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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi9 – 91Magnesium 1By similarity
Metal bindingi9 – 91Magnesium 2By similarity
Active sitei11 – 111Proton donorBy similarity
Metal bindingi11 – 111Magnesium 1By similarity
Metal bindingi11 – 111Magnesium 2; via carbonyl oxygenBy similarity
Binding sitei25 – 251SubstrateBy similarity
Binding sitei52 – 521SubstrateBy similarity
Binding sitei78 – 781SubstrateBy similarity
Sitei116 – 1161Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groupsBy similarity
Binding sitei147 – 1471SubstrateBy similarity
Sitei147 – 1471Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groupsBy similarity
Metal bindingi171 – 1711Magnesium 1By similarity
Metal bindingi172 – 1721Magnesium 1By similarity
Metal bindingi172 – 1721Magnesium 2By similarity

GO - Molecular functioni

  • beta-phosphoglucomutase activity Source: EcoCyc
  • hydrolase activity Source: InterPro
  • magnesium ion binding Source: UniProtKB

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 219219Beta-phosphoglucomutasePRO_0000108052Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 914-aspartylphosphateBy similarity

Post-translational modificationi

Autophosphorylated.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP77366.
PaxDbiP77366.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi4263195. 16 interactions.
IntActiP77366. 1 interaction.
STRINGi511145.b1317.

Structurei

Secondary structure

1
219
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Turni11 – 133Combined sources
Helixi18 – 3114Combined sources
Helixi40 – 445Combined sources
Helixi49 – 5911Combined sources
Helixi63 – 653Combined sources
Helixi68 – 8720Combined sources
Helixi91 – 933Combined sources
Helixi98 – 10710Combined sources
Beta strandi111 – 1144Combined sources
Helixi121 – 1277Combined sources
Helixi131 – 1333Combined sources
Beta strandi135 – 1373Combined sources
Helixi140 – 1423Combined sources
Helixi151 – 16010Combined sources
Helixi164 – 1663Combined sources
Beta strandi167 – 1737Combined sources
Helixi174 – 18310Combined sources
Beta strandi186 – 1916Combined sources
Beta strandi198 – 2036Combined sources
Helixi204 – 2063Combined sources
Helixi209 – 21911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4G9BX-ray1.70A1-219[»]
ProteinModelPortaliP77366.
SMRiP77366. Positions 1-219.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni9 – 113Substrate bindingBy similarity
Regioni44 – 496Substrate bindingBy similarity
Regioni116 – 1205Substrate bindingBy similarity

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
EntryMethodResolution (Å)ChainPositionsPDBsum
4G9BX-ray1.70A1-219[»]
ProteinModelPortaliP77366.
SMRiP77366. Positions 1-219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263195. 16 interactions.
IntActiP77366. 1 interaction.
STRINGi511145.b1317.

Proteomic databases

EPDiP77366.
PaxDbiP77366.

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: September 7, 2016
This is version 120 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.