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

Q9KI47 (BGAL_PLASS) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 46. 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
OrganismPlanococcus sp. (strain 'SOS Orange')
Taxonomic identifier128803 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPlanococcaceaePlanococcus

Protein attributes

Sequence length677 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes o-nitrophenyl-beta-D-galactopyranoside (ONPG), p-nitrophenyl-beta-D-galactopyranoside (PNPG), 5-bromo-4-chloro-3-indoyl-beta-D-galactosde (X-gal), o-nitrophenyl-beta-D-fucopyranoside (ONPF) and p-nitrophenyl-beta-D-fucopyranoside (PNPF) with greatest activity towards ONPG and PNPG and low levels of activity with ONPF and PNPF. Detectable, but very low levels of activity towards p-nitrophenyl-beta-lactose (PNPL), p-nitrophenyl-beta-cellobiose (PNPC), p-nitrophenyl-alpha-galactopyranoside (PNP-alpha-G), and p-nitrophenyl-beta-xylopyranoside (PNPX). Ref.1

Catalytic activity

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

Enzyme regulation

No activity is lost during treatment with 20 or 100 mM EDTA in Z buffer for 3 hours at 0 degrees Celsius, nor is activity greatly stimulated by the addition of cations. Inhibited by 1 mM zinc and 1 mM copper, the levels of activity decrease to 10% of the untreated control. Nickel, cobalt and manganese at concentrations of 10 mM decrease enzyme activity to either 40% (for nickel and cobalt) or 60% (for manganese) of the activity in untreated controls. No change in enzyme activity in the presence of calcium and magnesium at concentrations up to 50 mM. EDTA-treated enzyme exhibits a slight increase in relative specific activity when it is assayed in the presence of 50 mM NaCl or 50 mM KCl, it does not exhibit enhanced activity at concentrations greater than 250 mM. Maintains between 20 and 40% of activity in the presence of 4 M NaCl or 4 M KCl, and it is more active in the presence of KCl than in the presence of NaCl. Retains 50% of activity in the presence of 3 M KCl or 2.5 M NaCl. Ref.1

Subunit structure

Dimer. Ref.1

Biotechnological use

Possible reporter enzyme for halotolerant and halophilic organisms. May also be used in the food industry to digest plant polysaccharides in high-salt processes. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 42 family.

Biophysicochemical properties

Kinetic parameters:

KM=7.4 mM for ONPG (at 1.9 degrees Celsius and at pH 6.5) Ref.1

KM=4.5 mM for ONPG (at 10 degrees Celsius and at pH 6.5)

KM=5.4 mM for ONPG (at 20 degrees Celsius and at pH 6.5)

KM=5.0 mM for ONPG (at 30 degrees Celsius and at pH 6.5)

KM=4.9 mM for ONPG (at 39 degrees Celsius and at pH 6.5)

Vmax=63 µmol/min/mg enzyme with ONPG as substrate (at 1.9 degrees Celsius and pH 6.5)

Vmax=80 µmol/min/mg enzyme with ONPG as substrate (at 10 degrees Celsius and pH 6.5)

Vmax=223 µmol/min/mg enzyme with ONPG as substrate (at 20 degrees Celsius and pH 6.5)

Vmax=392 µmol/min/mg enzyme with ONPG as substrate (at 30 degrees Celsius and pH 6.5)

Vmax=467 µmol/min/mg enzyme with ONPG as substrate (at 39 degrees Celsius and pH 6.5)

pH dependence:

Optimum pH is 6.5.

Temperature dependence:

Optimum temperature is 42 degrees Celsius. Thermostable at temperatures at or below the optimal temperature for activity, but it is rapidly denatured at temperatures above 42 degrees Celsius. Irreversibly inactivated within 10 minutes at 55 degrees Celsius. Stable during storage at 5 degrees Celsius and loses no activity during storage for 4 months. Retains 10% of activity at 0 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 – 677677Beta-galactosidase BgaA
PRO_0000407692

Regions

Region357 – 3604Substrate binding

Sites

Active site1511Proton donor By similarity
Active site3091Nucleophile By similarity
Metal binding1161Zinc By similarity
Metal binding1561Zinc By similarity
Metal binding1581Zinc By similarity
Metal binding1611Zinc By similarity
Binding site1121Substrate By similarity
Binding site1501Substrate By similarity
Binding site3171Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KI47 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 2A1928DADC945E55

FASTA67777,484
        10         20         30         40         50         60 
MINDKLPKIW HGGDYNPEQW DSKEIWDEDV RMFKLAGIDV ATLNVFSWAL NQPNEDTYNF 

        70         80         90        100        110        120 
DWLDEKINRL YENGIYTCLA TSTAAHPAWM AKKYPDVLRV DFYGRKRKFG SRHNSCPNSP 

       130        140        150        160        170        180 
TYRKYSERIA ETLAERYKDH PAVLIWHVSN EYGGYCYCDN CQDAFRNWLS DKYGTLEKLN 

       190        200        210        220        230        240 
KAWNTGFWGH TFYEWDEIVA PNMLSEKRED NVSDFQGISL DYRRFQSDRL LDCYKLEYNA 

       250        260        270        280        290        300 
IRKHVPTSIP ITTNLMGTYP MLDYFKWAKE MDVVSWDNYP SIDTPFSYTA MTHDLMRGLK 

       310        320        330        340        350        360 
GGKPFMLMEQ TPSQQNWQPY NSLKRPGVMR LWSYQAIGRG ADTILYFQLR RSVGACEKYH 

       370        380        390        400        410        420 
GAVIEHVGHE HTRVFNEVAQ LGQELNGLSD TLLDARVNAK VAIVFDWENR WATELSSGPS 

       430        440        450        460        470        480 
VSLDYVNEVH KYYDALYKLN VQVDMIGVEE DLSKYDVVIA PVLYMVKEGY AAKVEKFVEN 

       490        500        510        520        530        540 
GGTFLTTFFS GIVNETDIVT LGGYPGELRK VLGIWAEEID ALHPDETNQI VVKGSRGILS 

       550        560        570        580        590        600 
GKYSCNLLFD LIHTEGAEAV AEYGSDFYKG MPVLTVNKFG KGKAWYVASS PDAEFLVDFL 

       610        620        630        640        650        660 
QTVCEEAGVE PLLDVPAGVE TTERVKDGQT YLFVLNHNND EVTIELHGSQ YREVLTDEQV 

       670 
SGNLVLKEKG VLILAKV 

« Hide

References

[1]"Characterization of a salt-tolerant family 42 beta-galactosidase from a psychrophilic antarctic Planococcus isolate."
Sheridan P.P., Brenchley J.E.
Appl. Environ. Microbiol. 66:2438-2444(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-8, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, BIOTECHNOLOGY.
Strain: SOS Orange.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF242542 Genomic DNA. Translation: AAF75984.1.

3D structure databases

ProteinModelPortalQ9KI47.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH42. Glycoside Hydrolase Family 42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.2.1.23. 4880.

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_PLASS
AccessionPrimary (citable) accession number: Q9KI47
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: October 1, 2000
Last modified: October 16, 2013
This is version 46 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