SitesBLAST
Comparing SMc01576 FitnessBrowser__Smeli:SMc01576 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 6 hits to proteins with known functional sites (download)
3if9A Crystal structure of glycine oxidase g51s/a54r/h244a mutant in complex with inhibitor glycolate (see paper)
23% identity, 77% coverage: 47:378/429 of query aligns to 22:338/364 of 3if9A
- active site: A47 (≠ V72), G48 (= G73), M49 (≠ L74)
- binding flavin-adenine dinucleotide: E34 (= E59), S35 (≠ A60), T42 (≠ G67), T43 (≠ S68), A46 (≠ N71), A47 (≠ V72), G48 (= G73), M49 (≠ L74), P173 (= P208), V174 (≠ L209), S202 (≠ T237), G203 (≠ N238), W205 (≠ Y240), F209 (≠ P248), G300 (= G344), R302 (≠ I346), H327 (≠ Y369), F328 (vs. gap), R329 (vs. gap), N330 (= N370), G331 (= G371), I332 (≠ R372)
- binding glycolic acid: Y246 (≠ R276), R302 (≠ I346), R329 (vs. gap)
Sites not aligning to the query:
1ng3A Complex of thio (glycine oxidase) with acetyl-glycine (see paper)
26% identity, 46% coverage: 47:243/429 of query aligns to 22:208/364 of 1ng3A
- active site: A47 (≠ V72), G48 (= G73), M49 (≠ L74)
- binding flavin-adenine dinucleotide: F33 (≠ I58), E34 (= E59), S35 (≠ A60), R41 (≠ G66), T42 (≠ G67), T43 (≠ S68), A46 (≠ N71), A47 (≠ V72), G48 (= G73), M49 (≠ L74), V174 (≠ L209), S202 (≠ T237), G203 (≠ N238), W205 (≠ Y240)
- binding phosphate ion: R89 (≠ E121)
Sites not aligning to the query:
- binding acetylamino-acetic acid: 246, 302, 329
- binding flavin-adenine dinucleotide: 11, 13, 15, 209, 300, 302, 327, 329, 330, 331, 332
- binding phosphate ion: 254
O31616 Glycine oxidase; GO; EC 1.4.3.19 from Bacillus subtilis (strain 168) (see 3 papers)
26% identity, 46% coverage: 47:243/429 of query aligns to 22:208/369 of O31616
- ES 34:35 (≠ EA 59:60) binding
- TT 42:43 (≠ GS 67:68) binding
- AGM 47:49 (≠ VGL 72:74) binding
- G51 (≠ N76) mutation to R: 130-fold decrease in catalytic efficiency on glycine and 28-fold increase in that on glyphosate.; mutation to S: 60-fold decrease in catalytic efficiency on glycine and 210-fold increase in that on glyphosate; when associated with R-54 and A-244.
- A54 (≠ M79) mutation to R: 20-fold decrease in catalytic efficiency on glycine and 34-fold increase in that on glyphosate. 60-fold decrease in catalytic efficiency on glycine and 210-fold increase in that on glyphosate; when associated with S-51 and A-244.
- V174 (≠ L209) binding
Sites not aligning to the query:
- 14:15 binding
- 244 H→A: 2-fold decrease in catalytic efficiency on glycine and similar catalytic efficiency on glyphosate. 60-fold decrease in catalytic efficiency on glycine and 210-fold increase in that on glyphosate; when associated with S-51 and R-54.
- 302 binding
- 327:333 binding
- 329 binding
S5FMM4 Glycine oxidase; GO; BliGO; EC 1.4.3.19 from Bacillus licheniformis (see paper)
23% identity, 81% coverage: 43:391/429 of query aligns to 18:349/369 of S5FMM4
- G51 (≠ N76) 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 (≠ M79) 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 (≠ G103) 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 (≠ T237) 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 (≠ R372) 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 (≠ L384) 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.
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)
28% identity, 48% coverage: 30:237/429 of query aligns to 26:224/824 of Q8GAI3
- W66 (≠ G69) mutation W->F,S: Contains a non-covalently bound FAD. Loss of enzyme activity.
- H67 (≠ R70) 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)
22% identity, 84% coverage: 31:390/429 of query aligns to 3:346/363 of 7cyxA
- binding flavin-adenine dinucleotide: I7 (≠ V35), G8 (= G36), G10 (= G38), V11 (≠ F39), I12 (≠ T40), V30 (≠ I58), E31 (= E59), K32 (≠ A60), E38 (≠ G66), A39 (≠ G67), S40 (= S68), A43 (≠ N71), G45 (= G73), L46 (= L74), V171 (≠ L209), G200 (≠ T237), G201 (≠ N238), W203 (≠ Y240), G298 (= G344), R300 (≠ I346), P301 (≠ G347), Y326 (≠ N370), R327 (≠ G371), N328 (≠ R372), G329 (= G373), I330 (= I374)
Query Sequence
>SMc01576 FitnessBrowser__Smeli:SMc01576
MATERALPNLWHATAPAAPRTAPLAGDLTVEVAIVGGGFTGLSAALHLAETGIRTAVIEA
RMIGFGGSGRNVGLVNAGMWVQPDDLIATLGAAAGNRLLDELGDGPSFVYDLVAKHGIEC
EAVRNGTLHMSVGAEGLKEIREREAQWKKRGAPVEVLSAEKAHALSGAEGFTGALLDRRA
GTIQPLAYARGLARAALAAGAEIFTDTPLLAASRQGDLWNLKTPRGTVTARHVILATNAY
GSLVTGVPWKEYRQELTILPYFQFATNPLPDNVAARILPERQGAWDTGLVMTSFRMDRQN
RLIFGSIGRLDAIAAGTHRAFAARSVRKLFPYIGDFRFEHWWDGRIGMTTNNLPAMHVLA
PNVVSISGYNGRGIAPGTVFGRALARHVTGDTSAIPLAETPVTPDPWRTLKSAFYHAGAQ
AKHFIDKRF
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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