVRNFS
     DKI
//
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