SitesBLAST
Comparing 199618 FitnessBrowser__MR1:199618 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)
P0A9P0 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes; Glycine cleavage system L protein; EC 1.8.1.4 from Escherichia coli (strain K12) (see 2 papers)
86% identity, 100% coverage: 1:475/475 of query aligns to 1:474/474 of P0A9P0
- M1 (= M1) modified: Initiator methionine, Removed
- K220 (≠ R221) modified: N6-acetyllysine
4jdrA Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli (see paper)
86% identity, 99% coverage: 2:473/475 of query aligns to 1:471/471 of 4jdrA
- active site: P15 (= P16), L40 (= L41), C44 (= C45), C49 (= C50), S52 (= S53), E77 (= E78), P78 (= P79), I184 (= I186), E188 (= E190), V324 (= V326), H442 (= H444), H444 (= H446), E449 (= E451), N467 (= N469), P468 (= P470)
- binding flavin-adenine dinucleotide: G12 (= G13), G14 (= G15), P15 (= P16), A16 (= A17), E35 (= E36), R36 (= R37), Y37 (≠ F38), V43 (= V44), C44 (= C45), G48 (= G49), C49 (= C50), K53 (= K54), L115 (≠ F116), G116 (= G117), A144 (= A146), G145 (= G147), I185 (= I187), G311 (= G313), D312 (= D314), M318 (= M320), L319 (= L321), A320 (= A322), H321 (= H323)
1bhyA Low temperature middle resolution structure of p64k from masc data (see paper)
64% identity, 95% coverage: 19:471/475 of query aligns to 19:481/482 of 1bhyA
- active site: L41 (= L41), C45 (= C45), C50 (= C50), S53 (= S53), I195 (= I186), E199 (= E190), H454 (= H444), H456 (= H446), E461 (= E451), P479 (≠ N469), Q480 (≠ P470)
- binding flavin-adenine dinucleotide: E36 (= E36), R37 (= R37), Y38 (≠ F38), G43 (= G43), V44 (= V44), C45 (= C45), G49 (= G49), C50 (= C50), K54 (= K54), D116 (≠ F116), G117 (= G117), Y135 (vs. gap), A156 (= A146), G157 (= G147), D324 (= D314), L331 (= L321), A332 (= A322)
Sites not aligning to the query:
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
44% identity, 95% coverage: 9:457/475 of query aligns to 9:459/470 of 6uziC
- active site: C45 (= C45), C50 (= C50), S53 (= S53), V187 (≠ I186), E191 (= E190), H448 (= H446), E453 (= E451)
- binding flavin-adenine dinucleotide: I12 (≠ L12), G13 (= G13), G15 (= G15), P16 (= P16), G17 (≠ A17), E36 (= E36), K37 (≠ R37), G43 (= G43), T44 (≠ V44), C45 (= C45), G49 (= G49), C50 (= C50), S53 (= S53), K54 (= K54), V117 (≠ F116), G118 (= G117), T147 (≠ A146), G148 (= G147), I188 (= I187), R276 (= R274), D316 (= D314), M322 (= M320), L323 (= L321), A324 (= A322)
- binding zinc ion: H448 (= H446), E453 (= E451)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
45% identity, 97% coverage: 5:463/475 of query aligns to 8:463/470 of P11959
- 39:47 (vs. 36:45, 60% identical) binding
- K56 (= K54) binding
- D314 (= D314) binding
- A322 (= A322) binding
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
45% identity, 96% coverage: 5:459/475 of query aligns to 2:453/455 of 1ebdA
- active site: P13 (= P16), L37 (= L41), C41 (= C45), C46 (= C50), S49 (= S53), N74 (≠ E78), V75 (≠ P79), Y180 (≠ I186), E184 (= E190), S320 (≠ V326), H438 (= H444), H440 (= H446), E445 (= E451)
- binding flavin-adenine dinucleotide: G10 (= G13), G12 (= G15), P13 (= P16), V32 (= V35), E33 (= E36), K34 (≠ R37), G39 (= G43), V40 (= V44), C41 (= C45), G45 (= G49), C46 (= C50), K50 (= K54), E112 (≠ F116), A113 (≠ G117), T141 (≠ A146), G142 (= G147), Y180 (≠ I186), I181 (= I187), R268 (= R274), D308 (= D314), A314 (≠ M320), L315 (= L321), A316 (= A322)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
42% identity, 99% coverage: 6:473/475 of query aligns to 4:478/478 of P14218
- 34:49 (vs. 36:45, 31% identical) binding
- C49 (= C45) modified: Disulfide link with 54, Redox-active
- C54 (= C50) modified: Disulfide link with 49, Redox-active
- K58 (= K54) binding
- G122 (= G117) binding
- D319 (= D314) binding
- A327 (= A322) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
43% identity, 98% coverage: 6:469/475 of query aligns to 2:472/472 of 5u8vA
- active site: P12 (= P16), L43 (= L41), C47 (= C45), C52 (= C50), S55 (= S53), G81 (≠ E78), V82 (≠ P79), V189 (≠ I186), E193 (= E190), S329 (≠ V326), F447 (≠ H444), H449 (= H446), E454 (= E451), N472 (= N469)
- binding flavin-adenine dinucleotide: I8 (≠ L12), G11 (= G15), P12 (= P16), G13 (≠ A17), E32 (= E36), G45 (= G43), T46 (≠ V44), C47 (= C45), G51 (= G49), C52 (= C50), K56 (= K54), H119 (≠ F116), G120 (= G117), A148 (= A145), S149 (≠ A146), G150 (= G147), S169 (= S166), I190 (= I187), R277 (= R274), G316 (= G313), D317 (= D314), M323 (= M320), L324 (= L321), A325 (= A322), H326 (= H323), H449 (= H446), P450 (= P447)
- binding nicotinamide-adenine-dinucleotide: I185 (≠ M182), G186 (= G183), G188 (= G185), V189 (≠ I186), I190 (= I187), L208 (≠ V205), E209 (= E206), A210 (≠ M207), V243 (= V239), V275 (≠ I272), G276 (= G273)
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
43% identity, 98% coverage: 6:469/475 of query aligns to 3:473/473 of 5u8wA
- active site: P13 (= P16), L44 (= L41), C48 (= C45), C53 (= C50), S56 (= S53), G82 (≠ E78), V83 (≠ P79), V190 (≠ I186), E194 (= E190), S330 (≠ V326), F448 (≠ H444), H450 (= H446), E455 (= E451), N473 (= N469)
- binding flavin-adenine dinucleotide: I9 (≠ L12), G12 (= G15), P13 (= P16), G14 (≠ A17), E33 (= E36), K34 (≠ R37), G46 (= G43), T47 (≠ V44), C48 (= C45), G52 (= G49), C53 (= C50), K57 (= K54), H120 (≠ F116), G121 (= G117), A149 (= A145), S150 (≠ A146), G151 (= G147), S170 (= S166), G317 (= G313), D318 (= D314), M324 (= M320), L325 (= L321), A326 (= A322), H327 (= H323), Y357 (= Y353), H450 (= H446), P451 (= P447)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (≠ M182), G189 (= G185), V190 (≠ I186), I191 (= I187), E194 (= E190), E210 (= E206), A211 (≠ M207), L212 (≠ F208), A275 (= A271), V276 (≠ I272), G277 (= G273), R278 (= R274), M324 (= M320), L325 (= L321), V355 (≠ I351), Y357 (= Y353)
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
43% identity, 98% coverage: 6:469/475 of query aligns to 6:476/477 of 5u8uD
- active site: P16 (= P16), L47 (= L41), C51 (= C45), C56 (= C50), S59 (= S53), G85 (≠ E78), V86 (≠ P79), V193 (≠ I186), E197 (= E190), S333 (≠ V326), F451 (≠ H444), H453 (= H446), E458 (= E451), N476 (= N469)
- binding flavin-adenine dinucleotide: I12 (≠ L12), G15 (= G15), P16 (= P16), G17 (≠ A17), E36 (= E36), K37 (≠ R37), G49 (= G43), T50 (≠ V44), C51 (= C45), G55 (= G49), C56 (= C50), K60 (= K54), H123 (≠ F116), G124 (= G117), A152 (= A145), S153 (≠ A146), G154 (= G147), I194 (= I187), R281 (= R274), G320 (= G313), D321 (= D314), M327 (= M320), L328 (= L321), A329 (= A322), H330 (= H323), H453 (= H446), P454 (= P447)
Sites not aligning to the query:
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
41% identity, 98% coverage: 6:471/475 of query aligns to 4:476/477 of P18925
- 34:49 (vs. 36:45, 31% identical) binding
- C49 (= C45) modified: Disulfide link with 54, Redox-active
- C54 (= C50) modified: Disulfide link with 49, Redox-active
- K58 (= K54) binding
- D319 (= D314) binding
- A327 (= A322) binding
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
43% identity, 95% coverage: 5:456/475 of query aligns to 13:470/482 of 6hg8B
- active site: C53 (= C45), C58 (= C50), S61 (= S53), V196 (≠ I186), E200 (= E190), H460 (= H446), E465 (= E451)
- binding flavin-adenine dinucleotide: I20 (≠ L12), G23 (= G15), P24 (= P16), G25 (≠ A17), E44 (= E36), K45 (≠ R37), N46 (≠ F38), G51 (= G43), T52 (≠ V44), C53 (= C45), G57 (= G49), C58 (= C50), K62 (= K54), Y126 (≠ F116), G127 (= G117), T156 (≠ A146), G157 (= G147), I197 (= I187), R288 (= R274), F291 (≠ N277), G327 (= G313), D328 (= D314), M334 (= M320), L335 (= L321), A336 (= A322), H337 (= H323)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
43% identity, 94% coverage: 5:452/475 of query aligns to 40:493/509 of P09622
- 71:80 (vs. 36:45, 60% identical) binding
- K72 (≠ R37) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K54) binding ; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (= K67) to T: in dbSNP:rs1130477
- G154 (= G117) binding
- TGS 183:185 (≠ AGS 146:148) binding
- 220:227 (vs. 183:190, 63% identical) binding
- E243 (= E206) binding
- V278 (= V239) binding
- G314 (= G273) binding
- D355 (= D314) binding
- MLAH 361:364 (= MLAH 320:323) binding
- E375 (= E334) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ Y342) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ H407) 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 (= E425) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ M432) 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 (= D438) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ L441) 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 (= H444) 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 (≠ H450) 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.
Sites not aligning to the query:
- 495 R → G: in DLDD; loss of enzyme activity; reduced interaction with PDHX; dbSNP:rs121964989
- 505 K→M: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
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)
42% identity, 95% coverage: 6:457/475 of query aligns to 3:461/472 of 3ladA
- active site: L44 (= L41), C48 (= C45), C53 (= C50), S56 (= S53), V190 (≠ I186), E194 (= E190), F448 (≠ H444), H450 (= H446), E455 (= E451)
- binding flavin-adenine dinucleotide: I9 (≠ L12), G10 (= G13), G12 (= G15), P13 (= P16), E33 (= E36), K34 (≠ R37), G46 (= G43), T47 (≠ V44), C48 (= C45), G52 (= G49), C53 (= C50), H120 (≠ F116), G121 (= G117), A149 (= A145), S150 (≠ A146), G151 (= G147), I191 (= I187), R278 (= R274), D318 (= D314), L325 (= L321), A326 (= A322)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
43% identity, 94% coverage: 5:452/475 of query aligns to 3:456/472 of 1zmdA
- active site: L39 (= L41), C43 (= C45), C48 (= C50), S51 (= S53), V186 (≠ I186), E190 (= E190), H448 (= H444), H450 (= H446), E455 (= E451)
- binding flavin-adenine dinucleotide: I10 (≠ L12), G11 (= G13), G13 (= G15), P14 (= P16), G15 (≠ A17), E34 (= E36), K35 (≠ R37), N36 (≠ F38), G41 (= G43), T42 (≠ V44), C43 (= C45), G47 (= G49), C48 (= C50), K52 (= K54), Y116 (≠ F116), G117 (= G117), T146 (≠ A146), G147 (= G147), S166 (= S166), R278 (= R274), F281 (≠ N277), G317 (= G313), D318 (= D314), M324 (= M320), L325 (= L321), A326 (= A322), H327 (= H323)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (≠ M182), G183 (= G183), G185 (= G185), V186 (≠ I186), I187 (= I187), E190 (= E190), E206 (= E206), F207 (≠ M207), L208 (≠ F208), I276 (= I272), G277 (= G273), R278 (= R274), M324 (= M320), L325 (= L321), V355 (≠ I351), Y357 (= Y353)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
43% identity, 94% coverage: 5:452/475 of query aligns to 3:456/472 of 1zmcA
- active site: L39 (= L41), C43 (= C45), C48 (= C50), S51 (= S53), V186 (≠ I186), E190 (= E190), H448 (= H444), H450 (= H446), E455 (= E451)
- binding flavin-adenine dinucleotide: I10 (≠ L12), G11 (= G13), G13 (= G15), P14 (= P16), G15 (≠ A17), E34 (= E36), K35 (≠ R37), N36 (≠ F38), G41 (= G43), T42 (≠ V44), C43 (= C45), G47 (= G49), C48 (= C50), K52 (= K54), Y116 (≠ F116), G117 (= G117), T146 (≠ A146), G147 (= G147), S166 (= S166), I187 (= I187), F281 (≠ N277), G317 (= G313), D318 (= D314), M324 (= M320), L325 (= L321), A326 (= A322), H327 (= H323)
- binding nicotinamide-adenine-dinucleotide: G183 (= G183), G185 (= G185), V205 (= V205), E206 (= E206), F207 (≠ M207), L208 (≠ F208), K240 (= K238), V241 (= V239), I276 (= I272), G277 (= G273), R278 (= R274), R297 (= R293), M324 (= M320)
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
44% identity, 95% coverage: 9:460/475 of query aligns to 6:451/460 of 2eq6A
- active site: V37 (≠ L41), C41 (= C45), C46 (= C50), T49 (≠ S53), A176 (≠ I186), E180 (= E190), H435 (= H444), H437 (= H446), E442 (= E451)
- binding flavin-adenine dinucleotide: I9 (≠ L12), G10 (= G13), G12 (= G15), P13 (= P16), G14 (≠ A17), E33 (= E36), A34 (≠ R37), G39 (= G43), V40 (= V44), C41 (= C45), G45 (= G49), C46 (= C50), K50 (= K54), F111 (= F116), A112 (≠ G117), A135 (= A145), T136 (≠ A146), G137 (= G147), S155 (= S166), R269 (≠ N277), D306 (= D314), L312 (≠ M320), L313 (= L321), A314 (= A322), H315 (= H323), Y344 (= Y353)
Sites not aligning to the query:
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
41% identity, 98% coverage: 6:469/475 of query aligns to 4:474/475 of 6awaA
- active site: L45 (= L41), C49 (= C45), C54 (= C50), S57 (= S53), V191 (≠ I186), E195 (= E190), F449 (≠ H444), H451 (= H446), E456 (= E451), N474 (= N469)
- binding adenosine monophosphate: I187 (≠ M182), E211 (= E206), A212 (≠ M207), L213 (≠ F208), V245 (= V239), V277 (≠ I272)
- binding flavin-adenine dinucleotide: I10 (≠ L12), G13 (= G15), P14 (= P16), G15 (≠ A17), E34 (= E36), K35 (≠ R37), T48 (≠ V44), C49 (= C45), G53 (= G49), C54 (= C50), K58 (= K54), H121 (≠ F116), G122 (= G117), S151 (≠ A146), G152 (= G147), I192 (= I187), R279 (= R274), G318 (= G313), D319 (= D314), M325 (= M320), L326 (= L321), A327 (= A322), Y358 (= Y353)
Sites not aligning to the query:
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, 95% coverage: 6:457/475 of query aligns to 37:491/501 of P31023
- 67:76 (vs. 36:45, 50% identical) binding
- C76 (= C45) modified: Disulfide link with 81, Redox-active
- C81 (= C50) modified: Disulfide link with 76, Redox-active
- G149 (= G117) binding
- D348 (= D314) binding
- MLAH 354:357 (= MLAH 320:323) 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, 95% coverage: 6:457/475 of query aligns to 3:457/467 of 1dxlA
- active site: L38 (= L41), C42 (= C45), C47 (= C50), S50 (= S53), Y184 (≠ I186), E188 (= E190), H444 (= H444), H446 (= H446), E451 (= E451)
- binding flavin-adenine dinucleotide: I9 (≠ L12), P13 (= P16), G14 (≠ A17), E33 (= E36), K34 (≠ R37), R35 (≠ F38), G40 (= G43), T41 (≠ V44), C42 (= C45), G46 (= G49), C47 (= C50), K51 (= K54), Y114 (≠ F116), G115 (= G117), T144 (≠ A146), G145 (= G147), Y184 (≠ I186), I185 (= I187), R274 (= R274), D314 (= D314), M320 (= M320), L321 (= L321), A322 (= A322), H323 (= H323)
Query Sequence
>199618 FitnessBrowser__MR1:199618
MSNEIKTQVVVLGAGPAGYSAAFRAADLGLETVIVERFSTLGGVCLNVGCIPSKALLHVA
KVIEEAKAVAAHGVVFGEPTIDLDKLRSFKQKVISQLTGGLGGMSKMRKVNVVNGFGKFS
GPNSLEVTAEDGTVTVVKFDQAIIAAGSRPIKLPFIPHEDPRIWDSTDALELKEVPGKLL
VMGGGIIGLEMGTVYSSLGSEIDVVEMFDQVIPAADKDVVRVFTKQIKKKFNLILETKVT
AVEAREDGIYVSMEGKSAPAEPVRYDAVLVAIGRTPNGKLIDAEKAGVKIDERGFINVDK
QLRTNVPHIYAIGDIVGQPMLAHKGVHEGHVAAEVIAGMKHYFDPKVIPSIAYTDPEVAW
VGLTEKEAKEQGIAYETATFPWAASGRAIASDCSEGMTKLIFDKDTHRVIGGAIVGVNGG
ELLGEIGLAIEMGCDAEDLALTIHAHPTLHESVGLAAEIYEGSITDLPNPKAKKK
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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