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Protein

Beta-phosphoglucomutase

Gene

ycjU

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C1 anomer of G1P. Glucose or lactose are used in preference to maltose, which is only utilized after glucose or lactose has been exhausted. It plays a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose.1 Publication

Catalytic activityi

Beta-D-glucose 1-phosphate = beta-D-glucose 6-phosphate.

Cofactori

Mg2+1 PublicationNote: Binds 2 magnesium ions per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi9Magnesium 1By similarity1
Metal bindingi9Magnesium 2By similarity1
Active sitei11Proton donorBy similarity1
Metal bindingi11Magnesium 1By similarity1
Metal bindingi11Magnesium 2; via carbonyl oxygenBy similarity1
Binding sitei25SubstrateBy similarity1
Binding sitei52SubstrateBy similarity1
Binding sitei78SubstrateBy similarity1
Sitei116Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groupsBy similarity1
Binding sitei147SubstrateBy similarity1
Sitei147Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groupsBy similarity1
Metal bindingi171Magnesium 1By similarity1
Metal bindingi172Magnesium 1By similarity1
Metal bindingi172Magnesium 2By similarity1

GO - Molecular functioni

  • beta-phosphoglucomutase activity Source: EcoCyc
  • magnesium ion binding Source: UniProtKB
  • phosphatase activity Source: GO_Central

GO - Biological processi

  • carbohydrate metabolic process Source: UniProtKB
  • cellular response to DNA damage stimulus Source: EcoCyc
  • DNA mediated transformation Source: EcoCyc
  • response to antibiotic Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:G6655-MONOMER.
ECOL316407:JW1310-MONOMER.
MetaCyc:G6655-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-phosphoglucomutase (EC:5.4.2.6)
Short name:
Beta-PGM
Gene namesi
Name:ycjU
Ordered Locus Names:b1317, JW1310
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13918. ycjU.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are only slightly more susceptible to nalidixic acid, but are more sensitive to UV irradiation than the wild-type.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001080521 – 219Beta-phosphoglucomutaseAdd BLAST219

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei94-aspartylphosphateBy similarity1

Post-translational modificationi

Autophosphorylated.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP77366.
PaxDbiP77366.
PRIDEiP77366.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi4263195. 16 interactors.
IntActiP77366. 1 interactor.
STRINGi511145.b1317.

Structurei

Secondary structure

1219
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Turni11 – 13Combined sources3
Helixi18 – 31Combined sources14
Helixi40 – 44Combined sources5
Helixi49 – 59Combined sources11
Helixi63 – 65Combined sources3
Helixi68 – 87Combined sources20
Helixi91 – 93Combined sources3
Helixi98 – 107Combined sources10
Beta strandi111 – 114Combined sources4
Helixi121 – 127Combined sources7
Helixi131 – 133Combined sources3
Beta strandi135 – 137Combined sources3
Helixi140 – 142Combined sources3
Helixi151 – 160Combined sources10
Helixi164 – 166Combined sources3
Beta strandi167 – 173Combined sources7
Helixi174 – 183Combined sources10
Beta strandi186 – 191Combined sources6
Beta strandi198 – 203Combined sources6
Helixi204 – 206Combined sources3
Helixi209 – 219Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4G9BX-ray1.70A1-219[»]
ProteinModelPortaliP77366.
SMRiP77366.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni9 – 11Substrate bindingBy similarity3
Regioni44 – 49Substrate bindingBy similarity6
Regioni116 – 120Substrate bindingBy similarity5

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107URF. Bacteria.
COG0637. LUCA.
HOGENOMiHOG000248341.
InParanoidiP77366.
KOiK01838.
OMAiKYHYLAW.
PhylomeDBiP77366.

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR010976. B-phosphoglucomutase_hydrolase.
IPR010972. Beta-phosphoglucomutase.
IPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR023198. PGP_dom2.
[Graphical view]
PfamiPF13419. HAD_2. 1 hit.
[Graphical view]
PRINTSiPR00413. HADHALOGNASE.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01990. bPGM. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR02009. PGMB-YQAB-SF. 1 hit.

Sequencei

Sequence statusi: Complete.

P77366-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLQGVIFDL DGVITDTAHL HFQAWQQIAA EIGISIDAQF NESLKGISRD
60 70 80 90 100
ESLRRILQHG GKEGDFNSQE RAQLAYRKNL LYVHSLRELT VNAVLPGIRS
110 120 130 140 150
LLADLRAQQI SVGLASVSLN APTILAALEL REFFTFCADA SQLKNSKPDP
160 170 180 190 200
EIFLAACAGL GVPPQACIGI EDAQAGIDAI NASGMRSVGI GAGLTGAQLL
210
LPSTESLTWP RLSAFWQNV
Length:219
Mass (Da):23,565
Last modified:February 1, 1997 - v1
Checksum:i1FE8C3CAE4EAE717
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74399.1.
AP009048 Genomic DNA. Translation: BAA14892.1.
PIRiH64880.
RefSeqiNP_415833.1. NC_000913.3.
WP_000775794.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74399; AAC74399; b1317.
BAA14892; BAA14892; BAA14892.
GeneIDi945891.
KEGGiecj:JW1310.
eco:b1317.
PATRICi32117906. VBIEscCol129921_1373.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74399.1.
AP009048 Genomic DNA. Translation: BAA14892.1.
PIRiH64880.
RefSeqiNP_415833.1. NC_000913.3.
WP_000775794.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4G9BX-ray1.70A1-219[»]
ProteinModelPortaliP77366.
SMRiP77366.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263195. 16 interactors.
IntActiP77366. 1 interactor.
STRINGi511145.b1317.

Proteomic databases

EPDiP77366.
PaxDbiP77366.
PRIDEiP77366.

Protocols and materials databases

DNASUi945891.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74399; AAC74399; b1317.
BAA14892; BAA14892; BAA14892.
GeneIDi945891.
KEGGiecj:JW1310.
eco:b1317.
PATRICi32117906. VBIEscCol129921_1373.

Organism-specific databases

EchoBASEiEB3677.
EcoGeneiEG13918. ycjU.

Phylogenomic databases

eggNOGiENOG4107URF. Bacteria.
COG0637. LUCA.
HOGENOMiHOG000248341.
InParanoidiP77366.
KOiK01838.
OMAiKYHYLAW.
PhylomeDBiP77366.

Enzyme and pathway databases

BioCyciEcoCyc:G6655-MONOMER.
ECOL316407:JW1310-MONOMER.
MetaCyc:G6655-MONOMER.

Miscellaneous databases

PROiP77366.

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR010976. B-phosphoglucomutase_hydrolase.
IPR010972. Beta-phosphoglucomutase.
IPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR023198. PGP_dom2.
[Graphical view]
PfamiPF13419. HAD_2. 1 hit.
[Graphical view]
PRINTSiPR00413. HADHALOGNASE.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01990. bPGM. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR02009. PGMB-YQAB-SF. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPGMB_ECOLI
AccessioniPrimary (citable) accession number: P77366
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: November 2, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The catalysis proceeds via a phosphoenzyme formed by reaction of an active-site nucleophile with the cofactor glucose 1,6-diphosphate (G1,6-diP). The phosphorylated mutase binds either G1P or G6P and transfers the phosphoryl group to the C6OH or C1OH, respectively (By similarity).By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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.