Gene_locus Report for: biflj-d6zvy3

Bifidobacterium longum Putative esterase

Comment

Other strains: Bifidobacterium longum subsp. longum (strain JDM301)

Relationship

Family	\|	Carb_B_Bacteria
Block	\|	C
Position in NCBI Life Tree	\|	Bifidobacterium longum

(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Bacteria: N E > Terrabacteria group: N E > Actinobacteria [phylum]: N E > Actinobacteria [class]: N E > Bifidobacteriales: N E > Bifidobacteriaceae: N E > Bifidobacterium: N E > Bifidobacterium longum: N E

There are 21 a/b hydrolases in Bifidobacterium longum view in a: Table

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-BL0186Bifidobacterium longum possible esterase, biflo-BL0682Bifidobacterium longum, Bifidobacterium sp., esterase, biflo-BL0807Bifidobacterium longum, Bifidobacterium breve, Bifidobacterium sp., hypothetical protein with similarity to lipases and esterases.
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 acide identity. You can retrieve all strain data

Molecular evidence		Database
No mutation No structure No kinetic No Substrate No inhibitor		2 Genbank : CP002010, CP008885 1 UniProt : D6ZVY3 1 UniProt : D6ZVY3 1 Interpro : D6ZVY3 1 Pfam : D6ZVY3 1 PIRSF : D6ZVY3 1 SUPERFAM : D6ZVY3

Sequence

Peptide

Graphical view for this peptide sequence: biflj-d6zvy3
Colored MSA for Carb_B_Bacteria (raw)
MVLRRVCTRYGEIEGMAVEDPVITVFRGVPFAKAPMNELRWRAPQPVEPW DGVLHAHDFAPSAMQPRWDSDDFYGREWQMDPDSPRNEDCLYVNVWTPAL HGSGAAQYDERIASQGGLPVMVWIHGGAYQCGSAAEKEFDGSALARLGVV VVSVTYRLNVFGFFTHTDLQHESDGIDVAEPCANFGLLDQRAAIEWVKNN VAVFGGNPEAITIFGQSAGAASVLAQICSPMNENLFQRAIMQSGAGLGMF NRHLRSLNDAQRLGSRFLDFIGVRSVEEARTVPAAELLDAAERFPALNQN HELFEGWPMPINWVPCVDGRFLTDQYGVTLAQGSQQPVDIIVGNTTGEFM ETAADGTVIAAGEQGNLELMQAWVQGGSNPPFYYRFDVAMPGDDAGAFHS SDLWFTFNNLGKCWRPFSGWHYELANMMSRYWSNFAATGNPNESFGIADR DVLLPEWTRFEPATQAAMLFGKSVSMQKNC
Legend This 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
MVLRRVCTRYGEIEGMAVEDPVITVFRGVPFAKAPMNELRWRAPQPVEPW
DGVLHAHDFAPSAMQPRWDSDDFYGREWQMDPDSPRNEDCLYVNVWTPAL
HGSGAAQYDERIASQGGLPVMVWIHGGAYQCGSAAEKEFDGSALARLGVV
VVSVTYRLNVFGFFTHTDLQHESDGIDVAEPCANFGLLDQRAAIEWVKNN
VAVFGGNPEAITIFGQSAGAASVLAQICSPMNENLFQRAIMQSGAGLGMF
NRHLRSLNDAQRLGSRFLDFIGVRSVEEARTVPAAELLDAAERFPALNQN
HELFEGWPMPINWVPCVDGRFLTDQYGVTLAQGSQQPVDIIVGNTTGEFM
ETAADGTVIAAGEQGNLELMQAWVQGGSNPPFYYRFDVAMPGDDAGAFHS
SDLWFTFNNLGKCWRPFSGWHYELANMMSRYWSNFAATGNPNESFGIADR
DVLLPEWTRFEPATQAAMLFGKSVSMQKNC

Reference

Title:

Wei YX, Zhang ZY, Liu C, Zhu YZ, Zhu YQ, Zheng H, Zhao GP, Wang S, Guo XK

Ref:

192

PubMed

Other Papers

Send your questions or comments to :Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.

For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page

webmaster

Acknowledgements and disclaimer