SitesBLAST
Comparing N515DRAFT_0947 FitnessBrowser__Dyella79:N515DRAFT_0947 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 20 (the maximum) hits to proteins with known functional sites (download)
8gxdA L-leucine dehydrogenase from exiguobacterium sibiricum
58% identity, 95% coverage: 2:349/367 of query aligns to 4:351/366 of 8gxdA
P13154 Leucine dehydrogenase; LeuDH; EC 1.4.1.9 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see 2 papers)
55% identity, 97% coverage: 2:356/367 of query aligns to 3:357/367 of P13154
- K68 (= K67) mutation to S: Completely modifies the activity of the enzyme, which is able to catalyze the reductive amination of ketones, and no longer displays leucine dehydrogenase activity; when associated with V-114, C-261 and C-291.
- K80 (= K79) active site
- E114 (= E113) mutation to V: Completely modifies the activity of the enzyme, which is able to catalyze the reductive amination of ketones, and no longer displays leucine dehydrogenase activity; when associated with S-68, C-261 and C-291.
- D261 (≠ N260) mutation to C: Completely modifies the activity of the enzyme, which is able to catalyze the reductive amination of ketones, and no longer displays leucine dehydrogenase activity; when associated with S-68, V-114 and C-291.
- V291 (= V290) mutation to C: Completely modifies the activity of the enzyme, which is able to catalyze the reductive amination of ketones, and no longer displays leucine dehydrogenase activity; when associated with S-68, V-114 and C-261.
6achA Structure of NAD+-bound leucine dehydrogenase from geobacillus stearothermophilus by cryo-em (see paper)
55% identity, 97% coverage: 2:356/367 of query aligns to 3:354/364 of 6achA
B2IXH4 L-tryptophan dehydrogenase; L-Trp dehydrogenase; TrpDH; EC 1.4.1.19 from Nostoc punctiforme (strain ATCC 29133 / PCC 73102) (see paper)
47% identity, 95% coverage: 1:349/367 of query aligns to 2:347/353 of B2IXH4
- L59 (= L58) mutation to F: Does not affect KM for L-tryptophan. 1.77-fold increase in Vmax. Retains 29% of the original activity after 24 hours of incubation at 4 degrees Celsius. Exhibits 6-fold increase in Vmax, high stability and retains 90% of the original activity after 24 hours of incubation at 4 degrees Celsius; when associated with G-168; D-234 and N-296 (TrpDH-4mut).
- D168 (≠ G171) mutation to G: Does not affect KM for L-tryptophan or Vmax. Retains 63% of the original activity after 24 hours of incubation at 4 degrees Celsius. Exhibits 6-fold increase in Vmax, high stability and retains 90% of the original activity after 24 hours of incubation at 4 degrees Celsius; when associated with F-59; D-234 and N-296 (TrpDH-4mut).
- A234 (= A237) mutation to D: Does not affect KM for L-tryptophan. 6.32-fold increase in Vmax. Retains 25% of the original activity after 24 hours of incubation at 4 degrees Celsius. Exhibits 6-fold increase in Vmax, high stability and retains 90% of the original activity after 24 hours of incubation at 4 degrees Celsius; when associated with F-59; G-168 and N-296 (TrpDH-4mut).
- I296 (≠ D298) mutation to N: Does not affect KM for L-tryptophan or Vmax. Retains 79% of the original activity after 24 hours of incubation at 4 degrees Celsius. Exhibits 6-fold increase in Vmax, high stability and retains 90% of the original activity after 24 hours of incubation at 4 degrees Celsius; when associated with F-59; G-168 and D-234 (TrpDH-4mut).
W8CV45 L-tryptophan dehydrogenase; L-Trp dehydrogenase; TrpDH; NpTrpDH; EC 1.4.1.19 from Nostoc punctiforme (see paper)
46% identity, 95% coverage: 1:349/367 of query aligns to 2:347/353 of W8CV45
- M40 (≠ L39) mutation to L: 1.7-fold decrease in catalytic efficiency.
- M65 (= M64) mutation to A: 80-fold decrease in catalytic efficiency.
- A69 (≠ N68) mutation to L: 400-fold decrease in catalytic efficiency.; mutation to M: 293-fold decrease in catalytic efficiency.
- V132 (= V132) mutation to A: 1.6-fold decrease in catalytic efficiency.
- V133 (≠ T133) mutation to A: 3.1-fold decrease in catalytic efficiency.
- L288 (≠ V290) mutation to M: 586-fold decrease in catalytic efficiency.
- V291 (= V293) mutation to A: 7-fold decrease in catalytic efficiency.
- Y292 (≠ S294) mutation to F: Slight increase in catalytic efficiency.; mutation to H: 2.6-fold decrease in catalytic efficiency.; mutation to W: 1.6-fold decrease in catalytic efficiency.
- M295 (≠ I297) mutation to A: 2.6-fold decrease in catalytic efficiency.
- I296 (≠ D298) mutation to A: 2.6-fold decrease in catalytic efficiency.
Q59224 Phenylalanine dehydrogenase; PheDH; EC 1.4.1.20 from Bacillus badius (see paper)
45% identity, 94% coverage: 2:347/367 of query aligns to 15:363/380 of Q59224
- V144 (≠ T133) mutation to D: 3-fold decrease in catalytic efficiency with L-phenylalanine, and 7-fold decrease in catalytic efficiency with L-tyrosine.; mutation to L: 2-fold increase in affinity for L-phenylalanine. Slight increase in catalytic efficiency with L-phenylalanine, while 3-fold decrease in catalytic efficiency with L-tyrosine, leading to an increase in the specificity ratio of phenylalanine over tyrosine by more than 4-folds.; mutation to N: 5-fold decrease in catalytic efficiency with L-phenylalanine, while 2-fold increase in catalytic efficiency with L-tyrosine.
O69056 Valine dehydrogenase; ValDH; EC 1.4.1.23 from Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858) (see 2 papers)
49% identity, 91% coverage: 10:343/367 of query aligns to 22:358/364 of O69056
- K79 (= K67) mutation to A: Loss of activity.
- K91 (= K79) mutation to A: Loss of activity.
- A124 (= A112) mutation to G: Displays lower activities toward aliphatic amino acids, but higher activities toward L-phenylalanine, L-tyrosine and L-methionine.
Q59771 Phenylalanine dehydrogenase; PheDH; EC 1.4.1.20 from Rhodococcus sp. (see 2 papers)
34% identity, 90% coverage: 12:341/367 of query aligns to 12:345/356 of Q59771
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1bxgA Phenylalanine dehydrogenase structure in ternary complex with NAD+ and beta-phenylpropionate (see paper)
34% identity, 90% coverage: 12:341/367 of query aligns to 11:344/349 of 1bxgA
- binding hydrocinnamic acid: G39 (= G40), G40 (= G41), K66 (= K67)
- binding nicotinamide-adenine-dinucleotide: T153 (= T149), G182 (= G179), G184 (= G181), A185 (≠ H182), V186 (= V183), D205 (= D202), T206 (≠ I203), C238 (= C236), A239 (= A237), M240 (≠ L238), A260 (= A258), A261 (= A259), N288 (= N286)
1c1xA L-phenylalanine dehydrogenase structure in ternary complex with NAD+ and l-3-phenyllactate (see paper)
35% identity, 87% coverage: 23:341/367 of query aligns to 22:344/348 of 1c1xA
- binding alpha-hydroxy-beta-phenyl-propionic acid: G39 (= G40), G40 (= G41), M63 (= M64), K66 (= K67), F137 (≠ T133), A292 (≠ V290), L295 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: S149 (≠ P145), T153 (= T149), G182 (= G179), G184 (= G181), A185 (≠ H182), V186 (= V183), D205 (= D202), T206 (≠ I203), R210 (≠ A207), L224 (= L222), C238 (= C236), A239 (= A237), M240 (≠ L238), A260 (= A258), N262 (= N260), N288 (= N286)
1bw9A Phenylalanine dehydrogenase structure in ternary complex with NAD+ and phenylpyruvate (see paper)
35% identity, 87% coverage: 23:341/367 of query aligns to 22:344/350 of 1bw9A
- binding nicotinamide-adenine-dinucleotide: K78 (= K79), P117 (≠ E113), D118 (= D114), V119 (= V115), G182 (= G179), G184 (= G181), A185 (≠ H182), V186 (= V183), A204 (≠ T201), D205 (= D202), T206 (≠ I203), R210 (≠ A207), C238 (= C236), A239 (= A237), M240 (≠ L238), A261 (= A259), N262 (= N260)
- binding 3-phenylpyruvic acid: G39 (= G40), G40 (= G41), M63 (= M64), K66 (= K67), F137 (≠ T133), G291 (= G289), A292 (≠ V290), L295 (vs. gap)
1c1dA L-phenylalanine dehydrogenase structure in ternary complex with nadh and l-phenylalanine (see paper)
35% identity, 87% coverage: 23:341/367 of query aligns to 22:344/349 of 1c1dA
- binding 1,4-dihydronicotinamide adenine dinucleotide: D118 (= D114), S149 (≠ P145), T153 (= T149), G182 (= G179), G184 (= G181), A185 (≠ H182), V186 (= V183), D205 (= D202), T206 (≠ I203), L224 (= L222), C238 (= C236), A239 (= A237), A260 (= A258), A261 (= A259), N262 (= N260), N288 (= N286)
- binding phenylalanine: G39 (= G40), G40 (= G41), M63 (= M64), K66 (= K67), A292 (≠ V290), L295 (vs. gap)
6yeiA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
34% identity, 71% coverage: 31:290/367 of query aligns to 57:340/409 of 6yeiA
- binding nicotinamide-adenine-dinucleotide: T184 (= T149), F213 (≠ C180), G214 (= G181), N215 (≠ H182), V216 (= V183), D236 (= D202), I237 (= I203), A288 (= A237), L289 (= L238), A310 (= A259), N311 (= N260), N336 (= N286)
Sites not aligning to the query:
6yeiF Arabidopsis thaliana glutamate dehydrogenase isoform 1 in complex with NAD (see paper)
34% identity, 71% coverage: 31:290/367 of query aligns to 58:341/410 of 6yeiF
- binding 2-oxoglutaric acid: K66 (≠ L39), G68 (= G41), M87 (= M64), K90 (= K67), K102 (= K79), A140 (= A112), V341 (= V290)
- binding nicotinamide-adenine-dinucleotide: R70 (= R43), D142 (= D114), M143 (≠ V115), T185 (= T149), F214 (≠ C180), G215 (= G181), N216 (≠ H182), V217 (= V183), D237 (= D202), I238 (= I203), A288 (≠ C236), A289 (= A237), A311 (= A259), N312 (= N260), N337 (= N286)
Sites not aligning to the query:
6yehA Arabidopsis thaliana glutamate dehydrogenase isoform 1 in apo form (see paper)
34% identity, 71% coverage: 31:290/367 of query aligns to 57:340/410 of 6yehA
Sites not aligning to the query:
8owmC Crystal structure of glutamate dehydrogenase 2 from arabidopsis thaliana binding ca, NAD and 2,2-dihydroxyglutarate (see paper)
34% identity, 71% coverage: 31:290/367 of query aligns to 60:343/413 of 8owmC
- binding nicotinamide-adenine-dinucleotide: D144 (= D114), M145 (≠ V115), R183 (≠ P145), T187 (= T149), F216 (≠ C180), G217 (= G181), N218 (≠ H182), V219 (= V183), D239 (= D202), I240 (= I203), C290 (= C236), A291 (= A237), A313 (= A259), N314 (= N260), N339 (= N286)
- binding 2,2-bis(oxidanyl)pentanedioic acid: K68 (≠ L39), G70 (= G41), M89 (= M64), K92 (= K67), K104 (= K79), A142 (= A112), R183 (≠ P145), N314 (= N260), V343 (= V290)
Sites not aligning to the query:
8xd5A Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADP and glu in the steady stage of reaction
30% identity, 85% coverage: 31:342/367 of query aligns to 61:407/419 of 8xd5A
- binding gamma-l-glutamic acid: K69 (≠ L39), M90 (= M64), K105 (= K79), A143 (= A112), D145 (= D114), S351 (≠ V293)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R73 (= R43), D145 (= D114), V146 (= V115), Y147 (≠ G116), T191 (= T149), Y220 (≠ C180), G221 (= G181), N222 (≠ H182), A223 (≠ V183), D244 (= D202), S245 (vs. gap), K264 (≠ V212), N281 (≠ L222), A295 (≠ C236), A296 (= A237), I297 (≠ L238), N319 (= N260), N344 (= N286)
8xcsA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus in complex with NADPH, akg and nh4 in the initial stage of reaction
29% identity, 85% coverage: 31:342/367 of query aligns to 60:406/418 of 8xcsA
- binding 2-oxoglutaric acid: K68 (≠ L39), G70 (= G41), M89 (= M64), K92 (= K67), K104 (= K79), A142 (= A112), D144 (= D114), G346 (= G289), S350 (≠ V293)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R72 (= R43), K112 (vs. gap), P143 (≠ E113), D144 (= D114), V145 (= V115), Y146 (≠ G116), T190 (≠ S146), Y219 (≠ C180), G220 (= G181), N221 (≠ H182), A222 (≠ V183), D243 (= D202), S244 (vs. gap), K263 (≠ V212), A295 (= A237), I296 (≠ L238), N318 (= N260)
8xcoA Cryo-em structure of glutamate dehydrogenase from thermococcus profundus incorporating NADPH in the initial stage of reaction
30% identity, 85% coverage: 31:342/367 of query aligns to 58:404/416 of 8xcoA
P80053 Glutamate dehydrogenase 2; GDH-2; EC 1.4.1.3 from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see paper)
31% identity, 72% coverage: 31:296/367 of query aligns to 65:355/420 of P80053
- K254 (vs. gap) modified: N6-methyllysine
- K260 (vs. gap) modified: N6-methyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylmethionine
- 372 modified: N6-methyllysine
- 391 modified: N6-methyllysine
- 392 modified: N6-methyllysine
Query Sequence
>N515DRAFT_0947 FitnessBrowser__Dyella79:N515DRAFT_0947
MIFETIAKTGHEEVVFCHNKDAGLKAIIAIHNTVLGPALGGLRMWPYKTEQDAVNDVLRL
SRGMTYKNAVAGLNLGGGKAVIIGDPSKDKSEALFRAFGRFVNSLNGRYITAEDVGIDVN
DMEYVFRETEYVTGVHQVHGGSGDPSPFTAFGTLQGLMAALQVKHGNEDVGKYSYAVQGC
GHVGSEFIKLLREQGAKVFVTDINKDAVQRCVDELGCEAVGLDEIYDVDADVYSPCALGG
TLNEQTIDRIKAKIICGAANNQLATDAIGDELTRRGVLYAPDYAVNAGGVMNVSLEIDGY
NRERAMRMMRTIYYNLGRIFEISKSENVPTYKAADRLAEERISSIGKIKLPHMGNGAPRF
AGRMRGQ
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