SitesBLAST
Comparing AO353_13335 FitnessBrowser__pseudo3_N2E3:AO353_13335 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 11 hits to proteins with known functional sites (download)
5i39A High resolution structure of l-amino acid deaminase from proteus vulgaris with the deletion of the specific insertion sequence (see paper)
26% identity, 86% coverage: 28:395/427 of query aligns to 25:379/383 of 5i39A
- active site: F66 (≠ N69), Q69 (≠ N74), A70 (= A75), Q248 (≠ Y255), P267 (= P273)
- binding flavin-adenine dinucleotide: V30 (≠ I33), G31 (= G34), G33 (= G36), I34 (≠ F37), L35 (≠ T38), V53 (≠ L56), E54 (= E57), K55 (≠ A58), Q62 (≠ G65), S63 (= S66), F66 (≠ N69), Y67 (≠ V70), Q69 (≠ N74), A196 (= A206), A197 (≠ V207), G226 (≠ S235), G227 (≠ N236), W229 (≠ Y238), Q248 (≠ Y255), Q250 (≠ Y256), G321 (= G338), M323 (≠ I340), T348 (≠ N364), G349 (= G365), W350 (≠ R366), G351 (= G367), M352 (≠ V368), T353 (= T369)
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)
25% identity, 84% coverage: 30:387/427 of query aligns to 28:388/824 of Q8GAI3
- W66 (≠ G67) mutation W->F,S: Contains a non-covalently bound FAD. Loss of enzyme activity.
- H67 (≠ R68) mutation to A: Contains a non-covalently bound FAD. Exhibits about 10% of the wild-type enzyme activity.
5hxwA L-amino acid deaminase from proteus vulgaris (see paper)
27% identity, 58% coverage: 28:275/427 of query aligns to 17:261/433 of 5hxwA
- active site: F58 (≠ N69), Q61 (≠ N74), A62 (= A75), Q240 (≠ Y255)
- binding flavin-adenine dinucleotide: V22 (≠ I33), G23 (= G34), G25 (= G36), I26 (≠ F37), L27 (≠ T38), E46 (= E57), K47 (≠ A58), E53 (≠ G64), Q54 (≠ G65), S55 (= S66), R57 (= R68), F58 (≠ N69), Y59 (≠ V70), G60 (= G71), Q61 (≠ N74), A188 (= A206), A189 (≠ V207), G218 (≠ S235), G219 (≠ N236), W221 (≠ Y238), Q240 (≠ Y255), Q242 (≠ Y256)
Sites not aligning to the query:
- active site: 284, 288
- binding cetyl-trimethyl-ammonium: 291, 294, 310, 311, 317, 318, 320, 373, 379, 399, 400
- binding flavin-adenine dinucleotide: 331, 371, 373, 398, 399, 400, 401, 402, 403
7cyxA Crystal strcuture of glycine oxidase from bacillus cereus atcc 14579 (see paper)
23% identity, 83% coverage: 29:382/427 of query aligns to 3:344/363 of 7cyxA
- binding flavin-adenine dinucleotide: I7 (= I33), G8 (= G34), G10 (= G36), V11 (≠ F37), I12 (≠ T38), V30 (≠ L56), E31 (= E57), K32 (≠ A58), E38 (≠ G64), A39 (≠ G65), S40 (= S66), A43 (≠ N69), G45 (= G71), L46 (= L72), V171 (= V207), G200 (≠ S235), G201 (≠ N236), W203 (≠ Y238), G298 (= G338), R300 (≠ A341), P301 (≠ F342), Y326 (≠ N364), R327 (≠ G365), N328 (≠ R366), G329 (= G367), I330 (≠ V368)
Q9UI17 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Homo sapiens (Human) (see 4 papers)
22% identity, 84% coverage: 28:387/427 of query aligns to 50:420/866 of Q9UI17
- CV 59:60 (≠ FT 37:38) binding
- EK 80:81 (≠ EA 57:58) binding
- 87:95 (vs. 64:72, 33% identical) binding
- H91 (≠ R68) modified: Tele-8alpha-FAD histidine
- H109 (≠ L100) to R: in DMGDHD; shows 10 fold lower catalytic efficiency due to lower cofactor saturation and reduced thermal stability; dbSNP:rs121908331
- V219 (= V207) binding
- S279 (≠ T264) to P: in dbSNP:rs532964
- F-GYGII 397:402 (≠ YNGRGVT 363:369) binding
Sites not aligning to the query:
- 530 A → G: in dbSNP:rs1805073
- 646 S → P: in dbSNP:rs1805074
4pabB Crystal structure of the precursor form of rat dmgdh complexed with tetrahydrofolate (see paper)
22% identity, 84% coverage: 28:387/427 of query aligns to 6:376/824 of 4pabB
- active site: T53 (≠ N74), E102 (≠ D137), H226 (≠ Y255), Y255 (≠ S287)
- binding flavin-adenine dinucleotide: I11 (= I33), G12 (= G34), G14 (= G36), C15 (≠ F37), V16 (≠ T38), L35 (= L56), E36 (= E57), K37 (≠ A58), G43 (= G64), S44 (≠ G65), T45 (≠ S66), H47 (≠ R68), A48 (≠ N69), A49 (≠ V70), G50 (= G71), L51 (= L72), V175 (= V207), A204 (≠ S235), G205 (≠ N236), W207 (≠ Y238), H226 (≠ Y255), Y228 (≠ Q257), G326 (= G338), I328 (= I340), F353 (≠ Y363), Y355 (≠ R366), G356 (= G367), I357 (≠ V368), I358 (≠ T369)
Sites not aligning to the query:
- active site: 536
- binding (6s)-5,6,7,8-tetrahydrofolate: 523, 536, 538, 550, 612, 613, 632, 639, 680, 700
Q63342 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Rattus norvegicus (Rat) (see 2 papers)
22% identity, 84% coverage: 28:387/427 of query aligns to 43:413/857 of Q63342
- CV 52:53 (≠ FT 37:38) binding
- EK 73:74 (≠ EA 57:58) binding
- 80:88 (vs. 64:72, 33% identical) binding
- H84 (≠ R68) modified: Tele-8alpha-FAD histidine
- V212 (= V207) binding
- W244 (≠ Y238) binding
- F-GYGII 390:395 (≠ YNGRGVT 363:369) binding
Sites not aligning to the query:
- 573:575 binding
- 669 binding
- 676:678 binding
- 737 binding
1ng3A Complex of thio (glycine oxidase) with acetyl-glycine (see paper)
32% identity, 17% coverage: 181:252/427 of query aligns to 148:221/364 of 1ng3A
Sites not aligning to the query:
- active site: 47, 48, 49
- binding acetylamino-acetic acid: 246, 302, 329
- binding flavin-adenine dinucleotide: 11, 13, 15, 33, 34, 35, 41, 42, 43, 46, 47, 48, 49, 300, 302, 327, 329, 330, 331, 332
- binding phosphate ion: 89, 254
3if9A Crystal structure of glycine oxidase g51s/a54r/h244a mutant in complex with inhibitor glycolate (see paper)
22% identity, 49% coverage: 45:252/427 of query aligns to 22:221/364 of 3if9A
- active site: A47 (≠ V70), G48 (= G71), M49 (≠ L72)
- binding flavin-adenine dinucleotide: E34 (= E57), S35 (≠ A58), T42 (≠ G65), T43 (≠ S66), A46 (≠ N69), A47 (≠ V70), G48 (= G71), M49 (≠ L72), P173 (≠ A206), V174 (= V207), S202 (= S235), G203 (≠ N236), W205 (≠ Y238), F209 (≠ D242)
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 11, 13, 15, 300, 302, 327, 328, 329, 330, 331, 332
- binding glycolic acid: 246, 302, 329
O31616 Glycine oxidase; GO; EC 1.4.3.19 from Bacillus subtilis (strain 168) (see 3 papers)
32% identity, 17% coverage: 181:252/427 of query aligns to 148:221/369 of O31616
Sites not aligning to the query:
- 14:15 binding
- 34:35 binding
- 42:43 binding
- 47:49 binding
- 51 G→R: 130-fold decrease in catalytic efficiency on glycine and 28-fold increase in that on glyphosate.; G→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.
- 54 A→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.
- 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)
24% identity, 50% coverage: 41:252/427 of query aligns to 18:221/369 of S5FMM4
- G51 (≠ N74) 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 (≠ M77) 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 (≠ I111) 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 (= S235) 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.
Sites not aligning to the query:
- 332 I→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.
- 342 M→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
>AO353_13335 FitnessBrowser__pseudo3_N2E3:AO353_13335
MPLREECLWEKLTPQRPDRAALKGEVTADVCVIGAGFTGLSAAVHLLEQGKSVCVLEAKR
CGQGGSGRNVGLVNAGMWIPPDEIEAGFGEAIGSQLNRMLGAAPALVFSLIDKYNIDCQL
RREGTLHMAHNARGEADLRSREEQWKRRGAPVELLTGAACEQATGTKKIAAALLDRRAGT
LNPMAYTSGLAKAAADLGGQLFDHSAVTRLERQGQRWSVQTDAGSVMAEQVVIASNAYTE
GDWTELRRNFFPGYYYQVASAPLTEEAAQLILPGGQGSWDTRQVLSSIRRDKDGRLLLGS
LGNGNQKPTWFLKAWADRVQQHYFPYLKPVDWECTWTGCIAFTPDHLMRLFEPAPGLVAV
TGYNGRGVTTGTVVGKAFADYLCNGNPQALPIPFAPMQPLAGVGLRSCLYEAGFSLYHAG
QCLRIVI
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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