SitesBLAST
Comparing WP_037571613.1 NCBI__GCF_000744815.1:WP_037571613.1 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)
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
48% identity, 96% coverage: 12:400/407 of query aligns to 2:376/383 of 4iv6B
- active site: L121 (≠ M131), T122 (≠ S132), G240 (= G264), E361 (= E385), K373 (≠ R397)
- binding dihydroflavine-adenine dinucleotide: L121 (≠ M131), T122 (≠ S132), G126 (≠ L136), G127 (= G137), S128 (= S138), W152 (= W164), I153 (≠ L165), S154 (≠ T166), R266 (= R290), S268 (≠ T292), F269 (= F293), I273 (= I297), H276 (= H300), V279 (≠ I303), R334 (= R358), V335 (≠ I359), G338 (= G362), L356 (≠ M380), G360 (= G384), T363 (= T387), E365 (= E389), I366 (= I390)
6es9A Methylsuccinyl-coa dehydrogenase of paracoccus denitrificans with bound flavin adenine dinucleotide (see paper)
42% identity, 96% coverage: 11:401/407 of query aligns to 160:545/545 of 6es9A
- active site: F281 (≠ M131), T282 (≠ S132), A408 (≠ G264), R541 (= R397)
- binding coenzyme a: F467 (≠ M323), W470 (≠ R326)
- binding flavin-adenine dinucleotide: A279 (≠ F129), F281 (≠ M131), T282 (≠ S132), G287 (= G137), S288 (= S138), W312 (= W164), I313 (≠ L165), T314 (= T166), E374 (≠ T230), R434 (= R290), Q436 (≠ T292), F437 (= F293), L441 (≠ I297), F444 (≠ H300), Q502 (≠ R358), I503 (= I359), G505 (= G361), G506 (= G362), F528 (≠ G384), A531 (≠ T387), E533 (= E389), I534 (= I390)
Sites not aligning to the query:
2a1tC Structure of the human mcad:etf e165betaa complex (see paper)
40% identity, 97% coverage: 12:404/407 of query aligns to 8:387/388 of 2a1tC
- active site: V127 (≠ M131), T128 (≠ S132), T247 (≠ G264), E368 (= E385), R380 (= R397)
- binding flavin-adenine dinucleotide: Y125 (≠ F129), V127 (≠ M131), T128 (≠ S132), G133 (= G137), S134 (= S138), Q155 (= Q161), W158 (= W164), W158 (= W164), I159 (≠ L165), T160 (= T166), R273 (= R290), T275 (= T292), F276 (= F293), L280 (≠ I297), H283 (= H300), I286 (= I303), Q341 (≠ R358), I342 (= I359), G345 (= G362), I363 (≠ M380), T370 (= T387), Q372 (≠ E389)
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
40% identity, 97% coverage: 12:404/407 of query aligns to 6:385/385 of 3mdeA
- active site: V125 (≠ M131), T126 (≠ S132), T245 (≠ G264), E366 (= E385), R378 (= R397)
- binding octanoyl-coenzyme a: T86 (≠ G92), E89 (≠ N95), L93 (≠ I99), S132 (= S138), V134 (= V140), S181 (≠ H191), F235 (= F254), M239 (= M258), F242 (≠ V261), R314 (= R333), Y365 (≠ G384), E366 (= E385), G367 (= G386)
- binding flavin-adenine dinucleotide: Y123 (≠ F129), V125 (≠ M131), T126 (≠ S132), G131 (= G137), S132 (= S138), W156 (= W164), I157 (≠ L165), T158 (= T166), R271 (= R290), T273 (= T292), F274 (= F293), L278 (≠ I297), H281 (= H300), Q339 (≠ R358), V340 (≠ I359), G343 (= G362), I361 (≠ M380), T368 (= T387), Q370 (≠ E389)
3mddA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
40% identity, 97% coverage: 12:404/407 of query aligns to 6:385/385 of 3mddA
- active site: V125 (≠ M131), T126 (≠ S132), T245 (≠ G264), E366 (= E385), R378 (= R397)
- binding flavin-adenine dinucleotide: Y123 (≠ F129), T126 (≠ S132), G131 (= G137), S132 (= S138), W156 (= W164), T158 (= T166), R271 (= R290), T273 (= T292), F274 (= F293), H281 (= H300), Q339 (≠ R358), V340 (≠ I359), G343 (= G362), I361 (≠ M380), T368 (= T387), Q370 (≠ E389)
1udyA Medium-chain acyl-coa dehydrogenase with 3-thiaoctanoyl-coa (see paper)
40% identity, 97% coverage: 12:404/407 of query aligns to 6:385/385 of 1udyA
- active site: V125 (≠ M131), T126 (≠ S132), T245 (≠ G264), E366 (= E385), R378 (= R397)
- binding 3-thiaoctanoyl-coenzyme a: L93 (≠ I99), Y123 (≠ F129), S132 (= S138), S181 (≠ H191), F235 (= F254), M239 (= M258), F242 (≠ V261), V249 (= V268), R314 (= R333), Y365 (≠ G384), E366 (= E385), G367 (= G386), I371 (= I390), I375 (= I394)
- binding flavin-adenine dinucleotide: Y123 (≠ F129), T126 (≠ S132), G131 (= G137), S132 (= S138), W156 (= W164), T158 (= T166), T273 (= T292), F274 (= F293), Q339 (≠ R358), V340 (≠ I359), G343 (= G362), T368 (= T387), Q370 (≠ E389)
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)
40% identity, 97% coverage: 12:404/407 of query aligns to 41:420/421 of P11310
- Y67 (≠ L38) to H: in ACADMD; mild; dbSNP:rs121434280
- L86 (= L57) mutation to M: Strongly reduced rate of electron transfer to ETF.
- L98 (= L69) mutation to W: Strongly reduced rate of electron transfer to ETF.
- L100 (≠ E71) mutation to Y: Strongly reduced rate of electron transfer to ETF.
- I108 (≠ V79) mutation to M: Strongly reduced rate of electron transfer to ETF.
- P132 (≠ M103) to R: in a breast cancer sample; somatic mutation; dbSNP:rs875989854
- 158:167 (vs. 129:138, 50% identical) binding in other chain
- S167 (= S138) binding octanoyl-CoA
- W191 (= W164) 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 (≠ WLT 164:166) binding in other chain
- T193 (= T166) to A: in ACADMD; the thermostability is markedly decreased; dbSNP:rs121434279
- E237 (≠ I220) mutation to A: Strongly reduced rate of electron transfer to ETF.
- D278 (≠ E262) binding octanoyl-CoA
- T280 (≠ G264) 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 (= R265) binding octanoyl-CoA; to T: in ACADMD; mild clinical phenotype; dbSNP:rs121434282
- RKT 306:308 (≠ RET 290:292) binding FAD
- HQ 316:317 (= HQ 300:301) binding in other chain
- K329 (= K313) to E: in ACADMD; may alter splicing; decreased fatty acid beta-oxidation; dbSNP:rs77931234
- QILGG 374:378 (≠ RIHGG 358:362) binding FAD
- E384 (= E368) 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 (= E385) 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 (≠ EGTAE 385:389) binding in other chain
P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 from Sus scrofa (Pig) (see 2 papers)
40% identity, 97% coverage: 12:404/407 of query aligns to 41:420/421 of P41367
- 158:167 (vs. 129:138, 50% identical) binding in other chain
- S167 (= S138) binding octanoyl-CoA
- WIT 191:193 (≠ WLT 164:166) binding in other chain
- S216 (≠ H191) binding octanoyl-CoA
- D278 (≠ E262) binding octanoyl-CoA
- R281 (= R265) binding octanoyl-CoA
- RKT 306:308 (≠ RET 290:292) binding FAD
- HQ 316:317 (= HQ 300:301) binding in other chain
- R349 (= R333) binding octanoyl-CoA
- T351 (≠ D335) binding octanoyl-CoA
- QVFGG 374:378 (≠ RIHGG 358:362) binding FAD
- E401 (= E385) active site, Proton acceptor; binding octanoyl-CoA
- GTAQ 402:405 (≠ GTAE 386:389) binding in other chain
1egcA Structure of t255e, e376g mutant of human medium chain acyl-coa dehydrogenase complexed with octanoyl-coa (see paper)
40% identity, 97% coverage: 12:404/407 of query aligns to 7:386/387 of 1egcA
- active site: V126 (≠ M131), T127 (≠ S132), E246 (≠ G264), G367 (≠ E385), R379 (= R397)
- binding octanoyl-coenzyme a: E90 (≠ N95), L94 (≠ I99), Y124 (≠ F129), S133 (= S138), V135 (= V140), N182 (≠ H191), F236 (= F254), M240 (= M258), F243 (≠ V261), D244 (≠ E262), R247 (= R265), Y366 (≠ G384), G367 (≠ E385), G368 (= G386)
- binding flavin-adenine dinucleotide: Y124 (≠ F129), V126 (≠ M131), T127 (≠ S132), G132 (= G137), S133 (= S138), W157 (= W164), T159 (= T166), R272 (= R290), T274 (= T292), F275 (= F293), L279 (≠ I297), H282 (= H300), I285 (= I303), Q340 (≠ R358), I341 (= I359), G344 (= G362), I362 (≠ M380), I365 (= I383), Y366 (≠ G384), T369 (= T387), Q371 (≠ E389)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
39% identity, 93% coverage: 23:400/407 of query aligns to 13:373/374 of 5lnxD
- active site: L122 (≠ M131), T123 (≠ S132), G239 (= G264), E358 (= E385), K370 (≠ R397)
- binding flavin-adenine dinucleotide: L122 (≠ M131), T123 (≠ S132), G128 (= G137), S129 (= S138), F153 (≠ W164), T155 (= T166), R265 (= R290), Q267 (≠ T292), F268 (= F293), I272 (= I297), N275 (≠ H300), I278 (= I303), Q331 (≠ R358), I332 (= I359), G335 (= G362), Y357 (≠ G384), T360 (= T387), E362 (= E389)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
36% identity, 98% coverage: 6:404/407 of query aligns to 1:384/385 of 7y0bA