Skip Header

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

A7H0K4 (DXR_CAMC5) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 32. 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
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
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:Ccur92_16920
ORF Names:CCV52592_0594
OrganismCampylobacter curvus (strain 525.92) [Complete proteome] [HAMAP]
Taxonomic identifier360105 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length365 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 – 3653651-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183
PRO_1000020236

Regions

Nucleotide binding4 – 3027NADP By similarity

Sites

Metal binding1341Divalent metal cation By similarity
Metal binding1361Divalent metal cation By similarity
Metal binding2031Divalent metal cation By similarity
Binding site1151Substrate By similarity
Binding site1361Substrate By similarity
Binding site1581Substrate By similarity
Binding site1811Substrate By similarity
Binding site2031Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A7H0K4 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: E941E52D95598B93

FASTA36539,640
        10         20         30         40         50         60 
MVILGSTGSI GTNTLEICSR HGVSVEALSC AKNIALLNEQ IARFRPKFVC VADESLASEV 

        70         80         90        100        110        120 
KILKKSQIFV GAGGLLEMLE ACHSQKVVNA IVGFAGLAPS LKTQELGKSL ALANKESLVA 

       130        140        150        160        170        180 
GGKFLDTAKI SPIDSEHFGL KFLLQNRTAP NRLIITASGG AFYRTPMKNL AKVTPSDALK 

       190        200        210        220        230        240 
HPNWSMGAKI TIDSATMANK LFEVMEAFWL YGTSRIDALI EPTSMVHALV EFMDGSCTAH 

       250        260        270        280        290        300 
ISRADMKLAI AHAVLENVSE NVVAHADLLA LKDIKFHKIN LKKYPIFSLK EQVLERADLG 

       310        320        330        340        350        360 
VVINAANEVG VFAFLKGECR FLDISRIVLA AAKRFADVKI ETKDEIFAID AEVRNFTKRG 


LNAKI

« Hide

References

[1]"Genome sequence of Campylobacter curvus 525.92 isolated from human feces."
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 525.92.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000767 Genomic DNA. Translation: EAU01416.2.
RefSeqYP_001408996.1. NC_009715.1.

3D structure databases

ProteinModelPortalA7H0K4.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7H0K4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5407090.
GenomeReviewsGene locus Ccur92_16920 in contig CP000767_GR.
KEGGccv:CCV52592_0594.
PATRIC20033995. VBICamCur47627_1782.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0743.
HOGENOMHBG430762.
OMAFEVLEAY.
ProtClustDBPRK05447.

Enzyme and pathway databases

BioCycCCUR360105:CCV52592_0594-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_CAMC5
AccessionPrimary (citable) accession number: A7H0K4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 11, 2007
Last modified: December 14, 2011
This is version 32 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