Reviewed,
UniProtKB/Swiss-Prot Q64XV2 (GLAB_BACFR)
Last modified
July 13, 2010.
Version 35.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and originHide
| Protein names | Recommended name: Alpha-1,3-galactosidase B EC=3.2.1.n1 EC=3.2.1.n2 | ||||
| Gene names |
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| Organism | Bacteroides fragilis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 817 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides |
Protein attributesHide
| Sequence length | 595 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)Hide
| 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. |
OntologiesHide
| Keywords | |
|---|---|
| Domain | Repeat Signal |
| Molecular function | Glycosidase Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | alpha-galactosidase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
SequencesHide
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ReferencesHide
| [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-referencesHide
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AP006841 Genomic DNA. Translation: BAD47674.1. |
| RefSeq | YP_098208.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3083038. |
| GenomeReviews | Gene locus BF0923 in contig AP006841_GR. |
| KEGG | bfr:BF0923. |
| NMPDR | fig|295405.3.peg.114. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG345842. |
| OMA | LTWTPEV. |
| ProtClustDB | CLSK823424. |
Enzyme and pathway databases | |
| BioCyc | BFRA295405:BF0923-MONOMER. |
Family and domain databases | |
| InterPro | IPR006626. PbH1. IPR011050. Pectin_lyase_fold/virulence. [Graphical view] |
| SMART | SM00710. PbH1. 3 hits. [Graphical view] |
| SUPFAM | SSF51126. Pectin_lyas_like. 1 hit. |
| ProtoNet | Search... |
Entry informationHide
| Entry name | GLAB_BACFR | ||||||||
| Accession | Primary (citable) accession number: Q64XV2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documentsHide
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

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