SitesBLAST
Comparing WP_010439151.1 NCBI__GCF_000192475.1:WP_010439151.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 5 hits to proteins with known functional sites (download)
S5FMM4 Glycine oxidase; GO; BliGO; EC 1.4.3.19 from Bacillus licheniformis (see paper)
27% identity, 79% coverage: 50:393/434 of query aligns to 18:349/369 of S5FMM4
- G51 (= G83) 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 (≠ Q86) 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 (= K113) 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 (≠ C244) 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.
7cyxA Crystal strcuture of glycine oxidase from bacillus cereus atcc 14579 (see paper)
22% identity, 82% coverage: 38:395/434 of query aligns to 3:349/363 of 7cyxA
- binding flavin-adenine dinucleotide: I7 (≠ V42), G8 (= G43), G10 (= G45), V11 (≠ Y46), I12 (≠ T47), V30 (≠ L65), E31 (= E66), K32 (≠ A67), E38 (≠ G73), A39 (= A74), S40 (= S75), A43 (≠ N78), G45 (= G80), L46 (≠ Q81), V171 (= V217), G200 (≠ C244), G201 (≠ N245), W203 (≠ Y247), G298 (= G346), R300 (≠ L348), P301 (≠ G349), Y326 (≠ S372), R327 (≠ G373), N328 (≠ H374), G329 (= G375), I330 (≠ V376)
3hzlA Tyr258phe mutant of nikd, an unusual amino acid oxidase essential for nikkomycin biosynthesis: open form at 1.55a resolution (see paper)
28% identity, 49% coverage: 49:259/434 of query aligns to 16:218/394 of 3hzlA
- active site: S45 (≠ N78), E48 (≠ Q81), R49 (≠ L82), R52 (≠ A85), E100 (≠ R143)
- binding pyridine-2-carboxylic acid: R52 (≠ A85), E100 (≠ R143)
- binding flavin-adenine dinucleotide: L32 (= L65), E33 (= E66), R34 (≠ A67), G43 (= G76), T44 (≠ R77), R49 (≠ L82), H50 (≠ G83), V175 (≠ T215), C203 (= C244), Y206 (= Y247)
Sites not aligning to the query:
- active site: 257, 271, 275, 304, 320, 354, 357
- binding pyridine-2-carboxylic acid: 241, 257, 354
- binding flavin-adenine dinucleotide: 10, 12, 13, 14, 320, 321, 350, 354, 355, 356, 357
1ng3A Complex of thio (glycine oxidase) with acetyl-glycine (see paper)
21% identity, 78% coverage: 54:393/434 of query aligns to 22:349/364 of 1ng3A
- active site: A47 (≠ G79), G48 (= G80), M49 (≠ Q81)
- binding acetylamino-acetic acid: Y246 (= Y295), R302 (≠ L348), R329 (≠ G373)
- binding flavin-adenine dinucleotide: F33 (≠ L65), E34 (= E66), S35 (≠ A67), R41 (≠ G73), T42 (≠ A74), T43 (≠ S75), A46 (≠ N78), A47 (≠ G79), G48 (= G80), M49 (≠ Q81), V174 (= V217), S202 (≠ C244), G203 (≠ N245), W205 (≠ Y247), F209 (≠ L251), G300 (= G346), R302 (≠ L348), H327 (≠ Y371), R329 (≠ G373), N330 (≠ H374), G331 (= G375), I332 (≠ V376)
- binding phosphate ion: R89 (≠ S121), R254 (= R303)
Sites not aligning to the query:
O31616 Glycine oxidase; GO; EC 1.4.3.19 from Bacillus subtilis (strain 168) (see 3 papers)
21% identity, 78% coverage: 54:393/434 of query aligns to 22:349/369 of O31616
- ES 34:35 (≠ EA 66:67) binding FAD
- TT 42:43 (≠ AS 74:75) binding FAD
- AGM 47:49 (≠ GGQ 79:81) binding FAD
- G51 (= G83) 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 (≠ Q86) 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 (= V217) binding FAD
- H244 (≠ N294) mutation to 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.
- R302 (≠ L348) binding substrate
- 327:333 (vs. 371:377, 14% identical) binding FAD
- R329 (≠ G373) binding substrate
Sites not aligning to the query:
Query Sequence
>WP_010439151.1 NCBI__GCF_000192475.1:WP_010439151.1
MNLLYSNDRKAEYPPSWYAATAHPFDRYPALVGDHTADVCIVGGGYTGLSAALHLAEAGF
DVVLLEAHRAGFGASGRNGGQLGSAQRMDQEDLERLVGDDDALKLWDLAEDAKDLVKSLI
SKHQIDCDLKPGIAVLGFNDSERAELHDHAAHLSGRYKYDQIEALDADAARGLCPSPAYA
GGYLDNGAAHLHPLNYALGLARAAVGAGLRLHEDTEVLGIDQGARVTVRTEKGKITADNV
ILACNGYLGDLNRQVASRVMPINNFIAATEPLGAEAQKVLAKDIAVADTKFVVNYFRLSA
DGRLLFGGGESYGYRFPEDIAAKVRKPMTEIYPHLRDVKIDYAWGGTLGITMRRMPYLAR
IAPNILSASGYSGHGVGTATHAGQLMALAIQGQAEGFDTMARVPALPFPGGPALRTPLLI
LAMTWYATRDRLGI
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