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Q5FJ41 (BGAL1_LACAC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 56. 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 LacZ

Short name=Beta-gal
EC=3.2.1.23
Gene names
Name:lacZ
Ordered Locus Names:LBA1462
OrganismLactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) [Complete proteome] [HAMAP]
Taxonomic identifier272621 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length667 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydrolysis of lactose to its constituent monosaccharides glucose and galactose. Ref.1

Catalytic activity

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

Biotechnological use

Has potential for lactose removal from dairy products at refrigerated temperatures. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 42 family.

Biophysicochemical properties

Kinetic parameters:

KM=3.84 mM for o-nitrophenyl-beta-D-galactopyranoside (ONPG) (at 37 degrees Celsius and pH 6.0) Ref.1

KM=88.9 mM for lactose (at 37 degrees Celsius and pH 6.0)

pH dependence:

Optimum pH is 6.0 for both lactose and ONPG hydrolysis, but lactose hydrolysis activity is more sensitive to changes in pH than ONPG hydrolysis activity.

Temperature dependence:

Optimum temperature is 37 degrees Celsius for both lactose and ONPG hydrolysis. Retains 16.5% of activity for ONPG hydrolysis and 11.2% of activity for lactose hydrolysis at 4 degrees Celsius. Stable at or below 25 degrees Celsius, but loses 50% of its activity after 1 hour at 37 degrees Celsius and is inactivated after only 40 minutes at 45 degrees Celsius. Can hydrolyze 73% of lactose in milk in 30 hours at 10 degrees Celsius.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
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

Chain1 – 667667Beta-galactosidase LacZ
PRO_0000407690

Regions

Region355 – 3584Substrate binding

Sites

Active site1481Proton donor By similarity
Active site3071Nucleophile By similarity
Metal binding1131Zinc By similarity
Metal binding1531Zinc By similarity
Metal binding1551Zinc By similarity
Metal binding1581Zinc By similarity
Binding site1091Substrate By similarity
Binding site1471Substrate By similarity
Binding site3151Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5FJ41 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 0034A0EC1C4438D2

FASTA66776,584
        10         20         30         40         50         60 
MTQLSRFLYG GDYNPDQWPE ETWSKDIHVF KKADINSATI NIFSWALLEP REGKYNFSKL 

        70         80         90        100        110        120 
DKVVQQLSDA NFDIVMGTAT AAMPAWMFKK YPDIARVDYQ DRRHVFGQRH NFCPNSSNYQ 

       130        140        150        160        170        180 
RLAGELVKQL VERYKDNKHI VVWHINNEYG GNCYCENCQN AFRKWLKNKY KTVEGLNKAW 

       190        200        210        220        230        240 
NMNVWSHTIY DWDEIVVPNE LGDVWGIEGS ETIVAGLSID YLRFQSESMQ NLFKMEKKII 

       250        260        270        280        290        300 
KKYDPETPVT TNFHGLPNKM VDYQKWAKGQ DIISYDSYPT YDAPAYKAAF LYDLMRSLKH 

       310        320        330        340        350        360 
QPFMLMESAP SQVNWQPYSP LKRPGQMEAT EFQAVAHGAD TVQFFQLKQA VGGSEKFHSA 

       370        380        390        400        410        420 
VIAHSQRTDT RVFKELADLG KKLKNAGPTI LGSKTKAKVA IVFDWSNFWS YEYVDGITQD 

       430        440        450        460        470        480 
LNYVDSILDY YRQFYERNIP TDIIGVDDDF SNYDLVVAPV LYMVKHGLDK KINDYVENGG 

       490        500        510        520        530        540 
NFVTTYMSGM VNSSDNVYLG GYPGPLKEVT GIWVEESDAV VPGQKIKVLM NGKDYDTGLI 

       550        560        570        580        590        600 
CNLIHPNDAK ILATYASEFY AGTPAVTENQ YGKGRAWYIG TRLEHQGLTQ LFNHIIFETG 

       610        620        630        640        650        660 
VESLVCDSHK LEITKRVTED GKELYFVLNM SNEERTLPSK FTGYEDILTG EKAHKDMKGW 


DVQVLRN 

« Hide

References

« Hide 'large scale' references
[1]"Functional identification of a putative beta-galactosidase gene in the special lac gene cluster of Lactobacillus acidophilus."
Pan Q., Zhu J., Liu L., Cong Y., Hu F., Li J., Yu X.
Curr. Microbiol. 60:172-178(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY.
Strain: ATCC 4356 / DSM 20079 / NBRC 13951 / JCM 1132 / NCIMB 8690.
[2]"Complete genome sequence of the probiotic lactic acid bacterium Lactobacillus acidophilus NCFM."
Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L., McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S., Hamrick A., Cano R., Klaenhammer T.R.
Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700396 / NCK56 / N2 / NCFM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EU590652 Genomic DNA. Translation: ACC38288.1.
CP000033 Genomic DNA. Translation: AAV43283.1.
RefSeqYP_194314.1. NC_006814.3.

3D structure databases

ProteinModelPortalQ5FJ41.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272621.LBA1462.

Protein family/group databases

CAZyGH42. Glycoside Hydrolase Family 42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV43283; AAV43283; LBA1462.
GeneID3251504.
KEGGlac:LBA1462.
PATRIC22197942. VBILacAci7974_1384.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1874.
HOGENOMHOG000117811.
KOK12308.
OMALFDWENW.
OrthoDBEOG6GTZGG.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
3.40.50.880. 1 hit.
InterProIPR013739. Beta_galactosidase_C.
IPR013738. Beta_galactosidase_Trimer.
IPR029062. Class_I_gatase-like.
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.
SSF52317. SSF52317. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBGAL1_LACAC
AccessionPrimary (citable) accession number: Q5FJ41
Secondary accession number(s): B2LWG4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: March 1, 2005
Last modified: June 11, 2014
This is version 56 of the entry and version 1 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