SitesBLAST
Comparing WP_050460862.1 NCBI__GCF_001189915.1:WP_050460862.1 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)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
40% identity, 100% coverage: 1:467/467 of query aligns to 1:472/477 of P18925
- 34:49 (vs. 35:43, 38% identical) binding FAD
- C49 (= C43) modified: Disulfide link with 54, Redox-active
- C54 (= C48) modified: Disulfide link with 49, Redox-active
- K58 (= K52) binding FAD
- D319 (= D313) binding FAD
- A327 (= A321) binding FAD
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)
40% identity, 99% coverage: 5:467/467 of query aligns to 3:471/472 of 3ladA
- active site: L44 (= L39), C48 (= C43), C53 (= C48), S56 (≠ T51), V190 (≠ A183), E194 (= E187), F448 (= F444), H450 (= H446), E455 (= E451)
- binding flavin-adenine dinucleotide: I9 (≠ V11), G10 (= G12), G12 (= G14), P13 (= P15), E33 (= E35), K34 (= K36), G46 (= G41), T47 (≠ I42), C48 (= C43), G52 (= G47), C53 (= C48), H120 (= H114), G121 (≠ A115), A149 (= A142), S150 (≠ T143), G151 (= G144), I191 (= I184), R278 (≠ I274), D318 (= D313), L325 (= L320), A326 (= A321)
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: 1:467/467 of query aligns to 1:472/475 of 6awaA
- active site: L45 (= L39), C49 (= C43), C54 (= C48), S57 (≠ T51), V191 (≠ A183), E195 (= E187), F449 (= F444), H451 (= H446), E456 (= E451)
- binding adenosine monophosphate: I187 (= I179), E211 (= E203), A212 (≠ M204), L213 (≠ A205), V245 (≠ I237), V277 (≠ A272)
- binding flavin-adenine dinucleotide: I10 (≠ V11), G13 (= G14), P14 (= P15), G15 (= G16), E34 (= E35), K35 (= K36), T48 (≠ I42), C49 (= C43), G53 (= G47), C54 (= C48), K58 (= K52), H121 (= H114), G122 (≠ A115), S151 (≠ T143), G152 (= G144), I192 (= I184), R279 (≠ I274), G318 (= G312), D319 (= D313), M325 (≠ W319), L326 (= L320), A327 (= A321), Y358 (= Y353)
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)
40% identity, 100% coverage: 1:467/467 of query aligns to 1:472/478 of P14218
- M1 (= M1) modified: Initiator methionine, Removed
- 34:49 (vs. 35:43, 38% identical) binding FAD
- C49 (= C43) modified: Disulfide link with 54, Redox-active
- C54 (= C48) modified: Disulfide link with 49, Redox-active
- K58 (= K52) binding FAD
- G122 (≠ A115) binding FAD
- D319 (= D313) binding FAD
- A327 (= A321) binding FAD
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
40% identity, 100% coverage: 1:467/467 of query aligns to 3:474/477 of 5u8uD
- active site: P16 (= P15), L47 (= L39), C51 (= C43), C56 (= C48), S59 (≠ T51), G85 (≠ A76), V86 (≠ P77), V193 (≠ A183), E197 (= E187), S333 (= S325), F451 (= F444), H453 (= H446), E458 (= E451)
- binding flavin-adenine dinucleotide: I12 (≠ V11), G15 (= G14), P16 (= P15), G17 (= G16), E36 (= E35), K37 (= K36), G49 (= G41), T50 (≠ I42), C51 (= C43), G55 (= G47), C56 (= C48), K60 (= K52), H123 (= H114), G124 (≠ A115), A152 (= A142), S153 (≠ T143), G154 (= G144), I194 (= I184), R281 (≠ I274), G320 (= G312), D321 (= D313), M327 (≠ W319), L328 (= L320), A329 (= A321), H330 (= H322), H453 (= H446), P454 (= P447)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
40% identity, 99% coverage: 5:467/467 of query aligns to 3:471/473 of 5u8wA
- active site: P13 (= P15), L44 (= L39), C48 (= C43), C53 (= C48), S56 (≠ T51), G82 (≠ A76), V83 (≠ P77), V190 (≠ A183), E194 (= E187), S330 (= S325), F448 (= F444), H450 (= H446), E455 (= E451)
- binding flavin-adenine dinucleotide: I9 (≠ V11), G12 (= G14), P13 (= P15), G14 (= G16), E33 (= E35), K34 (= K36), G46 (= G41), T47 (≠ I42), C48 (= C43), G52 (= G47), C53 (= C48), K57 (= K52), H120 (= H114), G121 (≠ A115), A149 (= A142), S150 (≠ T143), G151 (= G144), S170 (≠ Y163), G317 (= G312), D318 (= D313), M324 (≠ W319), L325 (= L320), A326 (= A321), H327 (= H322), Y357 (= Y353), H450 (= H446), P451 (= P447)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I179), G189 (= G182), V190 (≠ A183), I191 (= I184), E194 (= E187), E210 (= E203), A211 (≠ M204), L212 (≠ A205), A275 (= A271), V276 (≠ A272), G277 (= G273), R278 (≠ I274), M324 (≠ W319), L325 (= L320), V355 (≠ C351), Y357 (= Y353)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
40% identity, 99% coverage: 5:467/467 of query aligns to 2:470/472 of 5u8vA
- active site: P12 (= P15), L43 (= L39), C47 (= C43), C52 (= C48), S55 (≠ T51), G81 (≠ A76), V82 (≠ P77), V189 (≠ A183), E193 (= E187), S329 (= S325), F447 (= F444), H449 (= H446), E454 (= E451)
- binding flavin-adenine dinucleotide: I8 (≠ V11), G11 (= G14), P12 (= P15), G13 (= G16), E32 (= E35), G45 (= G41), T46 (≠ I42), C47 (= C43), G51 (= G47), C52 (= C48), K56 (= K52), H119 (= H114), G120 (≠ A115), A148 (= A142), S149 (≠ T143), G150 (= G144), S169 (≠ Y163), I190 (= I184), R277 (≠ I274), G316 (= G312), D317 (= D313), M323 (≠ W319), L324 (= L320), A325 (= A321), H326 (= H322), H449 (= H446), P450 (= P447)
- binding nicotinamide-adenine-dinucleotide: I185 (= I179), G186 (= G180), G188 (= G182), V189 (≠ A183), I190 (= I184), L208 (≠ I202), E209 (= E203), A210 (≠ M204), V243 (≠ I237), V275 (≠ A272), G276 (= G273)
Sites not aligning to the query:
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
40% identity, 99% coverage: 5:467/467 of query aligns to 6:470/470 of 6uziC
- active site: C45 (= C43), C50 (= C48), S53 (≠ T51), V187 (≠ A183), E191 (= E187), H448 (= H446), E453 (= E451)
- binding flavin-adenine dinucleotide: I12 (≠ V11), G13 (= G12), G15 (= G14), P16 (= P15), G17 (= G16), E36 (= E35), K37 (= K36), G43 (= G41), T44 (≠ I42), C45 (= C43), G49 (= G47), C50 (= C48), S53 (≠ T51), K54 (= K52), V117 (≠ H114), G118 (≠ A115), T147 (= T143), G148 (= G144), I188 (= I184), R276 (≠ I274), D316 (= D313), M322 (≠ W319), L323 (= L320), A324 (= A321)
- binding zinc ion: H448 (= H446), E453 (= E451)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
38% identity, 99% coverage: 7:467/467 of query aligns to 43:509/509 of P09622
- 71:80 (vs. 35:43, 60% identical) binding FAD
- K72 (= K36) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K52) binding FAD; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ R65) to T: in dbSNP:rs1130477
- G154 (≠ A115) binding FAD
- TGS 183:185 (≠ TGA 143:145) binding FAD
- 220:227 (vs. 180:187, 75% identical) binding NAD(+)
- E243 (= E203) binding NAD(+)
- V278 (≠ I237) binding NAD(+)
- G314 (= G273) binding NAD(+)
- D355 (= D313) binding FAD
- MLAH 361:364 (≠ WLAH 319:322) binding FAD
- E375 (= E333) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (= H341) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ G407) 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 (≠ G425) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ L432) 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 (≠ E438) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ A441) 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 (≠ F444) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P447) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (= S450) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E451) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ H454) to G: in DLDD; loss of enzyme activity; reduced interaction with PDHX; dbSNP:rs121964989
- K505 (≠ R463) 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.
38% identity, 99% coverage: 7:467/467 of query aligns to 16:482/482 of 6hg8B
- active site: C53 (= C43), C58 (= C48), S61 (≠ T51), V196 (≠ A183), E200 (= E187), H460 (= H446), E465 (= E451)
- binding flavin-adenine dinucleotide: I20 (≠ V11), G23 (= G14), P24 (= P15), G25 (= G16), E44 (= E35), K45 (= K36), N46 (≠ A37), G51 (= G41), T52 (≠ I42), C53 (= C43), G57 (= G47), C58 (= C48), K62 (= K52), Y126 (≠ H114), G127 (≠ A115), T156 (= T143), G157 (= G144), I197 (= I184), R288 (≠ I274), F291 (≠ N277), G327 (= G312), D328 (= D313), M334 (≠ W319), L335 (= L320), A336 (= A321), H337 (= H322)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
38% identity, 99% coverage: 7:467/467 of query aligns to 6:472/472 of 1zmdA
- active site: L39 (= L39), C43 (= C43), C48 (= C48), S51 (≠ T51), V186 (≠ A183), E190 (= E187), H448 (≠ F444), H450 (= H446), E455 (= E451)
- binding flavin-adenine dinucleotide: I10 (≠ V11), G11 (= G12), G13 (= G14), P14 (= P15), G15 (= G16), E34 (= E35), K35 (= K36), N36 (≠ A37), G41 (= G41), T42 (≠ I42), C43 (= C43), G47 (= G47), C48 (= C48), K52 (= K52), Y116 (≠ H114), G117 (≠ A115), T146 (= T143), G147 (= G144), S166 (≠ Y163), R278 (≠ I274), F281 (≠ N277), G317 (= G312), D318 (= D313), M324 (≠ W319), L325 (= L320), A326 (= A321), H327 (= H322)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I179), G183 (= G180), G185 (= G182), V186 (≠ A183), I187 (= I184), E190 (= E187), E206 (= E203), F207 (≠ M204), L208 (≠ A205), I276 (≠ A272), G277 (= G273), R278 (≠ I274), M324 (≠ W319), L325 (= L320), V355 (≠ C351), Y357 (= Y353)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
38% identity, 99% coverage: 7:467/467 of query aligns to 6:472/472 of 1zmcA
- active site: L39 (= L39), C43 (= C43), C48 (= C48), S51 (≠ T51), V186 (≠ A183), E190 (= E187), H448 (≠ F444), H450 (= H446), E455 (= E451)
- binding flavin-adenine dinucleotide: I10 (≠ V11), G11 (= G12), G13 (= G14), P14 (= P15), G15 (= G16), E34 (= E35), K35 (= K36), N36 (≠ A37), G41 (= G41), T42 (≠ I42), C43 (= C43), G47 (= G47), C48 (= C48), K52 (= K52), Y116 (≠ H114), G117 (≠ A115), T146 (= T143), G147 (= G144), S166 (≠ Y163), I187 (= I184), F281 (≠ N277), G317 (= G312), D318 (= D313), M324 (≠ W319), L325 (= L320), A326 (= A321), H327 (= H322)
- binding nicotinamide-adenine-dinucleotide: G183 (= G180), G185 (= G182), V205 (≠ I202), E206 (= E203), F207 (≠ M204), L208 (≠ A205), K240 (≠ R236), V241 (≠ I237), I276 (≠ A272), G277 (= G273), R278 (≠ I274), R297 (= R292), M324 (≠ W319)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
39% identity, 99% coverage: 6:466/467 of query aligns to 1:465/465 of 3urhB
- active site: Y35 (≠ L39), C39 (= C43), C44 (= C48), S47 (≠ T51), V183 (≠ A183), E187 (= E187), H443 (≠ F444), H445 (= H446), E450 (= E451)
- binding flavin-adenine dinucleotide: I6 (≠ V11), G7 (= G12), G9 (= G14), P10 (= P15), G11 (= G16), E30 (= E35), K31 (= K36), G37 (= G41), T38 (≠ I42), C39 (= C43), G43 (= G47), C44 (= C48), K48 (= K52), T111 (≠ H114), G112 (≠ A115), A140 (= A142), T141 (= T143), G142 (= G144), I184 (= I184), R273 (≠ I274), G312 (= G312), D313 (= D313), M319 (≠ W319), L320 (= L320), A321 (= A321), H322 (= H322)
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
41% identity, 99% coverage: 6:467/467 of query aligns to 4:458/460 of 2eq6A
- active site: V37 (≠ L39), C41 (= C43), C46 (= C48), T49 (= T51), A176 (= A183), E180 (= E187), H435 (≠ F444), H437 (= H446), E442 (= E451)
- binding flavin-adenine dinucleotide: I9 (≠ V11), G10 (= G12), G12 (= G14), P13 (= P15), G14 (= G16), E33 (= E35), A34 (≠ K36), G39 (= G41), V40 (≠ I42), C41 (= C43), G45 (= G47), C46 (= C48), K50 (= K52), F111 (≠ H114), A112 (= A115), A135 (= A142), T136 (= T143), G137 (= G144), S155 (≠ Y163), R269 (vs. gap), D306 (= D313), L312 (≠ W319), L313 (= L320), A314 (= A321), H315 (= H322), Y344 (= Y353)
Sites not aligning to the query:
7kmyA Structure of mtb lpd bound to 010705 (see paper)
41% identity, 97% coverage: 2:456/467 of query aligns to 1:454/465 of 7kmyA
- active site: W38 (≠ L39), C42 (= C43), C47 (= C48), S50 (≠ T51), A182 (= A183), E186 (= E187), H442 (≠ F444), H444 (= H446), E449 (= E451)
- binding flavin-adenine dinucleotide: L10 (≠ V11), G11 (= G12), G13 (= G14), P14 (= P15), V33 (= V34), E34 (= E35), P35 (≠ K36), Y37 (≠ Q38), G40 (= G41), V41 (≠ I42), C42 (= C43), G46 (= G47), C47 (= C48), K51 (= K52), Y113 (≠ H114), G114 (≠ A115), A142 (= A142), T143 (= T143), G144 (= G144), Y162 (= Y163), I183 (= I184), Y277 (≠ L281), G309 (= G312), D310 (= D313), Q316 (≠ W319), L317 (= L320), A318 (= A321)
- 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 (= Y18), R94 (≠ L95), G97 (= G98), F100 (≠ Y101), E322 (≠ S325), A382 (≠ V384), H444 (= H446), E449 (= E451)
Sites not aligning to the query:
4m52A Structure of mtb lpd bound to sl827 (see paper)
41% identity, 97% coverage: 2:456/467 of query aligns to 1:454/465 of 4m52A
- active site: W38 (≠ L39), C42 (= C43), C47 (= C48), S50 (≠ T51), A182 (= A183), E186 (= E187), H442 (≠ F444), H444 (= H446), E449 (= E451)
- binding flavin-adenine dinucleotide: L10 (≠ V11), G11 (= G12), G13 (= G14), P14 (= P15), V33 (= V34), E34 (= E35), P35 (≠ K36), Y37 (≠ Q38), V41 (≠ I42), C42 (= C43), G46 (= G47), C47 (= C48), K51 (= K52), Y113 (≠ H114), G114 (≠ A115), A142 (= A142), T143 (= T143), Y162 (= Y163), I183 (= I184), F270 (≠ I274), Y277 (≠ L281), G309 (= G312), D310 (= D313), Q316 (≠ W319), L317 (= L320), A318 (= A321)
- binding N~2~-[(2-amino-5-bromopyridin-3-yl)sulfonyl]-N-(4-methoxyphenyl)-N~2~-methylglycinamide: P14 (= P15), Y17 (= Y18), R94 (≠ L95), F100 (≠ Y101), E322 (≠ S325), A382 (≠ V384), H444 (= H446)
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)
41% identity, 97% coverage: 5:456/467 of query aligns to 3:453/464 of 8u0qA
- binding flavin-adenine dinucleotide: L9 (≠ V11), G10 (= G12), G12 (= G14), P13 (= P15), G14 (= G16), V32 (= V34), E33 (= E35), P34 (≠ K36), Y36 (≠ Q38), G39 (= G41), V40 (≠ I42), C41 (= C43), G45 (= G47), C46 (= C48), K50 (= K52), Y112 (≠ H114), G113 (≠ A115), A141 (= A142), T142 (= T143), G143 (= G144), Y161 (= Y163), I182 (= I184), Y276 (≠ L281), G308 (= G312), D309 (= D313), Q315 (≠ W319), L316 (= L320), A317 (= A321), H318 (= H322)
- binding N-(3-acetamidophenyl)-N~2~-[3-(difluoromethyl)-5-methylbenzene-1-sulfonyl]-N~2~-methylglycinamide: Y16 (= Y18), R93 (≠ L95), G96 (= G98), F99 (≠ Y101), E321 (≠ S325), A381 (≠ V384), A383 (≠ G386), H443 (= H446), E448 (= E451)
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
41% identity, 97% coverage: 5:456/467 of query aligns to 3:453/464 of 8ct4A
- binding flavin-adenine dinucleotide: L9 (≠ V11), G10 (= G12), G12 (= G14), P13 (= P15), E33 (= E35), P34 (≠ K36), Y36 (≠ Q38), G39 (= G41), V40 (≠ I42), C41 (= C43), G45 (= G47), C46 (= C48), K50 (= K52), Y112 (≠ H114), G113 (≠ A115), T142 (= T143), G143 (= G144), Y161 (= Y163), I182 (= I184), Y276 (≠ L281), D309 (= D313), Q315 (≠ W319), L316 (= L320), A317 (= A321)
- 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 (= Y18), R93 (≠ L95), F99 (≠ Y101), E321 (≠ S325), F377 (= F380), A381 (≠ V384), A383 (≠ G386), H443 (= H446), E448 (= E451), A449 (= A452), E452 (= E455)
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)
41% identity, 97% coverage: 5:456/467 of query aligns to 3:453/464 of P9WHH9
- D5 (= D7) mutation to A: Reduces lipoamide dehydrogenase activity by 95%.
- 33:41 (vs. 35:43, 44% identical) binding FAD
- C41 (= C43) modified: Disulfide link with 46, Redox-active
- N43 (= N45) mutation to A: Reduces lipoamide dehydrogenase activity by 89%.
- C46 (= C48) modified: Disulfide link with 41, Redox-active
- K50 (= K52) binding FAD
- R93 (≠ L95) mutation to A: Reduces lipoamide dehydrogenase activity by 94%.; mutation to E: Reduces lipoamide dehydrogenase activity by 96%.
- K103 (= K105) mutation to E: Reduces lipoamide dehydrogenase activity by 82%.
- D309 (= D313) binding FAD
- A317 (= A321) binding FAD
- H386 (≠ I389) 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)
41% identity, 97% coverage: 5:456/467 of query aligns to 2:452/463 of 3ii4A
- active site: W36 (≠ L39), C40 (= C43), C45 (= C48), S48 (≠ T51), A180 (= A183), E184 (= E187), H440 (≠ F444), H442 (= H446), E447 (= E451)
- 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 (≠ I274), R287 (= R292), G311 (= G316), Q314 (≠ W319), L315 (= L320), R346 (≠ A350), A347 (≠ C351)
- binding flavin-adenine dinucleotide: L8 (≠ V11), G9 (= G12), G11 (= G14), P12 (= P15), G13 (= G16), V31 (= V34), E32 (= E35), P33 (≠ K36), Y35 (≠ Q38), G38 (= G41), V39 (≠ I42), C40 (= C43), G44 (= G47), C45 (= C48), K49 (= K52), Y111 (≠ H114), G112 (≠ A115), A140 (= A142), T141 (= T143), G142 (= G144), Y160 (= Y163), I181 (= I184), Y275 (≠ L281), G307 (= G312), D308 (= D313), Q314 (≠ W319), L315 (= L320), A316 (= A321)
Query Sequence
>WP_050460862.1 NCBI__GCF_001189915.1:WP_050460862.1
MTQAQYDLVVVGGGPGGYVAAIRAAQLGLKTALVEKAQLGGICLNWGCIPTKALLRSADV
LRLVRDAGRFGVLTAAPQIDLAAMVERSRTVAAQLQGGVGYLMKKNKVTVLNGHARLAGR
GKLSVTNADGVSTLAARHIILATGARARPLPGLTPDGDSVWSYREALVPKRVPQHLVVIG
AGAIGIEFASFYHALGAKVSVIEMADRVLPVEDEEVSQYVGDVLRKQGMHLYTGSRILSS
SKRRVGQTQEWTLQLDGKHKDSLTADVILTAAGIIGNVEELGLEGTAVKVERSHIVTDAY
GATAEPGVYAIGDVAGAPWLAHKASHEAVICVEKIAGLAPHTLDITKIPACTYSHPQVAS
VGLTEAQARAGGRQVRVGKFPFAVNGKAIALGATAGFAKVVFDAASGELLGAHMVGEEVT
EMIQGYTVARELETTEAELMATIFPHPTQSEAMHEAVLAAYERSLHM
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