SitesBLAST
Comparing Ac3H11_4091 FitnessBrowser__acidovorax_3H11:Ac3H11_4091 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)
1bhyA Low temperature middle resolution structure of p64k from masc data (see paper)
68% identity, 80% coverage: 122:616/616 of query aligns to 1:482/482 of 1bhyA
- active site: L41 (= L162), C45 (= C166), C50 (= C171), S53 (= S174), I195 (= I313), E199 (= E317), H454 (= H588), H456 (= H590), E461 (= E595), P479 (= P613), Q480 (= Q614)
- binding flavin-adenine dinucleotide: L12 (= L133), P16 (= P137), G17 (= G138), E36 (= E157), R37 (= R158), Y38 (= Y159), G43 (= G164), V44 (= V165), C45 (= C166), G49 (= G170), C50 (= C171), K54 (= K175), D116 (≠ Y237), G117 (= G238), Y135 (≠ Q256), A156 (= A274), G157 (= G275), D324 (= D445), L331 (= L452), A332 (= A453)
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, 80% coverage: 123:615/616 of query aligns to 2:470/474 of P0A9P0
- K220 (= K348) 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)
60% identity, 80% coverage: 123:615/616 of query aligns to 1:469/471 of 4jdrA
- active site: P15 (= P137), L40 (= L162), C44 (= C166), C49 (= C171), S52 (= S174), E77 (≠ A199), P78 (= P200), I184 (= I313), E188 (= E317), V324 (= V457), H442 (= H588), H444 (= H590), E449 (= E595), N467 (≠ P613), P468 (≠ Q614)
- binding flavin-adenine dinucleotide: G12 (= G134), G14 (= G136), P15 (= P137), A16 (≠ G138), E35 (= E157), R36 (= R158), Y37 (= Y159), V43 (= V165), C44 (= C166), G48 (= G170), C49 (= C171), K53 (= K175), L115 (≠ Y237), G116 (= G238), A144 (= A274), G145 (= G275), I185 (= I314), G311 (= G444), D312 (= D445), M318 (= M451), L319 (= L452), A320 (= A453), H321 (= H454)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
43% identity, 78% coverage: 126:607/616 of query aligns to 8:463/470 of P11959
- 39:47 (vs. 157:166, 60% identical) binding
- K56 (= K175) binding
- D314 (= D445) binding
- A322 (= A453) binding
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
43% identity, 78% coverage: 126:604/616 of query aligns to 2:454/455 of 1ebdA
- active site: P13 (= P137), L37 (= L162), C41 (= C166), C46 (= C171), S49 (= S174), N74 (≠ A199), V75 (≠ P200), Y180 (≠ I313), E184 (= E317), S320 (≠ V457), H438 (= H588), H440 (= H590), E445 (= E595)
- binding flavin-adenine dinucleotide: G10 (= G134), G12 (= G136), P13 (= P137), V32 (= V156), E33 (= E157), K34 (≠ R158), G39 (= G164), V40 (= V165), C41 (= C166), G45 (= G170), C46 (= C171), K50 (= K175), E112 (≠ Y237), A113 (≠ G238), T141 (≠ A274), G142 (= G275), Y180 (≠ I313), I181 (= I314), R268 (= R405), D308 (= D445), A314 (≠ M451), L315 (= L452), A316 (= A453)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
40% identity, 77% coverage: 129:601/616 of query aligns to 2:456/465 of 3urhB
- active site: Y35 (≠ L162), C39 (= C166), C44 (= C171), S47 (= S174), V183 (≠ I313), E187 (= E317), H443 (= H588), H445 (= H590), E450 (= E595)
- binding flavin-adenine dinucleotide: I6 (≠ L133), G7 (= G134), G9 (= G136), P10 (= P137), G11 (= G138), E30 (= E157), K31 (≠ R158), G37 (= G164), T38 (≠ V165), C39 (= C166), G43 (= G170), C44 (= C171), K48 (= K175), T111 (≠ Y237), G112 (= G238), A140 (= A273), T141 (≠ A274), G142 (= G275), I184 (= I314), R273 (= R405), G312 (= G444), D313 (= D445), M319 (= M451), L320 (= L452), A321 (= A453), H322 (= H454)
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
40% identity, 77% coverage: 126:600/616 of query aligns to 13:470/482 of 6hg8B
- active site: C53 (= C166), C58 (= C171), S61 (= S174), V196 (≠ I313), E200 (= E317), H460 (= H590), E465 (= E595)
- binding flavin-adenine dinucleotide: I20 (≠ L133), G23 (= G136), P24 (= P137), G25 (= G138), E44 (= E157), K45 (≠ R158), N46 (≠ Y159), G51 (= G164), T52 (≠ V165), C53 (= C166), G57 (= G170), C58 (= C171), K62 (= K175), Y126 (= Y237), G127 (= G238), T156 (≠ A274), G157 (= G275), I197 (= I314), R288 (= R405), F291 (≠ N408), G327 (= G444), D328 (= D445), M334 (= M451), L335 (= L452), A336 (= A453), H337 (= H454)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
42% identity, 78% coverage: 129:606/616 of query aligns to 8:464/470 of 6uziC
- active site: C45 (= C166), C50 (= C171), S53 (= S174), V187 (≠ I313), E191 (= E317), H448 (= H590), E453 (= E595)
- binding flavin-adenine dinucleotide: I12 (≠ L133), G13 (= G134), G15 (= G136), P16 (= P137), G17 (= G138), E36 (= E157), K37 (≠ R158), G43 (= G164), T44 (≠ V165), C45 (= C166), G49 (= G170), C50 (= C171), S53 (= S174), K54 (= K175), V117 (≠ Y237), G118 (= G238), T147 (≠ A274), G148 (= G275), I188 (= I314), R276 (= R405), D316 (= D445), M322 (= M451), L323 (= L452), A324 (= A453)
- binding zinc ion: H448 (= H590), E453 (= E595)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
40% identity, 77% coverage: 126:597/616 of query aligns to 3:457/472 of 1zmdA
- active site: L39 (= L162), C43 (= C166), C48 (= C171), S51 (= S174), V186 (≠ I313), E190 (= E317), H448 (= H588), H450 (= H590), E455 (= E595)
- binding flavin-adenine dinucleotide: I10 (≠ L133), G11 (= G134), G13 (= G136), P14 (= P137), G15 (= G138), E34 (= E157), K35 (≠ R158), N36 (≠ Y159), G41 (= G164), T42 (≠ V165), C43 (= C166), G47 (= G170), C48 (= C171), K52 (= K175), Y116 (= Y237), G117 (= G238), T146 (≠ A274), G147 (= G275), S166 (= S293), R278 (= R405), F281 (≠ N408), G317 (= G444), D318 (= D445), M324 (= M451), L325 (= L452), A326 (= A453), H327 (= H454)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (≠ L309), G183 (= G310), G185 (= G312), V186 (≠ I313), I187 (= I314), E190 (= E317), E206 (= E333), F207 (≠ M334), L208 (≠ M335), I276 (≠ V403), G277 (= G404), R278 (= R405), M324 (= M451), L325 (= L452), V355 (= V490), Y357 (= Y492)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
40% identity, 77% coverage: 126:597/616 of query aligns to 3:457/472 of 1zmcA
- active site: L39 (= L162), C43 (= C166), C48 (= C171), S51 (= S174), V186 (≠ I313), E190 (= E317), H448 (= H588), H450 (= H590), E455 (= E595)
- binding flavin-adenine dinucleotide: I10 (≠ L133), G11 (= G134), G13 (= G136), P14 (= P137), G15 (= G138), E34 (= E157), K35 (≠ R158), N36 (≠ Y159), G41 (= G164), T42 (≠ V165), C43 (= C166), G47 (= G170), C48 (= C171), K52 (= K175), Y116 (= Y237), G117 (= G238), T146 (≠ A274), G147 (= G275), S166 (= S293), I187 (= I314), F281 (≠ N408), G317 (= G444), D318 (= D445), M324 (= M451), L325 (= L452), A326 (= A453), H327 (= H454)
- binding nicotinamide-adenine-dinucleotide: G183 (= G310), G185 (= G312), V205 (= V332), E206 (= E333), F207 (≠ M334), L208 (≠ M335), K240 (= K366), V241 (≠ T367), I276 (≠ V403), G277 (= G404), R278 (= R405), R297 (= R424), M324 (= M451)
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, 77% coverage: 126:597/616 of query aligns to 40:494/509 of P09622
- 71:80 (vs. 157:166, 60% identical) binding
- K72 (≠ R158) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K175) binding ; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ S188) to T: in dbSNP:rs1130477
- G154 (= G238) binding
- TGS 183:185 (≠ AGS 274:276) binding
- 220:227 (vs. 310:317, 63% identical) binding
- E243 (= E333) binding
- V278 (≠ T367) binding
- G314 (= G404) binding
- D355 (= D445) binding
- MLAH 361:364 (= MLAH 451:454) binding
- E375 (= E465) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ A481) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ E546) 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 (= E569) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ M576) 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 (= D582) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ K585) 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 (= H588) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P591) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (≠ G594) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E595) 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.
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
42% identity, 77% coverage: 129:605/616 of query aligns to 5:452/460 of 2eq6A
- active site: V37 (≠ L162), C41 (= C166), C46 (= C171), T49 (≠ S174), A176 (≠ I313), E180 (= E317), H435 (= H588), H437 (= H590), E442 (= E595)
- binding flavin-adenine dinucleotide: I9 (≠ L133), G10 (= G134), G12 (= G136), P13 (= P137), G14 (= G138), E33 (= E157), A34 (≠ Y159), G39 (= G164), V40 (= V165), C41 (= C166), G45 (= G170), C46 (= C171), K50 (= K175), F111 (≠ Y237), A112 (≠ G238), A135 (= A273), T136 (≠ A274), G137 (= G275), S155 (= S293), R269 (≠ N408), D306 (= D445), L312 (≠ M451), L313 (= L452), A314 (= A453), H315 (= H454), Y344 (= Y492)
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)
38% identity, 79% coverage: 129:616/616 of query aligns to 6:477/478 of P14218
- 34:49 (vs. 157:166, 38% identical) binding
- C49 (= C166) modified: Disulfide link with 54, Redox-active
- C54 (= C171) modified: Disulfide link with 49, Redox-active
- K58 (= K175) binding
- G122 (= G238) binding
- D319 (= D445) binding
- A327 (= A453) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
38% identity, 78% coverage: 129:611/616 of query aligns to 6:472/475 of 6awaA
- active site: L45 (= L162), C49 (= C166), C54 (= C171), S57 (= S174), V191 (≠ I313), E195 (= E317), F449 (≠ H588), H451 (= H590), E456 (= E595)
- binding adenosine monophosphate: I187 (≠ L309), E211 (= E333), A212 (≠ M334), L213 (≠ M335), V245 (≠ T367), V277 (= V403)
- binding flavin-adenine dinucleotide: I10 (≠ L133), G13 (= G136), P14 (= P137), G15 (= G138), E34 (= E157), K35 (≠ R158), T48 (≠ V165), C49 (= C166), G53 (= G170), C54 (= C171), K58 (= K175), H121 (≠ Y237), G122 (= G238), S151 (≠ A274), G152 (= G275), I192 (= I314), R279 (= R405), G318 (= G444), D319 (= D445), M325 (= M451), L326 (= L452), A327 (= A453), Y358 (= Y492)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
38% identity, 78% coverage: 129:606/616 of query aligns to 4:465/472 of 5u8vA
- active site: P12 (= P137), L43 (= L162), C47 (= C166), C52 (= C171), S55 (= S174), G81 (≠ A199), V82 (≠ P200), V189 (≠ I313), E193 (= E317), S329 (≠ V457), F447 (≠ H588), H449 (= H590), E454 (= E595)
- binding flavin-adenine dinucleotide: I8 (≠ L133), G11 (= G136), P12 (= P137), G13 (= G138), E32 (= E157), G45 (= G164), T46 (≠ V165), C47 (= C166), G51 (= G170), C52 (= C171), K56 (= K175), H119 (≠ Y237), G120 (= G238), A148 (= A273), S149 (≠ A274), G150 (= G275), S169 (= S293), I190 (= I314), R277 (= R405), G316 (= G444), D317 (= D445), M323 (= M451), L324 (= L452), A325 (= A453), H326 (= H454), H449 (= H590), P450 (= P591)
- binding nicotinamide-adenine-dinucleotide: I185 (≠ L309), G186 (= G310), G188 (= G312), V189 (≠ I313), I190 (= I314), L208 (≠ V332), E209 (= E333), A210 (≠ M334), V243 (≠ T367), V275 (= V403), G276 (= G404)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
38% identity, 78% coverage: 129:606/616 of query aligns to 5:466/473 of 5u8wA
- active site: P13 (= P137), L44 (= L162), C48 (= C166), C53 (= C171), S56 (= S174), G82 (≠ A199), V83 (≠ P200), V190 (≠ I313), E194 (= E317), S330 (≠ V457), F448 (≠ H588), H450 (= H590), E455 (= E595)
- binding flavin-adenine dinucleotide: I9 (≠ L133), G12 (= G136), P13 (= P137), G14 (= G138), E33 (= E157), K34 (≠ R158), G46 (= G164), T47 (≠ V165), C48 (= C166), G52 (= G170), C53 (= C171), K57 (= K175), H120 (≠ Y237), G121 (= G238), A149 (= A273), S150 (≠ A274), G151 (= G275), S170 (= S293), G317 (= G444), D318 (= D445), M324 (= M451), L325 (= L452), A326 (= A453), H327 (= H454), Y357 (= Y492), H450 (= H590), P451 (= P591)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (≠ L309), G189 (= G312), V190 (≠ I313), I191 (= I314), E194 (= E317), E210 (= E333), A211 (≠ M334), L212 (≠ M335), A275 (= A402), V276 (= V403), G277 (= G404), R278 (= R405), M324 (= M451), L325 (= L452), V355 (= V490), Y357 (= Y492)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
38% identity, 78% coverage: 129:606/616 of query aligns to 8:469/477 of 5u8uD
- active site: P16 (= P137), L47 (= L162), C51 (= C166), C56 (= C171), S59 (= S174), G85 (≠ A199), V86 (≠ P200), V193 (≠ I313), E197 (= E317), S333 (≠ V457), F451 (≠ H588), H453 (= H590), E458 (= E595)
- binding flavin-adenine dinucleotide: I12 (≠ L133), G15 (= G136), P16 (= P137), G17 (= G138), E36 (= E157), K37 (≠ R158), G49 (= G164), T50 (≠ V165), C51 (= C166), G55 (= G170), C56 (= C171), K60 (= K175), H123 (≠ Y237), G124 (= G238), A152 (= A273), S153 (≠ A274), G154 (= G275), I194 (= I314), R281 (= R405), G320 (= G444), D321 (= D445), M327 (= M451), L328 (= L452), A329 (= A453), H330 (= H454), H453 (= H590), P454 (= P591)
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)
38% identity, 79% coverage: 129:616/616 of query aligns to 6:477/477 of P18925
- 34:49 (vs. 157:166, 38% identical) binding
- C49 (= C166) modified: Disulfide link with 54, Redox-active
- C54 (= C171) modified: Disulfide link with 49, Redox-active
- K58 (= K175) binding
- D319 (= D445) binding
- A327 (= A453) 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)
38% identity, 77% coverage: 129:601/616 of query aligns to 5:461/472 of 3ladA
- active site: L44 (= L162), C48 (= C166), C53 (= C171), S56 (= S174), V190 (≠ I313), E194 (= E317), F448 (≠ H588), H450 (= H590), E455 (= E595)
- binding flavin-adenine dinucleotide: I9 (≠ L133), G10 (= G134), G12 (= G136), P13 (= P137), E33 (= E157), K34 (≠ R158), G46 (= G164), T47 (≠ V165), C48 (= C166), G52 (= G170), C53 (= C171), H120 (≠ Y237), G121 (= G238), A149 (= A273), S150 (≠ A274), G151 (= G275), I191 (= I314), R278 (= R405), D318 (= D445), L325 (= L452), A326 (= A453)
6bz0A 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from acinetobacter baumannii in complex with fad.
38% identity, 77% coverage: 129:601/616 of query aligns to 3:458/469 of 6bz0A
- active site: C45 (= C166), C50 (= C171), S53 (= S174), V187 (≠ I313), E191 (= E317), H447 (= H590), E452 (= E595)
- binding flavin-adenine dinucleotide: I7 (≠ L133), G10 (= G136), P11 (= P137), G12 (= G138), E31 (= E157), K32 (≠ R158), R33 (≠ Y159), G43 (= G164), T44 (≠ V165), C45 (= C166), G49 (= G170), C50 (= C171), K54 (= K175), T117 (≠ Y237), G118 (= G238), S147 (≠ A274), G148 (= G275), S167 (= S293), I188 (= I314), R275 (= R405), Y278 (≠ N408), D315 (= D445), M321 (= M451), L322 (= L452), A323 (= A453), A326 (= A456), Y354 (= Y492)
Query Sequence
>Ac3H11_4091 FitnessBrowser__acidovorax_3H11:Ac3H11_4091
MAIIDIKVPDIGDFAEVAIIEVLVKPGDTIKAEQSLITVESDKASMEIPSSHAGVVKELK
VKLGDKIAEGSVVLTLEVQGAGAAAPAPAAAPAPAVSEQKTASAPVQQAQVAINPVASSF
AGTADLDCDVLVLGGGPGGYSAAFRAADLGLKVVIVERYATLGGVCLNVGCIPSKALLHV
AAVMDEVSHMADLGVDFGAPAVNIDKLRGHKEKVIGKLTGGLAAMAKMRKVTTVRGYGAF
VGANHLEVEETTGTAQEKTGTKKVIAFKRAIIAAGSQAVRLPFMPDDPRVVDSTGALALK
EVPKRMLILGGGIIGLEMGTVYSTLGARLDVVEMMDGLMQGADRDLVKIWQKMNAKRFDN
IMLKTKTVGAKATPEGIEVTFAAAEEGGTAPAPQTYDLVLQAVGRTPNGKKIAADKAGVA
VTDRGFINVDIQMRTNVPHIFAIGDIVGQPMLAHKAVHEAHVAAEVIAGELQGNKELAAA
AFNARVIPSVAYTDPEVAWVGLTEDQAKAQGIKVKKGLFPWTASGRAIANGRDEGVTKLL
FDDSPEAHGHGKILGGGMVGTHAGDMIGEIALAIEMGADAVDIGKTIHPHPTLGESIGMA
AEIAHGSCTDVPPQKK
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