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Q65CX4 (BGAL2_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 70. 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 GanA

Short name=Beta-gal
EC=3.2.1.23
Alternative name(s):
Beta-1,4-galactooligomerase
Galactooligomerase
Gene names
Name:ganA
Synonyms:galO, lacA
Ordered Locus Names:BLi04277, BL00264
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length673 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes oligosaccharides released by the endo-1,4-beta-galactosidase GalA from arabinogalactan type I, a pectic plant polysaccharide. It is unable to use lactose as a sole carbon source By similarity. Catalyzes the hydrolysis of lactose to its constituent monosaccharides glucose and galactose. Possesses a low level of transgalactosylation activity for the production of galacto-oligosaccharides (GOS) from lactose. Ref.3

Catalytic activity

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Ref.3

Enzyme regulation

Inhibited by hydrolysis end products D-galactose and D-glucose. The hydrolysis of o-nitrophenyl-beta-D-galactopyranoside (ONPG) is slightly activated by monovalent ions, Na+ and K+. Concentrations of these ions in the range of 1-100 mM exert the stimulating effects. The presence of 1 mM Mn2+ together with the presence of 10 mM Na+ slightly stimulates the activity, while presence of 10 mM Mn2+ inhibits the activity by about 40%. Ref.3

Subunit structure

Homodimer. Ref.3

Biotechnological use

Has potential for partial lactose removal in food products and improving the quality of dairy products by increasing their solubility and sweetness. Ref.3

Sequence similarities

Belongs to the glycosyl hydrolase 42 family.

Biophysicochemical properties

Kinetic parameters:

KM=13.7 mM for ONPG (at 30 degrees Celsius and pH 6.5) Ref.3

KM=169 mM for lactose (at 30 degrees Celsius and pH 6.5)

Vmax=299 µmol/min/mg enzyme with ONPG as substrate (at 30 degrees Celsius and pH 6.5)

Vmax=13 µmol/min/mg enzyme with lactose as substrate (at 30 degrees Celsius and pH 6.5)

pH dependence:

Optimum pH is 6.5 for both lactose and ONPG hydrolysis. Stable at pH 5-8 and most stable at 6.5, retaining more than 90% and 80% of its activity when incubated at pH 6.5 and 37 degrees Celsius for 5 days and 1 month, respectively.

Temperature dependence:

Optimum temperature of the activity is 50 degrees Celsius when using both lactose and ONPG as substrates under 10 minutes assay conditions. Stable over a wide range of temperatures (4-42 degrees Celsius), and when kept at these temperatures up to 1 month. Most stable at 37 degrees Celsius, retaining 90% of its activity after 1 month at this temperature. Half-life time of activity of approximately 7 days, 5 hours, and 30 minutes at 55, 60 and 65 degrees Celsius, respectively. Approximately 45% of lactose is hydrolyzed within the first 3 hours of the reaction at 60 degrees Celsius, while about 20% is cleaved at 37 degrees Celsius when employing initial lactose concentration of 50 g/l at pH 6.5. For initial lactose concentrations of 200 and 50 g/l and at temperature of 60 degrees Celsius, the maximum GOS yields are approximately 12% and 7%, respectively. At the initial lactose concentration of 200 g/l, the GOS yields obtained at 60 degrees Celsius are significantly higher than at 37 degrees Celsius, with approximately 12% and 5% of total sugars, respectively.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
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 – 673673Beta-galactosidase GanA
PRO_0000367027

Regions

Region356 – 3594Substrate binding By similarity

Sites

Active site1441Proton donor By similarity
Active site3081Nucleophile By similarity
Metal binding1091Zinc By similarity
Metal binding1491Zinc By similarity
Metal binding1511Zinc By similarity
Metal binding1541Zinc By similarity
Binding site1051Substrate By similarity
Binding site1431Substrate By similarity
Binding site3161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65CX4 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: D21163244C361A34

FASTA67377,497
        10         20         30         40         50         60 
MLHGGDYNPD QWLDRPDILA DDIKLMKLAH TNTFSVGIFS WSALEPEEGV YTFEWLDDIF 

        70         80         90        100        110        120 
ESIHRNGGRI ILATPSGARP AWLSQKYPEV LRVNAERVKQ LHGGRHNHCF TSYVYREKTK 

       130        140        150        160        170        180 
EINRMLAERY GSQHALLMWH VSNEYGGECH CDQCQHAFRD WLKKKYNHDI KSLNDAWWTP 

       190        200        210        220        230        240 
FWSHTFNDWS QIESPSPIGE NAVHGLNLDW RRFVTDQTIS FFQNEIVPLK EITPNIPITT 

       250        260        270        280        290        300 
NFMADTHDLI PFQGLDYSKF AKHLDVISWD AYPAWHNDWE STADLAMKVG FINDLYRSLK 

       310        320        330        340        350        360 
QQPFLLMEST PSAVNWHDFN KAKRPGMHLL SSVQMIAHGS DSILYFQWRK SRGSSEKFHG 

       370        380        390        400        410        420 
AVVGHDNCSE NRVFKEVAKV GQTLEALSEV TGTIRPADVA ILYDWENHWA LQDAQGFGMK 

       430        440        450        460        470        480 
TKRYPQTLHE HYRAFWERDI PVDVITKEQD FSSYRLLIVP MLYLASEETI ARLKAFAANG 

       490        500        510        520        530        540 
GTLVMTYISG IVNESDLTYL GGWPKDLQEM FGMEPVETDT LYPGDKNAVR YQNRSYELKD 

       550        560        570        580        590        600 
YATVLKLSTA DPEGFYEDDF YADTTAVTSH PYKQGKTYYI GARLSSQFHR DFYGTLIKEL 

       610        620        630        640        650        660 
AIQPALDVKH QPGVSVQVRQ DEENDYIFIM NFTEKRQPVV LASAVKDMLT GETLAGEVTL 

       670 
EKYEARIAVK AKE 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[3]"Cloning, purification, and characterization of beta-galactosidase from Bacillus licheniformis DSM 13."
Juajun O., Nguyen T.H., Maischberger T., Iqbal S., Haltrich D., Yamabhai M.
Appl. Microbiol. Biotechnol. 89:645-654(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT, BIOTECHNOLOGY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000002 Genomic DNA. Translation: AAU25712.1.
AE017333 Genomic DNA. Translation: AAU43090.1.
RefSeqYP_006715544.1. NC_006322.1.
YP_081350.1. NC_006270.3.

3D structure databases

ProteinModelPortalQ65CX4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL00264.

Protein family/group databases

CAZyGH42. Glycoside Hydrolase Family 42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU25712; AAU25712; BL00264.
AAU43090; AAU43090; BLi04277.
GeneID3029925.
3098321.
KEGGbld:BLi04277.
bli:BL00264.
PATRIC18954384. VBIBacLic203714_4367.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1874.
HOGENOMHOG000117811.
KOK12308.
OMARIQPTED.
OrthoDBEOG6GTZGG.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-4231-MONOMER.

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 nameBGAL2_BACLD
AccessionPrimary (citable) accession number: Q65CX4
Secondary accession number(s): Q62NE9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: June 11, 2014
This is version 70 of the entry and version 2 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