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Protein

Phosphopentomutase

Gene

deoB

Organism
Escherichia coli (strain K12 / MC4100 / BW2952)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Phosphotransfer between the C1 and C5 carbon atoms of pentose.UniRule annotation

Catalytic activityi

Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate.UniRule annotation
2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-alpha-D-ribose 5-phosphate.UniRule annotation

Cofactori

Mn2+UniRule annotationNote: Binds 1 or 2 manganese ions.UniRule annotation

Pathway:i5-phospho-alpha-D-ribose 1-diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II).UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Phosphopentomutase (deoB)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
This subpathway is part of the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II), the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi10 – 101ManganeseUniRule annotation
Metal bindingi311 – 3111ManganeseUniRule annotation
Metal bindingi347 – 3471ManganeseUniRule annotation
Metal bindingi348 – 3481ManganeseUniRule annotation
Metal bindingi359 – 3591ManganeseUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciECOL595496:GI18-4248-MONOMER.
UniPathwayiUPA00087; UER00173.

Names & Taxonomyi

Protein namesi
Recommended name:
PhosphopentomutaseUniRule annotation (EC:5.4.2.7UniRule annotation)
Alternative name(s):
PhosphodeoxyribomutaseUniRule annotation
Gene namesi
Name:deoBUniRule annotation
Ordered Locus Names:BWG_4075
OrganismiEscherichia coli (strain K12 / MC4100 / BW2952)
Taxonomic identifieri595496 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 407407PhosphopentomutasePRO_1000212807Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei287 – 2871N6-acetyllysineUniRule annotation

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiC4ZT65.

Structurei

3D structure databases

ProteinModelPortaliC4ZT65.
SMRiC4ZT65. Positions 2-407.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphopentomutase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1015.
HOGENOMiHOG000008159.
KOiK01839.
OMAiYLGNCHA.
OrthoDBiEOG6R5C7J.

Family and domain databases

Gene3Di3.30.70.1250. 1 hit.
3.40.720.10. 2 hits.
HAMAPiMF_00740. Phosphopentomut.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR010045. DeoB.
IPR006124. Metalloenzyme.
IPR024052. Phosphopentomutase_DeoB_cap.
[Graphical view]
PfamiPF01676. Metalloenzyme. 1 hit.
[Graphical view]
PIRSFiPIRSF001491. Ppentomutase. 1 hit.
SUPFAMiSSF143856. SSF143856. 1 hit.
SSF53649. SSF53649. 2 hits.
TIGRFAMsiTIGR01696. deoB. 1 hit.

Sequencei

Sequence statusi: Complete.

C4ZT65-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRAFIMVLD SFGIGATEDA ERFGDVGADT LGHIAEACAK GEADNGRKGP
60 70 80 90 100
LNLPNLTRLG LAKAHEGSTG FIPAGMDGNA EVIGAYAWAH EMSSGKDTPS
110 120 130 140 150
GHWEIAGVPV LFEWGYFSDH ENSFPQELLD KLVERANLPG YLGNCHSSGT
160 170 180 190 200
VILDQLGEEH MKTGKPIFYT SADSVFQIAC HEETFGLDKL YELCEIAREE
210 220 230 240 250
LTNGGYNIGR VIARPFIGDK AGNFQRTGNR HDLAVEPPAP TVLQKLVDEK
260 270 280 290 300
HGQVVSVGKI ADIYANCGIT KKVKATGLDA LFDATIKEMK EAGDNTIVFT
310 320 330 340 350
NFVDFDSSWG HRRDVAGYAA GLELFDRRLP ELMSLLRDDD ILILTADHGC
360 370 380 390 400
DPTWTGTDHT REHIPVLVYG PKVKPGSLGH RETFADIGQT LAKYFGTSDM

EYGKAMF
Length:407
Mass (Da):44,370
Last modified:July 28, 2009 - v1
Checksum:i516F3018DC77A077
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001396 Genomic DNA. Translation: ACR64055.1.
RefSeqiWP_000816471.1. NC_012759.1.

Genome annotation databases

EnsemblBacteriaiACR64055; ACR64055; BWG_4075.
KEGGiebw:BWG_4075.
PATRICi18278047. VBIEscCol60876_4476.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001396 Genomic DNA. Translation: ACR64055.1.
RefSeqiWP_000816471.1. NC_012759.1.

3D structure databases

ProteinModelPortaliC4ZT65.
SMRiC4ZT65. Positions 2-407.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiC4ZT65.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACR64055; ACR64055; BWG_4075.
KEGGiebw:BWG_4075.
PATRICi18278047. VBIEscCol60876_4476.

Phylogenomic databases

eggNOGiCOG1015.
HOGENOMiHOG000008159.
KOiK01839.
OMAiYLGNCHA.
OrthoDBiEOG6R5C7J.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00173.
BioCyciECOL595496:GI18-4248-MONOMER.

Family and domain databases

Gene3Di3.30.70.1250. 1 hit.
3.40.720.10. 2 hits.
HAMAPiMF_00740. Phosphopentomut.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR010045. DeoB.
IPR006124. Metalloenzyme.
IPR024052. Phosphopentomutase_DeoB_cap.
[Graphical view]
PfamiPF01676. Metalloenzyme. 1 hit.
[Graphical view]
PIRSFiPIRSF001491. Ppentomutase. 1 hit.
SUPFAMiSSF143856. SSF143856. 1 hit.
SSF53649. SSF53649. 2 hits.
TIGRFAMsiTIGR01696. deoB. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiDEOB_ECOBW
AccessioniPrimary (citable) accession number: C4ZT65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: July 22, 2015
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.