Beta-galactosidase - Pseudoalteromonas haloplanktis

Preferred order of sections

Names and origin

Protein names

Recommended name:
Beta-galactosidase
Short name=Beta-gal
EC=3.2.1.23

Alternative name(s):
Beta-D-galactoside galactohydrolase
Lactase

Gene names

Name:

lacZ

Organism

Pseudoalteromonas haloplanktis (Alteromonas haloplanktis)

Taxonomic identifier

228 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Pseudoalteromonadaceae › Pseudoalteromonas

Protein attributes

Sequence length	1039 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Can also use manganese, lithium and calcium. 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: K_M=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

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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed Ref.1

Chain

2 – 1039

1038

Beta-galactosidase HAMAP-Rule MF_01687

PRO_0000057656

Regions

Region

536 – 539

4

Substrate binding By similarity

Sites

Active site

460

1

Proton donor By similarity

Active site

536

1

Nucleophile By similarity

Metal binding

201

1

Sodium By similarity

Metal binding

415

1

Magnesium 1 By similarity

Metal binding

417

1

Magnesium 1 By similarity

Metal binding

460

1

Magnesium 1 By similarity

Metal binding

596

1

Magnesium 2 By similarity

Metal binding

600

1

Sodium; via carbonyl oxygen By similarity

Metal binding

603

1

Sodium By similarity

Binding site

103

1

Substrate By similarity

Binding site

201

1

Substrate By similarity

Binding site

460

1

Substrate By similarity

Binding site

603

1

Substrate By similarity

Binding site

1012

1

Substrate By similarity

Site

356

1

Transition state stabilizer By similarity

Site

390

1

Transition state stabilizer By similarity

Site

1012

1

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

Sequences

Sequence

Length

Mass (Da)

Tools

P81650 [UniParc].

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

FASTA

1,039

118,199

        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

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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
ProteinModelPortal	P81650.
ModBase	Search...
Protein family/group databases
CAZy	GH2. Glycoside Hydrolase Family 2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	2.60.40.320. 2 hits. 2.70.98.10. 1 hit. 3.20.20.80. 1 hit.
HAMAP	MF_01687. Beta_gal.
InterPro	IPR004199. 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]
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.
SMART	SM01038. Bgal_small_N. 1 hit. [Graphical view]
SUPFAM	SSF49785. Gal_bind_like. 1 hit. SSF74650. Gal_mut_like. 1 hit. SSF49303. Glyco_hydro_2Ig. 2 hits. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00719. GLYCOSYL_HYDROL_F2_1. 1 hit. PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BGAL_PSEHA

Accession

Primary (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:	April 3, 2013
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

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

Protein family/group databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents