SitesBLAST
Comparing GFF65 FitnessBrowser__Marino:GFF65 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)
6cmzA 2.3 angstrom resolution crystal structure of dihydrolipoamide dehydrogenase from burkholderia cenocepacia in complex with fad and NAD
56% identity, 98% coverage: 7:460/461 of query aligns to 5:461/462 of 6cmzA
- active site: C42 (= C44), C47 (= C49), S50 (= S52), Y184 (= Y187), E188 (= E191), H441 (= H440), E446 (= E445)
- binding flavin-adenine dinucleotide: G11 (= G13), G13 (= G15), P14 (= P16), E34 (= E36), R35 (≠ A37), G40 (= G42), T41 (= T43), C42 (= C44), G46 (= G48), C47 (= C49), K51 (= K53), E116 (≠ W119), A117 (≠ G120), T145 (= T148), G146 (= G149), V180 (≠ I183), G181 (= G184), Y184 (= Y187), I185 (= I188), E204 (= E207), V268 (= V270), R270 (= R272), R273 (≠ V275), F277 (≠ W279), R289 (= R291), G308 (= G310), D309 (= D311), M315 (= M317), L316 (= L318), A317 (= A319), H318 (= H320)
- binding flavin mononucleotide: L152 (= L155), P153 (= P156)
6cmzB 2.3 angstrom resolution crystal structure of dihydrolipoamide dehydrogenase from burkholderia cenocepacia in complex with fad and NAD
56% identity, 98% coverage: 7:458/461 of query aligns to 5:459/459 of 6cmzB
- active site: C42 (= C44), C47 (= C49), S50 (= S52), Y184 (= Y187), E188 (= E191), H441 (= H440), E446 (= E445)
- binding adenosine-5'-diphosphate: V150 (= V153), L152 (= L155), G181 (= G184), G183 (= G186), A205 (≠ S208), V268 (= V270), G269 (= G271)
- binding flavin-adenine dinucleotide: G11 (= G13), G13 (= G15), P14 (= P16), E34 (= E36), R35 (≠ A37), T41 (= T43), C42 (= C44), G46 (= G48), C47 (= C49), K51 (= K53), E116 (≠ W119), A117 (≠ G120), T145 (= T148), G146 (= G149), S164 (= S167), Y184 (= Y187), I185 (= I188), R270 (= R272), F277 (≠ W279), G308 (= G310), D309 (= D311), M315 (= M317), L316 (= L318), A317 (= A319), H318 (= H320)
P09063 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of branched-chain alpha-keto acid dehydrogenase complex; LPD-Val; EC 1.8.1.4 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see paper)
55% identity, 100% coverage: 1:460/461 of query aligns to 1:458/459 of P09063
- 36:44 (vs. 36:44, 67% identical) binding
- C44 (= C44) modified: Disulfide link with 49, Redox-active
- C49 (= C49) modified: Disulfide link with 44, Redox-active
- K53 (= K53) binding
- A119 (≠ G120) binding
- A142 (= A147) binding
- GGGYI 179:183 (≠ GAGYI 184:188) binding
- Y182 (= Y187) binding
- E202 (= E207) binding
- V236 (≠ A241) binding
- AVGR 264:267 (≠ TVGR 269:272) binding
- D306 (= D311) binding
- M312 (= M317) binding
- A314 (= A319) binding
1lvlA The refined structure of pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45 angstroms resolution (see paper)
55% identity, 100% coverage: 2:460/461 of query aligns to 1:457/458 of 1lvlA
- active site: P15 (= P16), L39 (= L40), C43 (= C44), C48 (= C49), S51 (= S52), S79 (≠ E80), P80 (= P81), Y181 (= Y187), E185 (= E191), M317 (≠ S323), H435 (≠ Q438), H437 (= H440), E442 (= E445)
- binding flavin-adenine dinucleotide: I11 (≠ V12), G12 (= G13), E35 (= E36), G36 (≠ A37), G41 (= G42), T42 (= T43), C43 (= C44), G47 (= G48), C48 (= C49), K52 (= K53), W117 (= W119), A118 (≠ G120), A141 (= A147), T142 (= T148), G143 (= G149), Y181 (= Y187), R266 (= R272), R269 (≠ V275), D305 (= D311), L312 (= L318), A313 (= A319), H314 (= H320)
- binding nicotinamide-adenine-dinucleotide: V177 (≠ I183), G178 (= G184), Y181 (= Y187), I182 (= I188), E201 (= E207), A263 (≠ T269), V264 (= V270), G265 (= G271), R266 (= R272), E309 (= E315), M311 (= M317)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
45% identity, 99% coverage: 5:460/461 of query aligns to 8:466/470 of P11959
- 39:47 (vs. 36:44, 56% identical) binding
- K56 (= K53) binding
- D314 (= D311) binding
- A322 (= A319) binding
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
45% identity, 97% coverage: 5:451/461 of query aligns to 2:451/455 of 1ebdA
- active site: P13 (= P16), L37 (= L40), C41 (= C44), C46 (= C49), S49 (= S52), N74 (≠ P81), V75 (≠ P82), Y180 (= Y187), E184 (= E191), S320 (= S323), H438 (≠ Q438), H440 (= H440), E445 (= E445)
- binding flavin-adenine dinucleotide: G10 (= G13), G12 (= G15), P13 (= P16), V32 (= V35), E33 (= E36), K34 (≠ A37), G39 (= G42), V40 (≠ T43), C41 (= C44), G45 (= G48), C46 (= C49), K50 (= K53), E112 (≠ W119), A113 (≠ G120), T141 (= T148), G142 (= G149), Y180 (= Y187), I181 (= I188), R268 (= R272), D308 (= D311), A314 (≠ M317), L315 (= L318), A316 (= A319)
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, 99% coverage: 6:460/461 of query aligns to 3:470/472 of 3ladA
- active site: L44 (= L40), C48 (= C44), C53 (= C49), S56 (= S52), V190 (≠ Y187), E194 (= E191), F448 (≠ Q438), H450 (= H440), E455 (= E445)
- binding flavin-adenine dinucleotide: I9 (≠ V12), G10 (= G13), G12 (= G15), P13 (= P16), E33 (= E36), K34 (≠ A37), G46 (= G42), T47 (= T43), C48 (= C44), G52 (= G48), C53 (= C49), H120 (≠ W119), G121 (= G120), A149 (= A147), S150 (≠ T148), G151 (= G149), I191 (= I188), R278 (= R272), D318 (= D311), L325 (= L318), A326 (= A319)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
43% identity, 99% coverage: 6:460/461 of query aligns to 4:471/477 of P18925
- 34:49 (vs. 36:44, 38% identical) binding
- C49 (= C44) modified: Disulfide link with 54, Redox-active
- C54 (= C49) modified: Disulfide link with 49, Redox-active
- K58 (= K53) binding
- D319 (= D311) binding
- A327 (= A319) binding
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)
41% identity, 97% coverage: 1:445/461 of query aligns to 1:450/474 of P0A9P0
- M1 (= M1) modified: Initiator methionine, Removed
- K220 (≠ E222) modified: N6-acetyllysine
4jdrA Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli (see paper)
41% identity, 96% coverage: 2:445/461 of query aligns to 1:449/471 of 4jdrA
- active site: P15 (= P16), L40 (= L40), C44 (= C44), C49 (= C49), S52 (= S52), E77 (= E80), P78 (= P81), I184 (≠ Y187), E188 (= E191), V324 (≠ S323), H442 (≠ Q438), H444 (= H440), E449 (= E445)
- binding flavin-adenine dinucleotide: G12 (= G13), G14 (= G15), P15 (= P16), A16 (≠ G17), E35 (= E36), R36 (vs. gap), Y37 (≠ A37), V43 (≠ T43), C44 (= C44), G48 (= G48), C49 (= C49), K53 (= K53), L115 (≠ W119), G116 (= G120), A144 (≠ T148), G145 (= G149), I185 (= I188), G311 (= G310), D312 (= D311), M318 (= M317), L319 (= L318), A320 (= A319), H321 (= H320)
Sites not aligning to the query:
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
42% identity, 98% coverage: 9:460/461 of query aligns to 9:469/470 of 6uziC
- active site: C45 (= C44), C50 (= C49), S53 (= S52), V187 (≠ Y187), E191 (= E191), H448 (= H440), E453 (= E445)
- binding flavin-adenine dinucleotide: I12 (≠ V12), G13 (= G13), G15 (= G15), P16 (= P16), G17 (= G17), E36 (= E36), K37 (≠ A37), G43 (= G42), T44 (= T43), C45 (= C44), G49 (= G48), C50 (= C49), S53 (= S52), K54 (= K53), V117 (≠ W119), G118 (= G120), T147 (= T148), G148 (= G149), I188 (= I188), R276 (= R272), D316 (= D311), M322 (= M317), L323 (= L318), A324 (= A319)
- binding zinc ion: H448 (= H440), E453 (= E445)
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
42% identity, 99% coverage: 6:460/461 of query aligns to 4:471/475 of 6awaA
- active site: L45 (= L40), C49 (= C44), C54 (= C49), S57 (= S52), V191 (≠ Y187), E195 (= E191), F449 (≠ Q438), H451 (= H440), E456 (= E445)
- binding adenosine monophosphate: I187 (= I183), E211 (= E207), A212 (≠ S208), L213 (≠ S209), V245 (≠ A241), V277 (= V270)
- binding flavin-adenine dinucleotide: I10 (≠ V12), G13 (= G15), P14 (= P16), G15 (= G17), E34 (= E36), K35 (≠ A37), T48 (= T43), C49 (= C44), G53 (= G48), C54 (= C49), K58 (= K53), H121 (≠ W119), G122 (= G120), S151 (≠ T148), G152 (= G149), I192 (= I188), R279 (= R272), G318 (= G310), D319 (= D311), M325 (= M317), L326 (= L318), A327 (= A319), Y358 (≠ F350)
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)
41% identity, 99% coverage: 6:460/461 of query aligns to 4:471/478 of P14218
- 34:49 (vs. 36:44, 38% identical) binding
- C49 (= C44) modified: Disulfide link with 54, Redox-active
- C54 (= C49) modified: Disulfide link with 49, Redox-active
- K58 (= K53) binding
- G122 (= G120) binding
- D319 (= D311) binding
- A327 (= A319) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
41% identity, 99% coverage: 6:460/461 of query aligns to 2:469/472 of 5u8vA
- active site: P12 (= P16), L43 (= L40), C47 (= C44), C52 (= C49), S55 (= S52), G81 (≠ P81), V82 (≠ P82), V189 (≠ Y187), E193 (= E191), S329 (= S323), F447 (≠ Q438), H449 (= H440), E454 (= E445)
- binding flavin-adenine dinucleotide: I8 (≠ V12), G11 (= G15), P12 (= P16), G13 (= G17), E32 (= E36), G45 (= G42), T46 (= T43), C47 (= C44), G51 (= G48), C52 (= C49), K56 (= K53), H119 (≠ W119), G120 (= G120), A148 (= A147), S149 (≠ T148), G150 (= G149), S169 (= S167), I190 (= I188), R277 (= R272), G316 (= G310), D317 (= D311), M323 (= M317), L324 (= L318), A325 (= A319), H326 (= H320), H449 (= H440), P450 (= P441)
- binding nicotinamide-adenine-dinucleotide: I185 (= I183), G186 (= G184), G188 (= G186), V189 (≠ Y187), I190 (= I188), L208 (≠ V206), E209 (= E207), A210 (≠ S208), V243 (≠ A241), V275 (= V270), G276 (= G271)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
41% identity, 99% coverage: 6:460/461 of query aligns to 6:473/477 of 5u8uD
- active site: P16 (= P16), L47 (= L40), C51 (= C44), C56 (= C49), S59 (= S52), G85 (≠ P81), V86 (≠ P82), V193 (≠ Y187), E197 (= E191), S333 (= S323), F451 (≠ Q438), H453 (= H440), E458 (= E445)
- binding flavin-adenine dinucleotide: I12 (≠ V12), G15 (= G15), P16 (= P16), G17 (= G17), E36 (= E36), K37 (≠ A37), G49 (= G42), T50 (= T43), C51 (= C44), G55 (= G48), C56 (= C49), K60 (= K53), H123 (≠ W119), G124 (= G120), A152 (= A147), S153 (≠ T148), G154 (= G149), I194 (= I188), R281 (= R272), G320 (= G310), D321 (= D311), M327 (= M317), L328 (= L318), A329 (= A319), H330 (= H320), H453 (= H440), P454 (= P441)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
41% identity, 99% coverage: 6:460/461 of query aligns to 3:470/473 of 5u8wA
- active site: P13 (= P16), L44 (= L40), C48 (= C44), C53 (= C49), S56 (= S52), G82 (≠ P81), V83 (≠ P82), V190 (≠ Y187), E194 (= E191), S330 (= S323), F448 (≠ Q438), H450 (= H440), E455 (= E445)
- binding flavin-adenine dinucleotide: I9 (≠ V12), G12 (= G15), P13 (= P16), G14 (= G17), E33 (= E36), K34 (≠ A37), G46 (= G42), T47 (= T43), C48 (= C44), G52 (= G48), C53 (= C49), K57 (= K53), H120 (≠ W119), G121 (= G120), A149 (= A147), S150 (≠ T148), G151 (= G149), S170 (= S167), G317 (= G310), D318 (= D311), M324 (= M317), L325 (= L318), A326 (= A319), H327 (= H320), Y357 (≠ F350), H450 (= H440), P451 (= P441)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I183), G189 (= G186), V190 (≠ Y187), I191 (= I188), E194 (= E191), E210 (= E207), A211 (≠ S208), L212 (≠ S209), A275 (≠ T269), V276 (= V270), G277 (= G271), R278 (= R272), M324 (= M317), L325 (= L318), V355 (= V348), Y357 (≠ F350)
Sites not aligning to the query:
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)
39% identity, 98% coverage: 9:460/461 of query aligns to 40:500/501 of P31023
- 67:76 (vs. 36:44, 60% identical) binding
- C76 (= C44) modified: Disulfide link with 81, Redox-active
- C81 (= C49) modified: Disulfide link with 76, Redox-active
- G149 (= G120) binding
- D348 (= D311) binding
- MLAH 354:357 (= MLAH 317:320) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
38% identity, 96% coverage: 19:460/461 of query aligns to 16:466/467 of 1dxlA
- active site: L38 (= L40), C42 (= C44), C47 (= C49), S50 (= S52), Y184 (= Y187), E188 (= E191), H444 (≠ Q438), H446 (= H440), E451 (= E445)
- binding flavin-adenine dinucleotide: E33 (= E36), K34 (≠ A37), R35 (≠ D38), G40 (= G42), T41 (= T43), C42 (= C44), G46 (= G48), C47 (= C49), K51 (= K53), Y114 (≠ W119), G115 (= G120), T144 (= T148), G145 (= G149), Y184 (= Y187), I185 (= I188), R274 (= R272), D314 (= D311), M320 (= M317), L321 (= L318), A322 (= A319), H323 (= H320)
Sites not aligning to the query:
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
40% identity, 98% coverage: 9:460/461 of query aligns to 4:454/455 of 2yquB
- active site: P11 (= P16), L36 (= L40), C40 (= C44), C45 (= C49), S48 (= S52), G72 (≠ P81), V73 (≠ P82), V177 (≠ Y187), E181 (= E191), S314 (= S323), H432 (≠ Q438), H434 (= H440), E439 (= E445)
- binding carbonate ion: A310 (= A319), S314 (= S323), S423 (≠ T429), D426 (= D432)
- binding flavin-adenine dinucleotide: G8 (= G13), G10 (= G15), P11 (= P16), G12 (= G17), E31 (= E36), K32 (≠ A37), G38 (= G42), T39 (= T43), C40 (= C44), R42 (≠ T46), G44 (= G48), C45 (= C49), K49 (= K53), T110 (≠ W119), A111 (≠ G120), T137 (= T148), G138 (= G149), I178 (= I188), Y265 (≠ V275), G301 (= G310), D302 (= D311), M308 (= M317), L309 (= L318), A310 (= A319), H311 (= H320)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
40% identity, 98% coverage: 9:460/461 of query aligns to 4:454/455 of 2yquA
- active site: P11 (= P16), L36 (= L40), C40 (= C44), C45 (= C49), S48 (= S52), G72 (≠ P81), V73 (≠ P82), V177 (≠ Y187), E181 (= E191), S314 (= S323), H432 (≠ Q438), H434 (= H440), E439 (= E445)
- binding flavin-adenine dinucleotide: G8 (= G13), G10 (= G15), P11 (= P16), G12 (= G17), E31 (= E36), K32 (≠ A37), G38 (= G42), T39 (= T43), C40 (= C44), R42 (≠ T46), G44 (= G48), C45 (= C49), K49 (= K53), T110 (≠ W119), A111 (≠ G120), T137 (= T148), G138 (= G149), S157 (= S167), I178 (= I188), Y265 (≠ V275), G301 (= G310), D302 (= D311), M308 (= M317), L309 (= L318), A310 (= A319)
Query Sequence
>GFF65 FitnessBrowser__Marino:GFF65
MSEVIKTKVLVVGGGPGGYVAAIRCGQLGLDTVLVEADQLGGTCLTRGCIPSKAMIHAAS
EFSAMMKAASKPHLGISLSEPPKVDLAATVDWKDSIVKRLNTGVAALLKRAKVKVVKGWG
TFSDAKTCNVETADGVITIQSEHVILATGSAPVELPFLPLGGKVISSTEALSLPDVPSKL
VVIGAGYIGLELGIAYAKLGSDVTIVESSDRILPLYDEALVEPVRRWLDESAVKLHLNAR
ALGERDGGLAVELEGGSETVLPADNILVTVGRKPVTQGWGLENMALDMDGRYVRVDEQCA
TSMKNVWAIGDLVGEPMLAHKASAQGEVVAEVIAGKRRRFDPVAIPAVCFTEPEIVSVGA
EPSLAGTVTGVFPVAANGRALSMDAGDNGGFVRVVAHSETHRILGVQAVGTHISELTAAF
VTAVEMGATVDDIEGMIQAHPTLGEMFHEASLKILGHAIHA
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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