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D4QFE7 (BGAL_BIFBI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 14. 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 BbgII

Short name=Beta-gal
EC=3.2.1.23
Gene names
Name:bbgII
OrganismBifidobacterium bifidum
Taxonomic identifier1681 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length689 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 42 family.

Ontologies

Keywords
   Molecular functionGlycosidase
Hydrolase
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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 689689Beta-galactosidase BbgII
PRO_0000407684

Regions

Region368 – 3714Substrate binding

Sites

Active site1611Proton donor By similarity
Active site3201Nucleophile By similarity
Binding site1221Substrate By similarity
Binding site1601Substrate By similarity
Binding site3281Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
D4QFE7 [UniParc].

Last modified June 15, 2010. Version 1.
Checksum: 886064A1622193CC

FASTA68977,217
        10         20         30         40         50         60 
MSKRRKHSWP QPLKGAESRL WYGGDYNPDQ WPEEVWDDDI RLMKKAGVNL VSVGIFSWAK 

        70         80         90        100        110        120 
IEPEEGKYDF DWLDRAIDKL GKAGIAVDLA SATASPPMWL TQAHPEVLWK DERGDTVWPG 

       130        140        150        160        170        180 
AREHWRPTSP VFREYALNLC RRMAEHYKGN PYVVAWHVSN EYGCHNRFDY SDDAMRAFQK 

       190        200        210        220        230        240 
WCKKRYKTID AVNEAWGTAF WAQHMNDFSE IIPPRYIGDG NFMNPGKLLD YKRFSSDALK 

       250        260        270        280        290        300 
ELYIAERDVL ESITPGLPLT TNFMVSAGGS MLDYDDWGAE VDFVSNDHYF TPGEAHFDEV 

       310        320        330        340        350        360 
AYAASLMDGI SRKEPWFQME HSTSAVNWRP INYRAEPGSV VRDSLAQVAM GADAICYFQW 

       370        380        390        400        410        420 
RQSKAGAEKW HSSMVPHAGE DSQIFRDVCE LGADLGRLSD EGLMGTKTVK SKVAVVFDYE 

       430        440        450        460        470        480 
SQWATEYTAN PTQQVDHWTE PLDWFRALAD NGITADVVPV RSDWDSYEIA VLPCVYLLSE 

       490        500        510        520        530        540 
ETSRRVREFV ANGGKLFVTY YTGLSDENDH IWLGGYPGSI RDVVGVRVEE FAPMGNDMPG 

       550        560        570        580        590        600 
ALDHLDLDNG TVAHDFADVI TSTADTSTVL ASYKAERWTG MNEVPAIVAN GYGDGRTVYV 

       610        620        630        640        650        660 
GCRLGRQGLA KSLPAMLGSM GLSDLAGDGR VLRVERADAA AANHFEFVFN RTHEPVTVDV 

       670        680 
EGEAIAASLA HVDDGRATID PTGVVVLRR 

« Hide

References

[1]"Cooperation of beta-galactosidase and beta-N-acetylhexosaminidase from bifidobacteria in assimilation of human milk oligosaccharides with type 2 structure."
Miwa M., Horimoto T., Kiyohara M., Katayama T., Kitaoka M., Ashida H., Yamamoto K.
Glycobiology 20:1402-1409(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 20082 / JCM 1254 / KCTC 3440.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB542712 Genomic DNA. Translation: BAI94826.1.

3D structure databases

ProteinModelPortalD4QFE7.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR013739. Beta_galactosidase_C.
IPR013738. Beta_galactosidase_Trimer.
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_BIFBI
AccessionPrimary (citable) accession number: D4QFE7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: June 15, 2010
Last modified: October 16, 2013
This is version 14 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