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Q09HN2 (BGAL_PLASL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 29. 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-galactosidase BgaP

Short name=Beta-gal
EC=3.2.1.23
Gene names
Name:bgaP
Synonyms:galP
OrganismPlanococcus sp. (strain L4)
Taxonomic identifier377621 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPlanococcaceaePlanococcus

Protein attributes

Sequence length676 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes lactose, o-nitrophenyl-beta-D-galactopyranoside (ONPG), p-nitrophenyl-beta-D-galactopyranoside (PNPG), 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-gal), o-nitrophenyl-beta-D-fucopyranoside, p-nitrophenyl-beta-D-mannoside, o-nitrophenyl-beta-D-glucoside, p-nitrophenyl-beta-D-xyloside, p-nitrophenyl-beta-D-cellobioside, p-nitrophenyl-beta-D-arabinoside, p-nitrophenyl-beta-D-lactoside, p-nitrophenyl-beta-D-galacturonide, p-nitrophenyl-beta-D-glucuronide and p-nitrophenyl-alpha-D-galactoside with highest level of activity with ONPG as substrate, intermediate level of activity with PNPG and lower levels of activity with all other chromogenic nitrophenyl analogs. Able to hydrolyze 34% of milk lactose after 60 minutes at 5 degrees Celsius. Ref.1

Catalytic activity

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Ref.1

Enzyme regulation

No activity lost during treatment with 100 mM EDTA after 2 hours, and the addition of 1 mM MgCl2, 1 mM CaCl2 or 1 mM MnCl2 has no effect. However, the enzyme activity is inhibited by Zn2+, Cu2+, Ni2+ and Co2+ to different extents. Addition of Na+ or K+ slightly stimulates the enzyme activity at low concentrations and the optimal concentration is 250 mM. A further increase of their concentration of ions above the optimum value results in a decrease in enzyme activity. The enzyme is still active even in the presence of Na+ or K+ at a concentration up to 5 M. Ref.1

Subunit structure

Homodimer. Ref.1

Biotechnological use

Could conceivably be developed to fulfill the practical requirements to enable its use for lactose removal in milk and dairy products at low temperature or a reporter enzyme for psychrophilic genetic systems. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 42 family.

Biophysicochemical properties

Kinetic parameters:

KM=5.4 mM for ONPG (at 5 degrees Celsius and at pH 6.8) Ref.1

KM=3.8 mM for ONPG (at 10 degrees Celsius and at pH 6.8)

KM=2.9 mM for ONPG (at 20 degrees Celsius and at pH 6.8)

KM=20.4 mM for lactose (at 5 degrees Celsius and at pH 6.8)

KM=11.2 mM for lactose (at 10 degrees Celsius and at pH 6.8)

KM=10.4 mM for lactose (at 20 degrees Celsius and at pH 6.8)

pH dependence:

Optimum pH is 6.8. Exhibits above 80% of its maximal activity in the pH range 6.0-8.0 using ONPG as substrate at 20 degrees Celsius.

Temperature dependence:

Optimum temperature is 20 degrees Celsius. Lowering or raising the temperature from 20 degrees Celsius results in reduction of activity when ONPG is used as substrate. Rather stable at or below 25 degrees Celsius, but loses 58% of activity after 30 minutes at 40 degrees Celsius. Loses all activity in only 10 minutes at 45 degrees Celsius. Exhibits 27% of maximal activity even at 0 degrees Celsius, but enzyme activity decreases with a further increase in temperature until it is undetectable above 50 degrees Celsius.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological_processgalactose metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentbeta-galactosidase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionbeta-galactosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 676676Beta-galactosidase BgaP
PRO_0000407693

Regions

Region356 – 3594Substrate binding

Sites

Active site1511Proton donor By similarity
Active site3081Nucleophile By similarity
Metal binding1161Zinc By similarity
Metal binding1561Zinc By similarity
Metal binding1581Zinc By similarity
Metal binding1611Zinc By similarity
Binding site1121Substrate By similarity
Binding site1501Substrate By similarity
Binding site3161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q09HN2 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 6A2354F4544A752E

FASTA67677,312
        10         20         30         40         50         60 
MINDKLPKIW HGGDYNPEQW DSQEIWDEDV RMFKLAGIDV ATLNVFSWAL NQPNEDTYNF 

        70         80         90        100        110        120 
EWLDDKINRL YENGIYTCLA TSTAAHPAWM AKKYPDVLRV DFYGRKRKFG SRHNSCPNSP 

       130        140        150        160        170        180 
TYREYSEKIA DKLAERYKDH PAVLIWHVSN EYGGYCYCDN CQDAFRVWLS DKYGTLEKLN 

       190        200        210        220        230        240 
KAWNTGFWGH TFYEWDEIVA PNMLSEERED NVSDFQGISL DYRRFQSDSL LDCYKLEYNA 

       250        260        270        280        290        300 
IRKHTPNIPI TTNLMGTYPM LDYFKWAKEM DVVSWDNYPA IDTPFSYTAM THDLMRGLKS 

       310        320        330        340        350        360 
GQPFMLMEQT PSQQNWQPYN SLKRPGVMRL WSYQAIGRGA DTILYFQLRR SVGACEKYHG 

       370        380        390        400        410        420 
AVIEHVGHEH TRVFNEVAQI GKEFNQLGDT LLDARVNARV AIVFDWENRW ATELSSGPSV 

       430        440        450        460        470        480 
SLDYVNEVHK YYDALYKLNV QVDMVGVEED LSQYDVVIAP VLYMVKEGYA AKVESFVENG 

       490        500        510        520        530        540 
GTFITTFFSG IVNETDIVTL GGYPGELRKV LGIWAEEIDA LHPDETNEIV VNGSRGSLSG 

       550        560        570        580        590        600 
SYSCNLLFDL IHTEGAQAVA EYGSDFYQGM PVLTVNEFGK GKAWYVASSP DAEFLVDFLQ 

       610        620        630        640        650        660 
TVCEEAGVEP LLSVPEGVET TERVKDGQTY LFVLNHNNKV ESIDLKDSQY QELLSTQQLS 

       670 
GTVELEAKGV FILAKV 

« Hide

References

[1]"Molecular cloning and characterization of the gene encoding cold-active beta-galactosidase from a psychrotrophic and halotolerant Planococcus sp. L4."
Hu J.M., Li H., Cao L.X., Wu P.C., Zhang C.T., Sang S.L., Zhang X.Y., Chen M.J., Lu J.Q., Liu Y.H.
J. Agric. Food Chem. 55:2217-2224(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
Strain: L4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ899950 Genomic DNA. Translation: ABI64125.1.

3D structure databases

ProteinModelPortalQ09HN2.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH42. Glycoside Hydrolase Family 42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
3.40.50.880. 1 hit.
InterProIPR013739. Beta_galactosidase_C.
IPR013738. Beta_galactosidase_Trimer.
IPR029062. Class_I_gatase-like.
IPR003476. Glyco_hydro_42.
IPR013529. Glyco_hydro_42_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02449. Glyco_hydro_42. 1 hit.
PF08533. Glyco_hydro_42C. 1 hit.
PF08532. Glyco_hydro_42M. 1 hit.
[Graphical view]
PIRSFPIRSF001084. B-galactosidase. 1 hit.
SUPFAMSSF51445. SSF51445. 1 hit.
SSF52317. SSF52317. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBGAL_PLASL
AccessionPrimary (citable) accession number: Q09HN2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: October 17, 2006
Last modified: June 11, 2014
This is version 29 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