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Protein

Phosphopentomutase

Gene

deoB

Organism
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
Metal bindingi13ManganeseUniRule annotation1
Metal bindingi291ManganeseUniRule annotation1
Metal bindingi327ManganeseUniRule annotation1
Metal bindingi328ManganeseUniRule annotation1
Metal bindingi339ManganeseUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi5.4.2.7. 648.
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:BC_4087
OrganismiBacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Taxonomic identifieri226900 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000001417 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001998071 – 394PhosphopentomutaseAdd BLAST394

Proteomic databases

PRIDEiQ818Z9.

Interactioni

Protein-protein interaction databases

STRINGi226900.BC4087.

Structurei

Secondary structure

1394
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 12Combined sources8
Helixi23 – 26Combined sources4
Helixi33 – 40Combined sources8
Helixi47 – 52Combined sources6
Helixi54 – 57Combined sources4
Beta strandi70 – 76Combined sources7
Helixi85 – 92Combined sources8
Helixi110 – 120Combined sources11
Beta strandi124 – 129Combined sources6
Helixi132 – 146Combined sources15
Beta strandi149 – 153Combined sources5
Beta strandi155 – 164Combined sources10
Turni165 – 167Combined sources3
Helixi170 – 183Combined sources14
Helixi187 – 189Combined sources3
Beta strandi192 – 202Combined sources11
Beta strandi205 – 208Combined sources4
Beta strandi213 – 216Combined sources4
Helixi224 – 230Combined sources7
Beta strandi234 – 238Combined sources5
Helixi241 – 244Combined sources4
Turni245 – 249Combined sources5
Beta strandi251 – 254Combined sources4
Helixi259 – 270Combined sources12
Beta strandi275 – 282Combined sources8
Helixi284 – 288Combined sources5
Turni289 – 293Combined sources5
Helixi295 – 306Combined sources12
Helixi309 – 315Combined sources7
Beta strandi320 – 325Combined sources6
Beta strandi327 – 329Combined sources3
Beta strandi332 – 338Combined sources7
Beta strandi344 – 349Combined sources6
Beta strandi363 – 365Combined sources3
Helixi367 – 377Combined sources11
Helixi389 – 391Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3M8WX-ray1.85A/B/C2-394[»]
3M8YX-ray2.10A/B/C2-394[»]
3M8ZX-ray1.80A/B/C2-394[»]
3OT9X-ray1.75A/B/C2-394[»]
3TWZX-ray1.75A2-394[»]
3TX0X-ray2.26A2-394[»]
3UN2X-ray1.80A/B/C2-394[»]
3UN3X-ray1.80A/B/C2-394[»]
3UN5X-ray1.80A/B/C/D/E/F2-394[»]
3UNYX-ray1.95A/B/C/D/E/F2-394[»]
3UO0X-ray2.30A/B/C2-394[»]
4LR7X-ray2.10A/B/C2-394[»]
4LR8X-ray2.00A/B/C2-394[»]
4LR9X-ray2.10A/B/C2-394[»]
4LRAX-ray2.00A/B/C2-394[»]
4LRBX-ray2.00A/B/C2-394[»]
4LRCX-ray1.89A/B/C2-394[»]
4LRDX-ray1.78A2-394[»]
4LREX-ray2.10A/B/C2-394[»]
4LRFX-ray2.00A/B/C2-394[»]
ProteinModelPortaliQ818Z9.
SMRiQ818Z9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ818Z9.

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphopentomutase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CZG. Bacteria.
COG1015. LUCA.
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.

Q818Z9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKYKRIFLV VMDSVGIGEA PDAEQFGDLG SDTIGHIAEH MNGLQMPNMV
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 EVFAKLKEDD LLLITADHGN DPIHPGTDHT REYVPLLAYS
360 370 380 390
PSMKEGGQEL PLRQTFADIG ATVAENFGVK MPEYGTSFLN ELKK
Length:394
Mass (Da):44,020
Last modified:June 1, 2003 - v1
Checksum:i0B1E0804BC5FFAD2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP11006.1.
RefSeqiNP_833805.1. NC_004722.1.
WP_001046079.1. NC_004722.1.

Genome annotation databases

EnsemblBacteriaiAAP11006; AAP11006; BC_4087.
GeneIDi1206432.
KEGGibce:BC4087.
PATRICi32604238. VBIBacCer54481_4222.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP11006.1.
RefSeqiNP_833805.1. NC_004722.1.
WP_001046079.1. NC_004722.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3M8WX-ray1.85A/B/C2-394[»]
3M8YX-ray2.10A/B/C2-394[»]
3M8ZX-ray1.80A/B/C2-394[»]
3OT9X-ray1.75A/B/C2-394[»]
3TWZX-ray1.75A2-394[»]
3TX0X-ray2.26A2-394[»]
3UN2X-ray1.80A/B/C2-394[»]
3UN3X-ray1.80A/B/C2-394[»]
3UN5X-ray1.80A/B/C/D/E/F2-394[»]
3UNYX-ray1.95A/B/C/D/E/F2-394[»]
3UO0X-ray2.30A/B/C2-394[»]
4LR7X-ray2.10A/B/C2-394[»]
4LR8X-ray2.00A/B/C2-394[»]
4LR9X-ray2.10A/B/C2-394[»]
4LRAX-ray2.00A/B/C2-394[»]
4LRBX-ray2.00A/B/C2-394[»]
4LRCX-ray1.89A/B/C2-394[»]
4LRDX-ray1.78A2-394[»]
4LREX-ray2.10A/B/C2-394[»]
4LRFX-ray2.00A/B/C2-394[»]
ProteinModelPortaliQ818Z9.
SMRiQ818Z9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226900.BC4087.

Proteomic databases

PRIDEiQ818Z9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP11006; AAP11006; BC_4087.
GeneIDi1206432.
KEGGibce:BC4087.
PATRICi32604238. VBIBacCer54481_4222.

Phylogenomic databases

eggNOGiENOG4105CZG. Bacteria.
COG1015. LUCA.
KOiK01839.
OMAiYLGNCHA.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00173.
BRENDAi5.4.2.7. 648.

Miscellaneous databases

EvolutionaryTraceiQ818Z9.

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_BACCR
AccessioniPrimary (citable) accession number: Q818Z9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 92 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.