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g joobiniege g7  (ATCC)


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    Structured Review

    ATCC g joobiniege g7
    ( A ) Gene arrangement of Ahg943 compared to Ahg558 and Ahg786 in the G. <t>joobiniege</t> <t>G7</t> genome and the distribution of the conserved domain. The nucleotide numbers of the chromosomal region used for gene arrangement are presented above both ends of each DNA fragment based on the genomic data of G. joobiniege G7. Each ORF is indicated by an arrow with a stop codon at the arrowhead. The NCBI accession number is marked in each arrow with the annotated function in the lower row. Similar to Ahg558 and Ahg786, Ahg943 (WP_017446943.1) has a long conserved domain (cd08992) of the GH117 family spanning between N-61 and D-389 with an e-value of 3.96 xe -164 . Three putative catalytic residues, D-88, H-292, and E-293, are represented by triangles. ( B ) Phylogenetic tree of α-neoagarooligosaccharide hydrolases, including Ahg943. A phylogenetic tree was constructed by comparing 11 α-neoagarooligosaccharide hydrolases, including Ahg943, identified so far through the neighbor-joining method in MEGA 6. The tree was constructed to have branch lengths in the same units as the evolutionary distances used to infer phylogenetic trees. Sequence ID of each protein is indicated in parentheses. ( C ) Comparison of secondary structure of Ahg943 with ZgAhgB. Two-dimensional structures of Ahg943 and ZgAhgB were constructed using the NetSurfP-2.0 program server ( http://www.cbs.dtu.dk/services/NetSurfP/ ) for comparison. Two proteins were aligned depending on their amino acid sequence using Clustal Omega ( https://www.ebi.ac.uk/Tools/msa/clustalo/ ). The secondary structure of the protein is indicated at the top of Ahg943 and the bottom of ZgAhgB. The alpha-helix structure is shown as a thick line, and the beta-strand is shown as an arrow. The conserved residues constituting the active site are depicted with boxes.
    G Joobiniege G7, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 90 stars, based on 6 article reviews
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    Images

    1) Product Images from "Molecular Characterization of a Novel 1,3-α-3,6-Anhydro-L-Galactosidase, Ahg943, with Cold- and High-Salt-Tolerance from Gayadomonas joobiniege G7"

    Article Title: Molecular Characterization of a Novel 1,3-α-3,6-Anhydro-L-Galactosidase, Ahg943, with Cold- and High-Salt-Tolerance from Gayadomonas joobiniege G7

    Journal: Journal of Microbiology and Biotechnology

    doi: 10.4014/jmb.2008.08017

    ( A ) Gene arrangement of Ahg943 compared to Ahg558 and Ahg786 in the G. joobiniege G7 genome and the distribution of the conserved domain. The nucleotide numbers of the chromosomal region used for gene arrangement are presented above both ends of each DNA fragment based on the genomic data of G. joobiniege G7. Each ORF is indicated by an arrow with a stop codon at the arrowhead. The NCBI accession number is marked in each arrow with the annotated function in the lower row. Similar to Ahg558 and Ahg786, Ahg943 (WP_017446943.1) has a long conserved domain (cd08992) of the GH117 family spanning between N-61 and D-389 with an e-value of 3.96 xe -164 . Three putative catalytic residues, D-88, H-292, and E-293, are represented by triangles. ( B ) Phylogenetic tree of α-neoagarooligosaccharide hydrolases, including Ahg943. A phylogenetic tree was constructed by comparing 11 α-neoagarooligosaccharide hydrolases, including Ahg943, identified so far through the neighbor-joining method in MEGA 6. The tree was constructed to have branch lengths in the same units as the evolutionary distances used to infer phylogenetic trees. Sequence ID of each protein is indicated in parentheses. ( C ) Comparison of secondary structure of Ahg943 with ZgAhgB. Two-dimensional structures of Ahg943 and ZgAhgB were constructed using the NetSurfP-2.0 program server ( http://www.cbs.dtu.dk/services/NetSurfP/ ) for comparison. Two proteins were aligned depending on their amino acid sequence using Clustal Omega ( https://www.ebi.ac.uk/Tools/msa/clustalo/ ). The secondary structure of the protein is indicated at the top of Ahg943 and the bottom of ZgAhgB. The alpha-helix structure is shown as a thick line, and the beta-strand is shown as an arrow. The conserved residues constituting the active site are depicted with boxes.
    Figure Legend Snippet: ( A ) Gene arrangement of Ahg943 compared to Ahg558 and Ahg786 in the G. joobiniege G7 genome and the distribution of the conserved domain. The nucleotide numbers of the chromosomal region used for gene arrangement are presented above both ends of each DNA fragment based on the genomic data of G. joobiniege G7. Each ORF is indicated by an arrow with a stop codon at the arrowhead. The NCBI accession number is marked in each arrow with the annotated function in the lower row. Similar to Ahg558 and Ahg786, Ahg943 (WP_017446943.1) has a long conserved domain (cd08992) of the GH117 family spanning between N-61 and D-389 with an e-value of 3.96 xe -164 . Three putative catalytic residues, D-88, H-292, and E-293, are represented by triangles. ( B ) Phylogenetic tree of α-neoagarooligosaccharide hydrolases, including Ahg943. A phylogenetic tree was constructed by comparing 11 α-neoagarooligosaccharide hydrolases, including Ahg943, identified so far through the neighbor-joining method in MEGA 6. The tree was constructed to have branch lengths in the same units as the evolutionary distances used to infer phylogenetic trees. Sequence ID of each protein is indicated in parentheses. ( C ) Comparison of secondary structure of Ahg943 with ZgAhgB. Two-dimensional structures of Ahg943 and ZgAhgB were constructed using the NetSurfP-2.0 program server ( http://www.cbs.dtu.dk/services/NetSurfP/ ) for comparison. Two proteins were aligned depending on their amino acid sequence using Clustal Omega ( https://www.ebi.ac.uk/Tools/msa/clustalo/ ). The secondary structure of the protein is indicated at the top of Ahg943 and the bottom of ZgAhgB. The alpha-helix structure is shown as a thick line, and the beta-strand is shown as an arrow. The conserved residues constituting the active site are depicted with boxes.

    Techniques Used: Construct, Sequencing, Comparison



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    ( A ) Gene arrangement of Ahg943 compared to Ahg558 and Ahg786 in the G. <t>joobiniege</t> <t>G7</t> genome and the distribution of the conserved domain. The nucleotide numbers of the chromosomal region used for gene arrangement are presented above both ends of each DNA fragment based on the genomic data of G. joobiniege G7. Each ORF is indicated by an arrow with a stop codon at the arrowhead. The NCBI accession number is marked in each arrow with the annotated function in the lower row. Similar to Ahg558 and Ahg786, Ahg943 (WP_017446943.1) has a long conserved domain (cd08992) of the GH117 family spanning between N-61 and D-389 with an e-value of 3.96 xe -164 . Three putative catalytic residues, D-88, H-292, and E-293, are represented by triangles. ( B ) Phylogenetic tree of α-neoagarooligosaccharide hydrolases, including Ahg943. A phylogenetic tree was constructed by comparing 11 α-neoagarooligosaccharide hydrolases, including Ahg943, identified so far through the neighbor-joining method in MEGA 6. The tree was constructed to have branch lengths in the same units as the evolutionary distances used to infer phylogenetic trees. Sequence ID of each protein is indicated in parentheses. ( C ) Comparison of secondary structure of Ahg943 with ZgAhgB. Two-dimensional structures of Ahg943 and ZgAhgB were constructed using the NetSurfP-2.0 program server ( http://www.cbs.dtu.dk/services/NetSurfP/ ) for comparison. Two proteins were aligned depending on their amino acid sequence using Clustal Omega ( https://www.ebi.ac.uk/Tools/msa/clustalo/ ). The secondary structure of the protein is indicated at the top of Ahg943 and the bottom of ZgAhgB. The alpha-helix structure is shown as a thick line, and the beta-strand is shown as an arrow. The conserved residues constituting the active site are depicted with boxes.
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    Image Search Results


    ( A ) Gene arrangement of Ahg943 compared to Ahg558 and Ahg786 in the G. joobiniege G7 genome and the distribution of the conserved domain. The nucleotide numbers of the chromosomal region used for gene arrangement are presented above both ends of each DNA fragment based on the genomic data of G. joobiniege G7. Each ORF is indicated by an arrow with a stop codon at the arrowhead. The NCBI accession number is marked in each arrow with the annotated function in the lower row. Similar to Ahg558 and Ahg786, Ahg943 (WP_017446943.1) has a long conserved domain (cd08992) of the GH117 family spanning between N-61 and D-389 with an e-value of 3.96 xe -164 . Three putative catalytic residues, D-88, H-292, and E-293, are represented by triangles. ( B ) Phylogenetic tree of α-neoagarooligosaccharide hydrolases, including Ahg943. A phylogenetic tree was constructed by comparing 11 α-neoagarooligosaccharide hydrolases, including Ahg943, identified so far through the neighbor-joining method in MEGA 6. The tree was constructed to have branch lengths in the same units as the evolutionary distances used to infer phylogenetic trees. Sequence ID of each protein is indicated in parentheses. ( C ) Comparison of secondary structure of Ahg943 with ZgAhgB. Two-dimensional structures of Ahg943 and ZgAhgB were constructed using the NetSurfP-2.0 program server ( http://www.cbs.dtu.dk/services/NetSurfP/ ) for comparison. Two proteins were aligned depending on their amino acid sequence using Clustal Omega ( https://www.ebi.ac.uk/Tools/msa/clustalo/ ). The secondary structure of the protein is indicated at the top of Ahg943 and the bottom of ZgAhgB. The alpha-helix structure is shown as a thick line, and the beta-strand is shown as an arrow. The conserved residues constituting the active site are depicted with boxes.

    Journal: Journal of Microbiology and Biotechnology

    Article Title: Molecular Characterization of a Novel 1,3-α-3,6-Anhydro-L-Galactosidase, Ahg943, with Cold- and High-Salt-Tolerance from Gayadomonas joobiniege G7

    doi: 10.4014/jmb.2008.08017

    Figure Lengend Snippet: ( A ) Gene arrangement of Ahg943 compared to Ahg558 and Ahg786 in the G. joobiniege G7 genome and the distribution of the conserved domain. The nucleotide numbers of the chromosomal region used for gene arrangement are presented above both ends of each DNA fragment based on the genomic data of G. joobiniege G7. Each ORF is indicated by an arrow with a stop codon at the arrowhead. The NCBI accession number is marked in each arrow with the annotated function in the lower row. Similar to Ahg558 and Ahg786, Ahg943 (WP_017446943.1) has a long conserved domain (cd08992) of the GH117 family spanning between N-61 and D-389 with an e-value of 3.96 xe -164 . Three putative catalytic residues, D-88, H-292, and E-293, are represented by triangles. ( B ) Phylogenetic tree of α-neoagarooligosaccharide hydrolases, including Ahg943. A phylogenetic tree was constructed by comparing 11 α-neoagarooligosaccharide hydrolases, including Ahg943, identified so far through the neighbor-joining method in MEGA 6. The tree was constructed to have branch lengths in the same units as the evolutionary distances used to infer phylogenetic trees. Sequence ID of each protein is indicated in parentheses. ( C ) Comparison of secondary structure of Ahg943 with ZgAhgB. Two-dimensional structures of Ahg943 and ZgAhgB were constructed using the NetSurfP-2.0 program server ( http://www.cbs.dtu.dk/services/NetSurfP/ ) for comparison. Two proteins were aligned depending on their amino acid sequence using Clustal Omega ( https://www.ebi.ac.uk/Tools/msa/clustalo/ ). The secondary structure of the protein is indicated at the top of Ahg943 and the bottom of ZgAhgB. The alpha-helix structure is shown as a thick line, and the beta-strand is shown as an arrow. The conserved residues constituting the active site are depicted with boxes.

    Article Snippet: G. joobiniege G7 (ATCC BAA-2321 = DSM25250 T = KCTC23721 T ) was used as a genomic source for ahg943 (NCBI reference sequence: WP_017446943) [ ].

    Techniques: Construct, Sequencing, Comparison