SitesBLAST
Comparing WP_005454512.1 NCBI__GCF_000244975.1:WP_005454512.1 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)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
39% identity, 99% coverage: 5:455/457 of query aligns to 9:467/470 of P11959
- 39:47 (vs. 35:43, 67% identical) binding FAD
- K56 (= K52) binding FAD
- D314 (= D302) binding FAD
- A322 (= A310) binding FAD
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: 5:455/457 of query aligns to 37:501/501 of P31023
- 67:76 (vs. 35:43, 70% identical) binding FAD
- C76 (= C43) modified: Disulfide link with 81, Redox-active
- C81 (= C48) modified: Disulfide link with 76, Redox-active
- G149 (= G115) binding FAD
- D348 (= D302) binding FAD
- MLAH 354:357 (≠ QLAH 308:311) binding FAD
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: 5:455/457 of query aligns to 3:467/467 of 1dxlA
- active site: L38 (= L39), C42 (= C43), C47 (= C48), S50 (≠ T51), Y184 (≠ V178), E188 (= E182), H444 (= H432), H446 (= H434), E451 (= E439)
- binding flavin-adenine dinucleotide: I9 (≠ L11), P13 (≠ S15), G14 (= G16), E33 (= E35), K34 (= K36), R35 (≠ D37), G40 (= G41), T41 (= T42), C42 (= C43), G46 (= G47), C47 (= C48), K51 (= K52), Y114 (≠ T114), G115 (= G115), T144 (= T139), G145 (= G140), Y184 (≠ V178), I185 (= I179), R274 (= R263), D314 (= D302), M320 (≠ Q308), L321 (= L309), A322 (= A310), H323 (= H311)
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
40% identity, 97% coverage: 5:448/457 of query aligns to 3:455/455 of 1ebdA
- active site: P13 (≠ S15), L37 (= L39), C41 (= C43), C46 (= C48), S49 (≠ T51), N74 (≠ F76), V75 (≠ E77), Y180 (≠ V178), E184 (= E182), S320 (≠ F314), H438 (= H432), H440 (= H434), E445 (= E439)
- binding flavin-adenine dinucleotide: G10 (= G12), G12 (= G14), P13 (≠ S15), V32 (≠ I34), E33 (= E35), K34 (= K36), G39 (= G41), V40 (≠ T42), C41 (= C43), G45 (= G47), C46 (= C48), K50 (= K52), E112 (≠ T114), A113 (≠ G115), T141 (= T139), G142 (= G140), Y180 (≠ V178), I181 (= I179), R268 (= R263), D308 (= D302), A314 (≠ Q308), L315 (= L309), A316 (= A310)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
39% identity, 97% coverage: 7:451/457 of query aligns to 8:465/470 of 6uziC
- active site: C45 (= C43), C50 (= C48), S53 (≠ T51), V187 (= V178), E191 (= E182), H448 (= H434), E453 (= E439)
- binding flavin-adenine dinucleotide: I12 (≠ L11), G13 (= G12), G15 (= G14), P16 (≠ S15), G17 (= G16), E36 (= E35), K37 (= K36), G43 (= G41), T44 (= T42), C45 (= C43), G49 (= G47), C50 (= C48), S53 (≠ T51), K54 (= K52), V117 (≠ T114), G118 (= G115), T147 (= T139), G148 (= G140), I188 (= I179), R276 (= R263), D316 (= D302), M322 (≠ Q308), L323 (= L309), A324 (= A310)
- binding zinc ion: H448 (= H434), E453 (= E439)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
40% identity, 98% coverage: 7:455/457 of query aligns to 3:455/455 of 2yquB
- active site: P11 (≠ S15), L36 (= L39), C40 (= C43), C45 (= C48), S48 (≠ T51), G72 (≠ F76), V73 (≠ E77), V177 (= V178), E181 (= E182), S314 (≠ F314), H432 (= H432), H434 (= H434), E439 (= E439)
- binding carbonate ion: A310 (= A310), S314 (≠ F314), S423 (≠ F423), D426 (= D426)
- binding flavin-adenine dinucleotide: G8 (= G12), G10 (= G14), P11 (≠ S15), G12 (= G16), E31 (= E35), K32 (= K36), G38 (= G41), T39 (= T42), C40 (= C43), R42 (≠ H45), G44 (= G47), C45 (= C48), K49 (= K52), T110 (= T114), A111 (≠ G115), T137 (= T139), G138 (= G140), I178 (= I179), Y265 (≠ N266), G301 (= G301), D302 (= D302), M308 (≠ Q308), L309 (= L309), A310 (= A310), H311 (= H311)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
40% identity, 98% coverage: 7:455/457 of query aligns to 3:455/455 of 2yquA
- active site: P11 (≠ S15), L36 (= L39), C40 (= C43), C45 (= C48), S48 (≠ T51), G72 (≠ F76), V73 (≠ E77), V177 (= V178), E181 (= E182), S314 (≠ F314), H432 (= H432), H434 (= H434), E439 (= E439)
- binding flavin-adenine dinucleotide: G8 (= G12), G10 (= G14), P11 (≠ S15), G12 (= G16), E31 (= E35), K32 (= K36), G38 (= G41), T39 (= T42), C40 (= C43), R42 (≠ H45), G44 (= G47), C45 (= C48), K49 (= K52), T110 (= T114), A111 (≠ G115), T137 (= T139), G138 (= G140), S157 (= S158), I178 (= I179), Y265 (≠ N266), G301 (= G301), D302 (= D302), M308 (≠ Q308), L309 (= L309), A310 (= A310)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
40% identity, 98% coverage: 7:452/457 of query aligns to 3:452/452 of 2eq7A
- active site: P11 (≠ S15), L36 (= L39), C40 (= C43), C45 (= C48), S48 (≠ T51), G72 (≠ F76), V73 (≠ E77), V177 (= V178), E181 (= E182), S314 (≠ F314), H432 (= H432), H434 (= H434), E439 (= E439)
- binding flavin-adenine dinucleotide: G10 (= G14), P11 (≠ S15), G12 (= G16), E31 (= E35), K32 (= K36), G38 (= G41), T39 (= T42), C40 (= C43), R42 (≠ H45), G44 (= G47), C45 (= C48), K49 (= K52), T110 (= T114), A111 (≠ G115), T137 (= T139), G138 (= G140), S157 (= S158), I178 (= I179), R262 (= R263), Y265 (≠ N266), D302 (= D302), M308 (≠ Q308), L309 (= L309), A310 (= A310), H311 (= H311), Y341 (= Y342)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ D148), G174 (= G175), G176 (= G177), V177 (= V178), I178 (= I179), E197 (= E198), Y198 (≠ A199), V231 (≠ F232), V260 (= V261), G261 (= G262), R262 (= R263), M308 (≠ Q308), L309 (= L309), V339 (= V340)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
40% identity, 98% coverage: 7:454/457 of query aligns to 2:465/465 of 3urhB
- active site: Y35 (≠ L39), C39 (= C43), C44 (= C48), S47 (≠ T51), V183 (= V178), E187 (= E182), H443 (= H432), H445 (= H434), E450 (= E439)
- binding flavin-adenine dinucleotide: I6 (≠ L11), G7 (= G12), G9 (= G14), P10 (≠ S15), G11 (= G16), E30 (= E35), K31 (= K36), G37 (= G41), T38 (= T42), C39 (= C43), G43 (= G47), C44 (= C48), K48 (= K52), T111 (= T114), G112 (= G115), A140 (= A138), T141 (= T139), G142 (= G140), I184 (= I179), R273 (= R263), G312 (= G301), D313 (= D302), M319 (≠ Q308), L320 (= L309), A321 (= A310), H322 (= H311)
6aonA 1.72 angstrom resolution crystal structure of 2-oxoglutarate dehydrogenase complex subunit dihydrolipoamide dehydrogenase from bordetella pertussis in complex with fad
38% identity, 98% coverage: 7:454/457 of query aligns to 4:472/473 of 6aonA
- active site: P43 (vs. gap), C47 (= C43), C52 (= C48), S55 (≠ T51), V191 (= V178), E195 (= E182), H450 (= H432), H452 (= H434), E457 (= E439)
- binding calcium ion: A218 (≠ P205), A220 (≠ E207), Q222 (≠ E209)
- binding flavin-adenine dinucleotide: I8 (≠ L11), G11 (= G14), P12 (≠ S15), G13 (= G16), D32 (≠ E35), A33 (≠ K36), W34 (≠ D37), G45 (= G41), T46 (= T42), C47 (= C43), G51 (= G47), C52 (= C48), K56 (= K52), K119 (≠ T114), G120 (= G115), T151 (= T139), G152 (= G140), N171 (≠ S158), I192 (= I179), R280 (= R263), Y283 (≠ N266), G319 (= G301), D320 (= D302), M326 (≠ Q308), L327 (= L309), A328 (= A310), H329 (= H311)
4jdrA Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli (see paper)
39% identity, 97% coverage: 2:444/457 of query aligns to 2:454/471 of 4jdrA
- active site: P15 (≠ S15), L40 (= L39), C44 (= C43), C49 (= C48), S52 (≠ T51), E77 (≠ F76), P78 (≠ E77), I184 (≠ V178), E188 (= E182), V324 (≠ F314), H442 (= H432), H444 (= H434), E449 (= E439)
- binding flavin-adenine dinucleotide: G12 (= G12), G14 (= G14), P15 (≠ S15), A16 (≠ G16), E35 (= E35), R36 (≠ K36), Y37 (vs. gap), V43 (≠ T42), C44 (= C43), G48 (= G47), C49 (= C48), K53 (= K52), L115 (≠ T114), G116 (= G115), A144 (≠ T139), G145 (= G140), I185 (= I179), G311 (= G301), D312 (= D302), M318 (≠ Q308), L319 (= L309), A320 (= A310), H321 (= H311)
Sites not aligning to the query:
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)
39% identity, 97% coverage: 2:444/457 of query aligns to 3:455/474 of P0A9P0
- K220 (= K213) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
39% identity, 98% coverage: 5:454/457 of query aligns to 14:481/482 of 6hg8B
- active site: C53 (= C43), C58 (= C48), S61 (≠ T51), V196 (= V178), E200 (= E182), H460 (= H434), E465 (= E439)
- binding flavin-adenine dinucleotide: I20 (≠ L11), G23 (= G14), P24 (≠ S15), G25 (= G16), E44 (= E35), K45 (= K36), N46 (≠ D37), G51 (= G41), T52 (= T42), C53 (= C43), G57 (= G47), C58 (= C48), K62 (= K52), Y126 (≠ T114), G127 (= G115), T156 (= T139), G157 (= G140), I197 (= I179), R288 (= R263), F291 (≠ N266), G327 (= G301), D328 (= D302), M334 (≠ Q308), L335 (= L309), A336 (= A310), H337 (= H311)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
39% identity, 97% coverage: 5:447/457 of query aligns to 41:500/509 of P09622
- 71:80 (vs. 35:43, 70% 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 (= G115) binding FAD
- TGS 183:185 (= TGS 139:141) binding FAD
- 220:227 (vs. 175:182, 88% identical) binding NAD(+)
- E243 (= E198) binding NAD(+)
- V278 (≠ F232) binding NAD(+)
- G314 (= G262) binding NAD(+)
- D355 (= D302) binding FAD
- MLAH 361:364 (≠ QLAH 308:311) binding FAD
- E375 (= E322) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ P331) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (= D394) 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 (= E413) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ W420) 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 (= D426) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ P429) 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 (= H432) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P435) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (≠ T438) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E439) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ G442) to G: in DLDD; loss of enzyme activity; reduced interaction with PDHX; dbSNP:rs121964989
Sites not aligning to the query:
- 505 K→M: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
38% identity, 98% coverage: 7:455/457 of query aligns to 5:458/460 of 2eq6A
- active site: V37 (≠ L39), C41 (= C43), C46 (= C48), T49 (= T51), A176 (≠ V178), E180 (= E182), H435 (= H432), H437 (= H434), E442 (= E439)
- binding flavin-adenine dinucleotide: I9 (≠ L11), G10 (= G12), G12 (= G14), P13 (≠ S15), G14 (= G16), E33 (= E35), A34 (≠ K36), G39 (= G41), V40 (≠ T42), C41 (= C43), G45 (= G47), C46 (= C48), K50 (= K52), F111 (≠ T114), A112 (≠ G115), A135 (= A138), T136 (= T139), G137 (= G140), S155 (= S158), R269 (≠ N266), D306 (= D302), L312 (≠ Q308), L313 (= L309), A314 (= A310), H315 (= H311), Y344 (= Y342)
Sites not aligning to the query:
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
38% identity, 98% coverage: 5:454/457 of query aligns to 4:471/472 of 1zmdA
- active site: L39 (= L39), C43 (= C43), C48 (= C48), S51 (≠ T51), V186 (= V178), E190 (= E182), H448 (= H432), H450 (= H434), E455 (= E439)
- binding flavin-adenine dinucleotide: I10 (≠ L11), G11 (= G12), G13 (= G14), P14 (≠ S15), G15 (= G16), E34 (= E35), K35 (= K36), N36 (≠ D37), G41 (= G41), T42 (= T42), C43 (= C43), G47 (= G47), C48 (= C48), K52 (= K52), Y116 (≠ T114), G117 (= G115), T146 (= T139), G147 (= G140), S166 (= S158), R278 (= R263), F281 (≠ N266), G317 (= G301), D318 (= D302), M324 (≠ Q308), L325 (= L309), A326 (= A310), H327 (= H311)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (≠ L174), G183 (= G175), G185 (= G177), V186 (= V178), I187 (= I179), E190 (= E182), E206 (= E198), F207 (≠ A199), L208 (= L200), I276 (≠ V261), G277 (= G262), R278 (= R263), M324 (≠ Q308), L325 (= L309), V355 (= V340), Y357 (= Y342)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
38% identity, 98% coverage: 5:454/457 of query aligns to 4:471/472 of 1zmcA
- active site: L39 (= L39), C43 (= C43), C48 (= C48), S51 (≠ T51), V186 (= V178), E190 (= E182), H448 (= H432), H450 (= H434), E455 (= E439)
- binding flavin-adenine dinucleotide: I10 (≠ L11), G11 (= G12), G13 (= G14), P14 (≠ S15), G15 (= G16), E34 (= E35), K35 (= K36), N36 (≠ D37), G41 (= G41), T42 (= T42), C43 (= C43), G47 (= G47), C48 (= C48), K52 (= K52), Y116 (≠ T114), G117 (= G115), T146 (= T139), G147 (= G140), S166 (= S158), I187 (= I179), F281 (≠ N266), G317 (= G301), D318 (= D302), M324 (≠ Q308), L325 (= L309), A326 (= A310), H327 (= H311)
- binding nicotinamide-adenine-dinucleotide: G183 (= G175), G185 (= G177), V205 (= V197), E206 (= E198), F207 (≠ A199), L208 (= L200), K240 (= K231), V241 (≠ F232), I276 (≠ V261), G277 (= G262), R278 (= R263), R297 (= R281), M324 (≠ Q308)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
37% identity, 98% coverage: 7:455/457 of query aligns to 6:472/478 of P14218
- 34:49 (vs. 35:43, 44% 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 (= G115) binding FAD
- D319 (= D302) binding FAD
- A327 (= A310) binding FAD
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
37% identity, 98% coverage: 7:455/457 of query aligns to 5:471/472 of 3ladA
- active site: L44 (= L39), C48 (= C43), C53 (= C48), S56 (≠ T51), V190 (= V178), E194 (= E182), F448 (≠ H432), H450 (= H434), E455 (= E439)
- binding flavin-adenine dinucleotide: I9 (≠ L11), G10 (= G12), G12 (= G14), P13 (≠ S15), E33 (= E35), K34 (= K36), G46 (= G41), T47 (= T42), C48 (= C43), G52 (= G47), C53 (= C48), H120 (≠ T114), G121 (= G115), A149 (= A138), S150 (≠ T139), G151 (= G140), I191 (= I179), R278 (= R263), D318 (= D302), L325 (= L309), A326 (= A310)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
37% identity, 98% coverage: 7:455/457 of query aligns to 6:472/477 of P18925
- 34:49 (vs. 35:43, 50% 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 (= D302) binding FAD
- A327 (= A310) binding FAD
Query Sequence
>WP_005454512.1 NCBI__GCF_000244975.1:WP_005454512.1
MTDAEADLVILGGGSGGYAAAFRAAELGLSVTLIEKDKLGGTCLHRGCIPTKALLHAAEV
ADSARDGEQFGVKTTFEGVDIAGVHKYKDSVITRLYKGLQGLAKANKVNYVEGTGTFVGG
TTVDVEGTRYTGKNLVLATGSYSKTLPDLELGGRIITSDDALTLDFVPKKAVVLGGGVIG
VEFASVWASFGTEVTIVEALPRLVPAEDEFSSKQLERAFRRRKIAFKTGVKFTGAKQDAG
GVTVSLESGETLEADVLLVAVGRGPNTAGHGYDEAGLRMDRGFVLTDERLRTNLPGVYAV
GDIVPGLQLAHRGFQQGIFVAEDIAGLDPKPIDESGIPRVTYSHPEVASVGLTEAQAKEK
YGPDITTFTYDLAGNGKSQILKTSGAVKLIKAPDGPVVGLHLVGDRVGELIGEAQLIYNW
EAFPEDVAPLIHAHPTQTEALGEAHLALAGKPLHVHG
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