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P81650 (BGAL_PSEHA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. 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
Alternative name(s):
Beta-D-galactoside galactohydrolase
Lactase
Gene names
Name:lacZ
OrganismPseudoalteromonas haloplanktis (Alteromonas haloplanktis)
Taxonomic identifier228 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Protein attributes

Sequence length1039 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. HAMAP-Rule MF_01687

Cofactor

Binds 2 magnesium ions per monomer Probable. Ref.1

Binds 1 sodium ion per monomer By similarity. Ref.1

Enzyme regulation

Inhibited by zinc, copper and nickel ions. Activated by 2-mercaptoethanol and inhibited by EDTA in vitro. HAMAP-Rule MF_01687

Subunit structure

Homotetramer Probable. Ref.1

Biotechnological use

This cold-adapted beta-galactosidase could be used to hydrolyze lactose in milk and dairy products processed in refrigerated plants. It is in fact superior to the current commercial enzyme from K.marxiamus with respect to lactose removal, especially at low temperatures. HAMAP-Rule MF_01687

Sequence similarities

Belongs to the glycosyl hydrolase 2 family.

Biophysicochemical properties

Kinetic parameters:

KM=2.4 mM for lactose (at pH 7.5 and at 25 degrees Celsius) Ref.1

pH dependence:

Optimum pH is 8.5.

Temperature dependence:

Optimum temperature is 4 degrees Celsius. It does not grow at temperatures higher than 25 degrees Celsius.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 10391038Beta-galactosidase HAMAP-Rule MF_01687
PRO_0000057656

Regions

Region536 – 5394Substrate binding By similarity

Sites

Active site4601Proton donor By similarity
Active site5361Nucleophile By similarity
Metal binding2011Sodium By similarity
Metal binding4151Magnesium 1 By similarity
Metal binding4171Magnesium 1 By similarity
Metal binding4601Magnesium 1 By similarity
Metal binding5961Magnesium 2 By similarity
Metal binding6001Sodium; via carbonyl oxygen By similarity
Metal binding6031Sodium By similarity
Binding site1031Substrate By similarity
Binding site2011Substrate By similarity
Binding site4601Substrate By similarity
Binding site6031Substrate By similarity
Binding site10121Substrate By similarity
Site3561Transition state stabilizer By similarity
Site3901Transition state stabilizer By similarity
Site10121Important for ensuring that an appropriate proportion of lactose is converted to allolactose By similarity

Sequences

Sequence LengthMass (Da)Tools
P81650 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: D77713F653DE8231

FASTA1,039118,199
        10         20         30         40         50         60 
MTSLQHIINR RDWENPITVQ VNQVKAHSPL NGFKTIEDAR ENTQSQKKSL NGQWDFKLFD 

        70         80         90        100        110        120 
KPEAVDESLL YEKISKELSG DWQSITVPSN WQLHGFDKPI YCNVKYPFAV NPPFVPSDNP 

       130        140        150        160        170        180 
TGCYRTEFTI TPEQLTQRNH IIFEGVNSAF HLWCNGQWVG YSQDSRLPSE FDLSELLVVG 

       190        200        210        220        230        240 
TNRIAVMVIR WSDGSYLEDQ DMWWLSGIFR DVNLLTKPQS QIRDVFITPD LDACYRDATL 

       250        260        270        280        290        300 
HIKTAINAPN NYQVAVQIFD GKTSLCEPKI QSTNNKRVDE KGGWSDVVFQ TIAIRSPKKW 

       310        320        330        340        350        360 
TAETPYLYRC VVSLLDEQGN TVDVEAYNIG FRKVEMLNGQ LCVNGKPLLI RGVNRHEHHP 

       370        380        390        400        410        420 
ENGHAVSTAD MIEDIKLMKQ NNFNAVRTAH YPNHPLFYEL CDELGLYVVD EANIETHGMF 

       430        440        450        460        470        480 
PMGRLASDPL WAGAFMSRYT QMVERDKNHA SIIIWSLGNE CGHGANHDAM YGWSKSFDPS 

       490        500        510        520        530        540 
RPVQYEGGGA NTTATDIICP MYSRVDTDIK DDAVPKYSIK KWLSLPGETR PLILCEYAHA 

       550        560        570        580        590        600 
MGNSLGSFDD YWQAFREYPR LQGGFIWDWV DQGLSKIDEN GKHYWAYGGD FGDELNDRQF 

       610        620        630        640        650        660 
CINGLLFPDR TPHPSLFEAK YSQQHLQFTL REQNQNQNQN QYSIDVFSDY VFRHTDNEKL 

       670        680        690        700        710        720 
VWQLIQNGVC VEQGEMALNI APQSTHTLTI KTKTAFEHGA QYYLNLDVAL INDSHFANAN 

       730        740        750        760        770        780 
HVMDSEQFKL INSNNLNSKS FASATEKSVI SVNETDSHLS IENNTFKLVF NQQSGLIEQW 

       790        800        810        820        830        840 
LQDDTQVISS PLVDNFYRAP LDNDIGVSEV DNLDPNAWEA RWSRAGIGQW QRTCSSINAV 

       850        860        870        880        890        900 
QSSVDVRITC VFNYEFNGVL QAQTQWLYTL NNTGTISLNV DVNLNDTLPP MPRIGLSTTI 

       910        920        930        940        950        960 
NKQSDTKVNW LGLGPFENYP DRKSAARFGY YSLSLNELYT PYIFPTDNGL RSDCQLLSIN 

       970        980        990       1000       1010       1020 
NLIVTGAFLF AASEYSQNML TQAKHTNELI ADDCIHVHID HQHMGVGGDD SWSPSTHKEY 

      1030 
LLEQKNYNYS LTLTGGITT 

« Hide

References

[1]"Cold-adapted beta-galactosidase from the Antarctic psychrophile Pseudoalteromonas haloplanktis."
Hoyoux A., Jennes I., Dubois P., Genicot S., Dubail F., Francois J.M., Baise E., Feller G., Gerday C.
Appl. Environ. Microbiol. 67:1529-1535(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: TAE 79.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ131635 Genomic DNA. Translation: CAA10470.1.

3D structure databases

ProteinModelPortalP81650.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.120.260. 1 hit.
2.60.40.320. 2 hits.
2.70.98.10. 1 hit.
3.20.20.80. 1 hit.
HAMAPMF_01687. Beta_gal.
InterProIPR004199. B-gal_small/dom_5.
IPR011013. Gal_mutarotase_SF_dom.
IPR008979. Galactose-bd-like.
IPR014718. Glyco_hydro-type_carb-bd_sub.
IPR006101. Glyco_hydro_2.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR023232. Glyco_hydro_2_AS.
IPR023933. Glyco_hydro_2_beta_Galsidase.
IPR023230. Glyco_hydro_2_CS.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR006103. Glyco_hydro_2_TIM.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02929. Bgal_small_N. 1 hit.
PF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
PRINTSPR00132. GLHYDRLASE2.
SMARTSM01038. Bgal_small_N. 1 hit.
[Graphical view]
SUPFAMSSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 1 hit.
PROSITEPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGAL_PSEHA
AccessionPrimary (citable) accession number: P81650
Secondary accession number(s): Q9ZEM8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 76 of the entry and version 2 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