Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C4ZT65 (DEOB_ECOBW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 36. 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:BWG_4075
OrganismEscherichia coli (strain K12 / MC4100 / BW2952) [Complete proteome] [HAMAP]
Taxonomic identifier595496 [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_1000212807

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
C4ZT65 [UniParc].

Last modified July 28, 2009. 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]"Genomic sequencing reveals regulatory mutations and recombinational events in the widely used MC4100 lineage of Escherichia coli K-12."
Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R., Wang L.
J. Bacteriol. 191:4025-4029(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MC4100 / BW2952.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001396 Genomic DNA. Translation: ACR64055.1.
RefSeqYP_002929266.1. NC_012759.1.

3D structure databases

ProteinModelPortalC4ZT65.
SMRC4ZT65. Positions 2-407.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING595496.BWG_4075.

Proteomic databases

PRIDEC4ZT65.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR64055; ACR64055; BWG_4075.
GeneID7956149.
KEGGebw:BWG_4075.
PATRIC18278047. VBIEscCol60876_4476.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1015.
HOGENOMHOG000008159.
KOK01839.
OMAEHTREHI.
OrthoDBEOG6R5C7J.

Enzyme and pathway databases

BioCycECOL595496:GI18-4248-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_ECOBW
AccessionPrimary (citable) accession number: C4ZT65
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: May 14, 2014
This is version 36 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