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Q1BAD4 (Q1BAD4_MYCSS) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 49. 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 MF_00183
Short name=DXP reductoisomerase HAMAP MF_00183
EC=1.1.1.267 HAMAP MF_00183
Alternative name(s):
1-deoxyxylulose-5-phosphate reductoisomerase HAMAP MF_00183
2-C-methyl-D-erythritol 4-phosphate synthase HAMAP MF_00183
Gene names
Name:dxr HAMAP MF_00183
Ordered Locus Names:Mmcs_2042
OrganismMycobacterium sp. (strain MCS) [Complete proteome] [HAMAP]
Taxonomic identifier164756 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 SAAS SAAS003821

Catalytic activity

2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH. HAMAP MF_00183 SAAS SAAS003821

Cofactor

Divalent cation By similarity. HAMAP MF_00183 SAAS SAAS003821

Pathway

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. HAMAP MF_00183 SAAS SAAS003821

Sequence similarities

Belongs to the DXR family. HAMAP MF_00183

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential EMBL ABG08150.1
Chain27 – 392366 Potential EMBL ABG08150.1
PRO_5000124164

Regions

Nucleotide binding10 – 3930NADP By similarity HAMAP MF_00183

Sites

Metal binding1431Divalent metal cation By similarity HAMAP MF_00183
Metal binding1451Divalent metal cation By similarity HAMAP MF_00183
Metal binding2141Divalent metal cation By similarity HAMAP MF_00183
Binding site1201Substrate By similarity HAMAP MF_00183
Binding site1451Substrate By similarity HAMAP MF_00183
Binding site1691Substrate By similarity HAMAP MF_00183
Binding site1921Substrate By similarity HAMAP MF_00183
Binding site2141Substrate By similarity HAMAP MF_00183

Sequences

Sequence LengthMass (Da)Tools
Q1BAD4 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: 47F9C91055DADD97

FASTA39240,769
        10         20         30         40         50         60 
MGTRLRVLIL GSTGSIGTQA LDVIAANPDR FEVVGLAAGG ANPELLARQR AATGVHAIAV 

        70         80         90        100        110        120 
TDPAAAEKIG DVTYSGPDAV TRLVENTQAD VVLNALVGAL GLEPTLAALA TGARLALANK 

       130        140        150        160        170        180 
ESLVAGGPLV LRAAAPGQIV PVDSEHSAMA QCLRGGSADE VATLVLTASG GPFLGWSAED 

       190        200        210        220        230        240 
LQSVTPEQAG KHPTWSMGPM NTLNSATLVN KGLELIETHL LFGIDYDRIE VVVHPQSIVH 

       250        260        270        280        290        300 
SMATFTDGST LAQASPPDMK LPIALALGWP DRIPGAALAC DFTTASTWEF LPLDDDVFPA 

       310        320        330        340        350        360 
VRLAREAGRR GGSLTAVYNA ANEEAAAAFL DGRIRFPQIV ESVAEVLRAA DQWAAEPATV 

       370        380        390 
EEVLDAQRWA RDRAGRAVEH AATPPSKGLV TR

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References

[1]"Complete sequence of chromosome of Mycobacterium sp. MCS."
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., Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MCS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000384 Genomic DNA. Translation: ABG08150.1.
RefSeqYP_639206.1. NC_008146.1.

3D structure databases

ProteinModelPortalQ1BAD4.
SMRQ1BAD4. Positions 4-378.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1BAD4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000062871; EBMYCP00000061038; EBMYCG00000062866.
GeneID4110875.
GenomeReviewsGene locus Mmcs_2042 in contig CP000384_GR.
KEGGmmc:Mmcs_2042.
PATRIC18114272. VBIMycSp106721_2089.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0743.
GeneTreeEBGT00050000016490.
HOGENOMHBG430762.
OMAIHSMVEY.
ProtClustDBPRK05447.

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 nameQ1BAD4_MYCSS
AccessionPrimary (citable) accession number: Q1BAD4
Entry history
Integrated into UniProtKB/TrEMBL: July 11, 2006
Last sequence update: July 11, 2006
Last modified: December 14, 2011
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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