Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q64XV2 (GLAB_BACFR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. 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:
Alpha-1,3-galactosidase B

EC=3.2.1.n1
EC=3.2.1.n2
Alternative name(s):
Exo-alpha-galactosidase B
EC=3.2.1.22
Gene names
Name:glaB
Ordered Locus Names:BF0923
OrganismBacteroides fragilis (strain YCH46) [Complete proteome] [HAMAP]
Taxonomic identifier295405 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length595 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Alpha-galactosidase. Removes both branched alpha-1,3-linked galactose residues of blood group B antigens and linear alpha-1,3-linked galactose structures By similarity.

Catalytic activity

Hydrolysis of terminal, non-reducing branched (1->3)-alpha-D-galactosidic residues, producing free D-galactose.

Hydrolysis of terminal, non-reducing linear (1->3)-alpha-D-galactosidic residues, producing free D-galactose.

Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.

Sequence similarities

Belongs to the glycosyl hydrolase 110 family. B subfamily.

Contains 3 PbH1 repeats.

Ontologies

Keywords
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular functionraffinose alpha-galactosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 595573Alpha-1,3-galactosidase B
PRO_0000348477

Regions

Repeat432 – 45423PbH1 1
Repeat455 – 47723PbH1 2
Repeat488 – 54154PbH1 3

Sequences

Sequence LengthMass (Da)Tools
Q64XV2 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 9B80163520E631B7

FASTA59566,982
        10         20         30         40         50         60 
MKTILLFALS LLLSLSVSDV CAQERVYDIS QFGLKANSKK NASPVVRKAI AKIKAECRDG 

        70         80         90        100        110        120 
EKVILRFPAG RYNFHEAGST VREYYISNHD QDNPKKVGIA LEDMKNLTID GQGSEFVFYG 

       130        140        150        160        170        180 
RMIPVSLLRS ENCVLKNFSI DFEQPHIAQV QVVENDPEKG ITFEPAPWVD YRISKDSVFE 

       190        200        210        220        230        240 
GLGEGWVMRY SWGIAFDGKT KHVVYNTSDI GCPTKGAFEV APRRICSPKW KDARLVPGTV 

       250        260        270        280        290        300 
VAMRGWGRPT PGIFMSHDVN TSLLDVKVHY AEGMGLLAQL CEDITLDGFG VCLKGNNDPR 

       310        320        330        340        350        360 
YFTTQADATH FSGCKGKIVS KNGLYEGMMD DAINVHGTYL KVIKRVDDHT LIGRYMHDQS 

       370        380        390        400        410        420 
WGFEWGRPGD DVQFVRSETM ELIGKQNQIT AIRPYDKGEI QGAREFSITF KEAIDPAINE 

       430        440        450        460        470        480 
KSGFGIENLT WTPEVLFAGN TIRNNRARGT LFSTPKKTVV EDNLFDHTSG TAILLCGDCN 

       490        500        510        520        530        540 
GWFETGACRD VTIRRNRFIN ALTNMFQFTN AVISIYPEIP NLKDQQKYFH GGKDGGIVIE 

       550        560        570        580        590 
DNEFDTFDAP ILYAKSVDGL IFRNNVIKTN TEFKPFHWNK DRFLLERVTN VKISE 

« Hide

References

[1]"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation."
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed: 15466707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YCH46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006841 Genomic DNA. Translation: BAD47674.1.
RefSeqYP_098208.1. NC_006347.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3083038.
GenomeReviewsGene locus BF0923 in contig AP006841_GR.
KEGGbfr:BF0923.
NMPDRfig|295405.3.peg.114.
PATRIC21047602. VBIBacFra17906_0926.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG345842.
OMALTWTPEV.
ProtClustDBCLSK823424.

Enzyme and pathway databases

BioCycBFRA295405:BF0923-MONOMER.

Family and domain databases

InterProIPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 3 hits.
SMARTSM00710. PbH1. 3 hits.
[Graphical view]
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLAB_BACFR
AccessionPrimary (citable) accession number: Q64XV2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families