SitesBLAST
Comparing Ga0059261_1343 FitnessBrowser__Korea:Ga0059261_1343 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)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
58% identity, 99% coverage: 6:463/464 of query aligns to 1:465/465 of 3urhB
- active site: Y35 (≠ L40), C39 (= C44), C44 (= C49), S47 (= S52), V183 (= V182), E187 (= E186), H443 (= H441), H445 (= H443), E450 (= E448)
- binding flavin-adenine dinucleotide: I6 (= I11), G7 (= G12), G9 (= G14), P10 (= P15), G11 (= G16), E30 (= E35), K31 (≠ G36), G37 (= G42), T38 (= T43), C39 (= C44), G43 (= G48), C44 (= C49), K48 (= K53), T111 (≠ Y117), G112 (≠ A118), A140 (= A141), T141 (= T142), G142 (= G143), I184 (= I183), R273 (= R272), G312 (= G311), D313 (= D312), M319 (= M318), L320 (= L319), A321 (= A320), H322 (= H321)
P31023 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; Pyruvate dehydrogenase complex E3 subunit; E3; PDC-E3; EC 1.8.1.4 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see 2 papers)
56% identity, 99% coverage: 7:464/464 of query aligns to 39:501/501 of P31023
- 67:76 (vs. 35:44, 70% identical) binding FAD
- C76 (= C44) modified: Disulfide link with 81, Redox-active
- C81 (= C49) modified: Disulfide link with 76, Redox-active
- G149 (≠ A118) binding FAD
- D348 (= D312) binding FAD
- MLAH 354:357 (= MLAH 318:321) binding FAD
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
56% identity, 99% coverage: 7:464/464 of query aligns to 5:467/467 of 1dxlA
- active site: L38 (= L40), C42 (= C44), C47 (= C49), S50 (= S52), Y184 (≠ V182), E188 (= E186), H444 (= H441), H446 (= H443), E451 (= E448)
- binding flavin-adenine dinucleotide: I9 (= I11), P13 (= P15), G14 (= G16), E33 (= E35), K34 (≠ G36), R35 (= R37), G40 (= G42), T41 (= T43), C42 (= C44), G46 (= G48), C47 (= C49), K51 (= K53), Y114 (= Y117), G115 (≠ A118), T144 (= T142), G145 (= G143), Y184 (≠ V182), I185 (= I183), R274 (= R272), D314 (= D312), M320 (= M318), L321 (= L319), A322 (= A320), H323 (= H321)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
55% identity, 99% coverage: 5:464/464 of query aligns to 4:472/472 of 1zmdA
- active site: L39 (= L40), C43 (= C44), C48 (= C49), S51 (= S52), V186 (= V182), E190 (= E186), H448 (= H441), H450 (= H443), E455 (= E448)
- binding flavin-adenine dinucleotide: I10 (= I11), G11 (= G12), G13 (= G14), P14 (= P15), G15 (= G16), E34 (= E35), K35 (≠ G36), N36 (≠ R37), G41 (= G42), T42 (= T43), C43 (= C44), G47 (= G48), C48 (= C49), K52 (= K53), Y116 (= Y117), G117 (≠ A118), T146 (= T142), G147 (= G143), S166 (= S162), R278 (= R272), F281 (≠ N275), G317 (= G311), D318 (= D312), M324 (= M318), L325 (= L319), A326 (= A320), H327 (= H321)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I178), G183 (= G179), G185 (= G181), V186 (= V182), I187 (= I183), E190 (= E186), E206 (= E202), F207 (≠ Y203), L208 (= L204), I276 (= I270), G277 (= G271), R278 (= R272), M324 (= M318), L325 (= L319), V355 (= V349), Y357 (= Y351)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
55% identity, 99% coverage: 5:464/464 of query aligns to 4:472/472 of 1zmcA
- active site: L39 (= L40), C43 (= C44), C48 (= C49), S51 (= S52), V186 (= V182), E190 (= E186), H448 (= H441), H450 (= H443), E455 (= E448)
- binding flavin-adenine dinucleotide: I10 (= I11), G11 (= G12), G13 (= G14), P14 (= P15), G15 (= G16), E34 (= E35), K35 (≠ G36), N36 (≠ R37), G41 (= G42), T42 (= T43), C43 (= C44), G47 (= G48), C48 (= C49), K52 (= K53), Y116 (= Y117), G117 (≠ A118), T146 (= T142), G147 (= G143), S166 (= S162), I187 (= I183), F281 (≠ N275), G317 (= G311), D318 (= D312), M324 (= M318), L325 (= L319), A326 (= A320), H327 (= H321)
- binding nicotinamide-adenine-dinucleotide: G183 (= G179), G185 (= G181), V205 (= V201), E206 (= E202), F207 (≠ Y203), L208 (= L204), K240 (= K235), V241 (= V236), I276 (= I270), G277 (= G271), R278 (= R272), R297 (= R291), M324 (= M318)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
55% identity, 99% coverage: 5:464/464 of query aligns to 41:509/509 of P09622
- 71:80 (vs. 35:44, 80% identical) binding FAD
- K72 (≠ G36) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K53) binding FAD; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ G68) to T: in dbSNP:rs1130477
- G154 (≠ A118) binding FAD
- TGS 183:185 (= TGS 142:144) binding FAD
- 220:227 (vs. 179:186, 75% identical) binding NAD(+)
- E243 (= E202) binding NAD(+)
- V278 (= V236) binding NAD(+)
- G314 (= G271) binding NAD(+)
- D355 (= D312) binding FAD
- MLAH 361:364 (= MLAH 318:321) binding FAD
- E375 (= E332) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ I340) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (= D404) Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex; mutation to A: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.; mutation to N: Does not affect dihydrolipoyl dehydrogenase activity.
- E466 (≠ Q422) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ F429) Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex; mutation to A: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.; mutation to F: Does not affect dihydrolipoyl dehydrogenase activity.; mutation to H: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.
- D479 (= D435) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ Y438) to G: in DLDD; reduced enzyme activity; dbSNP:rs397514650; mutation to A: Does not affect dihydrolipoyl dehydrogenase activity.; mutation to M: Does not affect interaction with PDHX.
- H485 (= H441) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P444) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (= S447) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E448) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ K451) to G: in DLDD; loss of enzyme activity; reduced interaction with PDHX; dbSNP:rs121964989
- K505 (= K460) mutation to M: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
55% identity, 99% coverage: 5:464/464 of query aligns to 14:482/482 of 6hg8B
- active site: C53 (= C44), C58 (= C49), S61 (= S52), V196 (= V182), E200 (= E186), H460 (= H443), E465 (= E448)
- binding flavin-adenine dinucleotide: I20 (= I11), G23 (= G14), P24 (= P15), G25 (= G16), E44 (= E35), K45 (≠ G36), N46 (≠ R37), G51 (= G42), T52 (= T43), C53 (= C44), G57 (= G48), C58 (= C49), K62 (= K53), Y126 (= Y117), G127 (≠ A118), T156 (= T142), G157 (= G143), I197 (= I183), R288 (= R272), F291 (≠ N275), G327 (= G311), D328 (= D312), M334 (= M318), L335 (= L319), A336 (= A320), H337 (= H321)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
52% identity, 99% coverage: 6:464/464 of query aligns to 7:470/470 of 6uziC
- active site: C45 (= C44), C50 (= C49), S53 (= S52), V187 (= V182), E191 (= E186), H448 (= H443), E453 (= E448)
- binding flavin-adenine dinucleotide: I12 (= I11), G13 (= G12), G15 (= G14), P16 (= P15), G17 (= G16), E36 (= E35), K37 (≠ G36), G43 (= G42), T44 (= T43), C45 (= C44), G49 (= G48), C50 (= C49), S53 (= S52), K54 (= K53), V117 (≠ Y117), G118 (≠ A118), T147 (= T142), G148 (= G143), I188 (= I183), R276 (= R272), D316 (= D312), M322 (= M318), L323 (= L319), A324 (= A320)
- binding zinc ion: H448 (= H443), E453 (= E448)
2qaeA Crystal structure analysis of trypanosoma cruzi lipoamide dehydrogenase
53% identity, 96% coverage: 20:464/464 of query aligns to 17:465/465 of 2qaeA
- active site: L37 (= L40), C41 (= C44), C46 (= C49), S49 (= S52), V184 (= V182), E188 (= E186), H442 (= H441), H444 (= H443), E449 (= E448)
- binding flavin-adenine dinucleotide: E32 (= E35), K33 (≠ G36), R34 (= R37), G39 (= G42), T40 (= T43), C41 (= C44), G45 (= G48), C46 (= C49), K50 (= K53), E114 (≠ Y117), G115 (≠ A118), T144 (= T142), G145 (= G143), S164 (= S162), I185 (= I183), F274 (≠ N275), G310 (= G311), D311 (= D312), M318 (= M318), L319 (= L319), A320 (= A320), H321 (= H321)
Sites not aligning to the query:
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
52% identity, 99% coverage: 6:464/464 of query aligns to 2:455/455 of 2yquB
- active site: P11 (= P15), L36 (= L40), C40 (= C44), C45 (= C49), S48 (= S52), G72 (≠ K79), V73 (= V80), V177 (= V182), E181 (= E186), S314 (≠ E324), H432 (= H441), H434 (= H443), E439 (= E448)
- binding carbonate ion: A310 (= A320), S314 (≠ E324), S423 (≠ T432), D426 (= D435)
- binding flavin-adenine dinucleotide: G8 (= G12), G10 (= G14), P11 (= P15), G12 (= G16), E31 (= E35), K32 (≠ G36), G38 (= G42), T39 (= T43), C40 (= C44), R42 (≠ N46), G44 (= G48), C45 (= C49), K49 (= K53), T110 (≠ Y117), A111 (= A118), T137 (= T142), G138 (= G143), I178 (= I183), Y265 (≠ N275), G301 (= G311), D302 (= D312), M308 (= M318), L309 (= L319), A310 (= A320), H311 (= H321)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
52% identity, 99% coverage: 6:464/464 of query aligns to 2:455/455 of 2yquA
- active site: P11 (= P15), L36 (= L40), C40 (= C44), C45 (= C49), S48 (= S52), G72 (≠ K79), V73 (= V80), V177 (= V182), E181 (= E186), S314 (≠ E324), H432 (= H441), H434 (= H443), E439 (= E448)
- binding flavin-adenine dinucleotide: G8 (= G12), G10 (= G14), P11 (= P15), G12 (= G16), E31 (= E35), K32 (≠ G36), G38 (= G42), T39 (= T43), C40 (= C44), R42 (≠ N46), G44 (= G48), C45 (= C49), K49 (= K53), T110 (≠ Y117), A111 (= A118), T137 (= T142), G138 (= G143), S157 (= S162), I178 (= I183), Y265 (≠ N275), G301 (= G311), D302 (= D312), M308 (= M318), L309 (= L319), A310 (= A320)
P09624 Dihydrolipoyl dehydrogenase, mitochondrial; DLD; 2-oxoglutarate dehydrogenase complex component E3; OGDC-E3; OGDHC subunit E3; Alpha-ketoglutarate dehydrogenase complex subunit E3; alpha-KGDHC subunit E3; Dihydrolipoamide dehydrogenase; Dihydrolipoamide:NAD(+) oxidoreductase; Glycine decarboxylase complex subunit L; GDC subunit L; Lipoamide dehydrogenase component of pyruvate dehydrogenase complex; Pyruvate dehydrogenase complex E3 component; PDC subunit E3; PDH complex subunit E3; EC 1.8.1.4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
51% identity, 98% coverage: 7:463/464 of query aligns to 28:498/499 of P09624
- 56:65 (vs. 35:44, 70% identical) binding FAD
- C65 (= C44) modified: Disulfide link with 70, Redox-active
- C70 (= C49) modified: Disulfide link with 65, Redox-active
- K74 (= K53) binding FAD
- G139 (≠ A118) binding FAD
- D346 (= D312) binding FAD
- MLAH 352:355 (= MLAH 318:321) binding FAD
- H478 (= H443) active site, Proton acceptor
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
1v59A Crystal structure of yeast lipoamide dehydrogenase complexed with NAD+
51% identity, 98% coverage: 7:463/464 of query aligns to 7:477/478 of 1v59A
- active site: L40 (= L40), C44 (= C44), C49 (= C49), S52 (= S52), I193 (≠ V182), E197 (= E186), T349 (≠ G336), H455 (= H441), H457 (= H443), E462 (= E448)
- binding flavin-adenine dinucleotide: G14 (= G14), P15 (= P15), A16 (≠ G16), E35 (= E35), K36 (≠ G36), R37 (= R37), G42 (= G42), T43 (= T43), C44 (= C44), G48 (= G48), C49 (= C49), K53 (= K53), N117 (≠ Y117), G118 (≠ A118), T153 (= T142), G154 (= G143), R285 (= R272), Y288 (≠ N275), G324 (= G311), D325 (= D312), M331 (= M318), L332 (= L319), A333 (= A320), H334 (= H321), Y364 (= Y351)
- binding nicotinamide-adenine-dinucleotide: I189 (= I178), G190 (= G179), E213 (= E202), F214 (≠ Y203), K246 (= K235), V283 (≠ I270)
1jehA Crystal structure of yeast e3, lipoamide dehydrogenase (see paper)
51% identity, 98% coverage: 7:463/464 of query aligns to 7:477/478 of 1jehA
- active site: L40 (= L40), C44 (= C44), C49 (= C49), S52 (= S52), I193 (≠ V182), E197 (= E186), T349 (≠ G336), H455 (= H441), H457 (= H443), E462 (= E448)
- binding flavin-adenine dinucleotide: I11 (= I11), G14 (= G14), P15 (= P15), A16 (≠ G16), V34 (≠ A34), E35 (= E35), K36 (≠ G36), R37 (= R37), G42 (= G42), T43 (= T43), C44 (= C44), G48 (= G48), C49 (= C49), K53 (= K53), G118 (≠ A118), T153 (= T142), G154 (= G143), I194 (= I183), R285 (= R272), Y288 (≠ N275), L292 (= L279), G324 (= G311), D325 (= D312), M331 (= M318), L332 (= L319), A333 (= A320), H334 (= H321)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
52% identity, 98% coverage: 6:461/464 of query aligns to 2:452/452 of 2eq7A
- active site: P11 (= P15), L36 (= L40), C40 (= C44), C45 (= C49), S48 (= S52), G72 (≠ K79), V73 (= V80), V177 (= V182), E181 (= E186), S314 (≠ E324), H432 (= H441), H434 (= H443), E439 (= E448)
- binding flavin-adenine dinucleotide: G10 (= G14), P11 (= P15), G12 (= G16), E31 (= E35), K32 (≠ G36), G38 (= G42), T39 (= T43), C40 (= C44), R42 (≠ N46), G44 (= G48), C45 (= C49), K49 (= K53), T110 (≠ Y117), A111 (= A118), T137 (= T142), G138 (= G143), S157 (= S162), I178 (= I183), R262 (= R272), Y265 (≠ N275), D302 (= D312), M308 (= M318), L309 (= L319), A310 (= A320), H311 (= H321), Y341 (= Y351)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ G151), G174 (= G179), G176 (= G181), V177 (= V182), I178 (= I183), E197 (= E202), Y198 (= Y203), V231 (= V236), V260 (≠ I270), G261 (= G271), R262 (= R272), M308 (= M318), L309 (= L319), V339 (= V349)
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
52% identity, 99% coverage: 6:464/464 of query aligns to 5:472/475 of 6awaA
- active site: L45 (= L40), C49 (= C44), C54 (= C49), S57 (= S52), V191 (= V182), E195 (= E186), F449 (≠ H441), H451 (= H443), E456 (= E448)
- binding adenosine monophosphate: I187 (= I178), E211 (= E202), A212 (≠ Y203), L213 (= L204), V245 (= V236), V277 (≠ I270)
- binding flavin-adenine dinucleotide: I10 (= I11), G13 (= G14), P14 (= P15), G15 (= G16), E34 (vs. gap), K35 (vs. gap), T48 (= T43), C49 (= C44), G53 (= G48), C54 (= C49), K58 (= K53), H121 (≠ Y117), G122 (≠ A118), S151 (≠ T142), G152 (= G143), I192 (= I183), R279 (= R272), G318 (= G311), D319 (= D312), M325 (= M318), L326 (= L319), A327 (= A320), Y358 (= Y351)
Sites not aligning to the query:
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
52% identity, 99% coverage: 6:464/464 of query aligns to 5:472/478 of P14218
- 34:49 (vs. 34:44, 44% identical) binding FAD
- C49 (= C44) modified: Disulfide link with 54, Redox-active
- C54 (= C49) modified: Disulfide link with 49, Redox-active
- K58 (= K53) binding FAD
- G122 (≠ A118) binding FAD
- D319 (= D312) binding FAD
- A327 (= A320) binding FAD
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
52% identity, 99% coverage: 6:464/464 of query aligns to 7:474/477 of 5u8uD
- active site: P16 (= P15), L47 (= L40), C51 (= C44), C56 (= C49), S59 (= S52), G85 (≠ K79), V86 (= V80), V193 (= V182), E197 (= E186), S333 (≠ E324), F451 (≠ H441), H453 (= H443), E458 (= E448)
- binding flavin-adenine dinucleotide: I12 (= I11), G15 (= G14), P16 (= P15), G17 (= G16), E36 (vs. gap), K37 (vs. gap), G49 (= G42), T50 (= T43), C51 (= C44), G55 (= G48), C56 (= C49), K60 (= K53), H123 (≠ Y117), G124 (≠ A118), A152 (= A141), S153 (≠ T142), G154 (= G143), I194 (= I183), R281 (= R272), G320 (= G311), D321 (= D312), M327 (= M318), L328 (= L319), A329 (= A320), H330 (= H321), H453 (= H443), P454 (= P444)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
52% identity, 99% coverage: 6:464/464 of query aligns to 4:471/473 of 5u8wA
- active site: P13 (= P15), L44 (= L40), C48 (= C44), C53 (= C49), S56 (= S52), G82 (≠ K79), V83 (= V80), V190 (= V182), E194 (= E186), S330 (≠ E324), F448 (≠ H441), H450 (= H443), E455 (= E448)
- binding flavin-adenine dinucleotide: I9 (= I11), G12 (= G14), P13 (= P15), G14 (= G16), E33 (vs. gap), K34 (vs. gap), G46 (= G42), T47 (= T43), C48 (= C44), G52 (= G48), C53 (= C49), K57 (= K53), H120 (≠ Y117), G121 (≠ A118), A149 (= A141), S150 (≠ T142), G151 (= G143), S170 (= S162), G317 (= G311), D318 (= D312), M324 (= M318), L325 (= L319), A326 (= A320), H327 (= H321), Y357 (= Y351), H450 (= H443), P451 (= P444)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I178), G189 (= G181), V190 (= V182), I191 (= I183), E194 (= E186), E210 (= E202), A211 (≠ Y203), L212 (= L204), A275 (= A269), V276 (≠ I270), G277 (= G271), R278 (= R272), M324 (= M318), L325 (= L319), V355 (= V349), Y357 (= Y351)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
52% identity, 99% coverage: 6:464/464 of query aligns to 3:470/472 of 5u8vA
- active site: P12 (= P15), L43 (= L40), C47 (= C44), C52 (= C49), S55 (= S52), G81 (≠ K79), V82 (= V80), V189 (= V182), E193 (= E186), S329 (≠ E324), F447 (≠ H441), H449 (= H443), E454 (= E448)
- binding flavin-adenine dinucleotide: I8 (= I11), G11 (= G14), P12 (= P15), G13 (= G16), E32 (vs. gap), G45 (= G42), T46 (= T43), C47 (= C44), G51 (= G48), C52 (= C49), K56 (= K53), H119 (≠ Y117), G120 (≠ A118), A148 (= A141), S149 (≠ T142), G150 (= G143), S169 (= S162), I190 (= I183), R277 (= R272), G316 (= G311), D317 (= D312), M323 (= M318), L324 (= L319), A325 (= A320), H326 (= H321), H449 (= H443), P450 (= P444)
- binding nicotinamide-adenine-dinucleotide: I185 (= I178), G186 (= G179), G188 (= G181), V189 (= V182), I190 (= I183), L208 (≠ V201), E209 (= E202), A210 (≠ Y203), V243 (= V236), V275 (≠ I270), G276 (= G271)
Sites not aligning to the query:
Query Sequence
>Ga0059261_1343 FitnessBrowser__Korea:Ga0059261_1343
MAEYDFDVLVIGSGPGGYVAAIRAAQLGLKTACAEGRETLGGTCLNVGCIPSKALLHASE
LYEEAASGALAKLGVKLGKVELDLDAMHAQRLDAVKGLTGGIEFLFKKNKVEWLKGYATF
TGKDSVKVGDREVRAKNIVIATGSSVTPLPGVEIDQKIVVDSTGALELAKVPEHLVVIGG
GVIGLELGSVWRRVGAKVTVVEYLDQILPGFDADVRKEAARLFKKQGIEFKTGTKVTGVA
VKGGKATITVEPAAGGAAETIEADNVLVAIGRKPNTDGLGLDAAGLTVNQRGQIETDHSF
KTSVPGIWAIGDVIPGPMLAHKAEDEGIAVAENIAGLTGIVNHDVIPSVVYTMPEIAGVG
LTEEAAKAKGEVKVGKFPMAGNSRAKTNHEPDGFVKVIADAKTDRVLGVWIITSVAGTMI
AQAAQAMEFGATSEDIAYTCHAHPTHSEAIKEAAMAVTGKPIHI
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