SitesBLAST
Comparing AO356_15895 FitnessBrowser__pseudo5_N2C3_1:AO356_15895 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
7cyxA Crystal strcuture of glycine oxidase from bacillus cereus atcc 14579 (see paper)
31% identity, 95% coverage: 7:352/366 of query aligns to 4:348/363 of 7cyxA
- binding flavin-adenine dinucleotide: I7 (≠ V10), G8 (= G11), G10 (= G13), V11 (= V14), I12 (= I15), V30 (≠ L33), E31 (≠ D34), K32 (≠ R35), E38 (= E41), A39 (≠ S42), S40 (= S43), A43 (≠ G46), G45 (= G48), L46 (≠ I49), V171 (= V175), G200 (≠ A204), G201 (= G205), W203 (= W207), G298 (= G302), R300 (= R304), P301 (= P305), Y326 (= Y330), R327 (= R331), N328 (= N332), G329 (= G333), I330 (≠ L334)
3if9A Crystal structure of glycine oxidase g51s/a54r/h244a mutant in complex with inhibitor glycolate (see paper)
29% identity, 91% coverage: 21:352/366 of query aligns to 21:350/364 of 3if9A
- active site: A47 (≠ G47), G48 (= G48), M49 (≠ I49)
- binding flavin-adenine dinucleotide: E34 (≠ D34), S35 (≠ R35), T42 (≠ S42), T43 (≠ S43), A46 (≠ G46), A47 (≠ G47), G48 (= G48), M49 (≠ I49), P173 (≠ E174), V174 (= V175), S202 (≠ A204), G203 (= G205), W205 (= W207), F209 (≠ L211), G300 (= G302), R302 (= R304), H327 (= H329), F328 (≠ Y330), R329 (= R331), N330 (= N332), G331 (= G333), I332 (≠ L334)
- binding glycolic acid: Y246 (= Y248), R302 (= R304), R329 (= R331)
Sites not aligning to the query:
O31616 Glycine oxidase; GO; EC 1.4.3.19 from Bacillus subtilis (strain 168) (see 3 papers)
28% identity, 91% coverage: 21:352/366 of query aligns to 21:350/369 of O31616
- ES 34:35 (≠ DR 34:35) binding
- TT 42:43 (≠ SS 42:43) binding
- AGM 47:49 (≠ GGI 47:49) binding
- G51 (≠ S51) 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 (≠ Y54) 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 (= V175) binding
- H244 (≠ G246) 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 (= R304) binding
- 327:333 (vs. 329:335, 57% identical) binding
- R329 (= R331) binding
Sites not aligning to the query:
1ng3A Complex of thio (glycine oxidase) with acetyl-glycine (see paper)
28% identity, 91% coverage: 21:352/366 of query aligns to 21:350/364 of 1ng3A
- active site: A47 (≠ G47), G48 (= G48), M49 (≠ I49)
- binding acetylamino-acetic acid: Y246 (= Y248), R302 (= R304), R329 (= R331)
- binding flavin-adenine dinucleotide: F33 (≠ L33), E34 (≠ D34), S35 (≠ R35), R41 (≠ E41), T42 (≠ S42), T43 (≠ S43), A46 (≠ G46), A47 (≠ G47), G48 (= G48), M49 (≠ I49), V174 (= V175), S202 (≠ A204), G203 (= G205), W205 (= W207), F209 (≠ L211), G300 (= G302), R302 (= R304), H327 (= H329), R329 (= R331), N330 (= N332), G331 (= G333), I332 (≠ L334)
- binding phosphate ion: R89 (≠ Q89), R254 (≠ H256)
Sites not aligning to the query:
4yshA Crystal structure of glycine oxidase from geobacillus kaustophilus
30% identity, 93% coverage: 21:361/366 of query aligns to 20:364/370 of 4yshA
- active site: A45 (≠ G46), M48 (≠ I49), L49 (≠ V50), Q52 (≠ L53), I262 (≠ V259), L283 (= L280), G305 (= G302), N335 (= N332), L338 (≠ V335)
- binding flavin-adenine dinucleotide: F32 (≠ L33), E33 (≠ D34), K34 (≠ R35), G40 (≠ E41), A41 (≠ S42), S42 (= S43), A45 (≠ G46), A46 (≠ G47), G47 (= G48), M48 (≠ I49), V178 (= V175), S206 (≠ A204), G207 (= G205), W209 (= W207), R307 (= R304), H332 (= H329), R334 (= R331), N335 (= N332), G336 (= G333), I337 (≠ L334)
Sites not aligning to the query:
4yshB Crystal structure of glycine oxidase from geobacillus kaustophilus
30% identity, 93% coverage: 21:361/366 of query aligns to 20:364/368 of 4yshB
- active site: A45 (≠ G46), M48 (≠ I49), L49 (≠ V50), Q52 (≠ L53), I262 (≠ V259), L283 (= L280), G305 (= G302), N335 (= N332), L338 (≠ V335)
- binding flavin-adenine dinucleotide: F32 (≠ L33), E33 (≠ D34), K34 (≠ R35), G40 (≠ E41), A41 (≠ S42), S42 (= S43), A45 (≠ G46), A46 (≠ G47), M48 (≠ I49), V178 (= V175), S206 (≠ A204), W209 (= W207), R307 (= R304), H332 (= H329), R334 (= R331), N335 (= N332), G336 (= G333), I337 (≠ L334), L338 (≠ V335)
- binding glycine: G249 (= G246), Y251 (= Y248), Y251 (= Y248), A264 (≠ S261), R307 (= R304), R334 (= R331), R334 (= R331)
Sites not aligning to the query:
Q5L2C2 Glycine oxidase; GO; GOX; GOXK; EC 1.4.3.19 from Geobacillus kaustophilus (strain HTA426)
30% identity, 93% coverage: 21:361/366 of query aligns to 21:366/377 of Q5L2C2
- EK 34:35 (≠ DR 34:35) binding
- AS 42:43 (≠ SS 42:43) binding
- AGM 47:49 (≠ GGI 47:49) binding
- V180 (= V175) binding
- R309 (= R304) binding
- 334:340 (vs. 329:335, 71% identical) binding
- R336 (= R331) binding
Sites not aligning to the query:
S5FMM4 Glycine oxidase; GO; BliGO; EC 1.4.3.19 from Bacillus licheniformis (see paper)
26% identity, 90% coverage: 20:350/366 of query aligns to 20:348/369 of S5FMM4
- G51 (≠ S51) 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 (≠ Y54) 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 (≠ F81) 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 (≠ A204) 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 (≠ L334) 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 (≠ F344) 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.
5i39A High resolution structure of l-amino acid deaminase from proteus vulgaris with the deletion of the specific insertion sequence (see paper)
24% identity, 99% coverage: 1:361/366 of query aligns to 21:379/383 of 5i39A
- active site: F66 (≠ A45), Q69 (≠ G48), A70 (≠ I49), Q248 (≠ K225), P267 (≠ A244)
- binding flavin-adenine dinucleotide: V30 (= V10), G31 (= G11), G33 (= G13), I34 (≠ V14), L35 (≠ I15), V53 (≠ L33), E54 (≠ D34), K55 (≠ R35), Q62 (≠ E41), S63 (= S42), F66 (≠ A45), Y67 (≠ G46), Q69 (≠ G48), A196 (≠ E174), A197 (≠ V175), G226 (≠ A204), G227 (= G205), W229 (= W207), Q248 (≠ K225), Q250 (= Q227), G321 (= G302), M323 (≠ R304), T348 (≠ H329), G349 (≠ Y330), W350 (≠ R331), G351 (= G333), M352 (≠ L334), T353 (≠ V335)
6j39A Crystal structure of cmis2 with inhibitor (see paper)
27% identity, 93% coverage: 15:355/366 of query aligns to 11:359/368 of 6j39A
- binding (3R)-3-[(carboxymethyl)sulfanyl]nonanoic acid: M44 (≠ G48), P46 (≠ V50), N49 (≠ L53), R243 (≠ L243), Y252 (= Y248), Y267 (≠ L263), R308 (= R304), R334 (= R331), I335 (≠ N332)
- binding flavin-adenine dinucleotide: I11 (= I15), V29 (≠ L33), D30 (= D34), P31 (≠ R35), E32 (≠ S36), K36 (≠ Q40), A37 (≠ E41), S38 (= S42), V40 (≠ W44), S41 (≠ A45), A42 (≠ G46), G43 (= G47), M44 (≠ G48), A174 (≠ C173), A203 (= A204), W206 (= W207), I228 (≠ M228), Y252 (= Y248), R308 (= R304), S333 (≠ Y330), R334 (= R331), I335 (≠ N332), G336 (= G333), V337 (≠ L334), Q338 (≠ V335)
Sites not aligning to the query:
6j38A Crystal structure of cmis2 (see paper)
27% identity, 93% coverage: 15:355/366 of query aligns to 11:359/368 of 6j38A
- binding flavin-adenine dinucleotide: I11 (= I15), V29 (≠ L33), D30 (= D34), P31 (≠ R35), K36 (≠ Q40), A37 (≠ E41), S38 (= S42), S41 (≠ A45), A42 (≠ G46), G43 (= G47), M44 (≠ G48), A174 (≠ C173), A203 (= A204), W206 (= W207), G226 (= G226), G306 (= G302), R308 (= R304), S333 (≠ Y330), R334 (= R331), I335 (≠ N332), G336 (= G333), V337 (≠ L334), Q338 (≠ V335)
Sites not aligning to the query:
6pxsA Crystal structure of iminodiacetate oxidase (idaa) from chelativorans sp. Bnc1 (see paper)
28% identity, 98% coverage: 6:364/366 of query aligns to 2:367/370 of 6pxsA
- binding flavin-adenine dinucleotide: G7 (= G11), G9 (= G13), I10 (≠ V14), D30 (= D34), N32 (≠ S36), H33 (≠ S37), K36 (≠ Q40), A37 (≠ S42), T38 (≠ S43), A40 (= A45), G41 (= G46), A42 (≠ G47), G43 (= G48), V44 (≠ I49), Y174 (≠ C173), A203 (= A204), W206 (= W207), I210 (≠ L211), Y250 (= Y248), G305 (= G302), R307 (= R304), G333 (≠ Y330), A334 (≠ R331), S335 (≠ N332), G336 (= G333), L337 (= L334), T338 (≠ V335)
5hxwA L-amino acid deaminase from proteus vulgaris (see paper)
22% identity, 99% coverage: 1:361/366 of query aligns to 13:429/433 of 5hxwA
- active site: F58 (≠ A45), Q61 (≠ G48), A62 (≠ I49), Q240 (≠ G226), V284 (= V242), F288 (≠ G246)
- binding cetyl-trimethyl-ammonium: G291 (vs. gap), Y294 (vs. gap), N310 (vs. gap), E311 (vs. gap), F317 (≠ T262), M318 (≠ L263), S320 (≠ R265), M373 (≠ R304), E379 (≠ G310), G399 (≠ Y330), W400 (≠ R331)
- binding flavin-adenine dinucleotide: V22 (= V10), G23 (= G11), G25 (= G13), I26 (≠ V14), L27 (≠ I15), E46 (≠ D34), K47 (≠ R35), E53 (≠ Q40), Q54 (≠ E41), S55 (= S42), R57 (≠ W44), F58 (≠ A45), Y59 (≠ G46), G60 (= G47), Q61 (≠ G48), A188 (≠ E174), A189 (≠ V175), G218 (≠ A204), G219 (= G205), W221 (= W207), Q240 (≠ G226), Q242 (≠ M228), F331 (vs. gap), G371 (= G302), M373 (≠ R304), T398 (≠ H329), G399 (≠ Y330), W400 (≠ R331), G401 (= G333), M402 (≠ L334), T403 (≠ V335)
5fjnA Structure of l-amino acid deaminase from proteus myxofaciens in complex with anthranilate (see paper)
24% identity, 94% coverage: 18:361/366 of query aligns to 42:441/447 of 5fjnA
- active site: S67 (= S43), Y71 (≠ V50), S72 (= S51), L252 (vs. gap)
- binding 2-aminobenzoic acid: L252 (vs. gap), R289 (vs. gap), V411 (≠ Y330), W412 (≠ R331)
- binding flavin-adenine dinucleotide: L57 (= L33), E58 (≠ D34), K59 (≠ R35), E65 (= E41), Q66 (≠ S42), S67 (= S43), A70 (≠ I49), Y71 (≠ V50), S72 (= S51), Q73 (≠ P52), V201 (= V175), G230 (≠ A204), G231 (= G205), W233 (= W207), L252 (vs. gap), Q254 (vs. gap), F343 (vs. gap), V385 (≠ R304), T410 (≠ H329), V411 (≠ Y330), W412 (≠ R331), G413 (= G333), M414 (≠ L334), T415 (≠ V335)
Sites not aligning to the query:
5fjmA Structure of l-amino acid deaminase from proteus myxofaciens (see paper)
24% identity, 94% coverage: 18:361/366 of query aligns to 42:441/447 of 5fjmA
- active site: S67 (= S43), Y71 (≠ V50), S72 (= S51), L252 (vs. gap)
- binding flavin-adenine dinucleotide: L57 (= L33), E58 (≠ D34), K59 (≠ R35), E65 (= E41), Q66 (≠ S42), S67 (= S43), A70 (≠ I49), Y71 (≠ V50), S72 (= S51), Q73 (≠ P52), V201 (= V175), G230 (≠ A204), G231 (= G205), W233 (= W207), L252 (vs. gap), Q254 (vs. gap), F343 (vs. gap), V385 (≠ R304), T410 (≠ H329), V411 (≠ Y330), W412 (≠ R331), G413 (= G333), M414 (≠ L334), T415 (≠ V335)
Sites not aligning to the query:
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)
24% identity, 96% coverage: 6:356/366 of query aligns to 27:391/824 of Q8GAI3
- W66 (= W44) mutation W->F,S: Contains a non-covalently bound FAD. Loss of enzyme activity.
- H67 (≠ A45) mutation to A: Contains a non-covalently bound FAD. Exhibits about 10% of the wild-type enzyme activity.
2gagB Heteroteterameric sarcosine: structure of a diflavin metaloenzyme at 1.85 a resolution (see paper)
23% identity, 96% coverage: 3:353/366 of query aligns to 18:375/403 of 2gagB
- active site: A61 (≠ W44), T64 (≠ G47), T65 (≠ G48)
- binding flavin-adenine dinucleotide: G26 (= G11), G28 (= G13), G29 (≠ V14), H30 (≠ I15), E51 (≠ D34), K52 (≠ R35), G58 (≠ E41), N59 (≠ S42), M60 (≠ S43), R62 (≠ A45), N63 (≠ G46), T64 (≠ G47), I66 (= I49), V195 (= V175), G224 (≠ A204), A225 (≠ G205), H227 (≠ W207), L231 (= L211), L246 (≠ G226), G352 (≠ Y330), T353 (≠ R331), G354 (≠ N332), G355 (= G333), F356 (≠ L334), K357 (≠ V335)
- binding flavin mononucleotide: A61 (≠ W44), R62 (≠ A45), H171 (≠ V148), V250 (≠ L230), E278 (≠ H256), R321 (≠ G298), W323 (= W300)
- binding 2-furoic acid: T64 (≠ G47), I66 (= I49), R68 (≠ S51), M263 (≠ L243), Y270 (= Y248), K357 (≠ V335)
- binding sulfite ion: K170 (≠ N147), K276 (≠ D254)
Sites not aligning to the query:
Q9UI17 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Homo sapiens (Human) (see 4 papers)
23% identity, 98% coverage: 6:362/366 of query aligns to 51:429/866 of Q9UI17
- CV 59:60 (≠ VI 14:15) binding
- EK 80:81 (≠ DR 34:35) binding
- 87:95 (vs. 41:49, 33% identical) binding
- H91 (≠ A45) modified: Tele-8alpha-FAD histidine
- H109 (≠ A66) to R: in DMGDHD; shows 10 fold lower catalytic efficiency due to lower cofactor saturation and reduced thermal stability; dbSNP:rs121908331
- V219 (= V175) binding
- S279 (= S235) to P: in dbSNP:rs532964
- FGYGII 397:402 (≠ YRNGLV 330:335) binding
Sites not aligning to the query:
- 530 A → G: in dbSNP:rs1805073
- 646 S → P: in dbSNP:rs1805074
Q63342 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Rattus norvegicus (Rat) (see 2 papers)
23% identity, 98% coverage: 6:362/366 of query aligns to 44:422/857 of Q63342
- CV 52:53 (≠ VI 14:15) binding
- EK 73:74 (≠ DR 34:35) binding
- 80:88 (vs. 41:49, 33% identical) binding
- H84 (≠ A45) modified: Tele-8alpha-FAD histidine
- V212 (= V175) binding
- W244 (= W207) binding
- FGYGII 390:395 (≠ YRNGLV 330:335) binding
Sites not aligning to the query:
- 573:575 binding
- 669 binding
- 676:678 binding
- 737 binding
4pabB Crystal structure of the precursor form of rat dmgdh complexed with tetrahydrofolate (see paper)
23% identity, 98% coverage: 6:362/366 of query aligns to 7:385/824 of 4pabB
- active site: T53 (≠ S51), E102 (≠ D102), H226 (≠ G226), Y255 (≠ A249)
- binding flavin-adenine dinucleotide: I11 (≠ V10), G12 (= G11), G14 (= G13), C15 (≠ V14), V16 (≠ I15), L35 (= L33), E36 (≠ D34), K37 (≠ R35), G43 (≠ E41), S44 (= S42), T45 (≠ S43), H47 (≠ A45), A48 (≠ G46), A49 (≠ G47), G50 (= G48), L51 (≠ I49), V175 (= V175), A204 (= A204), G205 (= G205), W207 (= W207), H226 (≠ G226), Y228 (≠ M228), G326 (= G302), I328 (≠ R304), F353 (≠ Y330), Y355 (≠ N332), G356 (= G333), I357 (≠ L334), I358 (≠ V335)
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
Query Sequence
>AO356_15895 FitnessBrowser__pseudo5_N2C3_1:AO356_15895
MTRQQQVVIVGGGVIGLLTAFNLASEGQRVVLLDRSSVGQESSWAGGGIVSPLYPWRYSP
AVTALAHWSQDFYPQLGERLFAATGIDPQVHVTGLYWLDLDDQDEALAWAEREGRPLRAV
DISTVHDAVPVLGAGFSRAIYMAGVANVRNPRLVKSLKAALQALPNVTLHEHCEVNGFIR
DGGRVVGVDSSAGPMRGDQVVLAAGAWSGELLKTLGLKLPVEPVKGQMILYKCASDFLSS
MVLAKGRYAIPRRDGHILVGSTLEREGFDKTPTEVALESLKTSAQQLIPALAGAEVVGHW
AGLRPGSPEGIPYIGEVPGVAGLWLNCGHYRNGLVLAPASCQLFTDLMLGREPVIDPVPY
APAGRL
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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