SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 3608835 Dshi_2227 FAD dependent oxidoreductase (RefSeq) to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 3 hits to proteins with known functional sites (download)

Q8GAI3 4-methylaminobutanoate oxidase (formaldehyde-forming); MABO; Demethylating gamma-N-methylaminobutyrate oxidase; Gamma-N-methylaminobutyrate oxidase 1; EC 1.5.3.19 from Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans) (see paper)
27% identity, 82% coverage: 34:388/434 of query aligns to 23:381/824 of Q8GAI3

query
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Q8GAI3

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W66 (≠ G76) mutation W->F,S: Contains a non-covalently bound FAD. Loss of enzyme activity.
H67 (≠ R77) mutation to A: Contains a non-covalently bound FAD. Exhibits about 10% of the wild-type enzyme activity.

7cyxA Crystal strcuture of glycine oxidase from bacillus cereus atcc 14579 (see paper)
24% identity, 82% coverage: 38:395/434 of query aligns to 3:349/363 of 7cyxA

query
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7cyxA

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binding flavin-adenine dinucleotide: I7 (≠ V42), G8 (= G43), G9 (= G44), G10 (= G45), V11 (≠ Y46), I12 (≠ T47), V30 (≠ L65), E31 (= E66), K32 (≠ A67), E38 (≠ G73), A39 (= A74), S40 (= S75), A42 (≠ R77), A43 (≠ N78), A44 (≠ G79), G45 (= G80), L46 (≠ Q81), T169 (≠ S214), E170 (≠ Q215), V171 (= V216), A199 (= A243), G200 (= G244), G201 (≠ N245), W203 (≠ Y247), Y244 (≠ V292), G298 (= G346), R300 (≠ L348), P301 (≠ A349), H325 (≠ Y371), Y326 (≠ S372), R327 (≠ G373), N328 (≠ H374), G329 (= G375), I330 (≠ V376), L331 (≠ A377)

S5FMM4 Glycine oxidase; GO; BliGO; EC 1.4.3.19 from Bacillus licheniformis (see paper)
23% identity, 82% coverage: 50:403/434 of query aligns to 18:359/369 of S5FMM4

query
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S5FMM4

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G51 (≠ A83) mutation to 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.
A54 (≠ P86) mutation to 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.
K81 (≠ R113) mutation to 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.
S202 (≠ G244) 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 (≠ V376) 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 (= M386) 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.

Query Sequence

>3608835 Dshi_2227 FAD dependent oxidoreductase (RefSeq)
MDLLRANDRDGAYPPSYYASTVPARPALPAAQGPIHTDVCIVGGGYTGLSAALHLAERGY
DVVVLEAQRVGFGASGRNGGQVASGPRLDLSTLEARYGRETAHAQWALAREARKLVDELV
ARGLDCDLRAGVIYATDRAGDVAGYHAEAAHVQAAVGYDGVTPLDRDRIAALVGSAVYAG
GVLDAGAAHLNPLKLVLGLADLAQVAGAQIFEGSQVRSVADAGPHVVVTTDAATIAAEQV
ILAGNGYIGGLDSATAAHVMPINSYMVATEPLGPDADAILPEGHAVADNKFVVNYFRRAP
DGRLLFGGGESYRYRFTPDIAGKVRGPLERIFPQLRGIGIDYAWGGTLAITRSRLPFARK
VSPRVFSAGGYSGHGVALSLLFGKAMAEAAAGEPERFNQLAALPHAPFPGGAALRAPLLL
GAMSLAGLRDRLPF

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