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Q03C44 (PAGL1_LACC3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. 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:
6-phospho-alpha-glucosidase 1

EC=3.2.1.122
Gene names
Name:simA
Ordered Locus Names:LSEI_0369
OrganismLactobacillus casei (strain ATCC 334) [Complete proteome] [HAMAP]
Taxonomic identifier321967 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length442 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Is probably involved in the catabolism of alpha-glycosides accumulated via a phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). Hydrolyzes a wide variety of 6-phospho-alpha-D-glucosides including the five isomeric derivatives of sucrose, i.e. trehalulose-6'-phosphate, turanose-6'-phosphate, maltulose-6'-phosphate, leucrose-6'-phosphate, and palatinose-6'-phosphate, but is not active on sucrose-6-phosphate. Can also hydrolyze maltose-6'-phosphate and methyl-alpha-glucose-6-phosphate, and poorly, trehalose-6-phosphate. Fails to hydrolyze beta-O-linked phosphorylated disaccharides such as cellobiose-6'-phosphate and gentiobiose-6'-phosphate. Does not seem to be involved in maltose catabolism. Ref.2

Catalytic activity

Alpha-maltose 6'-phosphate + H2O = D-glucose + D-glucose 6-phosphate. Ref.2

Cofactor

Binds 1 divalent metal ion per subunit. Mn2+ is the most efficient metal, but can also use Co2+, Ni2+ and Fe2+, and to a lesser extent Mg2+. Can not use Zn2+. Ref.2

Binds 1 NAD+ per subunit. Ref.2

Enzyme regulation

Is inhibited by EDTA in vitro. Ref.2

Subunit structure

Homodimer. May also form homotetramer. Ref.2

Induction

By maltulose, leucrose and palatinose, but not by maltose, glucose or sucrose. Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 4 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4424426-phospho-alpha-glucosidase 1
PRO_0000389204

Regions

Nucleotide binding6 – 7267NAD By similarity

Sites

Active site1721Proton donor Probable
Active site2651Proton acceptor Probable
Metal binding1711Manganese By similarity
Metal binding2021Manganese By similarity
Binding site951Substrate By similarity
Binding site1491Substrate By similarity
Binding site2851Substrate By similarity
Site1111Increases basicity of active site Tyr By similarity

Sequences

Sequence LengthMass (Da)Tools
Q03C44 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: AE4D60737BACD491

FASTA44249,842
        10         20         30         40         50         60 
MDDRKFSVLI AGGGSTYTPG IVLTLLDHIQ KFPLRKLKFY DIDGERQQRV ADACEILVKE 

        70         80         90        100        110        120 
RAPEVEFLAT TDPEEAFTDV DFVMAQIRVG KYAMRSLDEK IPLKHGVVGQ ETTGPGGIAY 

       130        140        150        160        170        180 
GLRSIPGVIG LVDYMEKYSP NAWMLNYSNP AAIVAEATRR LRPHSRIINI CDMPIGIMDR 

       190        200        210        220        230        240 
MAQIVGLKDR NDLVFRYYGL NHFGWWTDVR DKTGKDLMPA LKQYVAKNGY WLGDKDKDTE 

       250        260        270        280        290        300 
ASWVSTFKKA ADVYALDPST LPNTYLKYYL YPKYVVEHSD PNYTRTDEVE AYREKHVFDE 

       310        320        330        340        350        360 
CDRIIAAGTA ADTHFKSDDH ATYIVDLCTA IAYDTKQRML AIVPNDGAIE NIDPEAMVEV 

       370        380        390        400        410        420 
PCLFGANGAE RLAMGKAATF QKGLITEQNC VEKLTVDAFE QQSYTKLWEA MSLCKIVPDA 

       430        440 
SVAKEILDEM VVANKDYWPE LK 

« Hide

References

« Hide 'large scale' references
[1]"Comparative genomics of the lactic acid bacteria."
Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., Hawkins T. expand/collapse author list , Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.
Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 334.
[2]"The sim operon facilitates the transport and metabolism of sucrose isomers in Lactobacillus casei ATCC 334."
Thompson J., Jakubovics N., Abraham B., Hess S., Pikis A.
J. Bacteriol. 190:3362-3373(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-30, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR, CATALYTIC MECHANISM, INDUCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000423 Genomic DNA. Translation: ABJ69228.1.
RefSeqYP_805670.1. NC_008526.1.

3D structure databases

ProteinModelPortalQ03C44.
SMRQ03C44. Positions 4-441.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING321967.LSEI_0369.

Protein family/group databases

CAZyGH4. Glycoside Hydrolase Family 4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ69228; ABJ69228; LSEI_0369.
GeneID4421568.
KEGGlca:LSEI_0369.
PATRIC22204458. VBILacCas62221_0390.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1486.
HOGENOMHOG000239810.
KOK01232.
OMAGECRKVI.
OrthoDBEOG632D2X.
ProtClustDBCLSK880767.

Enzyme and pathway databases

BioCycLCAS321967:GH4S-368-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProIPR019802. GlycHydrolase_4_CS.
IPR001088. Glyco_hydro_4.
IPR022616. Glyco_hydro_4_C.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF02056. Glyco_hydro_4. 1 hit.
PF11975. Glyco_hydro_4C. 1 hit.
[Graphical view]
PRINTSPR00732. GLHYDRLASE4.
SUPFAMSSF56327. SSF56327. 1 hit.
PROSITEPS01324. GLYCOSYL_HYDROL_F4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePAGL1_LACC3
AccessionPrimary (citable) accession number: Q03C44
Entry history
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: November 14, 2006
Last modified: February 19, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries