SitesBLAST
Comparing WP_051301765.1 NCBI__GCF_000428045.1:WP_051301765.1 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)
4jdrA Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli (see paper)
60% identity, 98% coverage: 13:484/484 of query aligns to 1:471/471 of 4jdrA
- active site: P15 (= P27), L40 (= L52), C44 (= C56), C49 (= C61), S52 (= S64), E77 (≠ K89), P78 (= P90), I184 (= I196), E188 (= E200), V324 (≠ T337), H442 (= H455), H444 (= H457), E449 (= E462), N467 (≠ P480), P468 (= P481)
- binding flavin-adenine dinucleotide: G12 (= G24), G14 (= G26), P15 (= P27), A16 (≠ G28), E35 (= E47), R36 (≠ K48), Y37 (≠ H49), V43 (= V55), C44 (= C56), G48 (= G60), C49 (= C61), K53 (= K65), L115 (≠ W127), G116 (= G128), A144 (≠ C156), G145 (= G157), I185 (= I197), G311 (= G324), D312 (= D325), M318 (= M331), L319 (= L332), A320 (= A333), H321 (= H334)
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)
60% identity, 98% coverage: 13:484/484 of query aligns to 2:472/474 of P0A9P0
- K220 (≠ R231) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1bhyA Low temperature middle resolution structure of p64k from masc data (see paper)
57% identity, 98% coverage: 12:484/484 of query aligns to 1:482/482 of 1bhyA
- active site: L41 (= L52), C45 (= C56), C50 (= C61), S53 (= S64), I195 (= I196), E199 (= E200), H454 (= H455), H456 (= H457), E461 (= E462), P479 (= P481), Q480 (≠ K482)
- binding flavin-adenine dinucleotide: L12 (= L23), P16 (= P27), G17 (= G28), E36 (= E47), R37 (≠ K48), Y38 (≠ H49), G43 (= G54), V44 (= V55), C45 (= C56), G49 (= G60), C50 (= C61), K54 (= K65), D116 (≠ W127), G117 (= G128), Y135 (vs. gap), A156 (≠ C156), G157 (= G157), D324 (= D325), L331 (= L332), A332 (= A333)
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: 12:474/484 of query aligns to 4:463/470 of P11959
- 39:47 (vs. 47:56, 80% identical) binding FAD
- K56 (= K65) binding FAD
- D314 (= D325) binding FAD
- A322 (= A333) binding FAD
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
45% identity, 94% coverage: 16:471/484 of query aligns to 2:454/455 of 1ebdA
- active site: P13 (= P27), L37 (= L52), C41 (= C56), C46 (= C61), S49 (= S64), N74 (≠ K89), V75 (≠ P90), Y180 (≠ I196), E184 (= E200), S320 (≠ T337), H438 (= H455), H440 (= H457), E445 (= E462)
- binding flavin-adenine dinucleotide: G10 (= G24), G12 (= G26), P13 (= P27), V32 (≠ I46), E33 (= E47), K34 (= K48), G39 (= G54), V40 (= V55), C41 (= C56), G45 (= G60), C46 (= C61), K50 (= K65), E112 (≠ W127), A113 (≠ G128), T141 (≠ C156), G142 (= G157), Y180 (≠ I196), I181 (= I197), R268 (= R285), D308 (= D325), A314 (≠ M331), L315 (= L332), A316 (= A333)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
44% identity, 94% coverage: 17:473/484 of query aligns to 6:464/470 of 6uziC
- active site: C45 (= C56), C50 (= C61), S53 (= S64), V187 (≠ I196), E191 (= E200), H448 (= H457), E453 (= E462)
- binding flavin-adenine dinucleotide: I12 (≠ L23), G13 (= G24), G15 (= G26), P16 (= P27), G17 (= G28), E36 (= E47), K37 (= K48), G43 (= G54), T44 (≠ V55), C45 (= C56), G49 (= G60), C50 (= C61), S53 (= S64), K54 (= K65), V117 (≠ W127), G118 (= G128), T147 (≠ C156), G148 (= G157), I188 (= I197), R276 (= R285), D316 (= D325), M322 (= M331), L323 (= L332), A324 (= A333)
- binding zinc ion: H448 (= H457), E453 (= E462)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
43% identity, 92% coverage: 19:464/484 of query aligns to 2:452/465 of 3urhB
- active site: Y35 (≠ L52), C39 (= C56), C44 (= C61), S47 (= S64), V183 (≠ I196), E187 (= E200), H443 (= H455), H445 (= H457), E450 (= E462)
- binding flavin-adenine dinucleotide: I6 (≠ L23), G7 (= G24), G9 (= G26), P10 (= P27), G11 (= G28), E30 (= E47), K31 (= K48), G37 (= G54), T38 (≠ V55), C39 (= C56), G43 (= G60), C44 (= C61), K48 (= K65), T111 (≠ W127), G112 (= G128), A140 (= A155), T141 (≠ C156), G142 (= G157), I184 (= I197), R273 (= R285), G312 (= G324), D313 (= D325), M319 (= M331), L320 (= L332), A321 (= A333), H322 (= H334)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
44% identity, 96% coverage: 19:484/484 of query aligns to 6:478/478 of P14218
- 34:49 (vs. 47:56, 38% identical) binding FAD
- C49 (= C56) modified: Disulfide link with 54, Redox-active
- C54 (= C61) modified: Disulfide link with 49, Redox-active
- K58 (= K65) binding FAD
- G122 (= G128) binding FAD
- D319 (= D325) binding FAD
- A327 (= A333) binding FAD
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
45% identity, 92% coverage: 19:464/484 of query aligns to 8:460/477 of 5u8uD
- active site: P16 (= P27), L47 (= L52), C51 (= C56), C56 (= C61), S59 (= S64), G85 (≠ K89), V86 (≠ P90), V193 (≠ I196), E197 (= E200), S333 (≠ T337), F451 (≠ H455), H453 (= H457), E458 (= E462)
- binding flavin-adenine dinucleotide: I12 (≠ L23), G15 (= G26), P16 (= P27), G17 (= G28), E36 (= E47), K37 (= K48), G49 (= G54), T50 (≠ V55), C51 (= C56), G55 (= G60), C56 (= C61), K60 (= K65), H123 (≠ W127), G124 (= G128), A152 (= A155), S153 (≠ C156), G154 (= G157), I194 (= I197), R281 (= R285), G320 (= G324), D321 (= D325), M327 (= M331), L328 (= L332), A329 (= A333), H330 (= H334), H453 (= H457), P454 (= P458)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
45% identity, 92% coverage: 19:464/484 of query aligns to 5:457/473 of 5u8wA
- active site: P13 (= P27), L44 (= L52), C48 (= C56), C53 (= C61), S56 (= S64), G82 (≠ K89), V83 (≠ P90), V190 (≠ I196), E194 (= E200), S330 (≠ T337), F448 (≠ H455), H450 (= H457), E455 (= E462)
- binding flavin-adenine dinucleotide: I9 (≠ L23), G12 (= G26), P13 (= P27), G14 (= G28), E33 (= E47), K34 (= K48), G46 (= G54), T47 (≠ V55), C48 (= C56), G52 (= G60), C53 (= C61), K57 (= K65), H120 (≠ W127), G121 (= G128), A149 (= A155), S150 (≠ C156), G151 (= G157), S170 (= S176), G317 (= G324), D318 (= D325), M324 (= M331), L325 (= L332), A326 (= A333), H327 (= H334), Y357 (= Y364), H450 (= H457), P451 (= P458)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (≠ V192), G189 (= G195), V190 (≠ I196), I191 (= I197), E194 (= E200), E210 (= E216), A211 (≠ L217), L212 (≠ Q218), A275 (= A282), V276 (= V283), G277 (= G284), R278 (= R285), M324 (= M331), L325 (= L332), V355 (= V362), Y357 (= Y364)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
45% identity, 92% coverage: 19:464/484 of query aligns to 4:456/472 of 5u8vA
- active site: P12 (= P27), L43 (= L52), C47 (= C56), C52 (= C61), S55 (= S64), G81 (≠ K89), V82 (≠ P90), V189 (≠ I196), E193 (= E200), S329 (≠ T337), F447 (≠ H455), H449 (= H457), E454 (= E462)
- binding flavin-adenine dinucleotide: I8 (≠ L23), G11 (= G26), P12 (= P27), G13 (= G28), E32 (= E47), G45 (= G54), T46 (≠ V55), C47 (= C56), G51 (= G60), C52 (= C61), K56 (= K65), H119 (≠ W127), G120 (= G128), A148 (= A155), S149 (≠ C156), G150 (= G157), S169 (= S176), I190 (= I197), R277 (= R285), G316 (= G324), D317 (= D325), M323 (= M331), L324 (= L332), A325 (= A333), H326 (= H334), H449 (= H457), P450 (= P458)
- binding nicotinamide-adenine-dinucleotide: I185 (≠ V192), G186 (= G193), G188 (= G195), V189 (≠ I196), I190 (= I197), L208 (≠ V215), E209 (= E216), A210 (≠ L217), V243 (= V250), V275 (= V283), G276 (= G284)
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)
43% identity, 96% coverage: 19:483/484 of query aligns to 6:477/477 of P18925
- 34:49 (vs. 47:56, 38% identical) binding FAD
- C49 (= C56) modified: Disulfide link with 54, Redox-active
- C54 (= C61) modified: Disulfide link with 49, Redox-active
- K58 (= K65) binding FAD
- D319 (= D325) binding FAD
- A327 (= A333) 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)
44% identity, 92% coverage: 19:464/484 of query aligns to 5:457/472 of 3ladA
- active site: L44 (= L52), C48 (= C56), C53 (= C61), S56 (= S64), V190 (≠ I196), E194 (= E200), F448 (≠ H455), H450 (= H457), E455 (= E462)
- binding flavin-adenine dinucleotide: I9 (≠ L23), G10 (= G24), G12 (= G26), P13 (= P27), E33 (= E47), K34 (= K48), G46 (= G54), T47 (≠ V55), C48 (= C56), G52 (= G60), C53 (= C61), H120 (≠ W127), G121 (= G128), A149 (= A155), S150 (≠ C156), G151 (= G157), I191 (= I197), R278 (= R285), D318 (= D325), L325 (= L332), A326 (= A333)
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
44% identity, 93% coverage: 17:464/484 of query aligns to 3:453/467 of 1dxlA
- active site: L38 (= L52), C42 (= C56), C47 (= C61), S50 (= S64), Y184 (≠ I196), E188 (= E200), H444 (= H455), H446 (= H457), E451 (= E462)
- binding flavin-adenine dinucleotide: I9 (≠ L23), P13 (= P27), G14 (= G28), E33 (= E47), K34 (= K48), R35 (≠ H49), G40 (= G54), T41 (≠ V55), C42 (= C56), G46 (= G60), C47 (= C61), K51 (= K65), Y114 (≠ W127), G115 (= G128), T144 (≠ C156), G145 (= G157), Y184 (≠ I196), I185 (= I197), R274 (= R285), D314 (= D325), M320 (= M331), L321 (= L332), A322 (= A333), H323 (= H334)
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)
44% identity, 93% coverage: 17:464/484 of query aligns to 37:487/501 of P31023
- 67:76 (vs. 47:56, 60% identical) binding FAD
- C76 (= C56) modified: Disulfide link with 81, Redox-active
- C81 (= C61) modified: Disulfide link with 76, Redox-active
- G149 (= G128) binding FAD
- D348 (= D325) binding FAD
- MLAH 354:357 (= MLAH 331:334) binding FAD
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
43% identity, 92% coverage: 19:464/484 of query aligns to 6:458/475 of 6awaA
- active site: L45 (= L52), C49 (= C56), C54 (= C61), S57 (= S64), V191 (≠ I196), E195 (= E200), F449 (≠ H455), H451 (= H457), E456 (= E462)
- binding adenosine monophosphate: I187 (≠ V192), E211 (= E216), A212 (≠ L217), L213 (≠ Q218), V245 (= V250), V277 (= V283)
- binding flavin-adenine dinucleotide: I10 (≠ L23), G13 (= G26), P14 (= P27), G15 (= G28), E34 (= E47), K35 (= K48), T48 (≠ V55), C49 (= C56), G53 (= G60), C54 (= C61), K58 (= K65), H121 (≠ W127), G122 (= G128), S151 (≠ C156), G152 (= G157), I192 (= I197), R279 (= R285), G318 (= G324), D319 (= D325), M325 (= M331), L326 (= L332), A327 (= A333), Y358 (= Y364)
Sites not aligning to the query:
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
43% identity, 92% coverage: 16:462/484 of query aligns to 3:455/472 of 1zmdA
- active site: L39 (= L52), C43 (= C56), C48 (= C61), S51 (= S64), V186 (≠ I196), E190 (= E200), H448 (= H455), H450 (= H457), E455 (= E462)
- binding flavin-adenine dinucleotide: I10 (≠ L23), G11 (= G24), G13 (= G26), P14 (= P27), G15 (= G28), E34 (= E47), K35 (= K48), N36 (≠ H49), G41 (= G54), T42 (≠ V55), C43 (= C56), G47 (= G60), C48 (= C61), K52 (= K65), Y116 (≠ W127), G117 (= G128), T146 (≠ C156), G147 (= G157), S166 (= S176), R278 (= R285), F281 (≠ N288), G317 (= G324), D318 (= D325), M324 (= M331), L325 (= L332), A326 (= A333), H327 (= H334)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (≠ V192), G183 (= G193), G185 (= G195), V186 (≠ I196), I187 (= I197), E190 (= E200), E206 (= E216), F207 (≠ L217), L208 (≠ Q218), I276 (≠ V283), G277 (= G284), R278 (= R285), M324 (= M331), L325 (= L332), V355 (= V362), Y357 (= Y364)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
43% identity, 92% coverage: 16:462/484 of query aligns to 3:455/472 of 1zmcA
- active site: L39 (= L52), C43 (= C56), C48 (= C61), S51 (= S64), V186 (≠ I196), E190 (= E200), H448 (= H455), H450 (= H457), E455 (= E462)
- binding flavin-adenine dinucleotide: I10 (≠ L23), G11 (= G24), G13 (= G26), P14 (= P27), G15 (= G28), E34 (= E47), K35 (= K48), N36 (≠ H49), G41 (= G54), T42 (≠ V55), C43 (= C56), G47 (= G60), C48 (= C61), K52 (= K65), Y116 (≠ W127), G117 (= G128), T146 (≠ C156), G147 (= G157), S166 (= S176), I187 (= I197), F281 (≠ N288), G317 (= G324), D318 (= D325), M324 (= M331), L325 (= L332), A326 (= A333), H327 (= H334)
- binding nicotinamide-adenine-dinucleotide: G183 (= G193), G185 (= G195), V205 (= V215), E206 (= E216), F207 (≠ L217), L208 (≠ Q218), K240 (= K249), V241 (= V250), I276 (≠ V283), G277 (= G284), R278 (= R285), R297 (= R304), M324 (= M331)
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, 93% coverage: 16:464/484 of query aligns to 40:494/509 of P09622
- 71:80 (vs. 47:56, 60% identical) binding FAD
- K72 (= K48) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K65) binding FAD; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ A78) to T: in dbSNP:rs1130477
- G154 (= G128) binding FAD
- TGS 183:185 (≠ CGS 156:158) binding FAD
- 220:227 (vs. 193:200, 63% identical) binding NAD(+)
- E243 (= E216) binding NAD(+)
- V278 (= V250) binding NAD(+)
- G314 (= G284) binding NAD(+)
- D355 (= D325) binding FAD
- MLAH 361:364 (= MLAH 331:334) binding FAD
- E375 (= E345) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ L353) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ R418) 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 (= E436) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ M443) 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 (= D449) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ L452) 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 (= H455) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P458) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (= S461) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E462) 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.
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
43% identity, 92% coverage: 16:462/484 of query aligns to 13:465/482 of 6hg8B
- active site: C53 (= C56), C58 (= C61), S61 (= S64), V196 (≠ I196), E200 (= E200), H460 (= H457), E465 (= E462)
- binding flavin-adenine dinucleotide: I20 (≠ L23), G23 (= G26), P24 (= P27), G25 (= G28), E44 (= E47), K45 (= K48), N46 (≠ H49), G51 (= G54), T52 (≠ V55), C53 (= C56), G57 (= G60), C58 (= C61), K62 (= K65), Y126 (≠ W127), G127 (= G128), T156 (≠ C156), G157 (= G157), I197 (= I197), R288 (= R285), F291 (≠ N288), G327 (= G324), D328 (= D325), M334 (= M331), L335 (= L332), A336 (= A333), H337 (= H334)
Query Sequence
>WP_051301765.1 NCBI__GCF_000428045.1:WP_051301765.1
MKNDSGSNSAQGAVDIQAEVVVLGAGPGGYTAAFRAADLGKKVVLIEKHSNLGGVCLNVG
CIPSKALLHSAAVINEAAEIEHMGISFGKPKIDLDKMRAGKEKVVSRLTQGLAALAKQRK
VEVVNGWGQFDSPNRISVDTEKGKVTIGFDNAIIACGSRPVAIPGFPNDDPRLINSTGAL
ELEDIPKKMLVVGGGIIGLEMGTVYATLGSQIDVVELQSSLIPGCDTDLVRPLQKRLKDQ
FNSIMLDTKVTEIKAQKGGLKVSFEGKNAPEKALVYDKVLVAVGRVPNGKLIGADLAGVK
VDERGFIAVDQHMRTNVSNIYAIGDVVGNPMLAHKATHEAKVAAEVIAGHHALFDPLAIP
SVAYTNPEVAWMGLTETEAKAQGIAYEKAAFPWAASGRALGIGREEGLTKLLFDPKTRRI
LGAGIVGVNAGELIGETVLALEMGADAEDIGLTIHPHPTLSETICFSAEMAEGSITDLMP
PKKK
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