SitesBLAST
Comparing Ga0059261_0740 FitnessBrowser__Korea:Ga0059261_0740 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
5ez3B Crystal structure acyl-coa dehydrogenase from brucella melitensis in complex with fad
48% identity, 98% coverage: 12:540/540 of query aligns to 2:541/541 of 5ez3B
- active site: M181 (= M188), T182 (= T189), T295 (= T304), E423 (= E426), R435 (= R438)
- binding flavin-adenine dinucleotide: M179 (= M186), M181 (= M188), T182 (= T189), G186 (= G193), G187 (= G194), T188 (≠ S195), F213 (= F221), M214 (≠ C222), S215 (= S223), K257 (= K266), S265 (= S274), R321 (= R330), V323 (≠ A332), F324 (= F333), L328 (= L337), Q331 (= Q340), M334 (= M343), E396 (= E399), C397 (= C400), G399 (= G402), G400 (= G403), Y403 (= Y406), V418 (≠ L421), I421 (= I424), W422 (= W425), E423 (= E426), S425 (= S428), N427 (= N430), V428 (= V431), L431 (= L434)
3u33A Crystal structure of the e. Coli adaptive response protein aidb in the space group p3(2) (see paper)
44% identity, 94% coverage: 12:517/540 of query aligns to 5:519/540 of 3u33A
- active site: M184 (= M188), T185 (= T189), T298 (= T304), E425 (= E426), R437 (= R438)
- binding flavin-adenine dinucleotide: M182 (= M186), G183 (≠ A187), M184 (= M188), T185 (= T189), G189 (= G193), G190 (= G194), S191 (= S195), F216 (= F221), F217 (≠ C222), S218 (= S223), K260 (= K266), S268 (= S274), R324 (= R330), V326 (≠ A332), F327 (= F333), L331 (= L337), Q334 (= Q340), M337 (= M343), E398 (= E399), V399 (≠ C400), G401 (= G402), G402 (= G403), Y405 (= Y406), V420 (≠ L421), I423 (= I424), W424 (= W425), E425 (= E426), G426 (= G427), S427 (= S428), N429 (= N430), I430 (≠ V431), L433 (= L434)
P33224 Putative acyl-CoA dehydrogenase AidB; EC 1.3.99.- from Escherichia coli (strain K12) (see paper)
44% identity, 94% coverage: 12:517/540 of query aligns to 5:519/541 of P33224
- 182:191 (vs. 186:195, 90% identical) binding
- T185 (= T189) binding
- S191 (= S195) binding
- FFS 216:218 (≠ FCS 221:223) binding
- S218 (= S223) binding
- 423:433 (vs. 424:434, 73% identical) binding
- N429 (= N430) binding
- R437 (= R438) mutation to Q: Does not affect DNA binding affinity.
- R518 (= R516) mutation to Q: Reduces DNA binding affinity.
4y9jB Crystal structure of caenorhabditis elegans acdh-11 in complex with c11-coa (see paper)
32% identity, 76% coverage: 31:443/540 of query aligns to 35:464/593 of 4y9jB
- active site: M190 (= M188), T191 (= T189), T315 (= T304), E446 (= E426), R458 (= R438)
- binding flavin-adenine dinucleotide: Q188 (≠ M186), W189 (≠ A187), M190 (= M188), T191 (= T189), G195 (= G193), G196 (= G194), S197 (= S195), F223 (= F221), S224 (≠ C222), S225 (= S223), T285 (≠ S274), R341 (= R330), V343 (≠ A332), F344 (= F333), Q348 (≠ L337), W351 (≠ Q340), H354 (≠ M343), E419 (= E399), C420 (= C400), F421 (≠ H401), G422 (= G402), G423 (= G403), Y426 (= Y406), I444 (= I424), W445 (= W425), T448 (≠ S428), N450 (= N430), V451 (= V431), L454 (= L434)
- binding S-{(3S,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} undecanethioate: S143 (= S137), C144 (= C138), A147 (≠ T141), M148 (= M142), Q188 (≠ M186), M190 (= M188), G196 (= G194), S197 (= S195), S249 (≠ Q237), R303 (= R292), V305 (= V294), A306 (= A295), S309 (≠ I298), L312 (≠ V301), N313 (≠ Q302), R316 (= R305), H318 (≠ D307), N319 (≠ C308), A322 (≠ G311), R396 (= R376), W445 (= W425), E446 (= E426), G447 (= G427), V451 (= V431), D455 (= D435), R458 (= R438)
Q9XWZ2 Acyl-CoA dehydrogenase family member 11; EC 1.3.99.- from Caenorhabditis elegans (see paper)
32% identity, 76% coverage: 31:443/540 of query aligns to 53:482/617 of Q9XWZ2
- E91 (≠ N70) mutation to K: In n5655; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- S156 (≠ A132) mutation to F: In n5657; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G158 (≠ S134) mutation to R: In n5661; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G214 (= G194) mutation to E: In n5879; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G443 (= G405) mutation to R: In n5877; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- R455 (= R417) mutation to H: In n5876; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
6sdaB Bd2924 c10 acyl-coenzymea bound form (see paper)
31% identity, 79% coverage: 26:454/540 of query aligns to 11:454/503 of 6sdaB
- active site: M171 (= M188), T172 (= T189), T296 (= T304), R439 (= R438)
- binding flavin-adenine dinucleotide: Q169 (≠ M186), W170 (≠ A187), M171 (= M188), T172 (= T189), G176 (= G193), G177 (= G194), S178 (= S195), F208 (= F221), T209 (≠ C222), T266 (≠ S274), R322 (= R330), A324 (= A332), F325 (= F333), L329 (= L337), H332 (≠ Q340), H335 (≠ M343), E400 (= E399), M401 (≠ C400), G403 (= G402), G404 (= G403), Y407 (= Y406), W426 (= W425), T429 (≠ S428), N431 (= N430), V432 (= V431), L435 (= L434)
- binding decanoyl-CoA: S127 (= S137), C128 (= C138), A131 (≠ T141), G177 (= G194), S178 (= S195), S230 (vs. gap), R231 (vs. gap), V286 (= V294), K287 (≠ A295), A290 (≠ I298), L293 (≠ V301), N294 (≠ Q302), T296 (= T304), R297 (= R305), N300 (≠ C308), R377 (= R376), W426 (= W425), E427 (= E426), V432 (= V431), D436 (= D435), R439 (= R438)
6sd8X Bd2924 apo-form (see paper)
31% identity, 79% coverage: 26:454/540 of query aligns to 11:454/503 of 6sd8X
- active site: M171 (= M188), T172 (= T189), T296 (= T304), R439 (= R438)
- binding flavin-adenine dinucleotide: Q169 (≠ M186), W170 (≠ A187), M171 (= M188), T172 (= T189), G176 (= G193), G177 (= G194), S178 (= S195), F208 (= F221), T209 (≠ C222), K258 (= K266), T266 (≠ S274), R322 (= R330), A324 (= A332), F325 (= F333), L329 (= L337), H332 (≠ Q340), H335 (≠ M343), E400 (= E399), M401 (≠ C400), G403 (= G402), G404 (= G403), Y407 (= Y406), V422 (≠ L421), I425 (= I424), W426 (= W425), T429 (≠ S428), N431 (= N430), V432 (= V431), L435 (= L434)
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
26% identity, 66% coverage: 86:440/540 of query aligns to 28:375/378 of 7p9xA
- binding 1-monoenoyl-CoA: L82 (≠ V147), I85 (≠ L150), D89 (≠ E154), S129 (= S195), L131 (≠ V197), L132 (≠ R198), T155 (≠ S223), S175 (≠ Q237), K176 (≠ G238), F229 (≠ V294), M233 (≠ I298), L236 (≠ V301), R240 (= R305), Y360 (≠ W425), T361 (≠ E426), G362 (= G427), I366 (≠ V431), M369 (≠ L434), R373 (= R438)
- binding flavin-adenine dinucleotide: L120 (≠ M186), A121 (= A187), A122 (≠ M188), T123 (= T189), G128 (= G194), S129 (= S195), F153 (= F221), I154 (≠ C222), T155 (≠ S223), K198 (= K266), N206 (≠ S274), L356 (= L421), Y360 (≠ W425), G362 (= G427), T363 (≠ S428), Q365 (≠ N430), I366 (≠ V431)
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
26% identity, 66% coverage: 86:440/540 of query aligns to 30:377/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: L84 (≠ V147), I87 (≠ L150), D91 (≠ E154), S131 (= S195), L133 (≠ V197), L134 (≠ R198), T157 (≠ S223), S177 (≠ Q237), K178 (≠ G238), F231 (≠ V294), M235 (≠ I298), L238 (≠ V301), N241 (≠ T304), R242 (= R305), Y362 (≠ W425), T363 (≠ E426), G364 (= G427), I368 (≠ V431), R375 (= R438)
- binding flavin-adenine dinucleotide: L122 (≠ M186), A124 (≠ M188), T125 (= T189), G130 (= G194), S131 (= S195), F155 (= F221), I156 (≠ C222), T157 (≠ S223), K200 (= K266), N208 (≠ S274), L358 (= L421), Y362 (≠ W425), G364 (= G427), T365 (≠ S428), Q367 (≠ N430), I368 (≠ V431)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
29% identity, 49% coverage: 174:440/540 of query aligns to 111:376/379 of 1ukwB