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B8FBU6 (B8FBU6_DESAA) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | 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 HAMAP-Rule MF_00183
Short name=DXP reductoisomerase HAMAP-Rule MF_00183
EC=1.1.1.267 HAMAP-Rule MF_00183
Alternative name(s):
1-deoxyxylulose-5-phosphate reductoisomerase HAMAP-Rule MF_00183
2-C-methyl-D-erythritol 4-phosphate synthase HAMAP-Rule MF_00183
Gene names
Name:dxr HAMAP-Rule MF_00183
Ordered Locus Names:Dalk_3159
OrganismDesulfatibacillum alkenivorans (strain AK-01) [Complete proteome] [HAMAP] EMBL ACL04849.1
Taxonomic identifier439235 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Desulfobacterales › Desulfobacteraceae › Desulfatibacillum ›

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-Rule MF_00183 SAAS SAAS026877

Catalytic activity

2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH. HAMAP-Rule MF_00183 SAAS SAAS026877

Cofactor

Divalent cation By similarity. HAMAP-Rule MF_00183 SAAS SAAS026877

Pathway

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. HAMAP-Rule MF_00183 SAAS SAAS026877

Sequence similarities

Belongs to the DXR family. HAMAP-Rule MF_00183

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding15 – 4430NADP By similarity HAMAP-Rule MF_00183

Sites

Metal binding1591Divalent metal cation By similarity HAMAP-Rule MF_00183
Metal binding1611Divalent metal cation By similarity HAMAP-Rule MF_00183
Metal binding2301Divalent metal cation By similarity HAMAP-Rule MF_00183
Binding site1341Substrate By similarity HAMAP-Rule MF_00183
Binding site1611Substrate By similarity HAMAP-Rule MF_00183
Binding site1851Substrate By similarity HAMAP-Rule MF_00183
Binding site2081Substrate By similarity HAMAP-Rule MF_00183
Binding site2301Substrate By similarity HAMAP-Rule MF_00183

Sequences

Sequence LengthMass (Da)Tools
B8FBU6 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: A338F31323840AC7

FASTA39443,109
        10         20         30         40         50         60 
MSLSDKIRVK NLTILGSTGS IGKSTLGVVR KFPDQFKIRA LAAHTSIDAL AEQVVEFLPE 

        70         80         90        100        110        120 
LVVVRDKDLA GKLSTALQGA STPHPYIMYG EEGYQKAATL DSVDMVVSSM VGAAGLLPTL 

       130        140        150        160        170        180 
AAIRARKQVA LANKETLVMA GALVMREARE NGVKLMPIDS EHSAIFQCLQ GNDRKDLDKI 

       190        200        210        220        230        240 
LLTASGGPFR TVSREKFESL KPEDALSHPT WDMGAKITID SSTLMNKGLE VIEAKWLFDV 

       250        260        270        280        290        300 
RQQDIQVVVH PQSIVHSMVA YKDGSVIAQL GVPDMAGAIA YAMSYPDRLP LGQPIPDFFA 

       310        320        330        340        350        360 
LGSLEFFEPD LEKFPCLALA QQACRDEQTY PAVLNAANEI AVQAFLDHQI RFPQIPQLIE 

       370        380        390 
KCLNVHTPSA RPDLEQILEA DAWARDYIKQ AARS

« Hide

References

[1]"Complete sequence of Desulfatibacillum alkenivorans AK-01."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Wawrik B., Richardson P.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AK-01.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001322 Genomic DNA. Translation: ACL04849.1.
RefSeqYP_002432317.1. NC_011768.1.

3D structure databases

ProteinModelPortalB8FBU6.
ModBaseSearch...

Protein-protein interaction databases

STRING439235.Dalk_3159.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL04849; ACL04849; Dalk_3159.
GeneID7167100.
KEGGdal:Dalk_3159.
PATRIC21653048. VBIDesAlk8144_3371.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0743.
HOGENOMHOG000007221.
KOK00099.
OMAAHPNWVM.
ProtClustDBPRK05447.

Enzyme and pathway databases

BioCycDALK439235:GHP2-3193-MONOMER.
UniPathwayUPA00056; UER00092.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00183. DXP_reductoisom.
InterProIPR003821. DXP_reductoisomerase.
IPR013644. DXP_reductoisomerase_C.
IPR013512. DXP_reductoisomerase_N.
IPR026877. DXPR_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR30525. PTHR30525. 1 hit.
PfamPF08436. DXP_redisom_C. 1 hit.
PF02670. DXP_reductoisom. 1 hit.
PF13288. DXPR_C. 1 hit.
[Graphical view]
PIRSFPIRSF006205. Dxp_reductismrs. 1 hit.
SUPFAMSSF69055. SSF69055. 1 hit.
TIGRFAMsTIGR00243. Dxr. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB8FBU6_DESAA
AccessionPrimary (citable) accession number: B8FBU6
Entry history
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: May 1, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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