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UniProtKB/Swiss-Prot entry Q8K9S7

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DXR_BUCAP
Primary accession number Q8K9S7
Secondary accession numbers None
Integrated into Swiss-Prot on November 8, 2002
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 39)
Name and origin of the protein
Protein name 1-deoxy-D-xylulose 5-phosphate reductoisomerase
Synonyms DXP reductoisomerase
EC 1.1.1.267
1-deoxyxylulose-5-phosphate reductoisomerase
2-C-methyl-D-erythritol 4-phosphate synthase
Gene name
Name: dxr
OrderedLocusNames: BUsg_229
From
Buchnera aphidicola subsp. Schizaphis graminum [TaxID: 98794] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE013218; AAM67788.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_660577.1; -.
3D structure databases
HSSP P45568; 1K5H. [HSSP ENTRY / PDB]
ModBase Q8K9S7.
Enzyme and pathway databases
BioCyc BAPH198804:BUSG229-MON; -.
Ontologies
GO
GO:0030604; Molecular function: 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity (inferred from electronic annotation from HAMAP).
GO:0046872; Molecular function: metal ion binding (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0016114; Biological process: terpenoid biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00183; -; 1.
PBIL [Tree]
InterPro IPR003821; DXP_reductoisomerase.
IPR013644; DXP_reductoisomerase_C.
IPR013512; DXP_reductoisomerase_N.
Graphical view of domain structure.
Pfam PF08436; DXP_redisom_C; 1.
PF02670; DXP_reductoisom; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF006205; Dxp_reductismrs; 1.
TIGRFAMs TIGR00243; Dxr; 1.
ProtoNet Q8K9S7.
Genome annotation databases
GeneID 1005428; -.
GenomeReviews AE013218_GR; BUsg_229.
KEGG bas:BUsg229; -.
Phylogenomic databases
HOGENOM Q8K9S7; -.
Genome annotation databases
CMR Q8K9S7; BUsg_229.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Isoprene biosynthesis; Metal-binding; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   398  398     1-deoxy-D-xylulose 5-phosphate reductoisomerase. PRO_0000163623
NP_BIND   7    36  30     NADP (By similarity). 
METAL   150   150        Divalent metal cation (By similarity). 
METAL   152   152        Divalent metal cation (By similarity). 
METAL   231   231        Divalent metal cation (By similarity). 
BINDING   125   125        Substrate (By similarity). 
BINDING   152   152        Substrate (By similarity). 
BINDING   186   186        Substrate (By similarity). 
BINDING   209   209        Substrate (By similarity). 
BINDING   231   231        Substrate (By similarity). 
Sequence information
Length: 398 AA [This is the length of the unprocessed precursor] Molecular weight: 43727 Da [This is the MW of the unprocessed precursor] CRC64: 386412F1393271B0 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKKITVLGST GSIGISTLSI VKNNPSLFKV IVLVANKNSS MMLEQCEYFS PDWAIMKNKK 

        70         80         90        100        110        120 
SAHILKKRLK DKKIKTQVLS GNKAICQLAA LKESDLVISA IVGMAGLLPT LSAINAGKTI 

       130        140        150        160        170        180 
LLANKESLIV CGIIFMKALS SNKAKIFPID SEHNAIFQVL PKFVQKNLGK VNLKKNGVKS 

       190        200        210        220        230        240 
IILTASGGPF YNFKRENLSF VTPLEACSHP NWSMGRKISI DSATMINKGF EYAEARLLFN 

       250        260        270        280        290        300 
ASSSEIDILI HPQSIIHSMV EYIDGTILAQ LSVPDMKVAI SYAMSWPNRI SSGAKFLNFN 

       310        320        330        340        350        360 
KLSNLSFFKP DFIQFPCLKL AIDAFSQGQA AMTVLNAVNE VTVSAFLDSK ISFNKISEIN 

       370        380        390 
TDILMSSSFS EPVSVEEVLE IDKKTRIKSQ KKISSLIF
Q8K9S7 in FASTA format

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