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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)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

BioCyciBCER226900:GJEU-4083-MONOMER.
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394PhosphopentomutasePRO_0000199807Add
BLAST

Proteomic databases

PRIDEiQ818Z9.

Interactioni

Protein-protein interaction databases

STRINGi226900.BC4087.

Structurei

Secondary structure

1
394
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 128Combined sources
Helixi23 – 264Combined sources
Helixi33 – 408Combined sources
Helixi47 – 526Combined sources
Helixi54 – 574Combined sources
Beta strandi70 – 767Combined sources
Helixi85 – 928Combined sources
Helixi110 – 12011Combined sources
Beta strandi124 – 1296Combined sources
Helixi132 – 14615Combined sources
Beta strandi149 – 1535Combined sources
Beta strandi155 – 16410Combined sources
Turni165 – 1673Combined sources
Helixi170 – 18314Combined sources
Helixi187 – 1893Combined sources
Beta strandi192 – 20211Combined sources
Beta strandi205 – 2084Combined sources
Beta strandi213 – 2164Combined sources
Helixi224 – 2307Combined sources
Beta strandi234 – 2385Combined sources
Helixi241 – 2444Combined sources
Turni245 – 2495Combined sources
Beta strandi251 – 2544Combined sources
Helixi259 – 27012Combined sources
Beta strandi275 – 2828Combined sources
Helixi284 – 2885Combined sources
Turni289 – 2935Combined sources
Helixi295 – 30612Combined sources
Helixi309 – 3157Combined sources
Beta strandi320 – 3256Combined sources
Beta strandi327 – 3293Combined sources
Beta strandi332 – 3387Combined sources
Beta strandi344 – 3496Combined sources
Beta strandi363 – 3653Combined sources
Helixi367 – 37711Combined sources
Helixi389 – 3913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-392.
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
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. Positions 2-392.
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.
BioCyciBCER226900:GJEU-4083-MONOMER.
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: September 7, 2016
This is version 90 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.