SitesBLAST
Comparing 3608572 FitnessBrowser__Dino:3608572 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)
63% identity, 81% coverage: 109:578/580 of query aligns to 4:473/474 of P0A9P0
- K220 (= K324) 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)
63% identity, 81% coverage: 109:577/580 of query aligns to 3:471/471 of 4jdrA
- active site: P15 (= P121), L40 (= L146), C44 (= C150), C49 (= C155), S52 (= S158), E77 (≠ K183), P78 (= P184), I184 (= I289), E188 (= E293), V324 (= V430), H442 (= H548), H444 (= H550), E449 (= E555), N467 (≠ P573), P468 (= P574)
- binding flavin-adenine dinucleotide: G12 (= G118), G14 (= G120), P15 (= P121), A16 (≠ G122), E35 (= E141), R36 (= R142), Y37 (= Y143), V43 (= V149), C44 (= C150), G48 (= G154), C49 (= C155), K53 (= K159), L115 (≠ Y221), G116 (= G222), A144 (= A250), G145 (= G251), I185 (= I290), G311 (= G417), D312 (= D418), M318 (= M424), L319 (= L425), A320 (= A426), H321 (= H427)
1bhyA Low temperature middle resolution structure of p64k from masc data (see paper)
59% identity, 78% coverage: 124:577/580 of query aligns to 19:482/482 of 1bhyA
- active site: L41 (= L146), C45 (= C150), C50 (= C155), S53 (= S158), I195 (= I289), E199 (= E293), H454 (= H548), H456 (= H550), E461 (= E555), P479 (= P574), Q480 (≠ K575)
- binding flavin-adenine dinucleotide: E36 (= E141), R37 (= R142), Y38 (= Y143), G43 (= G148), V44 (= V149), C45 (= C150), G49 (= G154), C50 (= C155), K54 (= K159), D116 (≠ Y221), G117 (= G222), Y135 (vs. gap), A156 (= A250), G157 (= G251), D324 (= D418), L331 (= L425), A332 (= A426)
Sites not aligning to the query:
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, 80% coverage: 113:577/580 of query aligns to 6:478/478 of P14218
- 34:49 (vs. 141:150, 38% identical) binding
- C49 (= C150) modified: Disulfide link with 54, Redox-active
- C54 (= C155) modified: Disulfide link with 49, Redox-active
- K58 (= K159) binding
- G122 (= G222) binding
- D319 (= D418) binding
- A327 (= A426) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
45% identity, 78% coverage: 113:566/580 of query aligns to 5:466/473 of 5u8wA
- active site: P13 (= P121), L44 (= L146), C48 (= C150), C53 (= C155), S56 (= S158), G82 (≠ K183), V83 (≠ P184), V190 (≠ I289), E194 (= E293), S330 (≠ V430), F448 (≠ H548), H450 (= H550), E455 (= E555)
- binding flavin-adenine dinucleotide: I9 (≠ L117), G12 (= G120), P13 (= P121), G14 (= G122), E33 (= E141), K34 (≠ R142), G46 (= G148), T47 (≠ V149), C48 (= C150), G52 (= G154), C53 (= C155), K57 (= K159), H120 (≠ Y221), G121 (= G222), A149 (= A249), S150 (≠ A250), G151 (= G251), S170 (= S269), G317 (= G417), D318 (= D418), M324 (= M424), L325 (= L425), A326 (= A426), H327 (= H427), Y357 (= Y457), H450 (= H550), P451 (= P551)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (≠ L285), G189 (= G288), V190 (≠ I289), I191 (= I290), E194 (= E293), E210 (= E309), A211 (≠ F310), L212 (≠ M311), A275 (= A375), V276 (= V376), G277 (= G377), R278 (= R378), M324 (= M424), L325 (= L425), V355 (= V455), Y357 (= Y457)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
45% identity, 78% coverage: 113:566/580 of query aligns to 4:465/472 of 5u8vA
- active site: P12 (= P121), L43 (= L146), C47 (= C150), C52 (= C155), S55 (= S158), G81 (≠ K183), V82 (≠ P184), V189 (≠ I289), E193 (= E293), S329 (≠ V430), F447 (≠ H548), H449 (= H550), E454 (= E555)
- binding flavin-adenine dinucleotide: I8 (≠ L117), G11 (= G120), P12 (= P121), G13 (= G122), E32 (= E141), G45 (= G148), T46 (≠ V149), C47 (= C150), G51 (= G154), C52 (= C155), K56 (= K159), H119 (≠ Y221), G120 (= G222), A148 (= A249), S149 (≠ A250), G150 (= G251), S169 (= S269), I190 (= I290), R277 (= R378), G316 (= G417), D317 (= D418), M323 (= M424), L324 (= L425), A325 (= A426), H326 (= H427), H449 (= H550), P450 (= P551)
- binding nicotinamide-adenine-dinucleotide: I185 (≠ L285), G186 (= G286), G188 (= G288), V189 (≠ I289), I190 (= I290), L208 (≠ V308), E209 (= E309), A210 (≠ F310), V243 (= V343), V275 (= V376), G276 (= G377)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
45% identity, 78% coverage: 113:566/580 of query aligns to 8:469/477 of 5u8uD
- active site: P16 (= P121), L47 (= L146), C51 (= C150), C56 (= C155), S59 (= S158), G85 (≠ K183), V86 (≠ P184), V193 (≠ I289), E197 (= E293), S333 (≠ V430), F451 (≠ H548), H453 (= H550), E458 (= E555)
- binding flavin-adenine dinucleotide: I12 (≠ L117), G15 (= G120), P16 (= P121), G17 (= G122), E36 (= E141), K37 (≠ R142), G49 (= G148), T50 (≠ V149), C51 (= C150), G55 (= G154), C56 (= C155), K60 (= K159), H123 (≠ Y221), G124 (= G222), A152 (= A249), S153 (≠ A250), G154 (= G251), I194 (= I290), R281 (= R378), G320 (= G417), D321 (= D418), M327 (= M424), L328 (= L425), A329 (= A426), H330 (= H427), H453 (= H550), P454 (= P551)
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, 79% coverage: 110:567/580 of query aligns to 8:463/470 of P11959
- 39:47 (vs. 141:150, 60% identical) binding
- K56 (= K159) binding
- D314 (= D418) binding
- A322 (= A426) binding
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
44% identity, 78% coverage: 110:563/580 of query aligns to 2:453/455 of 1ebdA
- active site: P13 (= P121), L37 (= L146), C41 (= C150), C46 (= C155), S49 (= S158), N74 (≠ K183), V75 (≠ P184), Y180 (≠ I289), E184 (= E293), S320 (≠ V430), H438 (= H548), H440 (= H550), E445 (= E555)
- binding flavin-adenine dinucleotide: G10 (= G118), G12 (= G120), P13 (= P121), V32 (≠ I140), E33 (= E141), K34 (≠ R142), G39 (= G148), V40 (= V149), C41 (= C150), G45 (= G154), C46 (= C155), K50 (= K159), E112 (≠ Y221), A113 (≠ G222), T141 (≠ A250), G142 (= G251), Y180 (≠ I289), I181 (= I290), R268 (= R378), D308 (= D418), A314 (≠ M424), L315 (= L425), A316 (= A426)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
44% identity, 77% coverage: 113:561/580 of query aligns to 8:459/470 of 6uziC
- active site: C45 (= C150), C50 (= C155), S53 (= S158), V187 (≠ I289), E191 (= E293), H448 (= H550), E453 (= E555)
- binding flavin-adenine dinucleotide: I12 (≠ L117), G13 (= G118), G15 (= G120), P16 (= P121), G17 (= G122), E36 (= E141), K37 (≠ R142), G43 (= G148), T44 (≠ V149), C45 (= C150), G49 (= G154), C50 (= C155), S53 (= S158), K54 (= K159), V117 (≠ Y221), G118 (= G222), T147 (≠ A250), G148 (= G251), I188 (= I290), R276 (= R378), D316 (= D418), M322 (= M424), L323 (= L425), A324 (= A426)
- binding zinc ion: H448 (= H550), E453 (= E555)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
43% identity, 80% coverage: 113:576/580 of query aligns to 6:477/477 of P18925
- 34:49 (vs. 141:150, 38% identical) binding
- C49 (= C150) modified: Disulfide link with 54, Redox-active
- C54 (= C155) modified: Disulfide link with 49, Redox-active
- K58 (= K159) binding
- D319 (= D418) binding
- A327 (= A426) binding
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)
43% identity, 78% coverage: 113:566/580 of query aligns to 5:466/472 of 3ladA
- active site: L44 (= L146), C48 (= C150), C53 (= C155), S56 (= S158), V190 (≠ I289), E194 (= E293), F448 (≠ H548), H450 (= H550), E455 (= E555)
- binding flavin-adenine dinucleotide: I9 (≠ L117), G10 (= G118), G12 (= G120), P13 (= P121), E33 (= E141), K34 (≠ R142), G46 (= G148), T47 (≠ V149), C48 (= C150), G52 (= G154), C53 (= C155), H120 (≠ Y221), G121 (= G222), A149 (= A249), S150 (≠ A250), G151 (= G251), I191 (= I290), R278 (= R378), D318 (= D418), L325 (= L425), A326 (= A426)
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
44% identity, 78% coverage: 113:564/580 of query aligns to 5:451/460 of 2eq6A
- active site: V37 (≠ L146), C41 (= C150), C46 (= C155), T49 (≠ S158), A176 (≠ I289), E180 (= E293), H435 (= H548), H437 (= H550), E442 (= E555)
- binding flavin-adenine dinucleotide: I9 (≠ L117), G10 (= G118), G12 (= G120), P13 (= P121), G14 (= G122), E33 (= E141), A34 (≠ Y143), G39 (= G148), V40 (= V149), C41 (= C150), G45 (= G154), C46 (= C155), K50 (= K159), F111 (≠ Y221), A112 (≠ G222), A135 (= A249), T136 (≠ A250), G137 (= G251), S155 (= S269), R269 (≠ N381), D306 (= D418), L312 (≠ M424), L313 (= L425), A314 (= A426), H315 (= H427), Y344 (= Y457)
Sites not aligning to the query:
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
43% identity, 77% coverage: 113:561/580 of query aligns to 2:456/465 of 3urhB
- active site: Y35 (≠ L146), C39 (= C150), C44 (= C155), S47 (= S158), V183 (≠ I289), E187 (= E293), H443 (= H548), H445 (= H550), E450 (= E555)
- binding flavin-adenine dinucleotide: I6 (≠ L117), G7 (= G118), G9 (= G120), P10 (= P121), G11 (= G122), E30 (= E141), K31 (≠ R142), G37 (= G148), T38 (≠ V149), C39 (= C150), G43 (= G154), C44 (= C155), K48 (= K159), T111 (≠ Y221), G112 (= G222), A140 (= A249), T141 (≠ A250), G142 (= G251), I184 (= I290), R273 (= R378), G312 (= G417), D313 (= D418), M319 (= M424), L320 (= L425), A321 (= A426), H322 (= H427)
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
42% identity, 78% coverage: 113:566/580 of query aligns to 6:467/475 of 6awaA
- active site: L45 (= L146), C49 (= C150), C54 (= C155), S57 (= S158), V191 (≠ I289), E195 (= E293), F449 (≠ H548), H451 (= H550), E456 (= E555)
- binding adenosine monophosphate: I187 (≠ L285), E211 (= E309), A212 (≠ F310), L213 (≠ M311), V245 (= V343), V277 (= V376)
- binding flavin-adenine dinucleotide: I10 (≠ L117), G13 (= G120), P14 (= P121), G15 (= G122), E34 (= E141), K35 (≠ R142), T48 (≠ V149), C49 (= C150), G53 (= G154), C54 (= C155), K58 (= K159), H121 (≠ Y221), G122 (= G222), S151 (≠ A250), G152 (= G251), I192 (= I290), R279 (= R378), G318 (= G417), D319 (= D418), M325 (= M424), L326 (= L425), A327 (= A426), Y358 (= Y457)
Sites not aligning to the query:
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
41% identity, 79% coverage: 106:563/580 of query aligns to 6:476/482 of 6hg8B
- active site: C53 (= C150), C58 (= C155), S61 (= S158), V196 (≠ I289), E200 (= E293), H460 (= H550), E465 (= E555)
- binding flavin-adenine dinucleotide: I20 (≠ L117), G23 (= G120), P24 (= P121), G25 (= G122), E44 (= E141), K45 (≠ R142), N46 (≠ Y143), G51 (= G148), T52 (≠ V149), C53 (= C150), G57 (= G154), C58 (= C155), K62 (= K159), Y126 (= Y221), G127 (= G222), T156 (≠ A250), G157 (= G251), I197 (= I290), R288 (= R378), F291 (≠ N381), G327 (= G417), D328 (= D418), M334 (= M424), L335 (= L425), A336 (= A426), H337 (= H427)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
41% identity, 78% coverage: 110:563/580 of query aligns to 40:503/509 of P09622
- 71:80 (vs. 141:150, 50% identical) binding
- K72 (≠ R142) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K159) binding ; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ E172) to T: in dbSNP:rs1130477
- G154 (= G222) binding
- TGS 183:185 (≠ AGS 250:252) binding
- 220:227 (vs. 286:293, 63% identical) binding
- E243 (= E309) binding
- V278 (= V343) binding
- G314 (= G377) binding
- D355 (= D418) binding
- MLAH 361:364 (= MLAH 424:427) binding
- E375 (= E438) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (= H446) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (= D511) 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 (= E529) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ M536) 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 (= D542) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ H545) 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 (= H548) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P551) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (= S554) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E555) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (vs. gap) 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.
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
41% identity, 78% coverage: 110:563/580 of query aligns to 3:466/472 of 1zmdA
- active site: L39 (= L146), C43 (= C150), C48 (= C155), S51 (= S158), V186 (≠ I289), E190 (= E293), H448 (= H548), H450 (= H550), E455 (= E555)
- binding flavin-adenine dinucleotide: I10 (≠ L117), G11 (= G118), G13 (= G120), P14 (= P121), G15 (= G122), E34 (= E141), K35 (≠ R142), N36 (≠ Y143), G41 (= G148), T42 (≠ V149), C43 (= C150), G47 (= G154), C48 (= C155), K52 (= K159), Y116 (= Y221), G117 (= G222), T146 (≠ A250), G147 (= G251), S166 (= S269), R278 (= R378), F281 (≠ N381), G317 (= G417), D318 (= D418), M324 (= M424), L325 (= L425), A326 (= A426), H327 (= H427)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (≠ L285), G183 (= G286), G185 (= G288), V186 (≠ I289), I187 (= I290), E190 (= E293), E206 (= E309), F207 (= F310), L208 (≠ M311), I276 (≠ V376), G277 (= G377), R278 (= R378), M324 (= M424), L325 (= L425), V355 (= V455), Y357 (= Y457)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
41% identity, 78% coverage: 110:563/580 of query aligns to 3:466/472 of 1zmcA
- active site: L39 (= L146), C43 (= C150), C48 (= C155), S51 (= S158), V186 (≠ I289), E190 (= E293), H448 (= H548), H450 (= H550), E455 (= E555)
- binding flavin-adenine dinucleotide: I10 (≠ L117), G11 (= G118), G13 (= G120), P14 (= P121), G15 (= G122), E34 (= E141), K35 (≠ R142), N36 (≠ Y143), G41 (= G148), T42 (≠ V149), C43 (= C150), G47 (= G154), C48 (= C155), K52 (= K159), Y116 (= Y221), G117 (= G222), T146 (≠ A250), G147 (= G251), S166 (= S269), I187 (= I290), F281 (≠ N381), G317 (= G417), D318 (= D418), M324 (= M424), L325 (= L425), A326 (= A426), H327 (= H427)
- binding nicotinamide-adenine-dinucleotide: G183 (= G286), G185 (= G288), V205 (= V308), E206 (= E309), F207 (= F310), L208 (≠ M311), K240 (= K342), V241 (= V343), I276 (≠ V376), G277 (= G377), R278 (= R378), R297 (= R397), M324 (= M424)
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)
43% identity, 79% coverage: 104:561/580 of query aligns to 30:491/501 of P31023
- 67:76 (vs. 141:150, 50% identical) binding
- C76 (= C150) modified: Disulfide link with 81, Redox-active
- C81 (= C155) modified: Disulfide link with 76, Redox-active
- G149 (= G222) binding
- D348 (= D418) binding
- MLAH 354:357 (= MLAH 424:427) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
Query Sequence
>3608572 FitnessBrowser__Dino:3608572
MDIKVPDIGDFTDVPVVSILVAVGDTVAEEDPLIELESDKATMEVPSPAAGVVKEIKVAE
GDNVSEGTVIMVFESSGAEEAPKGADEAPAAAAAPEAVAATGTATGPGDVHGEVVVLGSG
PGGYTAAFRAADLGKKVVLIERYPSLGGVCLNVGCIPSKALLHVAKVITEAEEMGAHGVS
FGKPKVDLDELRAFKDSVIGQLTGGLSGLAKGRKVEVVTGYGKFTGPNMIAVEGEDGVTT
VSFDQCIIAAGSEPVNLPFLPEDDRIIDSTGALELKDIPKRMLILGGGIIGLEMACVYDA
LGSDITVVEFMDQLMPGADKDIVKPLHKRIEGRYENILLKTKVTGVEALKKGLKVTFEDA
KGELTTDTFDKVLVAVGRKPNGALIDAEKAGVAVDERGFIAVDSQQRTGVAHIFAIGDLV
GQPMLAHKAVHEGKVAAEVCAGHNRHFDARLIPSVAYTDPEVAWCGVTETDAKAKGIAYE
KGVFPWAASGRSLSNGRSEGITKLLFDPEDDRVIGACIVGTNAGDLISEVALAIEMGADA
VDLGHTIHPHPTLSETVNFAAEMFEGTITDLMPPKKKKAH
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