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Comparing YP_004142576.1 NCBI__GCF_000185905.1:YP_004142576.1 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)
1rx0A Crystal structure of isobutyryl-coa dehydrogenase complexed with substrate/ligand. (see paper)
56% identity, 96% coverage: 14:386/388 of query aligns to 10:382/384 of 1rx0A
- active site: L129 (= L133), T130 (= T134), G245 (= G249), E367 (= E371), R379 (= R383)
- binding flavin-adenine dinucleotide: Y127 (= Y131), L129 (= L133), T130 (= T134), G135 (= G139), S136 (= S140), F160 (= F164), I161 (= I165), S162 (= S166), W207 (= W211), R271 (= R275), F274 (= F278), L278 (≠ I282), N281 (≠ F285), L284 (= L288), Q340 (= Q344), M341 (≠ L345), G343 (= G347), G344 (= G348), Y345 (= Y349), L366 (= L370), S369 (≠ T373), E371 (= E375)
1rx0C Crystal structure of isobutyryl-coa dehydrogenase complexed with substrate/ligand. (see paper)
56% identity, 96% coverage: 14:386/388 of query aligns to 9:381/383 of 1rx0C
- active site: L128 (= L133), T129 (= T134), G244 (= G249), E366 (= E371), R378 (= R383)
- binding methacrylyl-coenzyme a: I93 (= I98), Y126 (= Y131), S135 (= S140), V238 (≠ M243), L241 (= L246), N242 (≠ D247), R245 (= R250), V316 (≠ G321), E366 (= E371), G367 (= G372), L375 (≠ I380), R378 (= R383)
- binding flavin-adenine dinucleotide: Y126 (= Y131), L128 (= L133), T129 (= T134), G134 (= G139), S135 (= S140), F159 (= F164), I160 (= I165), S161 (= S166), R270 (= R275), F273 (= F278), N280 (≠ F285), L283 (= L288), Q339 (= Q344), M340 (≠ L345), G342 (= G347), G343 (= G348), Y344 (= Y349), L365 (= L370), S368 (≠ T373), E370 (= E375)
Q9UKU7 Isobutyryl-CoA dehydrogenase, mitochondrial; IBDH; Activator-recruited cofactor 42 kDa component; ARC42; Acyl-CoA dehydrogenase family member 8; ACAD-8; EC 1.3.8.5 from Homo sapiens (Human) (see 3 papers)
55% identity, 99% coverage: 1:386/388 of query aligns to 31:413/415 of Q9UKU7
- G137 (= G110) to R: in IBDD; loss of protein solubility; complete loss of isobutyryl-CoA dehydrogenase activity; dbSNP:rs371449613
- 158:167 (vs. 131:140, 100% identical) binding in other chain
- S167 (= S140) binding substrate
- FIS 191:193 (= FIS 164:166) binding in other chain
- NGGR 274:277 (≠ DGGR 247:250) binding substrate
- R302 (= R275) binding FAD; to Q: in IBDD; no effect on localization to the mitochondrion; complete loss of isobutyryl-CoA dehydrogenase activity; loss of protein expression in patient cells; dbSNP:rs121908422
- NQ 312:313 (≠ FQ 285:286) binding FAD
- A320 (= A293) to T: in IBDD; decreased isobutyryl-CoA dehydrogenase activity; less than 20% of wild-type; dbSNP:rs200620279
- QMHGG 371:375 (≠ QLLGG 344:348) binding FAD
- SNE 400:402 (≠ TNE 373:375) binding in other chain
- R410 (= R383) binding substrate
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
42% identity, 97% coverage: 12:386/388 of query aligns to 1:377/378 of 5ol2F
- active site: L124 (= L133), T125 (= T134), G241 (= G249), G374 (≠ R383)
- binding calcium ion: E29 (≠ D39), E33 (≠ N43), R35 (≠ H45)
- binding coenzyme a persulfide: L238 (= L246), R242 (= R250), E362 (= E371), G363 (= G372)
- binding flavin-adenine dinucleotide: F122 (≠ Y131), L124 (= L133), T125 (= T134), P127 (= P136), T131 (≠ S140), F155 (= F164), I156 (= I165), T157 (≠ S166), E198 (= E206), R267 (= R275), F270 (= F278), L274 (≠ I282), F277 (= F285), Q335 (= Q344), L336 (= L345), G338 (= G347), G339 (= G348), Y361 (≠ L370), T364 (= T373), E366 (= E375)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
41% identity, 97% coverage: 12:386/388 of query aligns to 3:378/380 of 4l1fA
- active site: L125 (= L133), T126 (= T134), G242 (= G249), E363 (= E371), R375 (= R383)
- binding coenzyme a persulfide: T132 (≠ S140), H179 (≠ K186), F232 (= F239), M236 (= M243), E237 (≠ A244), L239 (= L246), D240 (= D247), R243 (= R250), Y362 (≠ L370), E363 (= E371), G364 (= G372), R375 (= R383)
- binding flavin-adenine dinucleotide: F123 (≠ Y131), L125 (= L133), T126 (= T134), G131 (= G139), T132 (≠ S140), F156 (= F164), I157 (= I165), T158 (≠ S166), R268 (= R275), Q270 (≠ A277), F271 (= F278), I275 (= I282), F278 (= F285), L281 (= L288), Q336 (= Q344), I337 (≠ L345), G340 (= G348), I358 (≠ V366), Y362 (≠ L370), T365 (= T373), Q367 (≠ E375)
- binding 1,3-propandiol: L5 (= L14), Q10 (≠ R19)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
42% identity, 97% coverage: 12:386/388 of query aligns to 3:377/379 of 1ukwB
- active site: L124 (= L133), S125 (≠ T134), T241 (≠ G249), E362 (= E371), R374 (= R383)
- binding cobalt (ii) ion: D145 (≠ G154), H146 (≠ D155)
- binding flavin-adenine dinucleotide: F122 (≠ Y131), L124 (= L133), S125 (≠ T134), G130 (= G139), S131 (= S140), W155 (≠ F164), S157 (= S166), K200 (= K208), L357 (≠ V366), Y361 (≠ L370), E362 (= E371), T364 (= T373), E366 (= E375), L370 (≠ V379)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
42% identity, 97% coverage: 12:386/388 of query aligns to 3:377/379 of 1ukwA
- active site: L124 (= L133), S125 (≠ T134), T241 (≠ G249), E362 (= E371), R374 (= R383)
- binding flavin-adenine dinucleotide: F122 (≠ Y131), L124 (= L133), S125 (≠ T134), G130 (= G139), S131 (= S140), W155 (≠ F164), S157 (= S166), L357 (≠ V366), Y361 (≠ L370), E362 (= E371), T364 (= T373), E366 (= E375), L370 (≠ V379)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
41% identity, 96% coverage: 16:387/388 of query aligns to 4:374/374 of 5lnxD
- active site: L122 (= L133), T123 (= T134), G239 (= G249), E358 (= E371), K370 (≠ R383)
- binding flavin-adenine dinucleotide: L122 (= L133), T123 (= T134), G128 (= G139), S129 (= S140), F153 (= F164), T155 (≠ S166), R265 (= R275), Q267 (≠ A277), F268 (= F278), I272 (= I282), N275 (≠ F285), I278 (≠ L288), Q331 (= Q344), I332 (≠ L345), G335 (= G348), Y357 (≠ L370), T360 (= T373), E362 (= E375)
7w0jE Acyl-coa dehydrogenase, tfu_1647
41% identity, 97% coverage: 12:386/388 of query aligns to 5:381/382 of 7w0jE
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3S,4S)-5-azanyl-2,3,4-tris(oxidanyl)pentyl] hydrogen phosphate: S127 (≠ T134), W157 (≠ F164), R270 (= R275), Q272 (≠ A277), F273 (= F278), I277 (= I282), F280 (= F285), I283 (≠ L288), Q339 (= Q344), L340 (= L345), G343 (= G348), Y365 (≠ L370), E366 (= E371), T368 (= T373), Q370 (≠ E375), I371 (= I376)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
41% identity, 97% coverage: 12:386/388 of query aligns to 4:380/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S140), T134 (≠ A142), R180 (vs. gap), R234 (≠ G240), L237 (≠ M243), R238 (≠ A244), L240 (= L246), D241 (= D247), R244 (= R250), E365 (= E371), G366 (= G372), R377 (= R383)
- binding flavin-adenine dinucleotide: Y123 (= Y131), L125 (= L133), S126 (≠ T134), G131 (= G139), S132 (= S140), W156 (≠ F164), I157 (= I165), T158 (≠ S166), I360 (≠ V366), T367 (= T373), Q369 (≠ E375)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
41% identity, 97% coverage: 12:386/388 of query aligns to 4:380/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (= Y131), L125 (= L133), S126 (≠ T134), G131 (= G139), S132 (= S140), W156 (≠ F164), I157 (= I165), T158 (≠ S166), I360 (≠ V366), Y364 (≠ L370), T367 (= T373), Q369 (≠ E375)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
40% identity, 96% coverage: 15:385/388 of query aligns to 7:378/378 of 4n5fA
- active site: L126 (= L133), T127 (= T134), G243 (= G249), E364 (= E371), R376 (= R383)
- binding dihydroflavine-adenine dinucleotide: L126 (= L133), T127 (= T134), G132 (= G139), S133 (= S140), F157 (= F164), T159 (≠ S166), T210 (= T216), Y363 (≠ L370), T366 (= T373), E368 (= E375), M372 (≠ V379)
2a1tC Structure of the human mcad:etf e165betaa complex (see paper)
38% identity, 97% coverage: 12:388/388 of query aligns to 6:385/388 of 2a1tC
- active site: V127 (≠ L133), T128 (= T134), T247 (≠ G249), E368 (= E371), R380 (= R383)
- binding flavin-adenine dinucleotide: Y125 (= Y131), V127 (≠ L133), T128 (= T134), G133 (= G139), S134 (= S140), Q155 (≠ T161), W158 (≠ F164), W158 (≠ F164), I159 (= I165), T160 (≠ S166), R273 (= R275), T275 (≠ A277), F276 (= F278), L280 (≠ I282), H283 (≠ F285), I286 (≠ L288), Q341 (= Q344), I342 (≠ L345), G345 (= G348), I363 (≠ V366), T370 (= T373), Q372 (≠ E375)
P11310 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; Medium chain acyl-CoA dehydrogenase; MCADH; EC 1.3.8.7 from Homo sapiens (Human) (see 16 papers)
38% identity, 97% coverage: 12:388/388 of query aligns to 39:418/421 of P11310
- Y67 (≠ W40) to H: in ACADMD; mild; dbSNP:rs121434280
- L86 (= L59) mutation to M: Strongly reduced rate of electron transfer to ETF.
- L98 (≠ S71) mutation to W: Strongly reduced rate of electron transfer to ETF.
- L100 (= L73) mutation to Y: Strongly reduced rate of electron transfer to ETF.
- I108 (= I81) mutation to M: Strongly reduced rate of electron transfer to ETF.
- P132 (≠ M105) to R: in a breast cancer sample; somatic mutation; dbSNP:rs875989854
- 158:167 (vs. 131:140, 80% identical) binding in other chain
- S167 (= S140) binding octanoyl-CoA
- W191 (≠ F164) mutation to A: Loss of electron transfer to ETF.; mutation to F: Reduces rate of electron transfer to ETF about six-fold.
- WIT 191:193 (≠ FIS 164:166) binding in other chain
- T193 (≠ S166) to A: in ACADMD; the thermostability is markedly decreased; dbSNP:rs121434279
- E237 (= E206) mutation to A: Strongly reduced rate of electron transfer to ETF.
- D278 (= D247) binding octanoyl-CoA
- T280 (≠ G249) mutation to E: Narrower substrate specificity. Changed substrate specificity towards longer acyl chains; when associated with G-401. Loss of acyl-CoA dehydrogenase activity; when associated with T-410.
- R281 (= R250) binding octanoyl-CoA; to T: in ACADMD; mild clinical phenotype; dbSNP:rs121434282
- RKT 306:308 (≠ RKA 275:277) binding FAD
- HQ 316:317 (≠ FQ 285:286) binding in other chain
- K329 (≠ E298) to E: in ACADMD; may alter splicing; decreased fatty acid beta-oxidation; dbSNP:rs77931234
- QILGG 374:378 (≠ QLLGG 344:348) binding FAD
- E384 (≠ D354) mutation to A: Reduces rate of electron transfer to ETF three-fold.; mutation to Q: Reduces rate of electron transfer to ETF two-fold.
- E401 (= E371) active site, Proton acceptor; binding octanoyl-CoA; mutation to G: Changed substrate specificity towards longer acyl chains; when associated with E-280.; mutation to Q: Loss of acyl-CoA dehydrogenase activity.; mutation to T: Loss of acyl-CoA dehydrogenase activity; when associated with E-280.
- EGTSQ 401:405 (≠ EGTNE 371:375) binding in other chain
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
37% identity, 97% coverage: 12:388/388 of query aligns to 4:383/385 of 3mdeA
- active site: V125 (≠ L133), T126 (= T134), T245 (≠ G249), E366 (= E371), R378 (= R383)
- binding octanoyl-coenzyme a: T86 (≠ S94), E89 (≠ S97), L93 (≠ M101), S132 (= S140), V134 (≠ A142), S181 (≠ P185), F235 (= F239), M239 (= M243), F242 (≠ L246), R314 (≠ P318), Y365 (≠ L370), E366 (= E371), G367 (= G372)
- binding flavin-adenine dinucleotide: Y123 (= Y131), V125 (≠ L133), T126 (= T134), G131 (= G139), S132 (= S140), W156 (≠ F164), I157 (= I165), T158 (≠ S166), R271 (= R275), T273 (≠ A277), F274 (= F278), L278 (≠ I282), H281 (≠ F285), Q339 (= Q344), V340 (≠ L345), G343 (= G348), I361 (≠ V366), T368 (= T373), Q370 (≠ E375)
3mddA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
37% identity, 97% coverage: 12:388/388 of query aligns to 4:383/385 of 3mddA
- active site: V125 (≠ L133), T126 (= T134), T245 (≠ G249), E366 (= E371), R378 (= R383)
- binding flavin-adenine dinucleotide: Y123 (= Y131), T126 (= T134), G131 (= G139), S132 (= S140), W156 (≠ F164), T158 (≠ S166), R271 (= R275), T273 (≠ A277), F274 (= F278), H281 (≠ F285), Q339 (= Q344), V340 (≠ L345), G343 (= G348), I361 (≠ V366), T368 (= T373), Q370 (≠ E375)
1udyA Medium-chain acyl-coa dehydrogenase with 3-thiaoctanoyl-coa (see paper)
37% identity, 97% coverage: 12:388/388 of query aligns to 4:383/385 of 1udyA
- active site: V125 (≠ L133), T126 (= T134), T245 (≠ G249), E366 (= E371), R378 (= R383)
- binding 3-thiaoctanoyl-coenzyme a: L93 (≠ M101), Y123 (= Y131), S132 (= S140), S181 (≠ P185), F235 (= F239), M239 (= M243), F242 (≠ L246), V249 (≠ I253), R314 (≠ P318), Y365 (≠ L370), E366 (= E371), G367 (= G372), I371 (= I376), I375 (= I380)
- binding flavin-adenine dinucleotide: Y123 (= Y131), T126 (= T134), G131 (= G139), S132 (= S140), W156 (≠ F164), T158 (≠ S166), T273 (≠ A277), F274 (= F278), Q339 (= Q344), V340 (≠ L345), G343 (= G348), T368 (= T373), Q370 (≠ E375)
P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 from Sus scrofa (Pig) (see 2 papers)
37% identity, 97% coverage: 12:388/388 of query aligns to 39:418/421 of P41367
- 158:167 (vs. 131:140, 80% identical) binding in other chain
- S167 (= S140) binding octanoyl-CoA
- WIT 191:193 (≠ FIS 164:166) binding in other chain
- S216 (≠ P185) binding octanoyl-CoA
- D278 (= D247) binding octanoyl-CoA
- R281 (= R250) binding octanoyl-CoA
- RKT 306:308 (≠ RKA 275:277) binding FAD
- HQ 316:317 (≠ FQ 285:286) binding in other chain
- R349 (≠ P318) binding octanoyl-CoA
- T351 (≠ A320) binding octanoyl-CoA
- QVFGG 374:378 (≠ QLLGG 344:348) binding FAD
- E401 (= E371) active site, Proton acceptor; binding octanoyl-CoA
- GTAQ 402:405 (≠ GTNE 372:375) binding in other chain
1egcA Structure of t255e, e376g mutant of human medium chain acyl-coa dehydrogenase complexed with octanoyl-coa (see paper)
37% identity, 97% coverage: 12:388/388 of query aligns to 5:384/387 of 1egcA
- active site: V126 (≠ L133), T127 (= T134), E246 (≠ G249), G367 (≠ E371), R379 (= R383)
- binding octanoyl-coenzyme a: E90 (≠ S97), L94 (≠ M101), Y124 (= Y131), S133 (= S140), V135 (≠ A142), N182 (≠ P185), F236 (= F239), M240 (= M243), F243 (≠ L246), D244 (= D247), R247 (= R250), Y366 (≠ L370), G367 (≠ E371), G368 (= G372)
- binding flavin-adenine dinucleotide: Y124 (= Y131), V126 (≠ L133), T127 (= T134), G132 (= G139), S133 (= S140), W157 (≠ F164), T159 (≠ S166), R272 (= R275), T274 (≠ A277), F275 (= F278), L279 (≠ I282), H282 (≠ F285), I285 (≠ L288), Q340 (= Q344), I341 (≠ L345), G344 (= G348), I362 (≠ V366), I365 (= I369), Y366 (≠ L370), T369 (= T373), Q371 (≠ E375)
3pfdC Crystal structure of an acyl-coa dehydrogenase from mycobacterium thermoresistibile bound to reduced flavin adenine dinucleotide solved by combined iodide ion sad mr (see paper)
38% identity, 95% coverage: 20:386/388 of query aligns to 3:368/369 of 3pfdC
- active site: L116 (= L133), S117 (≠ T134), T233 (≠ G249), E353 (= E371), R365 (= R383)
- binding dihydroflavine-adenine dinucleotide: Y114 (= Y131), L116 (= L133), S117 (≠ T134), G122 (= G139), S123 (= S140), W147 (≠ F164), I148 (= I165), T149 (≠ S166), R259 (= R275), F262 (= F278), V266 (≠ I282), N269 (≠ F285), Q326 (= Q344), L327 (= L345), G330 (= G348), I348 (≠ V366), Y352 (≠ L370), T355 (= T373), Q357 (≠ E375)
Query Sequence
>YP_004142576.1 NCBI__GCF_000185905.1:YP_004142576.1
MDAAVDASTSQFELNEEQRAIQEMAQAFAADRVAPNALDWDRNKHFPADVIRETGPLGLG
GIYIRDDVGGSALGRLDAVLIFEALSHADPAFSSFISIHNMVASMIDRFGNDEQRQRFLP
KLTSMEWLASYCLTEPGSGSDAAALKTRAVKSGGDYVLNGTKQFISGAGDSDVYAVMVRT
GADGPKGISTIVVPRDAPGLSFGANEHKMGWHMQSTRQVIFEDCKVPAENLLSDEGAGFG
IAMAGLDGGRLNIAACSLGGAQSALDKALSYTAERKAFGSKINQFQALQFRLADMETELQ
AARIFLYAAASKLDRKAPDAGKWSAMAKRFVTDTGFNVANDALQLLGGYGYLHDYGIEKL
VRDLRVHQILEGTNEIMRVIIARALIGR
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