Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphopentomutase

Gene

deoB

Organism
Bacillus thuringiensis subsp. konkukian (strain 97-27)
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

Pathwayi: 5-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 bindingi13 – 131ManganeseUniRule annotation
Metal bindingi291 – 2911ManganeseUniRule annotation
Metal bindingi327 – 3271ManganeseUniRule annotation
Metal bindingi328 – 3281ManganeseUniRule annotation
Metal bindingi339 – 3391ManganeseUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciBTHU281309:GJID-3901-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:BT9727_3828
OrganismiBacillus thuringiensis subsp. konkukian (strain 97-27)
Taxonomic identifieri281309 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000001301 Componenti: Chromosome

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 – 394394PhosphopentomutasePRO_0000258275Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ6HE79.
SMRiQ6HE79. Positions 2-392.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphopentomutase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000008159.
KOiK01839.
OMAiYLGNCHA.

Family and domain databases

Gene3Di3.30.70.1250. 1 hit.
3.40.720.10. 2 hits.
HAMAPiMF_00740. Phosphopentomut. 1 hit.
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.

Q6HE79-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKYKRIFLV VMDSVGIGEA PDAEQFGDLG SDTIGHIAEH MNGLHMPNMV
60 70 80 90 100
KLGLGNIREM KGISKVEKPL GYYTKMQEKS TGKDTMTGHW EIMGLYIDTP
110 120 130 140 150
FQVFPEGFPK ELLDELEEKT GRKIIGNKPA SGTEILDELG QEQMETGSLI
160 170 180 190 200
VYTSADSVLQ IAAHEEVVPL DELYKICKIA RELTLDEKYM VGRVIARPFV
210 220 230 240 250
GEPGNFTRTP NRHDYALKPF GRTVMNELKD SDYDVIAIGK ISDIYDGEGV
260 270 280 290 300
TESLRTKSNM DGMDKLVDTL NMDFTGLSFL NLVDFDALFG HRRDPQGYGE
310 320 330 340 350
ALQEYDARLP EVFEKLKEDD LLLITADHGN DPVHHGTDHT REYVPLLAYS
360 370 380 390
PSMKEGGQEL PLRQTFADIG ATVAENFGVK MPEYGTSFLN ELKK
Length:394
Mass (Da):44,113
Last modified:July 19, 2004 - v1
Checksum:iC4DC4D244B43B0A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017355 Genomic DNA. Translation: AAT62526.1.
RefSeqiWP_001046067.1. NC_005957.1.
YP_038147.1. NC_005957.1.

Genome annotation databases

EnsemblBacteriaiAAT62526; AAT62526; BT9727_3828.
GeneIDi2856599.
KEGGibtk:BT9727_3828.
PATRICi18988712. VBIBacThu119411_4082.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017355 Genomic DNA. Translation: AAT62526.1.
RefSeqiWP_001046067.1. NC_005957.1.
YP_038147.1. NC_005957.1.

3D structure databases

ProteinModelPortaliQ6HE79.
SMRiQ6HE79. Positions 2-392.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT62526; AAT62526; BT9727_3828.
GeneIDi2856599.
KEGGibtk:BT9727_3828.
PATRICi18988712. VBIBacThu119411_4082.

Phylogenomic databases

HOGENOMiHOG000008159.
KOiK01839.
OMAiYLGNCHA.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00173.
BioCyciBTHU281309:GJID-3901-MONOMER.

Family and domain databases

Gene3Di3.30.70.1250. 1 hit.
3.40.720.10. 2 hits.
HAMAPiMF_00740. Phosphopentomut. 1 hit.
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...

Entry informationi

Entry nameiDEOB_BACHK
AccessioniPrimary (citable) accession number: Q6HE79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: July 19, 2004
Last modified: September 7, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

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

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 one 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.