Protein Info for BT1276 in Bacteroides thetaiotaomicron VPI-5482
Updated annotation (from data): L-fucose mutarotase FucU (EC 5.1.3.29)
Rationale: Specifically important for utilization of L-fucose and D-arabinose. The phenotype on D-arabinose is strand-dependent and may be a polar effect on the downstream permease.
Original annotation: conserved hypothetical protein (NCBI ptt file)
These analyses and tools can help you predict a protein's function, but be skeptical. For enzymes, over 10% of annotations from KEGG or SEED are probably incorrect. For other types of proteins, the error rates may be much higher. MetaCyc and Swiss-Prot have low error rates, but the best hits in these databases are often quite distant, so this protein's function may not be the same. TIGRFam has low error rates. Finally, many experimentally-characterized proteins are not in any of these databases. To find relevant papers, use PaperBLAST.
Protein Families and Features
Best Hits
KEGG orthology group: None (inferred from 100% identity to bth:BT_1276)Predicted SEED Role
"L-fucose mutarotase, type 2"
MetaCyc Pathways
- superpathway of fucose and rhamnose degradation (10/12 steps found)
- L-fucose degradation I (4/4 steps found)
- L-fucose degradation II (1/5 steps found)
- L-fucose degradation III (2/8 steps found)
Isozymes
No predicted isozymesUse Curated BLAST to search for 5.1.3.29
Sequence Analysis Tools
PaperBLAST (search for papers about homologs of this protein)
Search CDD (the Conserved Domains Database, which includes COG and superfam)
Predict protein localization: PSORTb (Gram-negative bacteria)
Predict transmembrane helices and signal peptides: Phobius
Check the current SEED with FIGfam search
Find homologs in fast.genomics or the ENIGMA genome browser
See Q8A896 at UniProt or InterPro
Protein Sequence (130 amino acids)
>BT1276 L-fucose mutarotase FucU (EC 5.1.3.29) (Bacteroides thetaiotaomicron VPI-5482) METPQTGYQVKTYNVPVKRYCQTLDLRDSPELIAEYRKRHSQAEVWPEILAGIREVGILE MEIYILGTRLFMIVETPVDFDWDTAMARLNTLPRQQEWEEYMSILQQAAPGMSSAEKWIP MERMFHLYNT