SitesBLAST
Comparing 352713 FitnessBrowser__Btheta:352713 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)
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
38% identity, 100% coverage: 1:446/447 of query aligns to 2:450/455 of 1ebdA
- active site: P13 (= P12), L37 (= L36), C41 (= C40), C46 (= C45), S49 (≠ T48), N74 (≠ E73), V75 (= V74), Y180 (≠ V176), E184 (= E180), S320 (≠ V316), H438 (≠ F434), H440 (= H436), E445 (= E441)
- binding flavin-adenine dinucleotide: G10 (= G9), G12 (= G11), P13 (= P12), V32 (≠ I31), E33 (= E32), K34 (= K33), G39 (= G38), V40 (= V39), C41 (= C40), G45 (= G44), C46 (= C45), K50 (= K49), E112 (= E111), A113 (= A112), T141 (= T136), G142 (= G137), Y180 (≠ V176), I181 (= I177), R268 (= R264), D308 (= D304), A314 (≠ L310), L315 (= L311), A316 (= A312)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
37% identity, 100% coverage: 1:446/447 of query aligns to 8:456/470 of P11959
- 39:47 (vs. 32:40, 89% identical) binding FAD
- K56 (= K49) binding FAD
- D314 (= D304) binding FAD
- A322 (= A312) 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)
37% identity, 100% coverage: 2:446/447 of query aligns to 3:460/472 of 3ladA
- active site: L44 (= L36), C48 (= C40), C53 (= C45), S56 (≠ T48), V190 (= V176), E194 (= E180), F448 (= F434), H450 (= H436), E455 (= E441)
- binding flavin-adenine dinucleotide: I9 (= I8), G10 (= G9), G12 (= G11), P13 (= P12), E33 (= E32), K34 (= K33), G46 (= G38), T47 (≠ V39), C48 (= C40), G52 (= G44), C53 (= C45), H120 (≠ E111), G121 (≠ A112), A149 (≠ C135), S150 (≠ T136), G151 (= G137), I191 (= I177), R278 (= R264), D318 (= D304), L325 (= L311), A326 (= A312)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
37% identity, 100% coverage: 2:446/447 of query aligns to 4:461/477 of P18925
- 34:49 (vs. 32:40, 38% identical) binding FAD
- C49 (= C40) modified: Disulfide link with 54, Redox-active
- C54 (= C45) modified: Disulfide link with 49, Redox-active
- K58 (= K49) binding FAD
- D319 (= D304) binding FAD
- A327 (= A312) binding FAD
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
36% identity, 100% coverage: 2:446/447 of query aligns to 6:458/470 of 6uziC
- active site: C45 (= C40), C50 (= C45), S53 (≠ T48), V187 (= V176), E191 (= E180), H448 (= H436), E453 (= E441)
- binding flavin-adenine dinucleotide: I12 (= I8), G13 (= G9), G15 (= G11), P16 (= P12), G17 (≠ A13), E36 (= E32), K37 (= K33), G43 (= G38), T44 (≠ V39), C45 (= C40), G49 (= G44), C50 (= C45), S53 (≠ T48), K54 (= K49), V117 (vs. gap), G118 (vs. gap), T147 (= T136), G148 (= G137), I188 (= I177), R276 (= R264), D316 (= D304), M322 (≠ L310), L323 (= L311), A324 (= A312)
- binding zinc ion: H448 (= H436), E453 (= E441)
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
40% identity, 99% coverage: 3:446/447 of query aligns to 4:447/460 of 2eq6A
- active site: V37 (≠ L36), C41 (= C40), C46 (= C45), T49 (= T48), A176 (≠ V176), E180 (= E180), H435 (≠ F434), H437 (= H436), E442 (= E441)
- binding flavin-adenine dinucleotide: I9 (= I8), G10 (= G9), G12 (= G11), P13 (= P12), G14 (≠ A13), E33 (= E32), A34 (≠ K33), G39 (= G38), V40 (= V39), C41 (= C40), G45 (= G44), C46 (= C45), K50 (= K49), F111 (≠ E111), A112 (= A112), A135 (≠ C135), T136 (= T136), G137 (= G137), S155 (≠ H156), R269 (≠ V267), D306 (= D304), L312 (= L310), L313 (= L311), A314 (= A312), H315 (= H313), Y344 (= Y343)
Sites not aligning to the query:
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
38% identity, 99% coverage: 4:446/447 of query aligns to 6:460/472 of 1zmdA
- active site: L39 (= L36), C43 (= C40), C48 (= C45), S51 (≠ T48), V186 (= V176), E190 (= E180), H448 (≠ F434), H450 (= H436), E455 (= E441)
- binding flavin-adenine dinucleotide: I10 (= I8), G11 (= G9), G13 (= G11), P14 (= P12), G15 (≠ A13), E34 (= E32), K35 (= K33), N36 (= N34), G41 (= G38), T42 (≠ V39), C43 (= C40), G47 (= G44), C48 (= C45), K52 (= K49), Y116 (≠ E111), G117 (≠ A112), T146 (= T136), G147 (= G137), S166 (≠ H156), R278 (= R264), F281 (≠ V267), G317 (= G303), D318 (= D304), M324 (≠ L310), L325 (= L311), A326 (= A312), H327 (= H313)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (≠ V172), G183 (= G173), G185 (= G175), V186 (= V176), I187 (= I177), E190 (= E180), E206 (= E196), F207 (≠ M197), L208 (≠ M198), I276 (≠ V262), G277 (= G263), R278 (= R264), M324 (≠ L310), L325 (= L311), V355 (= V341), Y357 (= Y343)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
38% identity, 99% coverage: 4:446/447 of query aligns to 6:460/472 of 1zmcA
- active site: L39 (= L36), C43 (= C40), C48 (= C45), S51 (≠ T48), V186 (= V176), E190 (= E180), H448 (≠ F434), H450 (= H436), E455 (= E441)
- binding flavin-adenine dinucleotide: I10 (= I8), G11 (= G9), G13 (= G11), P14 (= P12), G15 (≠ A13), E34 (= E32), K35 (= K33), N36 (= N34), G41 (= G38), T42 (≠ V39), C43 (= C40), G47 (= G44), C48 (= C45), K52 (= K49), Y116 (≠ E111), G117 (≠ A112), T146 (= T136), G147 (= G137), S166 (≠ H156), I187 (= I177), F281 (≠ V267), G317 (= G303), D318 (= D304), M324 (≠ L310), L325 (= L311), A326 (= A312), H327 (= H313)
- binding nicotinamide-adenine-dinucleotide: G183 (= G173), G185 (= G175), V205 (≠ I195), E206 (= E196), F207 (≠ M197), L208 (≠ M198), K240 (= K229), V241 (= V230), I276 (≠ V262), G277 (= G263), R278 (= R264), R297 (= R283), M324 (≠ L310)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
38% identity, 99% coverage: 4:446/447 of query aligns to 43:497/509 of P09622
- 71:80 (vs. 32:40, 70% identical) binding FAD
- K72 (= K33) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K49) binding FAD; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ S65) to T: in dbSNP:rs1130477
- G154 (≠ A112) binding FAD
- TGS 183:185 (= TGS 136:138) binding FAD
- 220:227 (vs. 173:180, 75% identical) binding NAD(+)
- E243 (= E196) binding NAD(+)
- V278 (= V230) binding NAD(+)
- G314 (= G263) binding NAD(+)
- D355 (= D304) binding FAD
- MLAH 361:364 (≠ LLAH 310:313) binding FAD
- E375 (≠ H324) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ A332) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ E397) 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 (≠ L415) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ L422) 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 (≠ A428) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ K431) 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 (≠ F434) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P437) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (≠ G440) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E441) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (= R444) 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.
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
36% identity, 99% coverage: 3:446/447 of query aligns to 1:455/465 of 3urhB