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P71447 (PGMB_LACLA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-phosphoglucomutase

Short name=Beta-PGM
EC=5.4.2.6
Gene names
Name:pgmB
Ordered Locus Names:LL0429
ORF Names:L0001
OrganismLactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Taxonomic identifier272623 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length221 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reversible transformation of glucose 6-phosphate and beta-glucose 1-phosphate.

Catalytic activity

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

Induction

By maltose, trehalose and sucrose and repressed by glucose and lactose.

Sequence similarities

Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family.

Biophysicochemical properties

Kinetic parameters:

KM=4.6 µM for beta-glucose 1-phosphate (at pH 7 and 25 degrees Celsius)

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 221221Beta-phosphoglucomutase
PRO_0000108053

Experimental info

Mutagenesis451K → A: 20'000-fold decrease in Kcat/KM. Ref.3
Mutagenesis461G → A: 1'000'000-fold decrease in Kcat/KM. Ref.3
Mutagenesis461G → P: 100'000-fold decrease in Kcat/KM. Ref.3
Mutagenesis461G → V: 10'000-fold decrease in Kcat/KM. Ref.3
Mutagenesis491R → K: 1'000'000-fold decrease in Kcat/KM. Ref.3
Mutagenesis521S → A: Wild-type activity. Ref.3
Sequence conflict1251K → R in CAA94734. Ref.1
Sequence conflict2061Y → H in CAA94734. Ref.1

Secondary structure

............................................... 221
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P71447 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: 53AC0BF0FA249EFC

FASTA22124,209
        10         20         30         40         50         60 
MFKAVLFDLD GVITDTAEYH FRAWKALAEE IGINGVDRQF NEQLKGVSRE DSLQKILDLA 

        70         80         90        100        110        120 
DKKVSAEEFK ELAKRKNDNY VKMIQDVSPA DVYPGILQLL KDLRSNKIKI ALASASKNGP 

       130        140        150        160        170        180 
FLLEKMNLTG YFDAIADPAE VAASKPAPDI FIAAAHAVGV APSESIGLED SQAGIQAIKD 

       190        200        210        220 
SGALPIGVGR PEDLGDDIVI VPDTSYYTLE FLKEVWLQKQ K 

« Hide

References

« Hide 'large scale' references
[1]"Product formation and phosphoglucomutase activities in Lactococcus lactis: cloning and characterization of a novel phosphoglucomutase gene."
Qian N., Stanley G.A., Bunte A., Raadstroem P.
Microbiology 143:855-865(1997) [PubMed: 9084169] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15.
Strain: ATCC 19435 / DSM 20481 / NCDO 604 / NCIB 6681 / NCTC 6681.
[2]"The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403."
Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A.
Genome Res. 11:731-753(2001) [PubMed: 11337471] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IL1403.
[3]"Analysis of the substrate specificity loop of the HAD superfamily cap domain."
Lahiri S.D., Zhang G., Dai J., Dunaway-Mariano D., Allen K.N.
Biochemistry 43:2812-2820(2004) [PubMed: 15005616] [Abstract]
Cited for: BIOPHYSICOCHEMICAL CHARACTERIZATION, MUTAGENESIS OF LYS-45; GLY-46; ARG-49 AND SER-52.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z70730 Genomic DNA. Translation: CAA94734.1.
AE005176 Genomic DNA. Translation: AAK04527.1.
PIRE86678.
RefSeqNP_266585.1. NC_002662.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LVHX-ray2.30A/B1-221[»]
1O03X-ray1.40A1-221[»]
1O08X-ray1.20A1-221[»]
1Z4NX-ray1.97A/B1-221[»]
1Z4OX-ray1.90A/B1-221[»]
1ZOLX-ray1.90A1-221[»]
2WF5X-ray1.30A1-221[»]
2WF6X-ray1.40A1-221[»]
2WF7X-ray1.05A1-221[»]
2WF8X-ray1.20A1-221[»]
2WF9X-ray1.40A1-221[»]
2WFAX-ray1.65A1-221[»]
2WHEX-ray1.55A1-221[»]
3FM9X-ray2.70A1-221[»]
ProteinModelPortalP71447.
SMRP71447. Positions 1-221.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1114041.
GenomeReviewsGene locus LL0429 in contig AE005176_GR.
KEGGlla:L0001.
NMPDRfig|272623.1.peg.438.
PATRIC22293074. VBILacLac136773_0467.

Phylogenomic databases

HOGENOMHBG742904.
OMAYIVDANE.
ProtClustDBCLSK876745.

Enzyme and pathway databases

BioCycLLAC272623:L0001-MONOMER.
MetaCyc:MONOMER-5821.
BRENDA5.4.2.6. 2903.

Family and domain databases

InterProIPR010976. B-phosphoglucomutase_hydrolase.
IPR010972. Beta-phosphoglucomutase.
IPR005834. Dehalogen-like_hydro.
IPR023214. HAD-like_dom.
IPR006402. HAD-SF_hydro_IA_v3.
IPR005833. Haloacid_DH/epoxide_hydro.
[Graphical view]
Gene3DG3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KOK01838.
PfamPF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00413. HADHALOGNASE.
SUPFAMSSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01990. BPGM. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR02009. PGMB-YQAB-SF. 1 hit.
ProtoNetSearch...

Entry information

Entry namePGMB_LACLA
AccessionPrimary (citable) accession number: P71447
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: April 27, 2001
Last modified: January 25, 2012
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families