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Q8GEA9 (BGAL1_THESP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 37. 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 BgaA

Short name=Beta-gal
EC=3.2.1.23
Gene names
Name:bgaA
OrganismThermus sp.
Taxonomic identifier275 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length645 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) and p-nitrophenyl-beta-D-galactoside (pNPGal). Ref.1

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 42 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.41 mM for pNPGal (at 70 degrees Celsius and pH 7.0) Ref.1

KM=42 mM for lactose (at 70 degrees Celsius and pH 7.0)

Vmax=140 µmol/min/mg enzyme with pNPGal as substrate (at 70 degrees Celsius and pH 7.0)

Vmax=8.5 µmol/min/mg enzyme with lactose as substrate (at 70 degrees Celsius and pH 7.0)

pH dependence:

Optimum pH is around 5.0-6.0. Retains more than 80% of activity at pH range between 4.5 and 6.5. Retains 10% of activity at pH 4.0.

Temperature dependence:

Optimum temperature is 90 degrees Celsius. Retains 90% of activity even at 95 degrees Celsius. Retains 80% of activity during a 12-hour period of incubation at 70 degrees Celsius. Half-lives at 80 and 90 degrees Celsius are 23 and 4.7 hours, respectively.

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 – 645645Beta-galactosidase BgaA
PRO_0000407695

Regions

Region360 – 3634Substrate binding

Sites

Active site1411Proton donor By similarity
Active site3121Nucleophile By similarity
Metal binding1061Zinc By similarity
Metal binding1501Zinc By similarity
Metal binding1521Zinc By similarity
Metal binding1551Zinc By similarity
Binding site1021Substrate By similarity
Binding site1401Substrate By similarity
Binding site3201Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8GEA9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E1F13D0D598857BE

FASTA64572,714
        10         20         30         40         50         60 
MLGVCYYPEH WPKARWKEDA RRMREAGLSY VRVGEFAWAL LEPEPGRLEW GWLDEALATL 

        70         80         90        100        110        120 
AAEGLKVVLG TPTATPPKWL VDRYPEVLPV DREGRRRRFG GRRHYCFSSP AYREEARRIV 

       130        140        150        160        170        180 
TLLAERYGGL EAVAGFQTDN EYGCHGTVRC YCPRCQEAFR GWLKARYGTI EALNEAWGTA 

       190        200        210        220        230        240 
FWSQRYRNFT EVELPHLTVA EPNPSHLLDY YRFASDQVRA FNRLQVEILR AHAPGKFITH 

       250        260        270        280        290        300 
NFMGFFTDLD AFALAQDLDF ASWDSYPLGF TDLMPLPPEE KLRYARTGHP DVAAFHHDLY 

       310        320        330        340        350        360 
RGVGRGRFWV MEQQPGPVNW APHNPSPTPG MVRLWTWEAL AHGAEVVSYF RWRQAPFAQE 

       370        380        390        400        410        420 
QMHAGLHRPD SAPDQGFFEA KQVAEELAAL ALPPVAQAPV ALVFDYEAAW VYEVQPQGAE 

       430        440        450        460        470        480 
WSYLGLIYLF YSALRRLGLD VDVVPPGASL RGYALTVVPS LPIVRGEALK AFQEAEGIVL 

       490        500        510        520        530        540 
FGPRSGSKTE TFQIPRELPP GPLQALLPLK VVRVESLPPG LLEVAEGPMG RFSLGLWREW 

       550        560        570        580        590        600 
VESPLRPWLA FADGGGALYR EGRYLYLAAW PSPELLGVLL AGLAQEAGLR PVFLPEGLRL 

       610        620        630        640 
RRRGPWVFAF NYGPEAVEAP APEGARFLLG GKRVGPYDLA VWEEA 

« Hide

References

[1]"Three forms of thermostable lactose-hydrolase from Thermus sp. IB-21: cloning, expression, and enzyme characterization."
Kang S.K., Cho K.K., Ahn J.K., Bok J.D., Kang S.H., Woo J.H., Lee H.G., You S.K., Choi Y.J.
J. Biotechnol. 116:337-346(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: ATCC 43815 / IB-21.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY130259 Genomic DNA. Translation: AAN05443.1.

3D structure databases

ProteinModelPortalQ8GEA9.
SMRQ8GEA9. Positions 1-644.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH42. Glycoside Hydrolase Family 42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
3.40.50.880. 1 hit.
InterProIPR013739. Beta_galactosidase_C.
IPR013738. Beta_galactosidase_Trimer.
IPR029062. Class_I_gatase-like.
IPR013780. Glyco_hydro_13_b.
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 nameBGAL1_THESP
AccessionPrimary (citable) accession number: Q8GEA9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: March 1, 2003
Last modified: June 11, 2014
This is version 37 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