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Protein

Beta-phosphoglucomutase

Gene

yvdM

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and 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. 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 (By similarity).By similarity

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

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds 2 magnesium ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi7Magnesium 1By similarity1
Metal bindingi7Magnesium 2By similarity1
Active sitei9Proton donorBy similarity1
Metal bindingi9Magnesium 1By similarity1
Metal bindingi9Magnesium 2; via carbonyl oxygenBy similarity1
Binding sitei23SubstrateBy similarity1
Binding sitei50SubstrateBy similarity1
Binding sitei76SubstrateBy similarity1
Sitei114Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groupsBy similarity1
Binding sitei145SubstrateBy similarity1
Sitei145Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groupsBy similarity1
Metal bindingi169Magnesium 1By similarity1
Metal bindingi170Magnesium 1By similarity1
Metal bindingi170Magnesium 2By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase
Biological processCarbohydrate metabolism
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU34550-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-phosphoglucomutase (EC:5.4.2.6)
Short name:
Beta-PGM
Gene namesi
Name:yvdM
Ordered Locus Names:BSU34550
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001080511 – 226Beta-phosphoglucomutaseAdd BLAST226

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei74-aspartylphosphateBy similarity1

Post-translational modificationi

Autophosphorylated.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO06995
PRIDEiO06995

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018716

Structurei

Secondary structure

1226
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 6Combined sources4
Turni10 – 12Combined sources3
Helixi15 – 29Combined sources15
Helixi36 – 41Combined sources6
Turni42 – 44Combined sources3
Helixi47 – 57Combined sources11
Turni61 – 63Combined sources3
Helixi66 – 85Combined sources20
Helixi89 – 91Combined sources3
Helixi96 – 105Combined sources10
Beta strandi109 – 112Combined sources4
Helixi119 – 125Combined sources7
Turni129 – 131Combined sources3
Beta strandi133 – 135Combined sources3
Helixi150 – 158Combined sources9
Helixi162 – 164Combined sources3
Beta strandi165 – 169Combined sources5
Helixi172 – 180Combined sources9
Beta strandi184 – 187Combined sources4
Helixi192 – 194Combined sources3
Beta strandi198 – 200Combined sources3
Helixi204 – 206Combined sources3
Helixi209 – 221Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NASX-ray3.00A/B2-224[»]
ProteinModelPortaliO06995
SMRiO06995
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO06995

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni7 – 9Substrate bindingBy similarity3
Regioni42 – 47Substrate bindingBy similarity6
Regioni114 – 118Substrate bindingBy similarity5

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107URF Bacteria
COG0637 LUCA
HOGENOMiHOG000248341
InParanoidiO06995
KOiK01838
OMAiAAWKEMF
PhylomeDBiO06995

Family and domain databases

Gene3Di1.10.150.240, 1 hit
3.40.50.1000, 2 hits
InterProiView protein in InterPro
IPR010976 B-phosphoglucomutase_hydrolase
IPR010972 Beta-phosphoglucomutase
IPR036412 HAD-like_sf
IPR006439 HAD-SF_hydro_IA
IPR023214 HAD_sf
IPR023198 PGP-like_dom2
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.

O06995-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAVIFDLDG VITDTAEYHF LAWKHIAEQI DIPFDRDMNE RLKGISREES
60 70 80 90 100
LESILIFGGA ETKYTNAEKQ ELMHRKNRDY QMLISKLTPE DLLPGIGRLL
110 120 130 140 150
CQLKNENIKI GLASSSRNAP KILRRLAIID DFHAIVDPTT LAKGKPDPDI
160 170 180 190 200
FLTAAAMLDV SPADCAAIED AEAGISAIKS AGMFAVGVGQ GQPMLGADLV
210 220
VRQTSDLTLE LLHEEWEQYR IRESIP
Length:226
Mass (Da):25,102
Last modified:July 1, 1997 - v1
Checksum:i593851AE23BF9DA7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z94043 Genomic DNA Translation: CAB08042.1
AL009126 Genomic DNA Translation: CAB15460.1
PIRiE70034
RefSeqiNP_391335.1, NC_000964.3
WP_003228210.1, NZ_JNCM01000033.1

Genome annotation databases

EnsemblBacteriaiCAB15460; CAB15460; BSU34550
GeneIDi938624
KEGGibsu:BSU34550
PATRICifig|224308.179.peg.3742

Entry informationi

Entry nameiPGMB_BACSU
AccessioniPrimary (citable) accession number: O06995
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: May 23, 2018
This is version 126 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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