SitesBLAST
Comparing 5211003 FitnessBrowser__PV4:5211003 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)
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: 1:474/475 of query aligns to 1:474/474 of P0A9P0
- M1 (= M1) modified: Initiator methionine, Removed
- K220 (≠ R220) modified: N6-acetyllysine
4jdrA Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli (see paper)
86% identity, 99% coverage: 2:472/475 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 (= I185), E188 (= E189), V324 (= V325), H442 (= H443), H444 (= H445), E449 (= E450), N467 (= N468), P468 (= P469)
- 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 (= L116), G116 (= G117), A144 (= A145), G145 (= G146), I185 (= I186), G311 (= G312), D312 (= D313), M318 (= M319), L319 (= L320), A320 (= A321), H321 (= H322)
1bhyA Low temperature middle resolution structure of p64k from masc data (see paper)
63% identity, 95% coverage: 19:470/475 of query aligns to 19:481/482 of 1bhyA
- active site: L41 (= L41), C45 (= C45), C50 (= C50), S53 (= S53), I195 (= I185), E199 (= E189), H454 (= H443), H456 (= H445), E461 (= E450), P479 (≠ N468), Q480 (≠ P469)
- binding flavin-adenine dinucleotide: E36 (= E36), R37 (= R37), Y38 (≠ F38), G43 (= G43), V44 (= V44), C45 (= C45), G49 (= G49), C50 (= C50), K54 (= K54), D116 (≠ L116), G117 (= G117), Y135 (vs. gap), A156 (= A145), G157 (= G146), D324 (= D313), L331 (= L320), A332 (= A321)
Sites not aligning to the query:
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
45% identity, 96% coverage: 5:462/475 of query aligns to 8:463/470 of P11959
- 39:47 (vs. 36:45, 60% identical) binding
- K56 (= K54) binding
- D314 (= D313) binding
- A322 (= A321) binding
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
45% identity, 96% coverage: 5:458/475 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 (≠ I185), E184 (= E189), S320 (≠ V325), H438 (= H443), H440 (= H445), E445 (= E450)
- 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 (≠ L116), A113 (≠ G117), T141 (≠ A145), G142 (= G146), Y180 (≠ I185), I181 (= I186), R268 (= R273), D308 (= D313), A314 (≠ M319), L315 (= L320), A316 (= A321)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
44% identity, 94% coverage: 9:456/475 of query aligns to 9:459/470 of 6uziC
- active site: C45 (= C45), C50 (= C50), S53 (= S53), V187 (≠ I185), E191 (= E189), H448 (= H445), E453 (= E450)
- 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 (≠ L116), G118 (= G117), T147 (≠ A145), G148 (= G146), I188 (= I186), R276 (= R273), D316 (= D313), M322 (= M319), L323 (= L320), A324 (= A321)
- binding zinc ion: H448 (= H445), E453 (= E450)
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, 98% coverage: 6:472/475 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 (= D313) binding
- A327 (= A321) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
43% identity, 97% coverage: 6:468/475 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 (≠ I185), E197 (= E189), S333 (≠ V325), F451 (≠ H443), H453 (= H445), E458 (= E450), N476 (= N468)
- 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 (≠ L116), G124 (= G117), A152 (= A144), S153 (≠ A145), G154 (= G146), I194 (= I186), R281 (= R273), G320 (= G312), D321 (= D313), M327 (= M319), L328 (= L320), A329 (= A321), H330 (= H322), H453 (= H445), P454 (= P446)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
43% identity, 97% coverage: 6:468/475 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 (≠ I185), E194 (= E189), S330 (≠ V325), F448 (≠ H443), H450 (= H445), E455 (= E450), N473 (= N468)
- 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 (≠ L116), G121 (= G117), A149 (= A144), S150 (≠ A145), G151 (= G146), S170 (= S165), G317 (= G312), D318 (= D313), M324 (= M319), L325 (= L320), A326 (= A321), H327 (= H322), Y357 (= Y352), H450 (= H445), P451 (= P446)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (≠ M181), G189 (= G184), V190 (≠ I185), I191 (= I186), E194 (= E189), E210 (= E205), A211 (≠ M206), L212 (≠ F207), A275 (= A270), V276 (≠ I271), G277 (= G272), R278 (= R273), M324 (= M319), L325 (= L320), V355 (≠ I350), Y357 (= Y352)
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
43% identity, 97% coverage: 6:468/475 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 (≠ I185), E193 (= E189), S329 (≠ V325), F447 (≠ H443), H449 (= H445), E454 (= E450), N472 (= N468)
- 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 (≠ L116), G120 (= G117), A148 (= A144), S149 (≠ A145), G150 (= G146), S169 (= S165), I190 (= I186), R277 (= R273), G316 (= G312), D317 (= D313), M323 (= M319), L324 (= L320), A325 (= A321), H326 (= H322), H449 (= H445), P450 (= P446)
- binding nicotinamide-adenine-dinucleotide: I185 (≠ M181), G186 (= G182), G188 (= G184), V189 (≠ I185), I190 (= I186), L208 (≠ V204), E209 (= E205), A210 (≠ M206), V243 (= V238), V275 (≠ I271), G276 (= G272)
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: 6:470/475 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 (= D313) binding
- A327 (= A321) binding
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
45% identity, 95% coverage: 9:459/475 of query aligns to 6:451/460 of 2eq6A
- active site: V37 (≠ L41), C41 (= C45), C46 (= C50), T49 (≠ S53), A176 (≠ I185), E180 (= E189), H435 (= H443), H437 (= H445), E442 (= E450)
- 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 (≠ L116), A112 (≠ G117), A135 (= A144), T136 (≠ A145), G137 (= G146), S155 (= S165), R269 (≠ N276), D306 (= D313), L312 (≠ M319), L313 (= L320), A314 (= A321), H315 (= H322), Y344 (= Y352)
Sites not aligning to the query:
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: 6:456/475 of query aligns to 3:461/472 of 3ladA
- active site: L44 (= L41), C48 (= C45), C53 (= C50), S56 (= S53), V190 (≠ I185), E194 (= E189), F448 (≠ H443), H450 (= H445), E455 (= E450)
- 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 (≠ L116), G121 (= G117), A149 (= A144), S150 (≠ A145), G151 (= G146), I191 (= I186), R278 (= R273), D318 (= D313), L325 (= L320), A326 (= A321)
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
43% identity, 95% coverage: 5:455/475 of query aligns to 13:470/482 of 6hg8B
- active site: C53 (= C45), C58 (= C50), S61 (= S53), V196 (≠ I185), E200 (= E189), H460 (= H445), E465 (= E450)
- 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 (≠ L116), G127 (= G117), T156 (≠ A145), G157 (= G146), I197 (= I186), R288 (= R273), F291 (≠ N276), G327 (= G312), D328 (= D313), M334 (= M319), L335 (= L320), A336 (= A321), H337 (= H322)
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: 5:451/475 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 145:147) binding
- 220:227 (vs. 182:189, 63% identical) binding
- E243 (= E205) binding
- V278 (= V238) binding
- G314 (= G272) binding
- D355 (= D313) binding
- MLAH 361:364 (= MLAH 319:322) binding
- E375 (= E333) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ Y341) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ H406) 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 (= E424) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ M431) 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 (= D437) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ L440) 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 (= H443) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P446) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (≠ H449) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E450) 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.
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
43% identity, 94% coverage: 5:451/475 of query aligns to 3:456/472 of 1zmdA
- active site: L39 (= L41), C43 (= C45), C48 (= C50), S51 (= S53), V186 (≠ I185), E190 (= E189), H448 (= H443), H450 (= H445), E455 (= E450)
- 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 (≠ L116), G117 (= G117), T146 (≠ A145), G147 (= G146), S166 (= S165), R278 (= R273), F281 (≠ N276), G317 (= G312), D318 (= D313), M324 (= M319), L325 (= L320), A326 (= A321), H327 (= H322)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (≠ M181), G183 (= G182), G185 (= G184), V186 (≠ I185), I187 (= I186), E190 (= E189), E206 (= E205), F207 (≠ M206), L208 (≠ F207), I276 (= I271), G277 (= G272), R278 (= R273), M324 (= M319), L325 (= L320), V355 (≠ I350), Y357 (= Y352)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
43% identity, 94% coverage: 5:451/475 of query aligns to 3:456/472 of 1zmcA
- active site: L39 (= L41), C43 (= C45), C48 (= C50), S51 (= S53), V186 (≠ I185), E190 (= E189), H448 (= H443), H450 (= H445), E455 (= E450)
- 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 (≠ L116), G117 (= G117), T146 (≠ A145), G147 (= G146), S166 (= S165), I187 (= I186), F281 (≠ N276), G317 (= G312), D318 (= D313), M324 (= M319), L325 (= L320), A326 (= A321), H327 (= H322)
- binding nicotinamide-adenine-dinucleotide: G183 (= G182), G185 (= G184), V205 (= V204), E206 (= E205), F207 (≠ M206), L208 (≠ F207), K240 (= K237), V241 (= V238), I276 (= I271), G277 (= G272), R278 (= R273), R297 (= R292), M324 (= M319)
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
41% identity, 97% coverage: 6:468/475 of query aligns to 4:474/475 of 6awaA
- active site: L45 (= L41), C49 (= C45), C54 (= C50), S57 (= S53), V191 (≠ I185), E195 (= E189), F449 (≠ H443), H451 (= H445), E456 (= E450), N474 (= N468)
- binding adenosine monophosphate: I187 (≠ M181), E211 (= E205), A212 (≠ M206), L213 (≠ F207), V245 (= V238), V277 (≠ I271)
- 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 (≠ L116), G122 (= G117), S151 (≠ A145), G152 (= G146), I192 (= I186), R279 (= R273), G318 (= G312), D319 (= D313), M325 (= M319), L326 (= L320), A327 (= A321), Y358 (= Y352)
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: 6:456/475 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 (= D313) binding
- MLAH 354:357 (= MLAH 319:322) 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: 6:456/475 of query aligns to 3:457/467 of 1dxlA
- active site: L38 (= L41), C42 (= C45), C47 (= C50), S50 (= S53), Y184 (≠ I185), E188 (= E189), H444 (= H443), H446 (= H445), E451 (= E450)
- 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 (≠ L116), G115 (= G117), T144 (≠ A145), G145 (= G146), Y184 (≠ I185), I185 (= I186), R274 (= R273), D314 (= D313), M320 (= M319), L321 (= L320), A322 (= A321), H323 (= H322)
Query Sequence
>5211003 FitnessBrowser__PV4:5211003
MSNEIKTQVVVLGAGPAGYSAAFRAADLGLETVIVERFSTLGGVCLNVGCIPSKALLHVS
KVIEEAKAISNHGVVFGEPQIDLDKLREFKQSVISQLTGGLGGMSKMRKVNVVNGLGKFT
GPNTIEVAGEDGVKVVHFEQAIIAAGSRPIQLPFIPHEDPRIWDSTDALELKEVPGKLLV
MGGGIIGLEMGTVYSSLGSEIDVVEMFDQVIPAADKDIVRVYTKKIKNKFNLILETKVTA
VEAKEDGIYVSMEGKKAPTEPVRYDAVLVAIGRTPNGKLIDADKAGVNIDERGFINVDKQ
MRTNVPHIYAIGDIVGQPMLAHKGVHEGHVAAEVIAGMKHYFDPKVIPSIAYTDPEVAWV
GLTEKEAKEQGIAYETASFPWAASGRAIASDCSEGMTKLIFDKETHRVIGGAIVGVNGGE
LLGEIGLAIEMGCDAEDLALTIHAHPTLHESVGLAAEIYEGSITDLPNPKAKKKK
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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