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P94804 (BGAL_HALL2) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 53. 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 BgaH

Short name=Beta-gal
EC=3.2.1.23
Gene names
Name:bgaH
OrganismHaloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2) (Haloferax sp. (strain Aa 2.2))
Taxonomic identifier2254 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloferax

Protein attributes

Sequence length663 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

When overexpressed, cleaves several different substrates including o-nitrophenyl-beta-D-galactopyranoside (ONPG), chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) and lactulose, but not lactose. Has also beta-D-fucosidase activity. No beta-L-fucosidase, beta-glucosidase, beta-arabinosidase or beta-xylosidase activity. Ref.3

Catalytic activity

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. Ref.1 Ref.3

Enzyme regulation

Requires 4 M NaCl for maximal activity. Loss of activity if DTT or beta-mercaptoethanol is omitted from buffers. Addition of 5-20 mM EDTA, 1 mM Cu2+ or 1 mM Zn2+ results in loss of activity. Ref.3

Subunit structure

Homodimer. Ref.3

Induction

Highest expression in cells grown on galactose. Glucose or glycerol, alone or in combination with galactose, gives an intermediate level of expression and peptone-containing media gives very low levels of expression. Ref.1 Ref.3

Sequence similarities

Belongs to the glycosyl hydrolase 42 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.87 mM for ONPG (in the presence of 2.5 M NaCl, at room temperature and pH 7.2) Ref.3

Vmax=110 µmol/min/mg enzyme with ONPG as substrate (in the presence of 2.5 M NaCl, at room temperature and pH 7.2)

Temperature dependence:

Stable in 3 M NaCl for several days at room temperature, but approximately 18% and 50% of specific activity is lost when samples are stored overnight at 4 and -20 degrees Celsius, respectively. Activity is irreversibly lost within minutes in low salt buffers. Activity low, but detectable in 30% sorbitol in the complete absence of salt and it is stable in 30% sorbitol for at least four months at -20 degrees Celsius, but at room temperature approximately 20% of specific activity is lost after 48 hours.

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

Initiator methionine11Removed Ref.3
Chain2 – 663662Beta-galactosidase BgaH
PRO_0000407697

Regions

Region359 – 3624Substrate binding

Sites

Active site1421Proton donor By similarity
Active site3111Nucleophile By similarity
Metal binding1071Zinc By similarity
Metal binding1511Zinc By similarity
Metal binding1531Zinc By similarity
Metal binding1561Zinc By similarity
Binding site1031Substrate By similarity
Binding site1411Substrate By similarity
Binding site3191Substrate By similarity

Experimental info

Sequence conflict211I → F AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P94804 [UniParc].

Last modified October 1, 2001. Version 2.
Checksum: 7ADF7634C5D13BE9

FASTA66374,460
        10         20         30         40         50         60 
MTVGVCYFPE HWSRERWETD ISQMAEAGIE YVRMGEFAWR RIEPERGTFD FAWLDEAVEL 

        70         80         90        100        110        120 
IGKFGMKAVL CTPTATPPKW LVDEHPDVRQ REQDGTPREW GSRRFTCFNS PTYRSETERI 

       130        140        150        160        170        180 
VSVLTDRYAD NPHVAGWQTD NEFGCHETVT CYCEDCGEAF SEWLADRYES VADLNDAWGT 

       190        200        210        220        230        240 
TFWSQQYDDF ESIDPPKPTP AANHPSRVLA YERFSNDSVA EYNRLHAALI REANDEWFVT 

       250        260        270        280        290        300 
HNFMGGFSLD AFRLAADLDF LSWDSYPTGF VQDRQPDTPT VDELRAGNPD QVSMNHDLQR 

       310        320        330        340        350        360 
GAKGKPFWVM EQQPGDINWP PQSPQPADGA MRLWAHHAVA HGADAVVYFR WRRCRQGQEQ 

       370        380        390        400        410        420 
YHAGLRRQDG SPDRGYREAS TAADELFDLD SVDASVALVH DYESLWATRS QPLSPDWDYW 

       430        440        450        460        470        480 
NHLRTYYDAL RARGVQVDIV SPEATLERYD AVVAPTLYLV GDELSTALTD YVDSGGCLLL 

       490        500        510        520        530        540 
GARTGEKDPY NRLHESLAPG PLTALTGAQV ARHETLPDHV ETRLSYDGAT YEFRTWASWL 

       550        560        570        580        590        600 
APEVGVPRGE YRTGEAAGNT AIVRNAAGDG SVTYCGCWPG DDLADALVTE LLDAAGVEYT 

       610        620        630        640        650        660 
ERFPDGVRVM ERDGYTWALN FTSDPVTLTV PDSTGFLLGE STVDAFDTAV LDGSIRGVGL 


ASE 

« Hide

References

[1]"Sequence and expression of a halobacterial beta-galactosidase gene."
Holmes M.L., Dyall-Smith M.L.
Mol. Microbiol. 36:114-122(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, INDUCTION.
Strain: SB1.
[2]Holmes M.L., Dyall-Smith M.L.
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO C-TERMINUS.
[3]"Purification and analysis of an extremely halophilic beta-galactosidase from Haloferax alicantei."
Holmes M.L., Scopes R.K., Moritz R.L., Simpson R.J., Englert C., Pfeifer F., Dyall-Smith M.L.
Biochim. Biophys. Acta 1337:276-286(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-26; 286-300; 410-424; 425-431 AND 493-512, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT.
Strain: SB1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U70664 Genomic DNA. Translation: AAB40123.2.
PIRT44793.

3D structure databases

ProteinModelPortalP94804.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH42. Glycoside Hydrolase Family 42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR013739. Beta_galactosidase_C.
IPR013738. Beta_galactosidase_Trimer.
IPR013780. Glyco_hydro_13_b.
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_HALL2
AccessionPrimary (citable) accession number: P94804
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: October 1, 2001
Last modified: October 16, 2013
This is version 53 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