Gene_locus Report for: bachk-q6hcl3

Bacillus thuringiensis (strains Al Hakam; subsp. konkukian; serovar israelensis ATCC 35646) hydrolase; possible prolyl aminopeptidase (EC 3.4.11.5)

Relationship

Family	\|	6_AlphaBeta_hydrolase
Block	\|	X
Position in NCBI Life Tree	\|	Bacillus thuringiensis

(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 > Firmicutes: N E > Bacilli: N E > Bacillales: N E > Bacillaceae: N E > Bacillus: N E > Bacillus cereus group: N E > Bacillus thuringiensis: N E

There are 27 a/b hydrolases in Bacillus thuringiensis view in a: Table

6_AlphaBeta_hydrolase : bacah-a0rcd1Bacillus thuringiensis (strain Al Hakam) hydrolase, alpha/beta fold family, bacah-a0rer5Bacillus thuringiensis, Bacillus cereus, Bacillus anthracis, Hydrolase, alpha/beta fold family, bachk-q6hgn4Bacillus thuringiensis, Bacillus cereus, Bacillus sp. Bifunctional nucleotide sugar epimerase/hydrolase Only C-term Abhydrolase_6, bachk-q6hgp9Bacillus thuringiensis (strains Al Hakam; subsp. konkukian) possible hydrolase, bachk-q6hig3Bacillus thuringiensis (subsp. konkukian) (and strain Al Hakam) hypothetical protein, bachk-q6hit8Bacillus thuringiensis (subsp. konkukian)(strain Al Hakam) hydrolase, alpha/beta fold family, bachk-q6hiv8Bacillus thuringiensis (subsp. konkukian) possible hydrolase, bachk-q6hkl2Bacillus thuringiensis (subsp. konkukian) hydrolase, alpha/beta fold family.
A85-EsteraseD-FGH : bacti-q3elq7Bacillus thuringiensis, Bacillus cereus, s-formylglutathione hydrolase (EC 3.1.2.12).
A85-IroE-IroD-Fes-Yiel : bactu-c3iam8Bacillus thuringiensis (strains IBL 200; serovar thuringiensis str. T01001; berliner ATCC 10792) Esterase.
Aclacinomycin-methylesterase_RdmC : bacah-a0rev7Bacillus thuringiensis (strain Al Hakam) Bacillus cereus (strains NVH0597-99; Rock3-42; 03BB108; BGSC 6E1; 03BB102) carboxylesterase (EC 3.1.1.1), bachk-q6hhz3Bacillus thuringiensis, Bacillus cereus, Bacillus thuringiensis, carboxylesterase (EC 3.1.1.1).
Bacillus_lip : bachk-q6hm10Bacillus thuringiensis (subsp. konkukian). hypothetical protein.
BioH : bacan-BA4338Bacillus anthracis, Bacillus thuringiensis, Bacillus cereus, bioh protein, putative.
Haloperoxidase : bactu-c3d3m5Bacillus thuringiensis (strains Bt407; serovar thuringiensis str. T01001; berliner ATCC 10792) Bacillus cereus AH621 Putative uncharacterized protein.
UCP033634 : bactu-a0a0f6j407Bacillus thuringiensis Uncharacterized protein, bactu-a0a0k0qdv6Bacillus thuringiensis Uncharacterized protein, bactu-a0a0s3byn5Bacillus thuringiensis Uncharacterized protein, bactu-a0a1c9bv37Bacillus thuringiensis Uncharacterized protein, bactu-a0a1e8ajc8Bacillus thuringiensis; Bacillus toyonensis Uncharacterized protein, bactu-a0a2b3pqz1Bacillus thuringiensis Alpha/beta hydrolase, bactu-a0a2j9bfp1Bacillus thuringiensis Alpha/beta hydrolase, bactu-a0a2t7yhx0Bacillus thuringiensis; Bacillus wiedmannii; Bacillus cereus; Bacillus bombysepticus; Streptococcus pneumoniae; Bacillus sp. Alpha beta hydrolase, bactu-a0a2v2hat7Bacillus thuringiensis; Bacillus cereus Alpha/beta hydrolase, bacah-a0rfk8Bacillus thuringiensis; Bacillus cereus Uncharacterized protein, bachk-q6hh51Bacillus thuringiensis; Bacillus anthracis; Streptococcus pneumoniae; Bacillus cereus Uncharacterized protein

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		3 Genbank : AE017355, AAJM01000103, CP000485 3 UniProt : Q6HCL3, Q3EUI7, A0RJR0 3 UniProt : Q6HCL3, Q3EUI7, A0RJR0 3 Interpro : Q6HCL3, Q3EUI7, A0RJR0 3 Pfam : Q6HCL3, Q3EUI7, A0RJR0 3 PIRSF : Q6HCL3, Q3EUI7, A0RJR0 3 SUPERFAM : Q6HCL3, Q3EUI7, A0RJR0

Sequence

Peptide

Graphical view for this peptide sequence: bachk-q6hcl3
Colored MSA for 6_AlphaBeta_hydrolase (raw)
MRRYILIIADIFRVALIYFYVLTDFMGKGRDIMWKQQMVNTKRGTFELFT KGSGEPLCITHHYSQFNETGDYFADVFTATHRVLLINLRDAGNSAKAQVE NELSMIETIHDLEAIREALQLPIWHFAGHSTGGMLGLLYAITYPKSLQSL VVVGAAASNYTETPFCIYHPEHPQFHYMQQLIENLKSPHLTNEERKELST ERTKLSLFKPENYNSYFCKPINKTMSISRMNAFANEYPSFDLREYLPSIQ TKTLIICGRYDVQCPIQYSIEIHEDICDSTFVTFEESNHYPFLEETTLFT STTQTFYKSLRQYRYY
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
MRRYILIIADIFRVALIYFYVLTDFMGKGRDIMWKQQMVNTKRGTFELFT
KGSGEPLCITHHYSQFNETGDYFADVFTATHRVLLINLRDAGNSAKAQVE
NELSMIETIHDLEAIREALQLPIWHFAGHSTGGMLGLLYAITYPKSLQSL
VVVGAAASNYTETPFCIYHPEHPQFHYMQQLIENLKSPHLTNEERKELST
ERTKLSLFKPENYNSYFCKPINKTMSISRMNAFANEYPSFDLREYLPSIQ
TKTLIICGRYDVQCPIQYSIEIHEDICDSTFVTFEESNHYPFLEETTLFT
STTQTFYKSLRQYRYY

Reference

Title:

Challacombe JF, Altherr MR, Xie G, Bhotika SS, Brown N, Bruce D, Campbell CS, Campbell ML, Chen J and Brettin TS <38 more author(s)>

Ref:

189

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.

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