DXR_ANAPZ
ID DXR_ANAPZ Reviewed; 385 AA.
AC Q2GKQ8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=APH_0440;
OS Anaplasma phagocytophilum (strain HZ).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma; phagocytophilum group.
OX NCBI_TaxID=212042;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ;
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
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; CP000235; ABD44127.1; -; Genomic_DNA.
DR RefSeq; WP_011450566.1; NC_007797.1.
DR AlphaFoldDB; Q2GKQ8; -.
DR SMR; Q2GKQ8; -.
DR STRING; 212042.APH_0440; -.
DR EnsemblBacteria; ABD44127; ABD44127; APH_0440.
DR GeneID; 56368562; -.
DR KEGG; aph:APH_0440; -.
DR eggNOG; COG0743; Bacteria.
DR HOGENOM; CLU_035714_0_0_5; -.
DR OMA; PIDSEHF; -.
DR OrthoDB; 1200722at2; -.
DR UniPathway; UPA00056; UER00092.
DR Proteomes; UP000001943; 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..385
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase"
FT /id="PRO_1000077331"
FT BINDING 7..36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 123
FT /ligand="substrate"
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 150
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183"
FT BINDING 150
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 385 AA; 41579 MW; 253AE0A7AF9BEB47 CRC64;
MKKVSVFGST GFIGKTTVGI LSGNTEDFKV IALVAGSNVS LLAQQAKLLN AEMAVIADDA
QYEELKRSLH GSGIRVAAGK EAVLEAAALS VDTAVMAITG IVALSAVMRL IESGVGTIAL
ASKESVVCGG VLLRDAACKS GTRIVPVDSE HNAVFRLLSQ GDNPYKITIT ASGGPFLHWS
HDQLKSVTIE DALVHPVWKM GKKISVDSAT MMNKALEVLE ASYLFELGYR KIDVVIHPES
IVHALAFYQD GTSTALMSLP DMSIPILHAL YWPHRKEVSV REVDLIAYGK LTFIRPDFER
FPALKAAFDI LQSSERDVAS IVFNAANEVA VESFLNSEIT FLEIVNIVLH VMNKVPYGKV
SSLADIMEYD LLGRCIAREV ISDAS
