SitesBLAST
Comparing WP_052664505.1 NCBI__GCF_000969705.1:WP_052664505.1 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)
4irnA Crystal structure of the prolyl acyl carrier protein oxidase anab (see paper)
40% identity, 98% coverage: 6:381/383 of query aligns to 3:376/378 of 4irnA
- active site: A124 (≠ I127), T125 (= T128), E241 (= E246), S362 (≠ G367), K374 (≠ R379)
- binding flavin-adenine dinucleotide: H122 (≠ F125), A124 (≠ I127), T125 (= T128), G130 (= G133), S131 (= S134), Y155 (≠ F158), T157 (= T160), H267 (≠ R272), Q269 (≠ A274), F270 (= F275), I274 (= I279), F277 (= F282), V280 (≠ I285), E335 (≠ Q340), I336 (≠ L341), G338 (= G343), A339 (≠ G344), F360 (≠ I365), E366 (= E371)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
41% identity, 100% coverage: 1:382/383 of query aligns to 1:378/380 of 4l1fA
- active site: L125 (≠ I127), T126 (= T128), G242 (≠ E246), E363 (≠ G367), R375 (= R379)
- binding coenzyme a persulfide: T132 (≠ S134), H179 (≠ N182), F232 (≠ W236), M236 (≠ F240), E237 (= E241), L239 (≠ F243), D240 (= D244), R243 (= R247), Y362 (≠ G366), E363 (≠ G367), G364 (= G368), R375 (= R379)
- binding flavin-adenine dinucleotide: F123 (= F125), L125 (≠ I127), T126 (= T128), G131 (= G133), T132 (≠ S134), F156 (= F158), I157 (= I159), T158 (= T160), R268 (= R272), Q270 (≠ A274), F271 (= F275), I275 (= I279), F278 (= F282), L281 (≠ I285), Q336 (= Q340), I337 (≠ L341), G340 (= G344), I358 (≠ L362), Y362 (≠ G366), T365 (= T369), Q367 (≠ E371)
- binding 1,3-propandiol: L5 (= L5), Q10 (= Q10)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
43% identity, 100% coverage: 1:383/383 of query aligns to 1:378/379 of 1ukwB
- active site: L124 (≠ I127), S125 (≠ T128), T241 (≠ E246), E362 (≠ G367), R374 (= R379)
- binding cobalt (ii) ion: D145 (= D148), H146 (≠ T149)
- binding flavin-adenine dinucleotide: F122 (= F125), L124 (≠ I127), S125 (≠ T128), G130 (= G133), S131 (= S134), W155 (≠ F158), S157 (≠ T160), K200 (= K204), L357 (= L362), Y361 (≠ G366), E362 (≠ G367), T364 (= T369), E366 (= E371), L370 (≠ M375)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
43% identity, 100% coverage: 1:383/383 of query aligns to 1:378/379 of 1ukwA
- active site: L124 (≠ I127), S125 (≠ T128), T241 (≠ E246), E362 (≠ G367), R374 (= R379)
- binding flavin-adenine dinucleotide: F122 (= F125), L124 (≠ I127), S125 (≠ T128), G130 (= G133), S131 (= S134), W155 (≠ F158), S157 (≠ T160), L357 (= L362), Y361 (≠ G366), E362 (≠ G367), T364 (= T369), E366 (= E371), L370 (≠ M375)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
41% identity, 95% coverage: 18:382/383 of query aligns to 17:377/378 of 5ol2F
- active site: L124 (≠ I127), T125 (= T128), G241 (≠ E246), G374 (≠ R379)
- binding calcium ion: E29 (= E30), E33 (≠ A34), R35 (= R36)
- binding coenzyme a persulfide: L238 (≠ F243), R242 (= R247), E362 (≠ G367), G363 (= G368)
- binding flavin-adenine dinucleotide: F122 (= F125), L124 (≠ I127), T125 (= T128), P127 (= P130), T131 (≠ S134), F155 (= F158), I156 (= I159), T157 (= T160), E198 (≠ L202), R267 (= R272), F270 (= F275), L274 (≠ I279), F277 (= F282), Q335 (= Q340), L336 (= L341), G338 (= G343), G339 (= G344), Y361 (≠ G366), T364 (= T369), E366 (= E371)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
41% identity, 98% coverage: 7:382/383 of query aligns to 4:373/374 of 5lnxD
- active site: L122 (≠ I127), T123 (= T128), G239 (≠ E246), E358 (≠ G367), K370 (≠ R379)
- binding flavin-adenine dinucleotide: L122 (≠ I127), T123 (= T128), G128 (= G133), S129 (= S134), F153 (= F158), T155 (= T160), R265 (= R272), Q267 (≠ A274), F268 (= F275), I272 (= I279), N275 (≠ F282), I278 (= I285), Q331 (= Q340), I332 (≠ L341), G335 (= G344), Y357 (≠ G366), T360 (= T369), E362 (= E371)
1egcA Structure of t255e, e376g mutant of human medium chain acyl-coa dehydrogenase complexed with octanoyl-coa (see paper)
39% identity, 99% coverage: 1:379/383 of query aligns to 3:379/387 of 1egcA
- active site: V126 (≠ I127), T127 (= T128), E246 (= E246), G367 (= G367), R379 (= R379)
- binding octanoyl-coenzyme a: E90 (≠ G90), L94 (≠ I95), Y124 (≠ F125), S133 (= S134), V135 (≠ T136), N182 (≠ G181), F236 (≠ W236), M240 (≠ F240), F243 (= F243), D244 (= D244), R247 (= R247), Y366 (≠ G366), G367 (= G367), G368 (= G368)
- binding flavin-adenine dinucleotide: Y124 (≠ F125), V126 (≠ I127), T127 (= T128), G132 (= G133), S133 (= S134), W157 (≠ F158), T159 (= T160), R272 (= R272), T274 (≠ A274), F275 (= F275), L279 (≠ I279), H282 (≠ F282), I285 (= I285), Q340 (= Q340), I341 (≠ L341), G344 (= G344), I362 (≠ L362), I365 (= I365), Y366 (≠ G366), T369 (= T369), Q371 (≠ E371)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
42% identity, 99% coverage: 1:381/383 of query aligns to 2:378/378 of 4n5fA
- active site: L126 (≠ I127), T127 (= T128), G243 (≠ E246), E364 (≠ G367), R376 (= R379)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ I127), T127 (= T128), G132 (= G133), S133 (= S134), F157 (= F158), T159 (= T160), T210 (= T212), Y363 (≠ G366), T366 (= T369), E368 (= E371), M372 (= M375)
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
39% identity, 99% coverage: 1:379/383 of query aligns to 2:378/385 of 3mdeA
- active site: V125 (≠ I127), T126 (= T128), T245 (≠ E246), E366 (≠ G367), R378 (= R379)
- binding octanoyl-coenzyme a: T86 (≠ L87), E89 (≠ G90), L93 (≠ I95), S132 (= S134), V134 (≠ T136), S181 (≠ G181), F235 (≠ W236), M239 (≠ F240), F242 (= F243), R314 (≠ E315), Y365 (≠ G366), E366 (≠ G367), G367 (= G368)
- binding flavin-adenine dinucleotide: Y123 (≠ F125), V125 (≠ I127), T126 (= T128), G131 (= G133), S132 (= S134), W156 (≠ F158), I157 (= I159), T158 (= T160), R271 (= R272), T273 (≠ A274), F274 (= F275), L278 (≠ I279), H281 (≠ F282), Q339 (= Q340), V340 (≠ L341), G343 (= G344), I361 (≠ L362), T368 (= T369), Q370 (≠ E371)
3mddA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
39% identity, 99% coverage: 1:379/383 of query aligns to 2:378/385 of 3mddA
- active site: V125 (≠ I127), T126 (= T128), T245 (≠ E246), E366 (≠ G367), R378 (= R379)
- binding flavin-adenine dinucleotide: Y123 (≠ F125), T126 (= T128), G131 (= G133), S132 (= S134), W156 (≠ F158), T158 (= T160), R271 (= R272), T273 (≠ A274), F274 (= F275), H281 (≠ F282), Q339 (= Q340), V340 (≠ L341), G343 (= G344), I361 (≠ L362), T368 (= T369), Q370 (≠ E371)
1udyA Medium-chain acyl-coa dehydrogenase with 3-thiaoctanoyl-coa (see paper)
39% identity, 99% coverage: 1:379/383 of query aligns to 2:378/385 of 1udyA
- active site: V125 (≠ I127), T126 (= T128), T245 (≠ E246), E366 (≠ G367), R378 (= R379)
- binding 3-thiaoctanoyl-coenzyme a: L93 (≠ I95), Y123 (≠ F125), S132 (= S134), S181 (≠ G181), F235 (≠ W236), M239 (≠ F240), F242 (= F243), V249 (≠ M250), R314 (≠ E315), Y365 (≠ G366), E366 (≠ G367), G367 (= G368), I371 (= I372), I375 (≠ V376)
- binding flavin-adenine dinucleotide: Y123 (≠ F125), T126 (= T128), G131 (= G133), S132 (= S134), W156 (≠ F158), T158 (= T160), T273 (≠ A274), F274 (= F275), Q339 (= Q340), V340 (≠ L341), G343 (= G344), T368 (= T369), Q370 (≠ E371)
P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 from Sus scrofa (Pig) (see 2 papers)
39% identity, 99% coverage: 1:379/383 of query aligns to 37:413/421 of P41367
- 158:167 (vs. 125:134, 60% identical) binding in other chain
- S167 (= S134) binding octanoyl-CoA
- WIT 191:193 (≠ FIT 158:160) binding in other chain
- S216 (≠ G181) binding octanoyl-CoA
- D278 (= D244) binding octanoyl-CoA
- R281 (= R247) binding octanoyl-CoA
- RKT 306:308 (≠ REA 272:274) binding FAD
- HQ 316:317 (≠ FG 282:283) binding in other chain
- R349 (≠ E315) binding octanoyl-CoA
- T351 (≠ Q317) binding octanoyl-CoA
- QVFGG 374:378 (≠ QLHGG 340:344) binding FAD
- E401 (≠ G367) active site, Proton acceptor; binding octanoyl-CoA
- GTAQ 402:405 (≠ GTTE 368:371) binding in other chain
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
40% identity, 98% coverage: 5:379/383 of query aligns to 8:382/387 of 1ivhA
- active site: M130 (≠ I127), S131 (≠ T128), E249 (= E246), A370 (≠ G367), R382 (= R379)
- binding coenzyme a persulfide: S137 (= S134), S185 (≠ G181), R186 (≠ N182), V239 (≠ L235), Y240 (≠ W236), M243 (≠ F240), E249 (= E246), R250 (= R247), G369 (= G366), A370 (≠ G367), G371 (= G368), V375 (≠ I372)
- binding flavin-adenine dinucleotide: L128 (≠ F125), M130 (≠ I127), S131 (≠ T128), G136 (= G133), S137 (= S134), W161 (≠ F158), T163 (= T160), R275 (= R272), F278 (= F275), F285 (= F282), M288 (≠ I285), Q343 (= Q340), C344 (≠ L341), G347 (= G344), T372 (= T369), E374 (= E371)
8sgrA Human liver mitochondrial isovaleryl-coa dehydrogenase (see paper)
40% identity, 98% coverage: 5:379/383 of query aligns to 12:386/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ T128), G140 (= G133), S141 (= S134), W165 (≠ F158), T167 (= T160), R279 (= R272), F282 (= F275), I286 (= I279), F289 (= F282), Q347 (= Q340), C348 (≠ L341), G351 (= G344), L369 (= L362), G375 (= G368), T376 (= T369), L382 (≠ M375)
P26440 Isovaleryl-CoA dehydrogenase, mitochondrial; IVD; Butyryl-CoA dehydrogenase; EC 1.3.8.4; EC 1.3.8.1 from Homo sapiens (Human) (see 5 papers)
40% identity, 98% coverage: 5:379/383 of query aligns to 45:419/426 of P26440
- 165:174 (vs. 125:134, 60% identical) binding FAD
- S174 (= S134) binding substrate
- WIT 198:200 (≠ FIT 158:160) binding FAD
- SR 222:223 (≠ GN 181:182) binding substrate
- G250 (≠ T209) to A: in IVA; uncertain significance
- Y277 (≠ W236) binding substrate
- DLER 284:287 (≠ DWER 244:247) binding substrate
- E286 (= E246) active site, Proton acceptor; mutation to D: Residual isovaleryl-CoA dehydrogenase activity.; mutation to G: Loss of isovaleryl-CoA dehydrogenase activity. Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 407-E.; mutation to Q: Loss of isovaleryl-CoA dehydrogenase activity.
- A291 (≠ I251) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R272) binding FAD
- Q323 (≠ G283) binding FAD
- I379 (= I339) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QLHGG 340:344) binding FAD
- R398 (= R358) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ A363) to N: in IVA; uncertain significance
- A407 (≠ G367) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ GG 367:368) binding substrate
- TSE 409:411 (≠ TTE 369:371) binding FAD
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
2a1tC Structure of the human mcad:etf e165betaa complex (see paper)
39% identity, 99% coverage: 1:379/383 of query aligns to 4:380/388 of 2a1tC
- active site: V127 (≠ I127), T128 (= T128), T247 (≠ E246), E368 (≠ G367), R380 (= R379)
- binding flavin-adenine dinucleotide: Y125 (≠ F125), V127 (≠ I127), T128 (= T128), G133 (= G133), S134 (= S134), Q155 (≠ T155), W158 (≠ F158), W158 (≠ F158), I159 (= I159), T160 (= T160), R273 (= R272), T275 (≠ A274), F276 (= F275), L280 (≠ I279), H283 (≠ F282), I286 (= I285), Q341 (= Q340), I342 (≠ L341), G345 (= G344), I363 (≠ L362), T370 (= T369), Q372 (≠ E371)
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)
39% identity, 99% coverage: 1:379/383 of query aligns to 37:413/421 of P11310
- Y67 (≠ R31) to H: in ACADMD; mild; dbSNP:rs121434280
- L86 (= L50) mutation to M: Strongly reduced rate of electron transfer to ETF.
- L98 (≠ S62) mutation to W: Strongly reduced rate of electron transfer to ETF.
- L100 (≠ A64) mutation to Y: Strongly reduced rate of electron transfer to ETF.
- I108 (≠ A72) mutation to M: Strongly reduced rate of electron transfer to ETF.
- P132 (= P99) to R: in a breast cancer sample; somatic mutation; dbSNP:rs875989854
- 158:167 (vs. 125:134, 60% identical) binding in other chain
- S167 (= S134) binding octanoyl-CoA
- W191 (≠ F158) 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 (≠ FIT 158:160) binding in other chain
- T193 (= T160) to A: in ACADMD; the thermostability is markedly decreased; dbSNP:rs121434279
- E237 (≠ L202) mutation to A: Strongly reduced rate of electron transfer to ETF.
- D278 (= D244) binding octanoyl-CoA
- T280 (≠ E246) 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 (= R247) binding octanoyl-CoA; to T: in ACADMD; mild clinical phenotype; dbSNP:rs121434282
- RKT 306:308 (≠ REA 272:274) binding FAD
- HQ 316:317 (≠ FG 282:283) binding in other chain
- K329 (≠ R295) to E: in ACADMD; may alter splicing; decreased fatty acid beta-oxidation; dbSNP:rs77931234
- QILGG 374:378 (≠ QLHGG 340:344) binding FAD
- E384 (= E350) 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 (≠ G367) 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 (≠ GGTTE 367:371) binding in other chain
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
40% identity, 99% coverage: 5:383/383 of query aligns to 2:377/383 of 4iv6B
- active site: L121 (≠ I127), T122 (= T128), G240 (≠ E246), E361 (≠ G367), K373 (≠ R379)
- binding dihydroflavine-adenine dinucleotide: L121 (≠ I127), T122 (= T128), G126 (≠ A132), G127 (= G133), S128 (= S134), W152 (≠ F158), I153 (= I159), S154 (≠ T160), R266 (= R272), S268 (≠ A274), F269 (= F275), I273 (= I279), H276 (≠ F282), V279 (≠ I285), R334 (≠ Q340), V335 (≠ L341), G338 (= G344), L356 (= L362), G360 (= G366), T363 (= T369), E365 (= E371), I366 (= I372)
Q9VSA3 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; EC 1.3.8.7 from Drosophila melanogaster (Fruit fly) (see paper)
40% identity, 98% coverage: 3:379/383 of query aligns to 35:409/419 of Q9VSA3
- S347 (≠ Q317) modified: Phosphoserine; by Pink1; mutation to A: Prevents phosphorylation by Pink1. Does not rescue climbing and flight defects in Pink1 mutants.; mutation to D: Phosphomimetic mutant that fully rescues climbing defects and significantly improves flight defects, and thorax and wing posture phenotypes in Pink1 mutants. No effect on acyl-CoA dehydrogenase activity.; mutation to DD: Phosphomimetic mutant that fully rescues climbing defects and significantly improves flight defects, and thorax and wing posture phenotypes in Pink1 mutants. No effect on acyl-CoA dehydrogenase activity.
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
38% identity, 98% coverage: 6:382/383 of query aligns to 7:380/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S134), T134 (= T136), R180 (≠ N182), R234 (≠ W236), L237 (≠ F240), R238 (≠ E241), L240 (≠ F243), D241 (= D244), R244 (= R247), E365 (≠ G367), G366 (= G368), R377 (= R379)
- binding flavin-adenine dinucleotide: Y123 (≠ F125), L125 (≠ I127), S126 (≠ T128), G131 (= G133), S132 (= S134), W156 (≠ F158), I157 (= I159), T158 (= T160), I360 (≠ L362), T367 (= T369), Q369 (≠ E371)
Query Sequence
>WP_052664505.1 NCBI__GCF_000969705.1:WP_052664505.1
MDFLLSEEQQAYVASVRAFAREHVAPGILERDRAGRWDQDVWEKVAGFGLAGLPLPTEYG
GSGADVLTTGLALEALAYGGMDAGLNLSLGAHLTIGAMPIALHGTEEQKQRWLPRMATGA
SIGAFAITEPDAGSDTAGMKTSARREGDTFVLNGTKTFITNGSLADVVTVVARTDPDAPA
GNAFTAFLVETDSPGFEVSKELKKLGNRTSPTVELSFTDVAVPESAILGDEGTALWAVGF
ECFDWERCCMIASAVGGMQRGLDDSIRYAKQREAFGKPIATFGAIQHKLAQMAIRLENAR
LLQRQAAWLKDNGHEHQMQASMAKAYVGEAAVESALDAIQLHGGWGYIDEFHVERGLRDA
KLATIGGGTTEIQEMVISRLLLA
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