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UniProtKB/Swiss-Prot entry Q9PMV3

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

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Entry information
Entry name DXR_CAMJE
Primary accession number Q9PMV3
Secondary accession number Q0P8R3
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 42)
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: Cj1346c
From
Campylobacter jejuni [TaxID: 197] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Campylobacteraceae; Campylobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NCTC 11168 / Serotype O:2;
DOI=10.1038/35001088; PubMed=10688204 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., Barrell B.G.;
"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences.";
Nature 403:665-668(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
AL111168; CAL35458.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G81278; G81278.
3D structure databases
HSSP P45568; 1K5H. [HSSP ENTRY / PDB]
ModBase Q9PMV3.
Enzyme and pathway databases
BioCyc CJEJ192222:CJ1346C-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 Q9PMV3.
Genome annotation databases
GenomeReviews AL111168_GR; Cj1346c.
KEGG cje:Cj1346c; -.
CMR Q9PMV3; Cj1346c.
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   356  356     1-deoxy-D-xylulose 5-phosphate reductoisomerase. PRO_0000163626
NP_BIND   4    30  27     NADP (By similarity). 
METAL   131   131        Divalent metal cation (By similarity). 
METAL   133   133        Divalent metal cation (By similarity). 
METAL   200   200        Divalent metal cation (By similarity). 
BINDING   112   112        Substrate (By similarity). 
BINDING   133   133        Substrate (By similarity). 
BINDING   155   155        Substrate (By similarity). 
BINDING   178   178        Substrate (By similarity). 
BINDING   200   200        Substrate (By similarity). 
Sequence information
Length: 356 AA [This is the length of the unprocessed precursor] Molecular weight: 39548 Da [This is the MW of the unprocessed precursor] CRC64: C6E4DCF376C06D45 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MILFGSTGSI GVNALKLAAL KNIPISALAC GDNIALLNEQ IARFKPKFVS IKDSKNKHLV 

        70         80         90        100        110        120 
KHDRVFIGQE GLEQILTECQ DKLLLNAIVG FAGLKSTLKA KELGKNIALA NKESLVVAGS 

       130        140        150        160        170        180 
FLKGAKFLPV DSEHAALKFL LEGKKNIAKL YITASGGAFY RYKIKDLNQV SVKDALKHPN 

       190        200        210        220        230        240 
WNMGAKITID SATMANKLFE IIEAYHLYDF KEIDALIEPR SLVHAMCEFK NGASTAYFSK 

       250        260        270        280        290        300 
ADMKLAISDA IFEKQDTPIL EAVDFSKMPA LKFHPISTKK YPIFKLKNTF LKEPNLGVII 

       310        320        330        340        350 
NAANEVGVYN FLENKSGFLD IAKCIFKALD HFGVPKISSI EEVFEYDFKT REYLRS
Q9PMV3 in FASTA format

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