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A3FEW8 (BGAL_ENTAG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 29. 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
Short name=Bga
EC=3.2.1.23
Alternative name(s):
Lactase
Transglycosylating beta-galactosidase
Gene names
Name:lacZ
OrganismEnterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans)
Taxonomic identifier549 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePantoea

Protein attributes

Sequence length1028 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This beta-galactosidase is also able to catalyze glycosyl transfer to a series of acceptors, including hexose, pentose, beta- or alpha-disaccharides, hexahydroxy alcohol, cyclitol, and aromatic glycosides, resulting in the production of galacto-oligosaccharides (GOS). Ref.1

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. Can also use manganese and iron.

Binds 1 sodium ion per monomer Probable. Can also use potassium.

Enzyme regulation

Completely inhibited by Hg2+, Cu2+ Ag2+, and partially inhibited by Zn2+, imidazole and EDTA. Activated by Ca2+, Co2+, Ni2+. Ref.1

Subunit structure

Homodimer. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 2 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.06 mM for o-nitrophenyl-beta-D-galactopyranoside (at 37 degrees Celsius) Ref.1

KM=114 mM for lactose (at 37 degrees Celsius)

Vmax=0.43 mmol/min/mg enzyme for o-nitrophenyl-beta-D-galactopyranoside (at 37 degrees Celsius)

Vmax=2.9 mmol/min/mg enzyme for o-nitrophenyl-beta-D-galactopyranoside (at 37 degrees Celsius)

pH dependence:

Optimum pH is 7.5-8.0. Stable between 7.5-10.0.

Temperature dependence:

Optimum temperature is 37-40 degrees Celsius. Stable below 37 degrees Celsius.

Sequence caution

The sequence ABN42680.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10281028Beta-galactosidase HAMAP-Rule MF_01687
PRO_0000366982

Regions

Region539 – 5424Substrate binding By similarity

Sites

Active site4631Proton donor By similarity
Active site5391Nucleophile By similarity
Metal binding2031Sodium By similarity
Metal binding4181Magnesium 1 By similarity
Metal binding4201Magnesium 1 By similarity
Metal binding4631Magnesium 1 By similarity
Metal binding5991Magnesium 2 By similarity
Metal binding6031Sodium; via carbonyl oxygen By similarity
Metal binding6061Sodium By similarity
Binding site1041Substrate By similarity
Binding site2031Substrate By similarity
Binding site4631Substrate By similarity
Binding site6061Substrate By similarity
Binding site10041Substrate By similarity
Site3591Transition state stabilizer By similarity
Site3931Transition state stabilizer By similarity
Site10041Important for ensuring that an appropriate proportion of lactose is converted to allolactose By similarity

Sequences

Sequence LengthMass (Da)Tools
A3FEW8 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: 5A72487AB243185D

FASTA1,028116,394
        10         20         30         40         50         60 
MFTASPMSLS KILARRDWEN PGVTQWHRLP AHAPFNSWRD EASARADDNA SRKRSLNGDW 

        70         80         90        100        110        120 
QFSYYAAPEQ VPDSWVTEDC ADAVTTPVPS NWQMQGFDTP IYTNDTYPIP VNPPFVPAEN 

       130        140        150        160        170        180 
PTGCYSLTFE VDEQWLESGQ TRIVFDGVNS AFYLWCNGKW MGYSQDSRLP AEFDLSAVLR 

       190        200        210        220        230        240 
PGTNRLAVLV LRWCDGSYLE DQDMWRMSGI FRDVSLLHKP HTHIADYHAV TELNADYDRA 

       250        260        270        280        290        300 
KLQVEVALAG EQFADCEVAV TLWRDGLSVA TVSAKPGSAI IDERGNWAER LNVTLPVKDP 

       310        320        330        340        350        360 
ALWSAETPEL YRLTFALRDG QGEILDVEAC DVGFRCVEIS NGLLKVNGKP LLIRGVNRHE 

       370        380        390        400        410        420 
HHPENGQVMD EATMCRDIEL MKQHNFNAVR CSHYPNHPLW YTLCDRYGLY VVDEANIETH 

       430        440        450        460        470        480 
GMVPMSRLAD DPRWLPAMSE RVTRMVLRDR NHPSIIIWSL GNESGHGANH DALYRWVKTT 

       490        500        510        520        530        540 
DPTRPVQYEG GGANTAATDI VCPMYARVDQ DQPFEAVPKW SLKKWIGMPD ETRPLILCEY 

       550        560        570        580        590        600 
AHAMGNSFGG FAKYWQAFRN HPRLQGGFVW DWVDQALTKK DDNGNAFWAY GGDFGDTPND 

       610        620        630        640        650        660 
RQFCLNGLVF PDRTPHPALF EAQRAQQFFT FTLVSTSPLV IDVHSDYLFR QCDNEQLRWN 

       670        680        690        700        710        720 
IARDGEVLAS GEVALTIAPQ QTQRIEIDAP EFAAAAGEIW LNVDIVQTAA TAWSPADHRC 

       730        740        750        760        770        780 
AWDQWQLPAP LYIAPPVEGT AKPDLKVKED VLEVSHQSQR WHFDRASGNL TQWWNNGTAT 

       790        800        810        820        830        840 
LLAPLSDNFT RAPLDNDIGV SEATRIDPNA WVERWKAAGM YNLTPRLLLC EGEQLAQAVT 

       850        860        870        880        890        900 
ITTLHAWESN GKALFLSRKV WKIDRAGVLH GDVQVQVAND IPQPARIGLS CQLAQTPQTA 

       910        920        930        940        950        960 
SWLGLGPDEN YPDRKLAARQ GRWTLPLDAL HTAYIFPTDN GLRCDTRELT FDTHQMQGDF 

       970        980        990       1000       1010       1020 
HFSLSRYSQQ QLRDTSHHHL LEAEPGCWLN IDAFHMGVGG DDSWSPSVSP EFILQRREMR 


YAFSWRQD 

« Hide

References

[1]"A novel beta-galactosidase capable of glycosyl transfer from Enterobacter agglomerans B1."
Lu L., Xiao M., Xu X., Li Z., Li Y.
Biochem. Biophys. Res. Commun. 356:78-84(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-9, FUNCTION AS TRANSGLYCOSYLATING BETA-GALACTOSIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
Strain: B1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF371803 Genomic DNA. Translation: ABN42680.1. Different initiation.

3D structure databases

ProteinModelPortalA3FEW8.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKA3FEW8.

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_ENTAG
AccessionPrimary (citable) accession number: A3FEW8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: February 19, 2014
This is version 29 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