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Protein

Beta-phosphoglucomutase

Gene

yvdM

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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

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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi7 – 71Magnesium 1By similarity
Metal bindingi7 – 71Magnesium 2By similarity
Active sitei9 – 91Proton donorBy similarity
Metal bindingi9 – 91Magnesium 1By similarity
Metal bindingi9 – 91Magnesium 2; via carbonyl oxygenBy similarity
Binding sitei23 – 231SubstrateBy similarity
Binding sitei50 – 501SubstrateBy similarity
Binding sitei76 – 761SubstrateBy similarity
Sitei114 – 1141Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groupsBy similarity
Binding sitei145 – 1451SubstrateBy similarity
Sitei145 – 1451Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groupsBy similarity
Metal bindingi169 – 1691Magnesium 1By similarity
Metal bindingi170 – 1701Magnesium 1By similarity
Metal bindingi170 – 1701Magnesium 2By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Magnesium, 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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 226226Beta-phosphoglucomutasePRO_0000108051Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 714-aspartylphosphateBy similarity

Post-translational modificationi

Autophosphorylated.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO06995.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018716.

Structurei

Secondary structure

1
226
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Turni10 – 123Combined sources
Helixi15 – 2915Combined sources
Helixi36 – 416Combined sources
Turni42 – 443Combined sources
Helixi47 – 5711Combined sources
Turni61 – 633Combined sources
Helixi66 – 8520Combined sources
Helixi89 – 913Combined sources
Helixi96 – 10510Combined sources
Beta strandi109 – 1124Combined sources
Helixi119 – 1257Combined sources
Turni129 – 1313Combined sources
Beta strandi133 – 1353Combined sources
Helixi150 – 1589Combined sources
Helixi162 – 1643Combined sources
Beta strandi165 – 1695Combined sources
Helixi172 – 1809Combined sources
Beta strandi184 – 1874Combined sources
Helixi192 – 1943Combined sources
Beta strandi198 – 2003Combined sources
Helixi204 – 2063Combined sources
Helixi209 – 22113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NASX-ray3.00A/B2-224[»]
ProteinModelPortaliO06995.
SMRiO06995. Positions 1-223.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO06995.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 93Substrate bindingBy similarity
Regioni42 – 476Substrate bindingBy similarity
Regioni114 – 1185Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107URF. Bacteria.
COG0637. LUCA.
HOGENOMiHOG000248341.
InParanoidiO06995.
KOiK01838.
OMAiEAWHEIA.
OrthoDBiEOG6KMBB8.
PhylomeDBiO06995.

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]
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.
PATRICi18978914. VBIBacSub10457_3619.

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.
PIRiE70034.
RefSeqiNP_391335.1. NC_000964.3.
WP_003228210.1. NZ_JNCM01000033.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NASX-ray3.00A/B2-224[»]
ProteinModelPortaliO06995.
SMRiO06995. Positions 1-223.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018716.

Proteomic databases

PaxDbiO06995.

Protocols and materials databases

DNASUi938624.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15460; CAB15460; BSU34550.
GeneIDi938624.
KEGGibsu:BSU34550.
PATRICi18978914. VBIBacSub10457_3619.

Phylogenomic databases

eggNOGiENOG4107URF. Bacteria.
COG0637. LUCA.
HOGENOMiHOG000248341.
InParanoidiO06995.
KOiK01838.
OMAiEAWHEIA.
OrthoDBiEOG6KMBB8.
PhylomeDBiO06995.

Enzyme and pathway databases

BioCyciBSUB:BSU34550-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO06995.

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]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01990. bPGM. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR02009. PGMB-YQAB-SF. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Denizot F.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "The crystal structure of beta-phosphoglucomutase from bacillus subtilis."
    New York structural genomix research consortium (NYSGXRC)
    Submitted (JUL-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-224, SUBUNIT.

Entry informationi

Entry nameiPGMB_BACSU
AccessioniPrimary (citable) accession number: O06995
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: May 11, 2016
This is version 116 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. 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

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.