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Reviewed, UniProtKB/Swiss-Prot A8MHH5 (DXR_ALKOO)

Last modified February 9, 2010. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: Clos_1519
OrganismAlkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain OhILAs)) [Complete proteome] [HAMAP]
Taxonomic identifier350688 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeAlkaliphilus

Protein attributes

Sequence length381 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3813811-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183
PRO_1000058411

Regions

Nucleotide binding7 – 3630NADP By similarity

Sites

Metal binding1471Divalent metal cation By similarity
Metal binding1491Divalent metal cation By similarity
Metal binding2181Divalent metal cation By similarity
Binding site1221Substrate By similarity
Binding site1491Substrate By similarity
Binding site1731Substrate By similarity
Binding site1961Substrate By similarity
Binding site2181Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A8MHH5-1 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 9716DB6257C55CA5

FASTA38142,523
        10         20         30         40         50         60 
MKNISILGST GSIGTQTLDV VRNHPEKFKI VALSASGNID AIENQIHEFH PEIVAVFHRE 

        70         80         90        100        110        120 
KAEILSARIG KKVKVVSGIE GLIEVATLDS ADIVVTSVVG SIGLIPTVEA IRCGKTIALA 

       130        140        150        160        170        180 
NKETLVVAGE LIKKEAEKHK VQIIPVDSEH SAIFQCLQGE DIHNISRIIL TASGGAFRNW 

       190        200        210        220        230        240 
EKQDIQHAKA QDALKHPTWN MGSKVTIDSA SLMNKGLEVM EARWLFNVEL DKIDVIVHPQ 

       250        260        270        280        290        300 
SIVHSMVEYN DFSIIAQIGA PDMRGPIQYA LSYPNRINSS IERLDFRKIS ALTFMAPDTD 

       310        320        330        340        350        360 
KFPCLSLAYE SLKIGKTMPC VLNGANEVLV EYFLEDRIGF YDIPKFIEKA MSAHKPWVYT 

       370        380 
DIEELLEVDR WVRNWIKEQI E 

« Hide

References

[1]"Complete genome of Alkaliphilus oremlandii OhILAs."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E., Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000853 Genomic DNA. Translation: ABW19062.1.
RefSeqYP_001513058.1.

3D structure databases

SMRA8MHH5. Positions 2-381.
ModBaseSearch...

Genome annotation databases

GeneID5676959.
GenomeReviewsGene locus Clos_1519 in contig CP000853_GR.
KEGGaoe:Clos_1519.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG430762.
OMAIHSMVEY.

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]
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_ALKOO
AccessionPrimary (citable) accession number: A8MHH5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 4, 2007
Last modified: February 9, 2010
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents