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UniProtKB/Swiss-Prot entry Q9PKW8

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

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Entry information
Entry name DXR_CHLMU
Primary accession number Q9PKW8
Secondary accession numbers None
Integrated into Swiss-Prot on February 21, 2001
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 50)
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: TC_0343
From
Chlamydia muridarum [TaxID: 83560] [HAMAP proteome]
Taxonomy Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MoPn / Nigg;
DOI=10.1093/nar/28.6.1397; PubMed=10684935 [NCBI, ExPASy, EBI, Israel, Japan]
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39.";
Nucleic Acids Res. 28:1397-1406(2000).
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
AE002160; AAF39204.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G81712; G81712.
RefSeq NP_296721.1; -.
3D structure databases
HSSP P45568; 1K5H. [HSSP ENTRY / PDB]
ModBase Q9PKW8.
Enzyme and pathway databases
BioCyc CMUR243161:TC_0343-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 Q9PKW8.
Genome annotation databases
GeneID 1246386; -.
GenomeReviews AE002160_GR; TC_0343.
KEGG cmu:TC0343; -.
TIGR TC_0343; -.
Phylogenomic databases
HOGENOM Q9PKW8; -.
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   379  379     1-deoxy-D-xylulose 5-phosphate reductoisomerase. PRO_0000163629
NP_BIND   7    36  30     NADP (By similarity). 
METAL   147   147        Divalent metal cation (By similarity). 
METAL   149   149        Divalent metal cation (By similarity). 
METAL   218   218        Divalent metal cation (By similarity). 
BINDING   122   122        Substrate (By similarity). 
BINDING   149   149        Substrate (By similarity). 
BINDING   173   173        Substrate (By similarity). 
BINDING   196   196        Substrate (By similarity). 
BINDING   218   218        Substrate (By similarity). 
Sequence information
Length: 379 AA [This is the length of the unprocessed precursor] Molecular weight: 41811 Da [This is the MW of the unprocessed precursor] CRC64: 8C897289B35087BC [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKRLALIGST GSIGKQVLQV IREIPDAFVI ETLAAYGRNR ESLISQIREF SPRVVAVRDE 

        70         80         90        100        110        120 
TTYKELRKLF PHIEILSGEE GLIAVATAAS VDMTIVASSG IDALPAVMAS IQERKTIALA 

       130        140        150        160        170        180 
NKESLVAAGE LVTTLAKKNH VQILPIDSEH NALFQCLEGR DPSTIKKLIL TASGGPLRNK 

       190        200        210        220        230        240 
SKEELQKVTL QEVLKHPIWD MGPKITVDSS TLVNKGLEII EAFWLFGLQA VEIEAVIHPQ 

       250        260        270        280        290        300 
SLIHGMVEFC DGTILSVMNP PSMLFPIQHV LTFPDRYPSI ISGLNFLTNQ TLEFLPIDDE 

       310        320        330        340        350        360 
RFPSIRLAKD VLREGGSMGC FFNGANEALV QRFLSGEIAW YQIVSKLQTL MDKYVVRSCL 

       370 
SLEDILQVDS EARALASEC
Q9PKW8 in FASTA format

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