(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Terrabacteria group: NE > Actinobacteria [phylum]: NE > Actinobacteria [class]: NE > Bifidobacteriales: NE > Bifidobacteriaceae: NE > Bifidobacterium: NE > Bifidobacterium longum: NE
6_AlphaBeta_hydrolase : biflo-BL0894Bifidobacterium longum esterase, biflo-BL1223Bifidobacterium longum possible alpha beta hydrolase, biflo-BL1804Bifidobacterium longum hypothetical protein. A85-Est-Putative : bifli-c2gxu7Bifidobacterium longum (and subsp. infantis ATCC 55813; CCUG 52486; DJO10A; ATCC15697/DSM2008/JCM1222/NCTC11817/S12) Esterase. AlphaBeta_hydrolase : biflo-BL0099Bifidobacterium longum hypothetical protein with possible acylase domain, biflo-BL0855Bifidobacterium longum hypothetical protein, biflo-BL1649Bifidobacterium longum hypothetical membrane protein possibly involved in transport. BD-FAE : biflo-BL0682Bifidobacterium longum, Bifidobacterium sp., esterase, biflo-BL0807Bifidobacterium longum, Bifidobacterium breve, Bifidobacterium sp., hypothetical protein with similarity to lipases and esterases. Carb_B_Bacteria : biflj-d6zvy3Bifidobacterium longum Putative esterase. DPP4N_Peptidase_S9 : biflo-BL0582Bifidobacterium longum, Bifidobacterium brev, Bifidobacterium sp., probable dipeptidyl peptidase IV. Hormone-sensitive_lipase_like : biflo-BL1109Bifidobacterium longum, Bifidobacterium breve, Bifidobacterium sp., possible carboxylesterase or lipase. LYsophospholipase_carboxylesterase : biflo-BL0073Bifidobacterium longum, subsp. longum, subsp. infantis, Bifidobacterium sp., possible phospholipase/carboxylesterase, biflo-BL0801Bifidobacterium longum hypothetical protein with carboxyesterase/lipase domain, biflo-BL1514Bifidobacterium longum, Bifidobacterium sp., possible phospholipase/carboxylesterase. Mbeg1-like : biflo-BL0336Bifidobacterium longum (and subsp. infantis longum), Bifidobacterium sp. hypothetical protein, biflo-BL0787Bifidobacterium longum (and subsp.: infantis, longum), Bifidobacterium breve, Bifidobacterium sp. narrowly conserved hypothetical protein. Monoglyceridelipase_lysophospholip : biflo-BL0581Bifidobacterium longum (and strains subsp. infantis), Bifidobacterium breve, hypothetical protein with alpha beta hydrolase domain at c-terminus. Proline_iminopeptidase : biflo-PAPBifidobacterium longum, Bifidobacterium adolescentis proline iminopeptidase. S9N_PREPL_Peptidase_S9 : biflo-PTRBBifidobacterium longum, Bifidobacterium sp., protease II
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acid identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Bifidobacterium longum subsp. longum ATCC 55813: N, E.
Bifidobacterium longum DJO10A: N, E.
Bifidobacterium longum subsp. infantis CCUG 52486: N, E.
Bifidobacterium longum subsp. infantis ATCC 15697: N, E.
Bifidobacterium longum subsp. longum JDM301: N, E.
Bifidobacterium longum subsp. longum: N, E.
Bifidobacterium longum subsp. longum 2-2B: N, E.
Bifidobacterium longum NCC2705: N, E.
Bifidobacterium longum subsp. longum F8: N, E.
Bifidobacterium longum subsp. infantis 157F: N, E.
Bifidobacterium longum subsp. longum JCM 1217: N, E.
Bifidobacterium longum subsp. longum 1-6B: N, E.
Bifidobacterium longum subsp. longum 35B: N, E.
Bifidobacterium longum subsp. longum KACC 91563: N, E.
Bifidobacterium longum subsp. longum 44B: N, E.
Bifidobacterium longum subsp. longum BBMN68: N, E.
Bifidobacterium longum E18: N, E.
Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088: N, E.
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MDIKPWEYADFPAFNEPVPGATRVPTTGDEIGVTYHPDVPYATAGTTPLH LQILVPQTRNQTDATTYPCMVHVQGSAWMKQDRTALVPTLSRIAERGFVV AIVEYRHSGIASFPAQIQDARNAVRFMRANAAQYHADADNLFLSGCSSGG QVALLAAVAHAADRTDMDDTSLSLAPNAADVSDATRGVIDYFGAVNGQMD DGFPSTVDHHLATSPEGMMMGHVDLRDRPDLRAAMTVESYLTPELALPPV LILHGTKDRLVNARQSASLYRRLRDVGKSAELYLLEGADHGGAEFWTDGM CRVATDFMRSNCAR
References
Title: Characterisation of a Hydroxycinnamic Acid Esterase From the Bifidobacterium longum subsp. longum Taxon Kelly SM, O'Callaghan J, Kinsella M, van Sinderen D Ref: Front Microbiol, 9:2690, 2018 : PubMed
Bifidobacterium longum subsp. longum, a common member of the human gut microbiota with perceived positive health effects, is capable of metabolising certain complex, plant-derived carbohydrates which are commonly found in the (adult) human diet. These plant glycans may be employed to favourably modulate the microbial communities in the intestine. Hydroxycinnamic acids (HCAs) are plant phenolic compounds, which are attached to glycans, and which are associated with anti-oxidant and other beneficial properties. However, very little information is available regarding metabolism of HCA-containing glycans by bifidobacteria. In the current study, a gene encoding a hydroxycinnamic acid esterase was found to be conserved across the B. longum subsp. longum taxon and was present in a conserved locus associated with plant carbohydrate utilisation. The esterase was shown to be active against various HCA-containing substrates and was biochemically characterised in terms of substrate preference, and pH and temperature optima of the enzyme. This novel hydroxycinnamic acid esterase is presumed to be responsible for the release of HCAs from plant-based dietary sources, a process that may have benefits for the gut environment and thus host health.
Bifidobacteria are Gram-positive prokaryotes that naturally colonize the human gastrointestinal tract (GIT) and vagina. Although not numerically dominant in the complex intestinal microflora, they are considered as key commensals that promote a healthy GIT. We determined the 2.26-Mb genome sequence of an infant-derived strain of Bifidobacterium longum, and identified 1,730 possible coding sequences organized in a 60%-GC circular chromosome. Bioinformatic analysis revealed several physiological traits that could partially explain the successful adaptation of this bacteria to the colon. An unexpectedly large number of the predicted proteins appeared to be specialized for catabolism of a variety of oligosaccharides, some possibly released by rare or novel glycosyl hydrolases acting on "nondigestible" plant polymers or host-derived glycoproteins and glycoconjugates. This ability to scavenge from a large variety of nutrients likely contributes to the competitiveness and persistence of bifidobacteria in the colon. Many genes for oligosaccharide metabolism were found in self-regulated modules that appear to have arisen in part from gene duplication or horizontal acquisition. Complete pathways for all amino acids, nucleotides, and some key vitamins were identified; however, routes for Asp and Cys were atypical. More importantly, genome analysis provided insights into the reciprocal interactions of bifidobacteria with their hosts. We identified polypeptides that showed homology to most major proteins needed for production of glycoprotein-binding fimbriae, structures that could possibly be important for adhesion and persistence in the GIT. We also found a eukaryotic-type serine protease inhibitor (serpin) possibly involved in the reported immunomodulatory activity of bifidobacteria.
