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O54315 (BGAL2_THESP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 49. 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), o-nitrophenyl-beta-D-galactopyranoside (ONPG) and lactose. 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=1.6 mM for ONPG (at 70 degrees Celsius and pH 7.0) Ref.1

Vmax=191000 nmol/min/mg enzyme with ONPG as substrate (at 70 degrees Celsius and pH 7.0)

Vmax=13000 nmol/min/mg enzyme with lactose as substrate (at 70 degrees Celsius and pH 7.0)

Vmax=435000 nmol/min/mg enzyme with ONPG as substrate (at 70 degrees Celsius and pH 5.0)

pH dependence:

Optimum pH is 5.0 with ONPG as substrate.

Temperature dependence:

Optimum temperature is 70 degrees Celsius with ONPG as substrate. Stable for several months at 4 or -20 degrees Celsius in the presence of 10% glycerol. Activity increases continuously from 30 to 90 degrees Celsius and drops dramatically at higher temperatures. Retains 50% of its initial activity after 1 hour incubation at 70 degrees Celsius. Retains 90% and 50% of activity after 30 minutes of incubation at 70 and 80 degrees Celsius, respectively. The residual activity of the enzyme decreases to an undetectable level after heating for 30 minutes at 90 degrees Celsius. The enzyme still maintains significant activity at 30 degrees Celsius.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect 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 – 645645Beta-galactosidase BgaA
PRO_0000407696

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

Experimental info

Sequence conflict2 – 32LG → ST AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
O54315 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 7A2AC9EAB6BAC944

FASTA64573,221
        10         20         30         40         50         60 
MLGVCYYPEH WPEERWEEDF KAMRALGLRY VRLGEFAWSA LEPTPGALRW GWLDRVLDLA 

        70         80         90        100        110        120 
QKEGLAVVLG TPTATPPKWL VDRYPEILPV DREGRRRNFG GRRHYCFSSP AYREETARIV 

       130        140        150        160        170        180 
ALLAERYGRH PAVVGFQVDN EFGCHGTVRC YCPNCREAFR GWLRAKYGTI DALNAAWGTV 

       190        200        210        220        230        240 
FWSQTYRDFG EVELPHLTVA EANPSHLLDY YRFASDQVRA YNRFQVDLLR DNAPGRFITH 

       250        260        270        280        290        300 
NFMGFFTDLD PFALAEDLDF AAWDSYPLGF TDLMPLPQEE KVQWARTGHP DVAAFHHDLY 

       310        320        330        340        350        360 
RGVGRGRFWV MEQQPGPVNW APHNPSPAPG MVRLWTWEAI AHGAEVVSYF RWRQAPFAQE 

       370        380        390        400        410        420 
QMQAGFNRPD FQPEVAFFEV QRVAEELSAL PLPPAGCAPV ALVYDSEAAW VFEIQPQGAE 

       430        440        450        460        470        480 
WKYLTLVFSF YSVFRRLGLE VDIFKPGAEL GGYGLVVVPS LPIVRKEALE ALSQADGLVI 

       490        500        510        520        530        540 
VGPRSGSKTE KFQIPPEIPP GALQALLPLK VVRVESLPPG LLEEAEGPWG RFAFGVWREW 

       550        560        570        580        590        600 
VETDLPPLLR FTDGGGILFR RGRYLYLAAW PSPELLFALC QSLAEEAGLH PRFLPEGLRL 

       610        620        630        640 
RRRGPLVFAF NYGPEVVEAP APPGVRFLLG DRRIPPHDLA VWEET 

« Hide

References

[1]"Structure of the beta-galactosidase gene from Thermus sp. strain T2: expression in Escherichia coli and purification in a single step of an active fusion protein."
Vian A., Carrascosa A.V., Garcia J.L., Cortes E.
Appl. Environ. Microbiol. 64:2187-2191(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-7, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: ATCC 27737 / T2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z93773 Genomic DNA. Translation: CAB07810.1.

3D structure databases

ProteinModelPortalO54315.
SMRO54315. 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 nameBGAL2_THESP
AccessionPrimary (citable) accession number: O54315
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: June 1, 1998
Last modified: June 11, 2014
This is version 49 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