SitesBLAST
Comparing WP_013518247.1 NCBI__GCF_000204645.1:WP_013518247.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 1 hits to proteins with known functional sites (download)
S5FMM4 Glycine oxidase; GO; BliGO; EC 1.4.3.19 from Bacillus licheniformis (see paper)
26% identity, 47% coverage: 188:392/432 of query aligns to 148:349/369 of S5FMM4
- S202 (≠ T243) mutation to C: Shows 7.1- and 8-fold increase of affinity and catalytic efficiency to glyphosate, respectively, while the substrate affinity to glycine decreases 235-fold and catalytic efficiency decreases 113-fold; when associated with S-51, R-54, R-81, V-332 and V-342.
- I332 (= I375) mutation to V: Shows 7.1- and 8-fold increase of affinity and catalytic efficiency to glyphosate, respectively, while the substrate affinity to glycine decreases 235-fold and catalytic efficiency decreases 113-fold; when associated with S-51, R-54, R-81, C-202 and V-342.
- M342 (≠ A385) mutation to V: Shows 7.1- and 8-fold increase of affinity and catalytic efficiency to glyphosate, respectively, while the substrate affinity to glycine decreases 235-fold and catalytic efficiency decreases 113-fold; when associated with S-51, R-54, R-81, C-202 and V-332.
Sites not aligning to the query:
- 51 G→S: Shows 4.3- and 107-fold increase of affinity to glyphosate and glycine, respectively. Shows 7.1- and 8-fold increase of affinity and catalytic efficiency to glyphosate, respectively, while the substrate affinity to glycine decreases 235-fold and catalytic efficiency decreases 113-fold; when associated with R-54, R-81, C-202, V-332 and V-342.
- 54 A→R: Shows 7.1- and 8-fold increase of affinity and catalytic efficiency to glyphosate, respectively, while the substrate affinity to glycine decreases 235-fold and catalytic efficiency decreases 113-fold; when associated with S-51, R-81, C-202, V-332 and V-342.
- 81 K→R: Shows 7.1- and 8-fold increase of affinity and catalytic efficiency to glyphosate, respectively, while the substrate affinity to glycine decreases 235-fold and catalytic efficiency decreases 113-fold; when associated with S-51, R-54, C-202, V-332 and V-342.
Query Sequence
>WP_013518247.1 NCBI__GCF_000204645.1:WP_013518247.1
MNTRSIASHPAAPSLWAATAPAAPDTPALGASVSTDVLVVGAGYTGLSTALHLAESGARV
CVLDAHAPGWGASGRNGGQVNPTLKYDPDDLVRIYGAERAEPLIDTVSRSADLVYGLIAR
HAIDCAPVRAGWLQVGYTQHAVDGMHARARQWERRGVRVEMLDRAAVAARIGTPAFAGGW
LDGRAGGVQPLAYARGLARAAQGLGVQVHGGSPVVALERQGMHWIATTAQGHRVQAQQVV
LGTNGYTDGLWPGLARTVLAANSFIVATRPLGPAGDGILPGGETGSTSQRLLLYFRKDAQ
GRLLMGGRGHFADPQGPQDFSHLERAVALMFPQLGPLQYEYRWAGRIAVTRDFMPHLHRP
APGITMALGYNGRGIAMATSLGRHAAALVAGSSAAACPFPVTPVQPIPLHGLQRFYIAAG
VAWYSLLDRLGA
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory