SitesBLAST
Comparing WP_083509555.1 NCBI__GCF_001541235.1:WP_083509555.1 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)
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)
59% identity, 99% coverage: 4:476/476 of query aligns to 2:474/474 of P0A9P0
- K220 (≠ A222) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4jdrA Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli (see paper)
59% identity, 99% coverage: 4:474/476 of query aligns to 1:471/471 of 4jdrA
- active site: P15 (= P18), L40 (= L43), C44 (= C47), C49 (= C52), S52 (= S55), E77 (≠ R80), P78 (= P81), I184 (= I187), E188 (= E191), V324 (= V327), H442 (= H445), H444 (= H447), E449 (= E452), N467 (≠ A470), P468 (≠ R471)
- binding flavin-adenine dinucleotide: G12 (= G15), G14 (= G17), P15 (= P18), A16 (≠ G19), E35 (= E38), R36 (= R39), Y37 (≠ G40), V43 (= V46), C44 (= C47), G48 (= G51), C49 (= C52), K53 (= K56), L115 (≠ F118), G116 (= G119), A144 (= A147), G145 (= G148), I185 (= I188), G311 (= G314), D312 (= D315), M318 (= M321), L319 (= L322), A320 (= A323), H321 (= H324)
1bhyA Low temperature middle resolution structure of p64k from masc data (see paper)
58% identity, 98% coverage: 4:468/476 of query aligns to 2:477/482 of 1bhyA
- active site: L41 (= L43), C45 (= C47), C50 (= C52), S53 (= S55), I195 (= I187), E199 (= E191), H454 (= H445), H456 (= H447), E461 (= E452)
- binding flavin-adenine dinucleotide: L12 (= L14), P16 (= P18), G17 (= G19), E36 (= E38), R37 (= R39), Y38 (≠ G40), G43 (= G45), V44 (= V46), C45 (= C47), G49 (= G51), C50 (= C52), K54 (= K56), D116 (≠ F118), G117 (= G119), Y135 (≠ H131), A156 (= A147), G157 (= G148), D324 (= D315), L331 (= L322), A332 (= A323)
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)
44% identity, 98% coverage: 7:471/476 of query aligns to 8:470/470 of P11959
- 39:47 (vs. 38:47, 70% identical) binding FAD
- K56 (= K56) binding FAD
- D314 (= D315) binding FAD
- A322 (= A323) binding FAD
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
45% identity, 95% coverage: 7:460/476 of query aligns to 2:453/455 of 1ebdA
- active site: P13 (= P18), L37 (= L43), C41 (= C47), C46 (= C52), S49 (= S55), N74 (≠ R80), V75 (≠ P81), Y180 (≠ I187), E184 (= E191), S320 (≠ V327), H438 (= H445), H440 (= H447), E445 (= E452)
- binding flavin-adenine dinucleotide: G10 (= G15), G12 (= G17), P13 (= P18), V32 (= V37), E33 (= E38), K34 (≠ R39), G39 (= G45), V40 (= V46), C41 (= C47), G45 (= G51), C46 (= C52), K50 (= K56), E112 (≠ F118), A113 (≠ G119), T141 (≠ A147), G142 (= G148), Y180 (≠ I187), I181 (= I188), R268 (= R275), D308 (= D315), A314 (≠ M321), L315 (= L322), A316 (= A323)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
43% identity, 98% coverage: 10:474/476 of query aligns to 6:478/478 of P14218
- 34:49 (vs. 38:47, 38% identical) binding FAD
- C49 (= C47) modified: Disulfide link with 54, Redox-active
- C54 (= C52) modified: Disulfide link with 49, Redox-active
- K58 (= K56) binding FAD
- G122 (= G119) binding FAD
- D319 (= D315) binding FAD
- A327 (= A323) binding FAD
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
44% identity, 95% coverage: 10:463/476 of query aligns to 4:465/472 of 5u8vA
- active site: P12 (= P18), L43 (= L43), C47 (= C47), C52 (= C52), S55 (= S55), G81 (≠ R80), V82 (≠ P81), V189 (≠ I187), E193 (= E191), S329 (≠ V327), F447 (≠ H445), H449 (= H447), E454 (= E452)
- binding flavin-adenine dinucleotide: I8 (≠ L14), G11 (= G17), P12 (= P18), G13 (= G19), E32 (= E38), G45 (= G45), T46 (≠ V46), C47 (= C47), G51 (= G51), C52 (= C52), K56 (= K56), H119 (≠ F118), G120 (= G119), A148 (= A146), S149 (≠ A147), G150 (= G148), S169 (= S167), I190 (= I188), R277 (= R275), G316 (= G314), D317 (= D315), M323 (= M321), L324 (= L322), A325 (= A323), H326 (= H324), H449 (= H447), P450 (= P448)
- binding nicotinamide-adenine-dinucleotide: I185 (≠ V183), G186 (= G184), G188 (= G186), V189 (≠ I187), I190 (= I188), L208 (≠ V206), E209 (= E207), A210 (= A208), V243 (= V241), V275 (= V273), G276 (= G274)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
44% identity, 95% coverage: 10:463/476 of query aligns to 5:466/473 of 5u8wA
- active site: P13 (= P18), L44 (= L43), C48 (= C47), C53 (= C52), S56 (= S55), G82 (≠ R80), V83 (≠ P81), V190 (≠ I187), E194 (= E191), S330 (≠ V327), F448 (≠ H445), H450 (= H447), E455 (= E452)
- binding flavin-adenine dinucleotide: I9 (≠ L14), G12 (= G17), P13 (= P18), G14 (= G19), E33 (= E38), K34 (≠ R39), G46 (= G45), T47 (≠ V46), C48 (= C47), G52 (= G51), C53 (= C52), K57 (= K56), H120 (≠ F118), G121 (= G119), A149 (= A146), S150 (≠ A147), G151 (= G148), S170 (= S167), G317 (= G314), D318 (= D315), M324 (= M321), L325 (= L322), A326 (= A323), H327 (= H324), Y357 (= Y354), H450 (= H447), P451 (= P448)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (≠ V183), G189 (= G186), V190 (≠ I187), I191 (= I188), E194 (= E191), E210 (= E207), A211 (= A208), L212 (≠ M209), A275 (= A272), V276 (= V273), G277 (= G274), R278 (= R275), M324 (= M321), L325 (= L322), V355 (= V352), Y357 (= Y354)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
44% identity, 95% coverage: 10:463/476 of query aligns to 8:469/477 of 5u8uD
- active site: P16 (= P18), L47 (= L43), C51 (= C47), C56 (= C52), S59 (= S55), G85 (≠ R80), V86 (≠ P81), V193 (≠ I187), E197 (= E191), S333 (≠ V327), F451 (≠ H445), H453 (= H447), E458 (= E452)
- binding flavin-adenine dinucleotide: I12 (≠ L14), G15 (= G17), P16 (= P18), G17 (= G19), E36 (= E38), K37 (≠ R39), G49 (= G45), T50 (≠ V46), C51 (= C47), G55 (= G51), C56 (= C52), K60 (= K56), H123 (≠ F118), G124 (= G119), A152 (= A146), S153 (≠ A147), G154 (= G148), I194 (= I188), R281 (= R275), G320 (= G314), D321 (= D315), M327 (= M321), L328 (= L322), A329 (= A323), H330 (= H324), H453 (= H447), P454 (= P448)
Sites not aligning to the query:
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
48% identity, 95% coverage: 10:461/476 of query aligns to 5:451/460 of 2eq6A
- active site: V37 (≠ L43), C41 (= C47), C46 (= C52), T49 (≠ S55), A176 (≠ I187), E180 (= E191), H435 (= H445), H437 (= H447), E442 (= E452)
- binding flavin-adenine dinucleotide: I9 (≠ L14), G10 (= G15), G12 (= G17), P13 (= P18), G14 (= G19), E33 (= E38), A34 (≠ R39), G39 (= G45), V40 (= V46), C41 (= C47), G45 (= G51), C46 (= C52), K50 (= K56), F111 (= F118), A112 (≠ G119), A135 (= A146), T136 (≠ A147), G137 (= G148), S155 (= S167), R269 (≠ N278), D306 (= D315), L312 (≠ M321), L313 (= L322), A314 (= A323), H315 (= H324), Y344 (= Y354)
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.
42% identity, 95% coverage: 10:463/476 of query aligns to 6:467/475 of 6awaA
- active site: L45 (= L43), C49 (= C47), C54 (= C52), S57 (= S55), V191 (≠ I187), E195 (= E191), F449 (≠ H445), H451 (= H447), E456 (= E452)
- binding adenosine monophosphate: I187 (≠ V183), E211 (= E207), A212 (= A208), L213 (≠ M209), V245 (= V241), V277 (= V273)
- binding flavin-adenine dinucleotide: I10 (≠ L14), G13 (= G17), P14 (= P18), G15 (= G19), E34 (= E38), K35 (≠ R39), T48 (≠ V46), C49 (= C47), G53 (= G51), C54 (= C52), K58 (= K56), H121 (≠ F118), G122 (= G119), S151 (≠ A147), G152 (= G148), I192 (= I188), R279 (= R275), G318 (= G314), D319 (= D315), M325 (= M321), L326 (= L322), A327 (= A323), Y358 (= Y354)
Sites not aligning to the query:
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
42% identity, 94% coverage: 10:458/476 of query aligns to 2:456/465 of 3urhB
- active site: Y35 (≠ L43), C39 (= C47), C44 (= C52), S47 (= S55), V183 (≠ I187), E187 (= E191), H443 (= H445), H445 (= H447), E450 (= E452)
- binding flavin-adenine dinucleotide: I6 (≠ L14), G7 (= G15), G9 (= G17), P10 (= P18), G11 (= G19), E30 (= E38), K31 (≠ R39), G37 (= G45), T38 (≠ V46), C39 (= C47), G43 (= G51), C44 (= C52), K48 (= K56), T111 (≠ F118), G112 (= G119), A140 (= A146), T141 (≠ A147), G142 (= G148), I184 (= I188), R273 (= R275), G312 (= G314), D313 (= D315), M319 (= M321), L320 (= L322), A321 (= A323), H322 (= H324)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
42% identity, 94% coverage: 10:458/476 of query aligns to 8:459/470 of 6uziC
- active site: C45 (= C47), C50 (= C52), S53 (= S55), V187 (≠ I187), E191 (= E191), H448 (= H447), E453 (= E452)
- binding flavin-adenine dinucleotide: I12 (≠ L14), G13 (= G15), G15 (= G17), P16 (= P18), G17 (= G19), E36 (= E38), K37 (≠ R39), G43 (= G45), T44 (≠ V46), C45 (= C47), G49 (= G51), C50 (= C52), S53 (= S55), K54 (= K56), V117 (≠ F118), G118 (= G119), T147 (≠ A147), G148 (= G148), I188 (= I188), R276 (= R275), D316 (= D315), M322 (= M321), L323 (= L322), A324 (= A323)
- binding zinc ion: H448 (= H447), E453 (= E452)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
42% identity, 94% coverage: 10:458/476 of query aligns to 6:462/477 of P18925
- 34:49 (vs. 38:47, 38% identical) binding FAD
- C49 (= C47) modified: Disulfide link with 54, Redox-active
- C54 (= C52) modified: Disulfide link with 49, Redox-active
- K58 (= K56) binding FAD
- D319 (= D315) binding FAD
- A327 (= A323) 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)
42% identity, 94% coverage: 10:458/476 of query aligns to 5:461/472 of 3ladA
- active site: L44 (= L43), C48 (= C47), C53 (= C52), S56 (= S55), V190 (≠ I187), E194 (= E191), F448 (≠ H445), H450 (= H447), E455 (= E452)
- binding flavin-adenine dinucleotide: I9 (≠ L14), G10 (= G15), G12 (= G17), P13 (= P18), E33 (= E38), K34 (≠ R39), G46 (= G45), T47 (≠ V46), C48 (= C47), G52 (= G51), C53 (= C52), H120 (≠ F118), G121 (= G119), A149 (= A146), S150 (≠ A147), G151 (= G148), I191 (= I188), R278 (= R275), D318 (= D315), L325 (= L322), A326 (= A323)
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
40% identity, 95% coverage: 7:457/476 of query aligns to 13:470/482 of 6hg8B
- active site: C53 (= C47), C58 (= C52), S61 (= S55), V196 (≠ I187), E200 (= E191), H460 (= H447), E465 (= E452)
- binding flavin-adenine dinucleotide: I20 (≠ L14), G23 (= G17), P24 (= P18), G25 (= G19), E44 (= E38), K45 (≠ R39), N46 (≠ G40), G51 (= G45), T52 (≠ V46), C53 (= C47), G57 (= G51), C58 (= C52), K62 (= K56), Y126 (≠ F118), G127 (= G119), T156 (≠ A147), G157 (= G148), I197 (= I188), R288 (= R275), F291 (≠ N278), G327 (= G314), D328 (= D315), M334 (= M321), L335 (= L322), A336 (= A323), H337 (= H324)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
40% identity, 95% coverage: 7:457/476 of query aligns to 3:460/472 of 1zmdA
- active site: L39 (= L43), C43 (= C47), C48 (= C52), S51 (= S55), V186 (≠ I187), E190 (= E191), H448 (= H445), H450 (= H447), E455 (= E452)
- binding flavin-adenine dinucleotide: I10 (≠ L14), G11 (= G15), G13 (= G17), P14 (= P18), G15 (= G19), E34 (= E38), K35 (≠ R39), N36 (≠ G40), G41 (= G45), T42 (≠ V46), C43 (= C47), G47 (= G51), C48 (= C52), K52 (= K56), Y116 (≠ F118), G117 (= G119), T146 (≠ A147), G147 (= G148), S166 (= S167), R278 (= R275), F281 (≠ N278), G317 (= G314), D318 (= D315), M324 (= M321), L325 (= L322), A326 (= A323), H327 (= H324)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (≠ V183), G183 (= G184), G185 (= G186), V186 (≠ I187), I187 (= I188), E190 (= E191), E206 (= E207), F207 (≠ A208), L208 (≠ M209), I276 (≠ V273), G277 (= G274), R278 (= R275), M324 (= M321), L325 (= L322), V355 (= V352), Y357 (= Y354)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
40% identity, 95% coverage: 7:457/476 of query aligns to 3:460/472 of 1zmcA
- active site: L39 (= L43), C43 (= C47), C48 (= C52), S51 (= S55), V186 (≠ I187), E190 (= E191), H448 (= H445), H450 (= H447), E455 (= E452)
- binding flavin-adenine dinucleotide: I10 (≠ L14), G11 (= G15), G13 (= G17), P14 (= P18), G15 (= G19), E34 (= E38), K35 (≠ R39), N36 (≠ G40), G41 (= G45), T42 (≠ V46), C43 (= C47), G47 (= G51), C48 (= C52), K52 (= K56), Y116 (≠ F118), G117 (= G119), T146 (≠ A147), G147 (= G148), S166 (= S167), I187 (= I188), F281 (≠ N278), G317 (= G314), D318 (= D315), M324 (= M321), L325 (= L322), A326 (= A323), H327 (= H324)
- binding nicotinamide-adenine-dinucleotide: G183 (= G184), G185 (= G186), V205 (= V206), E206 (= E207), F207 (≠ A208), L208 (≠ M209), K240 (= K240), V241 (= V241), I276 (≠ V273), G277 (= G274), R278 (= R275), R297 (= R294), M324 (= M321)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
40% identity, 95% coverage: 7:457/476 of query aligns to 40:497/509 of P09622
- 71:80 (vs. 38:47, 50% identical) binding FAD
- K72 (≠ R39) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K56) binding FAD; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ D69) to T: in dbSNP:rs1130477
- G154 (= G119) binding FAD
- TGS 183:185 (≠ AGS 147:149) binding FAD
- 220:227 (vs. 184:191, 63% identical) binding NAD(+)
- E243 (= E207) binding NAD(+)
- V278 (= V241) binding NAD(+)
- G314 (= G274) binding NAD(+)
- D355 (= D315) binding FAD
- MLAH 361:364 (= MLAH 321:324) binding FAD
- E375 (= E335) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ A343) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ H408) 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 (= E426) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ M433) 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 (= D439) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ G442) 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 (= H445) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P448) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (= S451) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E452) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ A455) 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.
6aonA 1.72 angstrom resolution crystal structure of 2-oxoglutarate dehydrogenase complex subunit dihydrolipoamide dehydrogenase from bordetella pertussis in complex with fad
41% identity, 94% coverage: 10:458/476 of query aligns to 4:463/473 of 6aonA
- active site: P43 (≠ L43), C47 (= C47), C52 (= C52), S55 (= S55), V191 (≠ I187), E195 (= E191), H450 (= H445), H452 (= H447), E457 (= E452)
- binding calcium ion: A218 (≠ S214), A220 (= A216), Q222 (≠ R218)
- binding flavin-adenine dinucleotide: I8 (≠ L14), G11 (= G17), P12 (= P18), G13 (= G19), D32 (≠ E38), A33 (≠ R39), W34 (vs. gap), G45 (= G45), T46 (≠ V46), C47 (= C47), G51 (= G51), C52 (= C52), K56 (= K56), K119 (≠ F118), G120 (= G119), T151 (≠ A147), G152 (= G148), N171 (≠ S167), I192 (= I188), R280 (= R275), Y283 (≠ N278), G319 (= G314), D320 (= D315), M326 (= M321), L327 (= L322), A328 (= A323), H329 (= H324)
Query Sequence
>WP_083509555.1 NCBI__GCF_001541235.1:WP_083509555.1
MVRAVDIEADIVVLGAGPGGYTAAFRAADLGKKVVVVERGPALGGVCLNVGCIPSKALLH
AAKVLEDADEMTEAGLGFTRPQLDLDKLRRWKSGIVSKLTGGLAALARQRKVIVVTGFGR
FVSPNEIEVTHEGATKRVAFTQAIIAAGSEPARLPIAPKHDSRILDSTGALDLQDVPPRL
LVVGGGIIGLEMATVYHALGSRVTVVEAMDQLISGADRDIVAPLMKRISTRYDAVHLGTK
VRNIASAAAELTVTFEGANAPEEQSFDKILVAVGRVPNSGTLGLAAAGVAVDQRGFIRVD
KQMRTNVPHIFAIGDVVGQPMLAHKAVHEGKVAAEVAAGLKAAFDARVIPSVAYTDPEVA
WVGLTEAEANANGVAYGKGSFPWEASGRALSQGRSEGLTKVLFDPETHRTLGCGIVGAHA
GELIGEMVLAIEMGADAADIAGTIHPHPTLSETIAQSAEMFEGTITDLIARQARQR
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