SitesBLAST
Comparing CA265_RS05155 FitnessBrowser__Pedo557:CA265_RS05155 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)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
43% identity, 100% coverage: 1:462/462 of query aligns to 4:470/470 of 6uziC
- active site: C45 (= C40), C50 (= C45), S53 (≠ T48), V187 (≠ A181), E191 (= E185), H448 (= H441), E453 (= E446)
- binding flavin-adenine dinucleotide: I12 (≠ L8), G13 (= G9), G15 (= G11), P16 (= P12), G17 (= G13), E36 (= E32), K37 (≠ R33), G43 (= G38), T44 (≠ I39), C45 (= C40), G49 (= G44), C50 (= C45), S53 (≠ T48), K54 (= K49), V117 (≠ T111), G118 (= G112), T147 (= T141), G148 (= G142), I188 (= I182), R276 (≠ I269), D316 (= D308), M322 (≠ A314), L323 (= L315), A324 (= A316)
- binding zinc ion: H448 (= H441), E453 (= E446)
8u0qA Co-crystal structure of optimized analog tdi-13537 provided new insights into the potency determinants of the sulfonamide inhibitor series (see paper)
44% identity, 100% coverage: 2:462/462 of query aligns to 3:464/464 of 8u0qA
- binding flavin-adenine dinucleotide: L9 (= L8), G10 (= G9), G12 (= G11), P13 (= P12), G14 (= G13), V32 (= V31), E33 (= E32), P34 (≠ R33), Y36 (≠ S35), G39 (= G38), V40 (≠ I39), C41 (= C40), G45 (= G44), C46 (= C45), K50 (= K49), Y112 (≠ T111), G113 (= G112), A141 (= A140), T142 (= T141), G143 (= G142), Y161 (= Y161), I182 (= I182), Y276 (≠ I276), G308 (= G307), D309 (= D308), Q315 (≠ A314), L316 (= L315), A317 (= A316), H318 (= H317)
- binding N-(3-acetamidophenyl)-N~2~-[3-(difluoromethyl)-5-methylbenzene-1-sulfonyl]-N~2~-methylglycinamide: Y16 (= Y15), R93 (≠ M92), G96 (= G95), F99 (= F98), E321 (≠ S320), A381 (= A379), A383 (≠ G381), H443 (= H441), E448 (= E446), N463 (≠ H461), F464 (≠ L462)
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
44% identity, 100% coverage: 2:462/462 of query aligns to 3:464/464 of 8ct4A
- binding flavin-adenine dinucleotide: L9 (= L8), G10 (= G9), G12 (= G11), P13 (= P12), E33 (= E32), P34 (≠ R33), Y36 (≠ S35), G39 (= G38), V40 (≠ I39), C41 (= C40), G45 (= G44), C46 (= C45), K50 (= K49), Y112 (≠ T111), G113 (= G112), T142 (= T141), G143 (= G142), Y161 (= Y161), I182 (= I182), Y276 (≠ I276), D309 (= D308), Q315 (≠ A314), L316 (= L315), A317 (= A316)
- 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 (= Y15), R93 (≠ M92), F99 (= F98), E321 (≠ S320), F377 (= F375), A381 (= A379), A383 (≠ G381), H443 (= H441), E448 (= E446), A449 (= A447), E452 (= E450), N463 (≠ H461)
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)
44% identity, 100% coverage: 2:462/462 of query aligns to 3:464/464 of P9WHH9
- D5 (= D4) mutation to A: Reduces lipoamide dehydrogenase activity by 95%.
- 33:41 (vs. 32:40, 44% identical) binding
- C41 (= C40) modified: Disulfide link with 46, Redox-active
- N43 (= N42) mutation to A: Reduces lipoamide dehydrogenase activity by 89%.
- C46 (= C45) modified: Disulfide link with 41, Redox-active
- K50 (= K49) binding
- R93 (≠ M92) mutation to A: Reduces lipoamide dehydrogenase activity by 94%.; mutation to E: Reduces lipoamide dehydrogenase activity by 96%.
- K103 (= K102) mutation to E: Reduces lipoamide dehydrogenase activity by 82%.
- D309 (= D308) binding
- A317 (= A316) binding
- H386 (≠ S384) mutation to K: Reduces lipoamide dehydrogenase activity by 91%.
- F464 (≠ L462) mutation to A: Reduces lipoamide dehydrogenase activity by 95%.
3ii4A Structure of mycobacterial lipoamide dehydrogenase bound to a triazaspirodimethoxybenzoyl inhibitor (see paper)
44% identity, 100% coverage: 2:462/462 of query aligns to 2:463/463 of 3ii4A
- active site: W36 (≠ L36), C40 (= C40), C45 (= C45), S48 (≠ T48), A180 (= A181), E184 (= E185), H440 (= H439), H442 (= H441), E447 (= E446)
- 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 (= R146), A180 (= A181), I181 (= I182), E184 (= E185), N208 (≠ V209), E209 (= E210), F268 (≠ I269), R287 (≠ K287), G311 (= G311), Q314 (≠ A314), L315 (= L315), R346 (≠ G345), A347 (≠ C346)
- binding flavin-adenine dinucleotide: L8 (= L8), G9 (= G9), G11 (= G11), P12 (= P12), G13 (= G13), V31 (= V31), E32 (= E32), P33 (≠ R33), Y35 (≠ S35), G38 (= G38), V39 (≠ I39), C40 (= C40), G44 (= G44), C45 (= C45), K49 (= K49), Y111 (≠ T111), G112 (= G112), A140 (= A140), T141 (= T141), G142 (= G142), Y160 (= Y161), I181 (= I182), Y275 (≠ I276), G307 (= G307), D308 (= D308), Q314 (≠ A314), L315 (= L315), A316 (= A316)
7kmyA Structure of mtb lpd bound to 010705 (see paper)
44% identity, 100% coverage: 2:462/462 of query aligns to 4:465/465 of 7kmyA
- active site: W38 (≠ L36), C42 (= C40), C47 (= C45), S50 (≠ T48), A182 (= A181), E186 (= E185), H442 (= H439), H444 (= H441), E449 (= E446)
- binding flavin-adenine dinucleotide: L10 (= L8), G11 (= G9), G13 (= G11), P14 (= P12), V33 (= V31), E34 (= E32), P35 (≠ R33), Y37 (≠ S35), G40 (= G38), V41 (≠ I39), C42 (= C40), G46 (= G44), C47 (= C45), K51 (= K49), Y113 (≠ T111), G114 (= G112), A142 (= A140), T143 (= T141), G144 (= G142), Y162 (= Y161), I183 (= I182), Y277 (≠ I276), G309 (= G307), D310 (= D308), Q316 (≠ A314), L317 (= L315), A318 (= A316)
- 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 (= Y15), R94 (≠ M92), G97 (= G95), F100 (= F98), E322 (≠ S320), A382 (= A379), H444 (= H441), E449 (= E446), N464 (≠ H461)
4m52A Structure of mtb lpd bound to sl827 (see paper)
44% identity, 100% coverage: 2:462/462 of query aligns to 4:465/465 of 4m52A
- active site: W38 (≠ L36), C42 (= C40), C47 (= C45), S50 (≠ T48), A182 (= A181), E186 (= E185), H442 (= H439), H444 (= H441), E449 (= E446)
- binding flavin-adenine dinucleotide: L10 (= L8), G11 (= G9), G13 (= G11), P14 (= P12), V33 (= V31), E34 (= E32), P35 (≠ R33), Y37 (≠ S35), V41 (≠ I39), C42 (= C40), G46 (= G44), C47 (= C45), K51 (= K49), Y113 (≠ T111), G114 (= G112), A142 (= A140), T143 (= T141), Y162 (= Y161), I183 (= I182), F270 (≠ I269), Y277 (≠ I276), G309 (= G307), D310 (= D308), Q316 (≠ A314), L317 (= L315), A318 (= A316)
- binding N~2~-[(2-amino-5-bromopyridin-3-yl)sulfonyl]-N-(4-methoxyphenyl)-N~2~-methylglycinamide: P14 (= P12), Y17 (= Y15), R94 (≠ M92), F100 (= F98), E322 (≠ S320), A382 (= A379), H444 (= H441), N464 (≠ H461)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
44% identity, 99% coverage: 3:461/462 of query aligns to 1:465/465 of 3urhB
- active site: Y35 (≠ L36), C39 (= C40), C44 (= C45), S47 (≠ T48), V183 (≠ A181), E187 (= E185), H443 (= H439), H445 (= H441), E450 (= E446)
- binding flavin-adenine dinucleotide: I6 (≠ L8), G7 (= G9), G9 (= G11), P10 (= P12), G11 (= G13), E30 (= E32), K31 (vs. gap), G37 (= G38), T38 (≠ I39), C39 (= C40), G43 (= G44), C44 (= C45), K48 (= K49), T111 (= T111), G112 (= G112), A140 (= A140), T141 (= T141), G142 (= G142), I184 (= I182), R273 (≠ I269), G312 (= G307), D313 (= D308), M319 (≠ A314), L320 (= L315), A321 (= A316), H322 (= H317)
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)
41% identity, 99% coverage: 4:462/462 of query aligns to 39:501/501 of P31023
- 67:76 (vs. 32:40, 60% identical) binding
- C76 (= C40) modified: Disulfide link with 81, Redox-active
- C81 (= C45) modified: Disulfide link with 76, Redox-active
- G149 (= G112) binding
- D348 (= D308) binding
- MLAH 354:357 (≠ ALAH 314:317) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
41% identity, 99% coverage: 4:462/462 of query aligns to 5:467/467 of 1dxlA
- active site: L38 (= L36), C42 (= C40), C47 (= C45), S50 (≠ T48), Y184 (≠ A181), E188 (= E185), H444 (= H439), H446 (= H441), E451 (= E446)
- binding flavin-adenine dinucleotide: I9 (≠ L8), P13 (= P12), G14 (= G13), E33 (= E32), K34 (vs. gap), R35 (= R33), G40 (= G38), T41 (≠ I39), C42 (= C40), G46 (= G44), C47 (= C45), K51 (= K49), Y114 (≠ T111), G115 (= G112), T144 (= T141), G145 (= G142), Y184 (≠ A181), I185 (= I182), R274 (≠ I269), D314 (= D308), M320 (≠ A314), L321 (= L315), A322 (= A316), H323 (= H317)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
42% identity, 99% coverage: 4:462/462 of query aligns to 11:467/470 of P11959
- 39:47 (vs. 32:40, 56% identical) binding
- K56 (= K49) binding
- D314 (= D308) binding
- A322 (= A316) binding
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
41% identity, 100% coverage: 3:462/462 of query aligns to 5:472/475 of 6awaA
- active site: L45 (= L36), C49 (= C40), C54 (= C45), S57 (≠ T48), V191 (≠ A181), E195 (= E185), F449 (≠ H439), H451 (= H441), E456 (= E446)
- binding adenosine monophosphate: I187 (≠ V177), E211 (= E201), A212 (≠ F202), L213 (≠ M203), V245 (= V235), V277 (≠ A267)
- binding flavin-adenine dinucleotide: I10 (≠ L8), G13 (= G11), P14 (= P12), G15 (= G13), E34 (= E32), K35 (≠ R33), T48 (≠ I39), C49 (= C40), G53 (= G44), C54 (= C45), K58 (= K49), H121 (≠ T111), G122 (= G112), S151 (≠ T141), G152 (= G142), I192 (= I182), R279 (≠ I269), G318 (= G307), D319 (= D308), M325 (≠ A314), L326 (= L315), A327 (= A316), Y358 (= Y348)
Sites not aligning to the query:
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
42% identity, 97% coverage: 4:452/462 of query aligns to 5:451/455 of 1ebdA
- active site: P13 (= P12), L37 (= L36), C41 (= C40), C46 (= C45), S49 (≠ T48), N74 (≠ G73), V75 (≠ A74), Y180 (≠ A181), E184 (= E185), S320 (= S320), H438 (= H439), H440 (= H441), E445 (= E446)
- binding flavin-adenine dinucleotide: G10 (= G9), G12 (= G11), P13 (= P12), V32 (= V31), E33 (= E32), K34 (≠ R33), G39 (= G38), V40 (≠ I39), C41 (= C40), G45 (= G44), C46 (= C45), K50 (= K49), E112 (≠ T111), A113 (≠ G112), T141 (= T141), G142 (= G142), Y180 (≠ A181), I181 (= I182), R268 (≠ I269), D308 (= D308), A314 (= A314), L315 (= L315), A316 (= A316)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
41% identity, 100% coverage: 3:462/462 of query aligns to 2:455/455 of 2yquB
- active site: P11 (= P12), L36 (= L36), C40 (= C40), C45 (= C45), S48 (≠ T48), G72 (= G73), V73 (≠ A74), V177 (≠ A181), E181 (= E185), S314 (= S320), H432 (= H439), H434 (= H441), E439 (= E446)
- binding carbonate ion: A310 (= A316), S314 (= S320), S423 (≠ T430), D426 (≠ E433)
- binding flavin-adenine dinucleotide: G8 (= G9), G10 (= G11), P11 (= P12), G12 (= G13), E31 (= E32), K32 (≠ R33), G38 (= G38), T39 (≠ I39), C40 (= C40), R42 (≠ N42), G44 (= G44), C45 (= C45), K49 (= K49), T110 (= T111), A111 (≠ G112), T137 (= T141), G138 (= G142), I178 (= I182), Y265 (≠ N272), G301 (= G307), D302 (= D308), M308 (≠ A314), L309 (= L315), A310 (= A316), H311 (= H317)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
41% identity, 100% coverage: 3:462/462 of query aligns to 2:455/455 of 2yquA
- active site: P11 (= P12), L36 (= L36), C40 (= C40), C45 (= C45), S48 (≠ T48), G72 (= G73), V73 (≠ A74), V177 (≠ A181), E181 (= E185), S314 (= S320), H432 (= H439), H434 (= H441), E439 (= E446)
- binding flavin-adenine dinucleotide: G8 (= G9), G10 (= G11), P11 (= P12), G12 (= G13), E31 (= E32), K32 (≠ R33), G38 (= G38), T39 (≠ I39), C40 (= C40), R42 (≠ N42), G44 (= G44), C45 (= C45), K49 (= K49), T110 (= T111), A111 (≠ G112), T137 (= T141), G138 (= G142), S157 (≠ Y161), I178 (= I182), Y265 (≠ N272), G301 (= G307), D302 (= D308), M308 (≠ A314), L309 (= L315), A310 (= A316)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
41% identity, 98% coverage: 3:456/462 of query aligns to 2:449/452 of 2eq7A
- active site: P11 (= P12), L36 (= L36), C40 (= C40), C45 (= C45), S48 (≠ T48), G72 (= G73), V73 (≠ A74), V177 (≠ A181), E181 (= E185), S314 (= S320), H432 (= H439), H434 (= H441), E439 (= E446)
- binding flavin-adenine dinucleotide: G10 (= G11), P11 (= P12), G12 (= G13), E31 (= E32), K32 (≠ R33), G38 (= G38), T39 (≠ I39), C40 (= C40), R42 (≠ N42), G44 (= G44), C45 (= C45), K49 (= K49), T110 (= T111), A111 (≠ G112), T137 (= T141), G138 (= G142), S157 (≠ Y161), I178 (= I182), R262 (≠ I269), Y265 (≠ N272), D302 (= D308), M308 (≠ A314), L309 (= L315), A310 (= A316), H311 (= H317), Y341 (= Y348)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ N150), G174 (= G178), G176 (= G180), V177 (≠ A181), I178 (= I182), E197 (= E201), Y198 (≠ F202), V231 (= V235), V260 (≠ A267), G261 (= G268), R262 (≠ I269), M308 (≠ A314), L309 (= L315), V339 (≠ C346)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
39% identity, 100% coverage: 3:462/462 of query aligns to 5:472/478 of P14218
- 34:49 (vs. 32:40, 31% identical) binding
- C49 (= C40) modified: Disulfide link with 54, Redox-active
- C54 (= C45) modified: Disulfide link with 49, Redox-active
- K58 (= K49) binding
- G122 (= G112) binding
- D319 (= D308) binding
- A327 (= A316) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
39% identity, 100% coverage: 2:462/462 of query aligns to 4:472/477 of P18925
- 34:49 (vs. 32:40, 31% identical) binding
- C49 (= C40) modified: Disulfide link with 54, Redox-active
- C54 (= C45) modified: Disulfide link with 49, Redox-active
- K58 (= K49) binding
- D319 (= D308) binding
- A327 (= A316) binding
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
39% identity, 100% coverage: 3:462/462 of query aligns to 3:470/472 of 5u8vA
- active site: P12 (= P12), L43 (= L36), C47 (= C40), C52 (= C45), S55 (≠ T48), G81 (= G73), V82 (≠ A74), V189 (≠ A181), E193 (= E185), S329 (= S320), F447 (≠ H439), H449 (= H441), E454 (= E446)
- binding flavin-adenine dinucleotide: I8 (≠ L8), G11 (= G11), P12 (= P12), G13 (= G13), E32 (= E32), G45 (= G38), T46 (≠ I39), C47 (= C40), G51 (= G44), C52 (= C45), K56 (= K49), H119 (≠ T111), G120 (= G112), A148 (= A140), S149 (≠ T141), G150 (= G142), S169 (≠ Y161), I190 (= I182), R277 (≠ I269), G316 (= G307), D317 (= D308), M323 (≠ A314), L324 (= L315), A325 (= A316), H326 (= H317), H449 (= H441), P450 (= P442)
- binding nicotinamide-adenine-dinucleotide: I185 (≠ V177), G186 (= G178), G188 (= G180), V189 (≠ A181), I190 (= I182), L208 (≠ V200), E209 (= E201), A210 (≠ F202), V243 (= V235), V275 (≠ A267), G276 (= G268)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
39% identity, 100% coverage: 3:462/462 of query aligns to 7:474/477 of 5u8uD
- active site: P16 (= P12), L47 (= L36), C51 (= C40), C56 (= C45), S59 (≠ T48), G85 (= G73), V86 (≠ A74), V193 (≠ A181), E197 (= E185), S333 (= S320), F451 (≠ H439), H453 (= H441), E458 (= E446)
- binding flavin-adenine dinucleotide: I12 (≠ L8), G15 (= G11), P16 (= P12), G17 (= G13), E36 (= E32), K37 (≠ R33), G49 (= G38), T50 (≠ I39), C51 (= C40), G55 (= G44), C56 (= C45), K60 (= K49), H123 (≠ T111), G124 (= G112), A152 (= A140), S153 (≠ T141), G154 (= G142), I194 (= I182), R281 (≠ I269), G320 (= G307), D321 (= D308), M327 (≠ A314), L328 (= L315), A329 (= A316), H330 (= H317), H453 (= H441), P454 (= P442)
Sites not aligning to the query:
Query Sequence
>CA265_RS05155 FitnessBrowser__Pedo557:CA265_RS05155
MNYDVIVLGSGPGGYVAAIRASQLGLKVAIVERESLGGICLNWGCIPTKALLKSAQVFEY
INHAADYGITTAGATADFAAVVKRSRGVADGMSKGVQFLMKKNKIDVIMGTGKVKPGNKL
EVKGADGSQQELSAKNIIIATGARSRELPNLKQDGKKIIGYRQAMVLPELPKSMVVVGSG
AIGVEFAYFYATMGTKVTIVEFMDNVVPVEDEDVSKQLLRSLKKVGIDVMTSASVESVDT
SGAGCKVSVKTASGMQTIEADIVLSAAGIVANIENIGLEETGIKTEKGKIVTDEFYNTSV
KGYYAIGDVVGGQALAHVASAEGIICVEKIAGQHAEPLDYNNIPGCTYCTPEIASVGYTE
KAAKAAGYELKIGKFPFSASGKASAAGAKDGFVKLIFDAKYGELLGAHMIGANVTEMIAE
IVVARKLETTGHEMIKSVHPHPTMSEAIMEAAADAYGEVIHL
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