Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q81WL4 (DXR2_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1-deoxy-D-xylulose 5-phosphate reductoisomerase 2

Short name=DXP reductoisomerase 2
EC=1.1.1.267
Alternative name(s):
1-deoxyxylulose-5-phosphate reductoisomerase 2
2-C-methyl-D-erythritol 4-phosphate synthase 2
Gene names
Name:dxr2
Synonyms:dxr-2
Ordered Locus Names:BA_3959, GBAA_3959, BAS3672
OrganismBacillus anthracis
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length380 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP) By similarity. HAMAP MF_00183

Catalytic activity

2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH. HAMAP MF_00183

Cofactor

Divalent cation By similarity. HAMAP MF_00183

Pathway

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. HAMAP MF_00183

Sequence similarities

Belongs to the DXR family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3803801-deoxy-D-xylulose 5-phosphate reductoisomerase 2 HAMAP MF_00183
PRO_0000163601

Regions

Nucleotide binding7 – 3630NADP By similarity

Sites

Metal binding1461Divalent metal cation By similarity
Metal binding1481Divalent metal cation By similarity
Metal binding2171Divalent metal cation By similarity
Binding site1211Substrate By similarity
Binding site1481Substrate By similarity
Binding site1721Substrate By similarity
Binding site1951Substrate By similarity
Binding site2171Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81WL4 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 689DDF159E83D1B4

FASTA38042,239
        10         20         30         40         50         60 
MKNISLLGAS GSIGTQTLDV LRSHPDQFRL VAFSVGKNID YAVKVIQEFS PQIVSVQREE 

        70         80         90        100        110        120 
DVLKLQAVSG NTKIVYGSEG LLEVALHPDA EIVVNAVVGS VGLLPTLRAI EAKKTIGIAN 

       130        140        150        160        170        180 
KETLVTAGHL VMEAARKHNV SLLPVDSEHS AIFQCLNGEN EKRISRLIIT ASGGSFRDKT 

       190        200        210        220        230        240 
RDELHHVTVE DALRHPNWSM GSKITIDSAT MMNKGLEVIE AHWLFGIPYE QIDVVLHKES 

       250        260        270        280        290        300 
IIHSMVEFED RSVMAQLGSP DMRVPIQYAL TYPDRLPLSD TKQLNLWEIG TLHFEKMNQE 

       310        320        330        340        350        360 
RFRCLRFAYE AGKAGGSMPA VMNAANEVAV EAFLQKRIGF LTVEDLIEKA MNHHNVIARP 

       370        380 
SLEEILEIDA ATRRFVMEQI 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP27688.1.
AE017334 Genomic DNA. Translation: AAT33073.1.
AE017225 Genomic DNA. Translation: AAT55974.1.
RefSeqNP_846202.1. NC_003997.3.
YP_020598.1. NC_007530.2.
YP_029923.1. NC_005945.1.

3D structure databases

ProteinModelPortalQ81WL4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000010342; EBBACP00000010098; EBBACG00000010334.
EBBACT00000016898; EBBACP00000016519; EBBACG00000016889.
EBBACT00000021953; EBBACP00000021438; EBBACG00000021944.
GeneID1086817.
2819523.
2849846.
GenomeReviewsGene locus BA_3959 in contig AE016879_GR.
Gene locus BAS3672 in contig AE017225_GR.
Gene locus GBAA_3959 in contig AE017334_GR.
KEGGban:BA_3959.
bar:GBAA_3959.
bat:BAS3672.
TIGRBA_3959.
GBAA_3959.

Phylogenomic databases

GeneTreeEBGT00050000001768.
HOGENOMHBG430762.
OMAIHSMVEY.
ProtClustDBPRK05447.

Enzyme and pathway databases

BioCycBANT260799:BAS3672-MONOMER.
BANT261594:GBAA3959-MONOMER.

Family and domain databases

HAMAPMF_00183. DXP_reductoisom.
[Tree]
InterProIPR003821. DXP_reductoisomerase.
IPR013644. DXP_reductoisomerase_C.
IPR013512. DXP_reductoisomerase_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00099.
PfamPF08436. DXP_redisom_C. 1 hit.
PF02670. DXP_reductoisom. 1 hit.
[Graphical view]
PIRSFPIRSF006205. Dxp_reductismrs. 1 hit.
TIGRFAMsTIGR00243. Dxr. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDXR2_BACAN
AccessionPrimary (citable) accession number: Q81WL4
Secondary accession number(s): Q6HUR5, Q6KNZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: December 14, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families