Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C8WV58 (BGAL_ALIAD) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 26. 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 BglY

Short name=Beta-gal
EC=3.2.1.23
Gene names
Name:bglY
Ordered Locus Names:Aaci_2891
OrganismAlicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / 104-1A) (Bacillus acidocaldarius) [Complete proteome] [HAMAP]
Taxonomic identifier521098 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesAlicyclobacillaceaeAlicyclobacillus

Protein attributes

Sequence length688 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes o-nitrophenyl-beta-D-galactopyranoside (ONPG) and p-nitrophenyl-beta-D-fucopyranoside (PNPF), but not p-nitrophenyl-beta-D-glucopyranoside (PNPG), p-nitrophenyl-beta-D-xylopyranoside (PNPX) or p-nitrophenyl-beta-D-arabinopyranoside (PNPA). Also hydrolyzes lactose, including lactose in milk. Ref.1

Catalytic activity

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

Enzyme regulation

Ca2+, Mg2+ and EDTA have little effect on enzyme activity at 1-10 mM. Zn2+ at 3, 5, 7 or 10 mM inhibits activity by 20%, 30%, 40% and 65%, respectively. Ref.1

Biotechnological use

Has potential use in hydrolyzing lactose in neutral pH dairy products such as whole milk or whey. Also could be used in milk lactose hydrolysis during pasteurization at high temperatures. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 42 family.

Biophysicochemical properties

Kinetic parameters:

KM=6 mM for ONPG (at 60 degrees Celsius and pH 6.0) Ref.1

KM=3.5 mM for PNPF (at 60 degrees Celsius and pH 6.0)

pH dependence:

Optimum pH is 5.8. Approximately 80% of activity retained after incubating the enzyme for 40 minutes in buffers ranging from pH 5.0 to pH 10.5.

Temperature dependence:

Optimum temperature is 70 degrees Celsius. Retains 90% of activity when heated at 70 degrees Celsius for 30 minutes. Approximately 48% of lactose in milk is hydrolyzed following treatment with enzyme at 65 degrees Celsius over 60 minutes.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Direct protein sequencing
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 – 688688Beta-galactosidase BglY
PRO_0000407679

Regions

Region361 – 3644Substrate binding

Sites

Active site1571Proton donor By similarity
Active site3131Nucleophile By similarity
Metal binding1221Zinc By similarity
Metal binding1621Zinc By similarity
Metal binding1641Zinc By similarity
Metal binding1671Zinc By similarity
Binding site1181Substrate By similarity
Binding site1561Substrate By similarity
Binding site3211Substrate By similarity

Experimental info

Sequence conflict543 – 5442Missing AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
C8WV58 [UniParc].

Last modified November 3, 2009. Version 1.
Checksum: 686AFEA665822767

FASTA68877,869
        10         20         30         40         50         60 
MAKHAPIFPN VQGFLHGGDY NPDQWLAYPD VLEQDVQLMR EAKWNVVSLG IFSWVSLEPE 

        70         80         90        100        110        120 
EGLFTFEWLD EAIERLTHAG VRILLATPSG ARPAWLSAKY PEVLRVGPDG RRNRHGGRHN 

       130        140        150        160        170        180 
HCYTSPIYRE KVRIINRKLA ERYAHHPGVI GWHVSNEYGG ECHCPLCQEA FREWLKRKYK 

       190        200        210        220        230        240 
TLDALNHAWW TPFWSHTYTD WSQIESPMPH GETSIHGLNL DWKRFVTDQT VDFCRHEIEP 

       250        260        270        280        290        300 
LKQVNPNLPV TTNFMGTYPG LNYWRFRDVL DVISWDSYPR WHAHETLVPE AVHTAMVHDL 

       310        320        330        340        350        360 
NRSILKKPFL LMESTPSVTN WQAVSKQKRP GVHVLVSLQA VAHGADSVQY FQWRKSRGSY 

       370        380        390        400        410        420 
EKFHGAVVDH VGHANTRVFR DVQAVGEMLE RLAPMAGAEV KADAAVIFDW ENRWALEDAK 

       430        440        450        460        470        480 
GPRNIGMHYE ETVVNHYAAL WRMGVPMDVI DEEQPLDGYK LVVAPMLYMV RPGVAERMKA 

       490        500        510        520        530        540 
FVERGGSLVL TYWSGIVDEN DLVFLGGFPG PLRELAGVWA EEIDALYDGE RVPVRVADGN 

       550        560        570        580        590        600 
PLGLAGHYEA RELCEVVHLE GAEPIAVYGA DYYEGMPAAT VHRVGKGKVY YVAARLEDAF 

       610        620        630        640        650        660 
LRDFFARVAA EAGVARAIER ELPDGVSAMV RSGDGVEYVM LMNFTPEARE VALDEAEYKP 

       670        680 
LYGEAPTDGA VRLPAYGVSV LERPARNG 

« Hide

References

« Hide 'large scale' references
[1]"Heterologous expression of a gene encoding a thermostable beta-galactosidase from Alicyclobacillus acidocaldarius."
Yuan T., Yang P., Wang Y., Meng K., Luo H., Zhang W., Wu N., Fan Y., Yao B.
Biotechnol. Lett. 30:343-348(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-8; 536-551 AND 637-649, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY.
Strain: ATCC 27009 / DSM 446 / 104-1A.
[2]"The complete chromosome of Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446."
US DOE Joint Genome Institute (JGI-PGF)
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Chertkov O., Sims D., Brettin T., Detter J.C., Han C. expand/collapse author list , Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Klenk H.-P., Eisen J.A.
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27009 / DSM 446 / 104-1A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ887754 Genomic DNA. Translation: ABI84370.1.
CP001727 Genomic DNA. Translation: ACV59895.1.
RefSeqYP_003186284.1. NC_013205.1.

3D structure databases

ProteinModelPortalC8WV58.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING521098.Aaci_2891.

Protein family/group databases

CAZyGH42. Glycoside Hydrolase Family 42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACV59895; ACV59895; Aaci_2891.
GeneID8426432.
KEGGaac:Aaci_2891.
PATRIC20849346. VBIAliAci73240_2885.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1874.
HOGENOMHOG000117811.
KOK12308.
OMAFWSHTYA.
OrthoDBEOG6GTZGG.

Enzyme and pathway databases

BioCycAACI521098:GCIO-2974-MONOMER.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR013739. Beta_galactosidase_C.
IPR013738. Beta_galactosidase_Trimer.
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.
ProtoNetSearch...

Entry information

Entry nameBGAL_ALIAD
AccessionPrimary (citable) accession number: C8WV58
Secondary accession number(s): Q06GJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: November 3, 2009
Last modified: November 13, 2013
This is version 26 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