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Q7NVY8 (DXR_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
1-deoxy-D-xylulose 5-phosphate reductoisomerase
Short name=DXP reductoisomerase
EC=1.1.1.267
Alternative name(s):
1-deoxyxylulose-5-phosphate reductoisomerase
2-C-methyl-D-erythritol 4-phosphate synthase
Gene names
Name:dxr
Ordered Locus Names:CV_2202
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium

Protein attributes

Sequence length394 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.

Ontologies

Keywords
   Biological processIsoprene biosynthesis
   LigandMetal-binding
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processisoprenoid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function1-deoxy-D-xylulose-5-phosphate reductoisomerase activity

Inferred from electronic annotation. Source: EC

NADPH binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3943941-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183
PRO_0000163635

Regions

Nucleotide binding10 – 3930NADP By similarity

Sites

Metal binding1531Divalent metal cation By similarity
Metal binding1551Divalent metal cation By similarity
Metal binding2291Divalent metal cation By similarity
Binding site1281Substrate By similarity
Binding site1551Substrate By similarity
Binding site1841Substrate By similarity
Binding site2071Substrate By similarity
Binding site2291Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NVY8 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 482DEAA31A2275F0

FASTA39441,674
        10         20         30         40         50         60 
MTKPQGIAVL GATGSVGCNT LDVVARHPER YRVVALTAHR QLDKLFEQAR RFCPDYLVVA 

        70         80         90        100        110        120 
DADAAARLRA RLAEAGLRSE VLHGADALVQ VAALPEVDAV MASIVGAAGL PSALAAARAG 

       130        140        150        160        170        180 
KRILLANKES LVVAGRLFMD AVRASGSALL PVDSEHSAIF QSLPADYAGN PDGAGVRKII 

       190        200        210        220        230        240 
LTASGGPFRN RPAADLAHVT PDEACRHPNW SMGRKISVDS ATLMNKGLEV IEARWLFNVP 

       250        260        270        280        290        300 
PSRIEVAVHP QSVIHSMVQY RDGSVMAQLG SPDMRTPIAC ALAWPERIDA GVEPMDFFSL 

       310        320        330        340        350        360 
SDLTFEKPDL ERFPCLQLAF DALEMGGDAP AVLNAANEVA VAAFLAGRLR FVDIPRVVAA 

       370        380        390 
SLSGVSCAAS DSLEGLLARD EEARRFAEGG VAAC

« Hide

References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016825 Genomic DNA. Translation: AAQ59875.1.
RefSeqNP_901872.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7NVY8.
SMRQ7NVY8. Positions 5-391.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2549212.
GenomeReviewsGene locus CV_2202 in contig AE016825_GR.
KEGGcvi:CV_2202.
NMPDRfig|243365.1.peg.2202.
PATRIC21439186. VBIChrVio67196_2149.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG430762.
OMAIHSMVEY.
PhylomeDBQ7NVY8.
ProtClustDBPRK05447.

Enzyme and pathway databases

BioCycCVIO243365:CV_2202-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 nameDXR_CHRVO
AccessionPrimary (citable) accession number: Q7NVY8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: January 25, 2012
This is version 60 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents