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D2P6R2 (D2P6R2_LISM2) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Phosphopentomutase HAMAP-Rule MF_00740

EC=5.4.2.7 HAMAP-Rule MF_00740
Alternative name(s):
Phosphodeoxyribomutase HAMAP-Rule MF_00740
Gene names
Name:drm EMBL ADB71947.1
Synonyms:deoB HAMAP-Rule MF_00740
Ordered Locus Names:LM5923_2106 EMBL ADB71947.1
OrganismListeria monocytogenes serotype 1/2a (strain 08-5923) [Complete proteome] [HAMAP] EMBL ADB71947.1
Taxonomic identifier637381 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Phosphotransfer between the C1 and C5 carbon atoms of pentose By similarity. HAMAP-Rule MF_00740 SAAS SAAS006124

Catalytic activity

2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-alpha-D-ribose 5-phosphate. HAMAP-Rule MF_00740 SAAS SAAS006124

Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate. HAMAP-Rule MF_00740 SAAS SAAS006124

Cofactor

Binds 1 or 2 manganese ions By similarity. HAMAP-Rule MF_00740 SAAS SAAS006124

Pathway

Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II): step 1/3. HAMAP-Rule MF_00740 SAAS SAAS006124

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00740 SAAS SAAS006124.

Sequence similarities

Belongs to the phosphopentomutase family. HAMAP-Rule MF_00740

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding141Manganese By similarity HAMAP-Rule MF_00740
Metal binding2921Manganese By similarity HAMAP-Rule MF_00740
Metal binding3281Manganese By similarity HAMAP-Rule MF_00740
Metal binding3291Manganese By similarity HAMAP-Rule MF_00740
Metal binding3401Manganese By similarity HAMAP-Rule MF_00740

Sequences

Sequence LengthMass (Da)Tools
D2P6R2 [UniParc].

Last modified March 2, 2010. Version 1.
Checksum: 1D2D6202D2C95D23

FASTA39443,746
        10         20         30         40         50         60 
MPDKFKRVHV VVMDSVGIGE APDAAKFGDF DVDTFGHIAK HVGGLKMPEM GKLGLSNIRE 

        70         80         90        100        110        120 
IEGIKKAEKP LAYYTKMQEA SNGKDTMTGH WEIMGLYIDT PFRVFPDGFP DDLINQIEEK 

       130        140        150        160        170        180 
TGRKVIGNKP ASGTEIMAEL GEEHVKTGAL IVYTSADSVL QIAAHEDVVP LEELYEICEF 

       190        200        210        220        230        240 
CRKITLDDPY MLGRIIARPF VGEPGAFVRT PNRHDYALKP FKPTVMDALK DGGKDVIAIG 

       250        260        270        280        290        300 
KISDIFDGEG VTESIRTKSN MDGMDQFIAV LDKDFNGMSF LNLVDFDALF GHRRDPQGYA 

       310        320        330        340        350        360 
DALVDFDGRL VEVMEKLTDD DLLIITADHG NDPTYTGTDH TREFVPLLVY SPRFKNGGSE 

       370        380        390 
LELRKTFADL GATVADNFDV KMPEYGTSFL RDLK 

« Hide

References

[1]"High-throughput genome sequencing of two Listeria monocytogenes clinical isolates during a large foodborne outbreak."
Gilmour M.W., Graham M., Van Domselaar G., Tyler S., Kent H., Trout-Yakel K.M., Larios O., Allen V., Lee B., Nadon C.
BMC Genomics 11:120-120(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 08-5923 EMBL ADB71947.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001604 Genomic DNA. Translation: ADB71947.1.
RefSeqYP_003417309.1. NC_013768.1.

3D structure databases

ProteinModelPortalD2P6R2.
SMRD2P6R2. Positions 3-393.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADB71947; ADB71947; LM5923_2106.
GeneID8758900.
KEGGlmy:LM5923_2106.
PATRIC32258044. VBILisMon5116_2123.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000008159.
KOK01839.
OMACHASGTE.

Enzyme and pathway databases

BioCycLMON637381:GH7Z-2142-MONOMER.
UniPathwayUPA00087; UER00173.

Family and domain databases

Gene3D3.30.70.1250. 1 hit.
3.40.720.10. 2 hits.
HAMAPMF_00740. Phosphopentomut.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR010045. DeoB.
IPR006124. Metalloenzyme.
IPR024052. Phosphopentomutase_DeoB_cap.
[Graphical view]
PfamPF01676. Metalloenzyme. 1 hit.
[Graphical view]
PIRSFPIRSF001491. Ppentomutase. 1 hit.
SUPFAMSSF143856. SSF143856. 1 hit.
SSF53649. SSF53649. 2 hits.
TIGRFAMsTIGR01696. deoB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameD2P6R2_LISM2
AccessionPrimary (citable) accession number: D2P6R2
Entry history
Integrated into UniProtKB/TrEMBL: March 2, 2010
Last sequence update: March 2, 2010
Last modified: February 19, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)