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C7ASJ5 (BGAL2_ARTSP) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 13. 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

Short name=Beta-gal
EC=3.2.1.23
OrganismArthrobacter sp.
Taxonomic identifier1667 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length694 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes p-nitrophenyl-beta-D-galactopyranoside (PNPG), o-nitrophenyl-beta-D-galactopyranoside (ONPG) and chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-gal), with highest activity against PNPG. Also acts on p-nitrophenyl-beta-D-glucopyranoside (PNPGlu) and o-nitrophenyl-beta-D-glucopyranoside (ONPGlu), but with significantly lower activity. Ref.1

Catalytic activity

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

Enzyme regulation

Strongly inhibited by glucose. No activity is lost during treatment with 100 mM EDTA after 2 hours. Activity not considerably affected by metal ions (5 mM), including Na+, K+, Mg2+, Co2+ and Ca2+. Completely inhibited by Cu2+ and Zn2+ (5 mM) and is strongly inhibited by Mn2+ (11%), Fe2+ (25%) and Ni2+ (38%) in comparison with the activity in the absence of cations (100%). Activity not affected by dithiothreitol, beta-mercaptoethanol and L-cysteine whereas reduced glutathione almost completely inactivates it. With ONPG as substrate, the addition of ethanol up to 20% still slightly stimulates activity. The activity increases up to 120% in the presence of 8% v/v ethanol at pH 5.5. Ref.1

Subunit structure

Homotrimer. Ref.1

Biotechnological use

Has potential use in lactose removal in milk and dairy products at low temperatures and for cheese whey bioremediation processes with simultaneous bio-ethanol production. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 42 family.

Biophysicochemical properties

Kinetic parameters:

KM=5.75 mM for ONPG (at 10 degrees Celsius) Ref.1

KM=4.86 mM for ONPG (at 20 degrees Celsius)

KM=3.46 mM for ONPG (at 30 degrees Celsius)

KM=3.15 mM for ONPG (at 40 degrees Celsius)

KM=2.62 mM for ONPG (at 50 degrees Celsius)

KM=5.11 mM for ONPG (at 55 degrees Celsius)

KM=77.54 mM for lactose (at 10 degrees Celsius)

KM=67.82 mM for lactose (at 20 degrees Celsius)

KM=52.67 mM for lactose (at 30 degrees Celsius)

KM=44.31 mM for lactose (at 40 degrees Celsius)

KM=39.73 mM for lactose (at 50 degrees Celsius)

pH dependence:

Optimum pH is 6.5 with ONPG as substrate. Over 90% of activity in the pH range 6.5-8.5. Highly efficient at pH range 4.5-9.5.

Temperature dependence:

Optimum temperature is 50 degrees Celsius with ONPG as substrate. Active at 4-8 degrees Celsius. 60% of the maximum activity is detected at 25 degrees Celsius and 15% at 0 degrees Celsius. Over 50% activity at 30 degrees Celsius.

Ontologies

Keywords
   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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 694694Beta-galactosidase
PRO_0000407681

Regions

Region389 – 3924Substrate binding

Sites

Active site1831Proton donor By similarity
Active site3411Nucleophile By similarity
Binding site1441Substrate By similarity
Binding site1821Substrate By similarity
Binding site3491Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
C7ASJ5 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: 2A352EDCF797BE74

FASTA69475,915
        10         20         30         40         50         60 
MGKRFPSGWF SPRVHPPRRQ RSPMTNQATP GTASVWNNIE GIGFGGDYNP EQWPVSVRLE 

        70         80         90        100        110        120 
DLELMQEAGV NFLSVGIFSW ALLEPAEGQY DFGWLDDVMD NLHGIGVKVA LATATAAPPA 

       130        140        150        160        170        180 
WLVRKHPEIL PVTADGTTLG PGSRRHYTPS SAVYRKYAAG ITRVLAERYK DHPALALWHV 

       190        200        210        220        230        240 
DNELGCHVSE FYGEEDAAAF RLWLERRYGT IDALNAAWGT AFWSQHYGSF EEILPPGVAP 

       250        260        270        280        290        300 
STLNPGQQLD FQRFNSWALM DYYRSLVAVL REVTPAVPCT TNLMASSATK SMDYFSWAKD 

       310        320        330        340        350        360 
LDVIANDHYL VAADPERHIE LAFSADLTRG IAGGDPWILM EHSTSAVNWQ PRNQPKMPGE 

       370        380        390        400        410        420 
MLRNSLAHVA RGADAVMFFQ WRQSFAGSEK FHSAMVPHGG RDTRVWREVV DLGAALQLLA 

       430        440        450        460        470        480 
PVRGSRVESR AAIVFDYEAW WASEIDSKPS IDVRYLDLLR AFHRSLFLRG VSVDMVHPSA 

       490        500        510        520        530        540 
SLDGYDLVLV CTLYSVTDEA AANIAAAAAG GATVLVSYFS GITDEKDHVR LGGYPGAFRE 

       550        560        570        580        590        600 
LLGVRVEEFH PLLAGSQLKL SDGTVSSIWS EHVHLDGAEA FQTFTGYPLE GVPSLTRRAV 

       610        620        630        640        650        660 
GTGAAWYLAT FPDRDGIESL VDRLLAESGV SPVAEADAGV ELTRRRSADG GSFLFAINHT 

       670        680        690 
RAAASVRASG TDVLSGERFT GTVEAGSVAV IAED 

« Hide

References

[1]"A new cold-adapted beta-D-galactosidase from the Antarctic Arthrobacter sp. 32c - gene cloning, overexpression, purification and properties."
Hildebrandt P., Wanarska M., Kur J.
BMC Microbiol. 9:151-151(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, BIOTECHNOLOGY.
Strain: 32c.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FJ609657 Genomic DNA. Translation: ACU00913.1.

3D structure databases

ProteinModelPortalC7ASJ5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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 nameBGAL2_ARTSP
AccessionPrimary (citable) accession number: C7ASJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: September 22, 2009
Last modified: October 16, 2013
This is version 13 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