SitesBLAST
Comparing BWI76_RS14145 FitnessBrowser__Koxy:BWI76_RS14145 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)
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)
42% identity, 99% coverage: 3:464/465 of query aligns to 36:500/501 of P31023
- 67:76 (vs. 34:42, 60% identical) binding
- C76 (= C42) modified: Disulfide link with 81, Redox-active
- C81 (= C47) modified: Disulfide link with 76, Redox-active
- G149 (≠ A114) binding
- D348 (= D310) binding
- MLAH 354:357 (≠ CLAH 316:319) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
42% identity, 99% coverage: 3:464/465 of query aligns to 2:466/467 of 1dxlA
- active site: L38 (= L38), C42 (= C42), C47 (= C47), S50 (≠ T50), Y184 (≠ A183), E188 (= E187), H444 (≠ F442), H446 (= H444), E451 (= E449)
- binding flavin-adenine dinucleotide: I9 (= I10), P13 (= P14), G14 (= G15), E33 (= E34), K34 (= K35), R35 (≠ Q36), G40 (= G40), T41 (≠ I41), C42 (= C42), G46 (= G46), C47 (= C47), K51 (= K51), Y114 (≠ T113), G115 (≠ A114), T144 (= T143), G145 (= G144), Y184 (≠ A183), I185 (= I184), R274 (≠ V271), D314 (= D310), M320 (≠ C316), L321 (= L317), A322 (= A318), H323 (= H319)
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
45% identity, 99% coverage: 5:464/465 of query aligns to 4:457/460 of 2eq6A
- active site: V37 (≠ L38), C41 (= C42), C46 (= C47), T49 (= T50), A176 (= A183), E180 (= E187), H435 (≠ F442), H437 (= H444), E442 (= E449)
- binding flavin-adenine dinucleotide: I9 (= I10), G10 (= G11), G12 (= G13), P13 (= P14), G14 (= G15), E33 (= E34), A34 (≠ K35), G39 (= G40), V40 (≠ I41), C41 (= C42), G45 (= G46), C46 (= C47), K50 (= K51), F111 (≠ T113), A112 (= A114), A135 (= A142), T136 (= T143), G137 (= G144), S155 (≠ Y163), R269 (≠ N274), D306 (= D310), L312 (≠ C316), L313 (= L317), A314 (= A318), H315 (= H319), Y344 (= Y351)
Sites not aligning to the query:
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
39% identity, 99% coverage: 5:464/465 of query aligns to 1:465/465 of 3urhB
- active site: Y35 (≠ L38), C39 (= C42), C44 (= C47), S47 (≠ T50), V183 (≠ A183), E187 (= E187), H443 (≠ F442), H445 (= H444), E450 (= E449)
- binding flavin-adenine dinucleotide: I6 (= I10), G7 (= G11), G9 (= G13), P10 (= P14), G11 (= G15), E30 (= E34), K31 (= K35), G37 (= G40), T38 (≠ I41), C39 (= C42), G43 (= G46), C44 (= C47), K48 (= K51), T111 (= T113), G112 (≠ A114), A140 (= A142), T141 (= T143), G142 (= G144), I184 (= I184), R273 (≠ V271), G312 (= G309), D313 (= D310), M319 (≠ C316), L320 (= L317), A321 (= A318), H322 (= H319)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
39% identity, 99% coverage: 3:461/465 of query aligns to 5:465/470 of 6uziC
- active site: C45 (= C42), C50 (= C47), S53 (≠ T50), V187 (≠ A183), E191 (= E187), H448 (= H444), E453 (= E449)
- binding flavin-adenine dinucleotide: I12 (= I10), G13 (= G11), G15 (= G13), P16 (= P14), G17 (= G15), E36 (= E34), K37 (= K35), G43 (= G40), T44 (≠ I41), C45 (= C42), G49 (= G46), C50 (= C47), S53 (≠ T50), K54 (= K51), V117 (≠ T113), G118 (≠ A114), T147 (= T143), G148 (= G144), I188 (= I184), R276 (≠ V271), D316 (= D310), M322 (≠ C316), L323 (= L317), A324 (= A318)
- binding zinc ion: H448 (= H444), E453 (= E449)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
37% identity, 99% coverage: 6:464/465 of query aligns to 11:466/470 of P11959
- 39:47 (vs. 34:42, 67% identical) binding
- K56 (= K51) binding
- D314 (= D310) binding
- A322 (= A318) binding
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
42% identity, 99% coverage: 5:464/465 of query aligns to 2:454/455 of 2yquB
- active site: P11 (= P14), L36 (= L38), C40 (= C42), C45 (= C47), S48 (≠ T50), G72 (≠ E75), V73 (= V76), V177 (≠ A183), E181 (= E187), S314 (= S322), H432 (≠ F442), H434 (= H444), E439 (= E449)
- binding carbonate ion: A310 (= A318), S314 (= S322), S423 (≠ T433), D426 (≠ S436)
- binding flavin-adenine dinucleotide: G8 (= G11), G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (= K35), G38 (= G40), T39 (≠ I41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (= C47), K49 (= K51), T110 (= T113), A111 (= A114), T137 (= T143), G138 (= G144), I178 (= I184), Y265 (≠ N274), G301 (= G309), D302 (= D310), M308 (≠ C316), L309 (= L317), A310 (= A318), H311 (= H319)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
42% identity, 99% coverage: 5:464/465 of query aligns to 2:454/455 of 2yquA
- active site: P11 (= P14), L36 (= L38), C40 (= C42), C45 (= C47), S48 (≠ T50), G72 (≠ E75), V73 (= V76), V177 (≠ A183), E181 (= E187), S314 (= S322), H432 (≠ F442), H434 (= H444), E439 (= E449)
- binding flavin-adenine dinucleotide: G8 (= G11), G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (= K35), G38 (= G40), T39 (≠ I41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (= C47), K49 (= K51), T110 (= T113), A111 (= A114), T137 (= T143), G138 (= G144), S157 (≠ Y163), I178 (= I184), Y265 (≠ N274), G301 (= G309), D302 (= D310), M308 (≠ C316), L309 (= L317), A310 (= A318)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
38% identity, 100% coverage: 1:464/465 of query aligns to 1:471/477 of P18925
- 34:49 (vs. 34:42, 38% identical) binding
- C49 (= C42) modified: Disulfide link with 54, Redox-active
- C54 (= C47) modified: Disulfide link with 49, Redox-active
- K58 (= K51) binding
- D319 (= D310) binding
- A327 (= A318) binding
3ladA Refined crystal structure of lipoamide dehydrogenase from azotobacter vinelandii at 2.2 angstroms resolution. A comparison with the structure of glutathione reductase (see paper)
39% identity, 99% coverage: 4:464/465 of query aligns to 3:470/472 of 3ladA
- active site: L44 (= L38), C48 (= C42), C53 (= C47), S56 (≠ T50), V190 (≠ A183), E194 (= E187), F448 (= F442), H450 (= H444), E455 (= E449)
- binding flavin-adenine dinucleotide: I9 (= I10), G10 (= G11), G12 (= G13), P13 (= P14), E33 (= E34), K34 (= K35), G46 (= G40), T47 (≠ I41), C48 (= C42), G52 (= G46), C53 (= C47), H120 (≠ T113), G121 (≠ A114), A149 (= A142), S150 (≠ T143), G151 (= G144), I191 (= I184), R278 (≠ V271), D318 (= D310), L325 (= L317), A326 (= A318)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
42% identity, 98% coverage: 5:462/465 of query aligns to 2:452/452 of 2eq7A
- active site: P11 (= P14), L36 (= L38), C40 (= C42), C45 (= C47), S48 (≠ T50), G72 (≠ E75), V73 (= V76), V177 (≠ A183), E181 (= E187), S314 (= S322), H432 (≠ F442), H434 (= H444), E439 (= E449)
- binding flavin-adenine dinucleotide: G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (= K35), G38 (= G40), T39 (≠ I41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (= C47), K49 (= K51), T110 (= T113), A111 (= A114), T137 (= T143), G138 (= G144), S157 (≠ Y163), I178 (= I184), R262 (≠ V271), Y265 (≠ N274), D302 (= D310), M308 (≠ C316), L309 (= L317), A310 (= A318), H311 (= H319), Y341 (= Y351)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ G152), G174 (= G180), G176 (= G182), V177 (≠ A183), I178 (= I184), E197 (= E203), Y198 (≠ Q204), V231 (≠ L237), V260 (≠ A269), G261 (= G270), R262 (≠ V271), M308 (≠ C316), L309 (= L317), V339 (≠ C349)
7kmyA Structure of mtb lpd bound to 010705 (see paper)
42% identity, 97% coverage: 5:453/465 of query aligns to 5:453/465 of 7kmyA
- active site: W38 (≠ L38), C42 (= C42), C47 (= C47), S50 (≠ T50), A182 (= A183), E186 (= E187), H442 (≠ F442), H444 (= H444), E449 (= E449)
- binding flavin-adenine dinucleotide: L10 (≠ I10), G11 (= G11), G13 (= G13), P14 (= P14), V33 (= V33), E34 (= E34), P35 (≠ K35), Y37 (≠ H37), G40 (= G40), V41 (≠ I41), C42 (= C42), G46 (= G46), C47 (= C47), K51 (= K51), Y113 (≠ T113), G114 (≠ A114), A142 (= A142), T143 (= T143), G144 (= G144), Y162 (= Y163), I183 (= I184), Y277 (≠ L278), G309 (= G309), D310 (= D310), Q316 (≠ C316), L317 (= L317), A318 (= A318)
- binding N~2~-methyl-N~2~-[(5-methyl-1H-indazol-7-yl)sulfonyl]-N-(1-methyl-2-oxo-1,2-dihydropyridin-4-yl)glycinamide: Y17 (= Y17), R94 (≠ L94), G97 (= G97), F100 (≠ Y100), E322 (≠ S322), A382 (≠ G382), H444 (= H444), E449 (= E449)
Sites not aligning to the query:
4m52A Structure of mtb lpd bound to sl827 (see paper)
42% identity, 97% coverage: 5:453/465 of query aligns to 5:453/465 of 4m52A
- active site: W38 (≠ L38), C42 (= C42), C47 (= C47), S50 (≠ T50), A182 (= A183), E186 (= E187), H442 (≠ F442), H444 (= H444), E449 (= E449)
- binding flavin-adenine dinucleotide: L10 (≠ I10), G11 (= G11), G13 (= G13), P14 (= P14), V33 (= V33), E34 (= E34), P35 (≠ K35), Y37 (≠ H37), V41 (≠ I41), C42 (= C42), G46 (= G46), C47 (= C47), K51 (= K51), Y113 (≠ T113), G114 (≠ A114), A142 (= A142), T143 (= T143), Y162 (= Y163), I183 (= I184), F270 (≠ V271), Y277 (≠ L278), G309 (= G309), D310 (= D310), Q316 (≠ C316), L317 (= L317), A318 (= A318)
- binding N~2~-[(2-amino-5-bromopyridin-3-yl)sulfonyl]-N-(4-methoxyphenyl)-N~2~-methylglycinamide: P14 (= P14), Y17 (= Y17), R94 (≠ L94), F100 (≠ Y100), E322 (≠ S322), A382 (≠ G382), H444 (= H444)
Sites not aligning to the query:
8u0qA Co-crystal structure of optimized analog tdi-13537 provided new insights into the potency determinants of the sulfonamide inhibitor series (see paper)
42% identity, 97% coverage: 5:453/465 of query aligns to 4:452/464 of 8u0qA
- binding flavin-adenine dinucleotide: L9 (≠ I10), G10 (= G11), G12 (= G13), P13 (= P14), G14 (= G15), V32 (= V33), E33 (= E34), P34 (≠ K35), Y36 (≠ H37), G39 (= G40), V40 (≠ I41), C41 (= C42), G45 (= G46), C46 (= C47), K50 (= K51), Y112 (≠ T113), G113 (≠ A114), A141 (= A142), T142 (= T143), G143 (= G144), Y161 (= Y163), I182 (= I184), Y276 (≠ L278), G308 (= G309), D309 (= D310), Q315 (≠ C316), L316 (= L317), A317 (= A318), H318 (= H319)
- binding N-(3-acetamidophenyl)-N~2~-[3-(difluoromethyl)-5-methylbenzene-1-sulfonyl]-N~2~-methylglycinamide: Y16 (= Y17), R93 (≠ L94), G96 (= G97), F99 (≠ Y100), E321 (≠ S322), A381 (≠ G382), A383 (≠ G384), H443 (= H444), E448 (= E449)
Sites not aligning to the query:
8ct4A Cryo-em structure of mtb lpd bound to inhibitor complex with 2-((2- cyano-n,5-dimethyl-1h-indole)-7-sulfonamido)-n-(4-(oxetan-3-yl)-3,4- dihydro-2h-benzo[b] [1,4]oxazin-7-yl)acetamide
42% identity, 97% coverage: 5:453/465 of query aligns to 4:452/464 of 8ct4A
- binding flavin-adenine dinucleotide: L9 (≠ I10), G10 (= G11), G12 (= G13), P13 (= P14), E33 (= E34), P34 (≠ K35), Y36 (≠ H37), G39 (= G40), V40 (≠ I41), C41 (= C42), G45 (= G46), C46 (= C47), K50 (= K51), Y112 (≠ T113), G113 (≠ A114), T142 (= T143), G143 (= G144), Y161 (= Y163), I182 (= I184), Y276 (≠ L278), D309 (= D310), Q315 (≠ C316), L316 (= L317), A317 (= A318)
- binding N~2~-(2-cyano-5-methyl-1H-indole-7-sulfonyl)-N~2~-methyl-N-[4-(oxetan-3-yl)-3,4-dihydro-2H-1,4-benzoxazin-7-yl]glycinamide: Y16 (= Y17), R93 (≠ L94), F99 (≠ Y100), E321 (≠ S322), F377 (= F378), A381 (≠ G382), A383 (≠ G384), H443 (= H444), E448 (= E449), A449 (= A450), E452 (= E453)
Sites not aligning to the query:
P9WHH9 Dihydrolipoyl dehydrogenase; LPD; Component of peroxynitrite reductase/peroxidase complex; Component of PNR/P; Dihydrolipoamide dehydrogenase; E3 component of alpha-ketoacid dehydrogenase complexes; EC 1.8.1.4 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
42% identity, 97% coverage: 5:453/465 of query aligns to 4:452/464 of P9WHH9
- D5 (= D6) mutation to A: Reduces lipoamide dehydrogenase activity by 95%.
- 33:41 (vs. 34:42, 44% identical) binding
- C41 (= C42) modified: Disulfide link with 46, Redox-active
- N43 (= N44) mutation to A: Reduces lipoamide dehydrogenase activity by 89%.
- C46 (= C47) modified: Disulfide link with 41, Redox-active
- K50 (= K51) binding
- R93 (≠ L94) mutation to A: Reduces lipoamide dehydrogenase activity by 94%.; mutation to E: Reduces lipoamide dehydrogenase activity by 96%.
- K103 (= K104) mutation to E: Reduces lipoamide dehydrogenase activity by 82%.
- D309 (= D310) binding
- A317 (= A318) binding
- H386 (≠ L387) mutation to K: Reduces lipoamide dehydrogenase activity by 91%.
Sites not aligning to the query:
- 464 F→A: Reduces lipoamide dehydrogenase activity by 95%.
3ii4A Structure of mycobacterial lipoamide dehydrogenase bound to a triazaspirodimethoxybenzoyl inhibitor (see paper)
42% identity, 97% coverage: 5:453/465 of query aligns to 3:451/463 of 3ii4A
- active site: W36 (≠ L38), C40 (= C42), C45 (= C47), S48 (≠ T50), A180 (= A183), E184 (= E187), H440 (≠ F442), H442 (= H444), E447 (= E449)
- binding N-[2-(2,4-dichlorophenyl)ethyl]-2-{8-[(2,4-dimethoxyphenyl)carbonyl]-4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-3-yl}acetamide: R146 (= R148), A180 (= A183), I181 (= I184), E184 (= E187), N208 (≠ V211), E209 (= E212), F268 (≠ V271), R287 (= R289), G311 (= G313), Q314 (≠ C316), L315 (= L317), R346 (≠ G348), A347 (≠ C349)
- binding flavin-adenine dinucleotide: L8 (≠ I10), G9 (= G11), G11 (= G13), P12 (= P14), G13 (= G15), V31 (= V33), E32 (= E34), P33 (≠ K35), Y35 (≠ H37), G38 (= G40), V39 (≠ I41), C40 (= C42), G44 (= G46), C45 (= C47), K49 (= K51), Y111 (≠ T113), G112 (≠ A114), A140 (= A142), T141 (= T143), G142 (= G144), Y160 (= Y163), I181 (= I184), Y275 (≠ L278), G307 (= G309), D308 (= D310), Q314 (≠ C316), L315 (= L317), A316 (= A318)
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
37% identity, 97% coverage: 6:454/465 of query aligns to 5:450/455 of 1ebdA
- active site: P13 (= P14), L37 (= L38), C41 (= C42), C46 (= C47), S49 (≠ T50), N74 (≠ E75), V75 (= V76), Y180 (≠ A183), E184 (= E187), S320 (= S322), H438 (≠ F442), H440 (= H444), E445 (= E449)
- binding flavin-adenine dinucleotide: G10 (= G11), G12 (= G13), P13 (= P14), V32 (= V33), E33 (= E34), K34 (= K35), G39 (= G40), V40 (≠ I41), C41 (= C42), G45 (= G46), C46 (= C47), K50 (= K51), E112 (≠ T113), A113 (= A114), T141 (= T143), G142 (= G144), Y180 (≠ A183), I181 (= I184), R268 (≠ V271), D308 (= D310), A314 (≠ C316), L315 (= L317), A316 (= A318)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
37% identity, 100% coverage: 1:464/465 of query aligns to 1:471/478 of P14218
- M1 (= M1) modified: Initiator methionine, Removed
- 34:49 (vs. 34:42, 38% identical) binding
- C49 (= C42) modified: Disulfide link with 54, Redox-active
- C54 (= C47) modified: Disulfide link with 49, Redox-active
- K58 (= K51) binding
- G122 (≠ A114) binding
- D319 (= D310) binding
- A327 (= A318) binding
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
37% identity, 100% coverage: 1:464/465 of query aligns to 3:473/477 of 5u8uD
- active site: P16 (= P14), L47 (= L38), C51 (= C42), C56 (= C47), S59 (≠ T50), G85 (≠ E75), V86 (= V76), V193 (≠ A183), E197 (= E187), S333 (= S322), F451 (= F442), H453 (= H444), E458 (= E449)
- binding flavin-adenine dinucleotide: I12 (= I10), G15 (= G13), P16 (= P14), G17 (= G15), E36 (= E34), K37 (= K35), G49 (= G40), T50 (≠ I41), C51 (= C42), G55 (= G46), C56 (= C47), K60 (= K51), H123 (≠ T113), G124 (≠ A114), A152 (= A142), S153 (≠ T143), G154 (= G144), I194 (= I184), R281 (≠ V271), G320 (= G309), D321 (= D310), M327 (≠ C316), L328 (= L317), A329 (= A318), H330 (= H319), H453 (= H444), P454 (= P445)
Sites not aligning to the query:
Query Sequence
>BWI76_RS14145 FitnessBrowser__Koxy:BWI76_RS14145
MHDKYDVLIIGGGPGGYVAAIRAGQLGLRTALVEKQHLGGICLNWGCIPTKALLHGAEVA
HTIAHADRLGFSLSEVSFDLQKLVQFSRAVSQQLTGGVEYLLKKNGVTVIAGTARLRGKG
QVTVADPQGEERDYRADHVILATGARPRALPGVEPDGERIWTYFEALQPERLPESLLIIG
SGAIGVEFASLYNDLGSNVTLVEQAAQILPVEDAEVSATVRKSFERRGIHVHSQTLLTQV
KRTDTGVRCALKTTGAEQTLEVERVLLAAGVQPNVEGLGLEALGVELDRGFIKTDAACRT
NVFGLYAIGDVAGPPCLAHKASHEGVICVETLAGVEGVRPLNCDYVPGCTYARPQVASLG
LTEAKARETGRPIKVGKFAYQGNGKALASGETEGFVKTIFDAETGELLGAHMVGEQVTEQ
IQGFGIAHHLEATDESLLSMIFAHPTLSEAMHESILAASGQPLHQ
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