strains corallococcus Search Results


90
China Center for Type Culture Collection corallococcus sp. egb
Alignment of the GH16 domain sequence of the GH16 family β-glucanases. The proteins (and PDB numbers) were as follows: LamC <t>from</t> <t>Corallococcus</t> sp. <t>EGB;</t> PDB no. 3ATG, endo-β-(1,3)-glucanase from Cellulosimicrobium cellulans; PDB no. 2HYK, endo-β-(1,3)-glucanase of from Nocardiopsis sp. strain F96; PDB no. 4BQ1, ZgLamA from Z. galactanivorans; PDB no. 3AZX, laminarinase from T. maritima Msb8; PDB no. 2VY0, pfLamA from P. furiosus; and PDB no. 3DGT, endo-β-(1,3)-glucanase from S. sioyaensis. The protein sequence alignments were generated using the MUSCLE alignment in MEGA 7.0 (38). Secondary structures are labeled based on their appearance in 2HYK following a previous annotation (28). The stars identify the catalytic amino acids, including Glu-304, Asp-306, and Glu-309 (LamC numbering), and the conserved Trp residues are marked by the symbol ○ above the column. The numbers on the right are the amino acid residue positions in the whole sequence. The colors highlight other identities between sequences.
Corallococcus Sp. Egb, supplied by China Center for Type Culture Collection, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/corallococcus sp. egb/product/China Center for Type Culture Collection
Average 90 stars, based on 1 article reviews
corallococcus sp. egb - by Bioz Stars, 2026-06
90/100 stars
  Buy from Supplier

Image Search Results


Alignment of the GH16 domain sequence of the GH16 family β-glucanases. The proteins (and PDB numbers) were as follows: LamC from Corallococcus sp. EGB; PDB no. 3ATG, endo-β-(1,3)-glucanase from Cellulosimicrobium cellulans; PDB no. 2HYK, endo-β-(1,3)-glucanase of from Nocardiopsis sp. strain F96; PDB no. 4BQ1, ZgLamA from Z. galactanivorans; PDB no. 3AZX, laminarinase from T. maritima Msb8; PDB no. 2VY0, pfLamA from P. furiosus; and PDB no. 3DGT, endo-β-(1,3)-glucanase from S. sioyaensis. The protein sequence alignments were generated using the MUSCLE alignment in MEGA 7.0 (38). Secondary structures are labeled based on their appearance in 2HYK following a previous annotation (28). The stars identify the catalytic amino acids, including Glu-304, Asp-306, and Glu-309 (LamC numbering), and the conserved Trp residues are marked by the symbol ○ above the column. The numbers on the right are the amino acid residue positions in the whole sequence. The colors highlight other identities between sequences.

Journal: Applied and Environmental Microbiology

Article Title: Functional Analysis of a Novel β-(1,3)-Glucanase from Corallococcus sp. Strain EGB Containing a Fascin-Like Module

doi: 10.1128/AEM.01016-17

Figure Lengend Snippet: Alignment of the GH16 domain sequence of the GH16 family β-glucanases. The proteins (and PDB numbers) were as follows: LamC from Corallococcus sp. EGB; PDB no. 3ATG, endo-β-(1,3)-glucanase from Cellulosimicrobium cellulans; PDB no. 2HYK, endo-β-(1,3)-glucanase of from Nocardiopsis sp. strain F96; PDB no. 4BQ1, ZgLamA from Z. galactanivorans; PDB no. 3AZX, laminarinase from T. maritima Msb8; PDB no. 2VY0, pfLamA from P. furiosus; and PDB no. 3DGT, endo-β-(1,3)-glucanase from S. sioyaensis. The protein sequence alignments were generated using the MUSCLE alignment in MEGA 7.0 (38). Secondary structures are labeled based on their appearance in 2HYK following a previous annotation (28). The stars identify the catalytic amino acids, including Glu-304, Asp-306, and Glu-309 (LamC numbering), and the conserved Trp residues are marked by the symbol ○ above the column. The numbers on the right are the amino acid residue positions in the whole sequence. The colors highlight other identities between sequences.

Article Snippet: Corallococcus sp. EGB (CCTCC no. M2012528) was cultivated in CTT medium (pH 7.6), consisting of 1% (wt/vol) Casitone, 8 mM MgSO 4 , 10 mM Tris-HCl, and 1 mM potassium phosphate .

Techniques: Sequencing, Generated, Labeling, Residue