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UniProtKB - O06995 (PGMB_BACSU)
Protein
Beta-phosphoglucomutase
Gene
yvdM
Organism
Bacillus subtilis (strain 168)
Status
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 similarityMiscellaneous
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
- EC:5.4.2.6
Cofactori
Mg2+By similarityNote: Binds 2 magnesium ions per subunit.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 7 | Magnesium 1By similarity | 1 | |
Metal bindingi | 7 | Magnesium 2By similarity | 1 | |
Active sitei | 9 | Proton donorBy similarity | 1 | |
Metal bindingi | 9 | Magnesium 1By similarity | 1 | |
Metal bindingi | 9 | Magnesium 2; via carbonyl oxygenBy similarity | 1 | |
Binding sitei | 23 | SubstrateBy similarity | 1 | |
Binding sitei | 50 | SubstrateBy similarity | 1 | |
Binding sitei | 76 | SubstrateBy similarity | 1 | |
Sitei | 114 | Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groupsBy similarity | 1 | |
Binding sitei | 145 | SubstrateBy similarity | 1 | |
Sitei | 145 | Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groupsBy similarity | 1 | |
Metal bindingi | 169 | Magnesium 1By similarity | 1 | |
Metal bindingi | 170 | Magnesium 1By similarity | 1 | |
Metal bindingi | 170 | Magnesium 2By similarity | 1 |
GO - Molecular functioni
- beta-phosphoglucomutase activity Source: UniProtKB
- magnesium ion binding Source: UniProtKB
GO - Biological processi
- carbohydrate metabolic process Source: UniProtKB
Keywordsi
Molecular function | Isomerase |
Biological process | Carbohydrate metabolism |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | BSUB:BSU34550-MONOMER |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:yvdM Ordered Locus Names:BSU34550 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm Curated
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000108051 | 1 – 226 | Beta-phosphoglucomutaseAdd BLAST | 226 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 7 | 4-aspartylphosphateBy similarity | 1 |
Post-translational modificationi
Autophosphorylated.By similarity
Keywords - PTMi
PhosphoproteinProteomic databases
PaxDbi | O06995 |
Interactioni
Subunit structurei
Homodimer.
1 PublicationProtein-protein interaction databases
STRINGi | 224308.BSU34550 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | O06995 |
SMRi | O06995 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | O06995 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 7 – 9 | Substrate bindingBy similarity | 3 | |
Regioni | 42 – 47 | Substrate bindingBy similarity | 6 | |
Regioni | 114 – 118 | Substrate bindingBy similarity | 5 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0637, Bacteria |
InParanoidi | O06995 |
OMAi | ANGYHIV |
PhylomeDBi | O06995 |
Family and domain databases
CDDi | cd02598, HAD_BPGM, 1 hit |
Gene3Di | 1.10.150.240, 1 hit 3.40.50.1000, 1 hit |
InterProi | View protein in InterPro IPR010976, B-phosphoglucomutase_hydrolase IPR010972, Beta-phosphoglucomutase IPR036412, HAD-like_sf IPR006439, HAD-SF_hydro_IA IPR041492, HAD_2 IPR023214, HAD_sf IPR023198, PGP-like_dom2 |
Pfami | View protein in Pfam PF13419, HAD_2, 1 hit |
SUPFAMi | SSF56784, SSF56784, 1 hit |
TIGRFAMsi | TIGR01990, bPGM, 1 hit TIGR01509, HAD-SF-IA-v3, 1 hit TIGR02009, PGMB-YQAB-SF, 1 hit |
i Sequence
Sequence statusi: Complete.
O06995-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z94043 Genomic DNA Translation: CAB08042.1 AL009126 Genomic DNA Translation: CAB15460.1 |
PIRi | E70034 |
RefSeqi | NP_391335.1, NC_000964.3 WP_003228210.1, NZ_JNCM01000033.1 |
Genome annotation databases
EnsemblBacteriai | CAB15460; CAB15460; BSU_34550 |
GeneIDi | 938624 |
KEGGi | bsu:BSU34550 |
PATRICi | fig|224308.179.peg.3742 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z94043 Genomic DNA Translation: CAB08042.1 AL009126 Genomic DNA Translation: CAB15460.1 |
PIRi | E70034 |
RefSeqi | NP_391335.1, NC_000964.3 WP_003228210.1, NZ_JNCM01000033.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3NAS | X-ray | 3.00 | A/B | 2-224 | [»] | |
AlphaFoldDBi | O06995 | |||||
SMRi | O06995 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 224308.BSU34550 |
Proteomic databases
PaxDbi | O06995 |
Protocols and materials databases
DNASUi | 938624 |
Genome annotation databases
EnsemblBacteriai | CAB15460; CAB15460; BSU_34550 |
GeneIDi | 938624 |
KEGGi | bsu:BSU34550 |
PATRICi | fig|224308.179.peg.3742 |
Phylogenomic databases
eggNOGi | COG0637, Bacteria |
InParanoidi | O06995 |
OMAi | ANGYHIV |
PhylomeDBi | O06995 |
Enzyme and pathway databases
BioCyci | BSUB:BSU34550-MONOMER |
Miscellaneous databases
EvolutionaryTracei | O06995 |
Family and domain databases
CDDi | cd02598, HAD_BPGM, 1 hit |
Gene3Di | 1.10.150.240, 1 hit 3.40.50.1000, 1 hit |
InterProi | View protein in InterPro IPR010976, B-phosphoglucomutase_hydrolase IPR010972, Beta-phosphoglucomutase IPR036412, HAD-like_sf IPR006439, HAD-SF_hydro_IA IPR041492, HAD_2 IPR023214, HAD_sf IPR023198, PGP-like_dom2 |
Pfami | View protein in Pfam PF13419, HAD_2, 1 hit |
SUPFAMi | SSF56784, SSF56784, 1 hit |
TIGRFAMsi | TIGR01990, bPGM, 1 hit TIGR01509, HAD-SF-IA-v3, 1 hit TIGR02009, PGMB-YQAB-SF, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PGMB_BACSU | |
Accessioni | O06995Primary (citable) accession number: O06995 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 15, 1998 |
Last sequence update: | July 1, 1997 | |
Last modified: | May 25, 2022 | |
This is version 140 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families