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B6I6N0 (DEOB_ECOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. 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

Names and origin

Protein namesRecommended name:
Phosphopentomutase

EC=5.4.2.7
Alternative name(s):
Phosphodeoxyribomutase
Gene names
Name:deoB
Ordered Locus Names:ECSE_4658
OrganismEscherichia coli (strain SE11) [Complete proteome] [HAMAP]
Taxonomic identifier409438 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length407 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

Catalytic activity

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

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

Cofactor

Binds 1 or 2 manganese ions Potential.

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

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00740.

Sequence similarities

Belongs to the phosphopentomutase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 407407Phosphopentomutase HAMAP-Rule MF_00740
PRO_1000133074

Sites

Metal binding101Manganese By similarity
Metal binding3111Manganese By similarity
Metal binding3471Manganese By similarity
Metal binding3481Manganese By similarity
Metal binding3591Manganese By similarity

Amino acid modifications

Modified residue2871N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B6I6N0 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 516F3018DC77A077

FASTA40744,370
        10         20         30         40         50         60 
MKRAFIMVLD SFGIGATEDA ERFGDVGADT LGHIAEACAK GEADNGRKGP LNLPNLTRLG 

        70         80         90        100        110        120 
LAKAHEGSTG FIPAGMDGNA EVIGAYAWAH EMSSGKDTPS GHWEIAGVPV LFEWGYFSDH 

       130        140        150        160        170        180 
ENSFPQELLD KLVERANLPG YLGNCHSSGT VILDQLGEEH MKTGKPIFYT SADSVFQIAC 

       190        200        210        220        230        240 
HEETFGLDKL YELCEIAREE LTNGGYNIGR VIARPFIGDK AGNFQRTGNR HDLAVEPPAP 

       250        260        270        280        290        300 
TVLQKLVDEK HGQVVSVGKI ADIYANCGIT KKVKATGLDA LFDATIKEMK EAGDNTIVFT 

       310        320        330        340        350        360 
NFVDFDSSWG HRRDVAGYAA GLELFDRRLP ELMSLLRDDD ILILTADHGC DPTWTGTDHT 

       370        380        390        400 
REHIPVLVYG PKVKPGSLGH RETFADIGQT LAKYFGTSDM EYGKAMF 

« Hide

References

[1]"Complete genome sequence and comparative analysis of the wild-type commensal Escherichia coli strain SE11 isolated from a healthy adult."
Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.
DNA Res. 15:375-386(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SE11.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009240 Genomic DNA. Translation: BAG80182.1.
RefSeqYP_002295933.1. NC_011415.1.

3D structure databases

ProteinModelPortalB6I6N0.
SMRB6I6N0. Positions 2-407.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING409438.ECSE_4658.

Proteomic databases

PRIDEB6I6N0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG80182; BAG80182; ECSE_4658.
GeneID7003043.
KEGGecy:ECSE_4658.
PATRIC18428068. VBIEscCol83070_4848.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1015.
HOGENOMHOG000008159.
KOK01839.
OMAEHTREHI.
OrthoDBEOG6R5C7J.

Enzyme and pathway databases

BioCycECOL409438:GHUU-4761-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 nameDEOB_ECOSE
AccessionPrimary (citable) accession number: B6I6N0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: December 16, 2008
Last modified: May 14, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways