Beta-galactosidase - Enterobacter agglomerans (Erwinia herbicola)

Names and origin

Protein names

Recommended 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

Organism

Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans)

Taxonomic identifier

549 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pantoea

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Protein attributes

Sequence length	1028 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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 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: K_M=0.06 mM for o-nitrophenyl-beta-D-galactopyranoside (at 37 degrees Celsius) HAMAP MF_01687 K_M=114 mM for lactose (at 37 degrees Celsius) V_max=0.43 mmol/min/mg enzyme for o-nitrophenyl-beta-D-galactopyranoside (at 37 degrees Celsius) V_max=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.

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Ontologies

Keywords
Ligand	Magnesium Metal-binding Sodium
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	beta-galactosidase complex Inferred from electronic annotation. Source: InterPro
Molecular function	beta-galactosidase activity Inferred from electronic annotation. Source: EC carbohydrate binding Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: HAMAP sodium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1028

1028

Beta-galactosidase HAMAP MF_01687

PRO_0000366982

Regions

Region

539 – 542

4

Substrate binding By similarity

Sites

Active site

463

1

Proton donor By similarity

Active site

539

1

Nucleophile By similarity

Metal binding

203

1

Sodium By similarity

Metal binding

418

1

Magnesium 1 By similarity

Metal binding

420

1

Magnesium 1 By similarity

Metal binding

463

1

Magnesium 1 By similarity

Metal binding

599

1

Magnesium 2 By similarity

Metal binding

603

1

Sodium; via carbonyl oxygen By similarity

Metal binding

606

1

Sodium By similarity

Binding site

104

1

Substrate By similarity

Binding site

203

1

Substrate By similarity

Binding site

463

1

Substrate By similarity

Binding site

606

1

Substrate By similarity

Binding site

1004

1

Substrate By similarity

Site

359

1

Transition state stabilizer By similarity

Site

393

1

Transition state stabilizer By similarity

Site

1004

1

Important for ensuring that an appropriate proportion of lactose is converted to allolactose By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

A3FEW8-1 [UniParc].

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

1,028

116,394

        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

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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: 17336932] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-9, FUNCTION AS TRANSGLYCOSYLATING BETA-GALACTOSIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
Strain: B1.

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Cross-references

Sequence databases
	EF371803 Genomic DNA. Translation: ABN42680.1. Different initiation.
3D structure databases
ModBase	Search...
Family and domain databases
HAMAP	MF_01687. [Tree]
InterPro	IPR014718. Glyco_hydro-type_carb-bd_sub. IPR006101. Glyco_hydro_2. IPR013812. Glyco_hydro_2/20_Ig-like. IPR006104. Glyco_hydro_2_carb-bd. IPR006102. Glyco_hydro_2_Ig-like. IPR006103. Glyco_hydro_2_TIM. IPR004199. Glyco_hydro_42_D5. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:2.60.40.320. Glyco_hydro_2/20_Ig-like. 2 hits. G3DSA:2.70.98.10. Glyco_hydro_42_D5. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF02929. 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]
PRINTS	PR00132. GLHYDRLASE2.
PROSITE	PS00719. GLYCOSYL_HYDROL_F2_1. 1 hit. PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

BGAL_ENTAG

Accession

Primary (citable) accession number: A3FEW8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	March 24, 2009
Last modified:	October 13, 2009
This is version 11 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Family and domain databases

Entry information

Relevant documents