SitesBLAST
Comparing WP_017597307.1 NCBI__GCF_000341125.1:WP_017597307.1 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)
Q9VSA3 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; EC 1.3.8.7 from Drosophila melanogaster (Fruit fly) (see paper)
37% identity, 99% coverage: 1:403/409 of query aligns to 25:411/419 of Q9VSA3
- S347 (≠ D338) 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.
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
38% identity, 96% coverage: 13:403/409 of query aligns to 5:376/379 of 1ukwB
- active site: L124 (≠ S134), S125 (= S135), T241 (≠ S267), E362 (= E389), R374 (= R401)
- binding cobalt (ii) ion: D145 (= D157), H146 (≠ E158)
- binding flavin-adenine dinucleotide: F122 (= F132), L124 (≠ S134), S125 (= S135), G130 (= G140), S131 (= S141), W155 (= W167), S157 (≠ T169), K200 (= K212), L357 (≠ I384), Y361 (≠ F388), E362 (= E389), T364 (≠ A391), E366 (= E393), L370 (= L397)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
38% identity, 96% coverage: 13:403/409 of query aligns to 5:376/379 of 1ukwA
- active site: L124 (≠ S134), S125 (= S135), T241 (≠ S267), E362 (= E389), R374 (= R401)
- binding flavin-adenine dinucleotide: F122 (= F132), L124 (≠ S134), S125 (= S135), G130 (= G140), S131 (= S141), W155 (= W167), S157 (≠ T169), L357 (≠ I384), Y361 (≠ F388), E362 (= E389), T364 (≠ A391), E366 (= E393), L370 (= L397)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
37% identity, 94% coverage: 14:399/409 of query aligns to 5:372/378 of 5ol2F
- active site: L124 (≠ S134), T125 (≠ S135), G241 (≠ S267)
- binding calcium ion: E29 (= E38), E33 (≠ R42), R35 (≠ E44)
- binding coenzyme a persulfide: L238 (≠ F264), R242 (= R268), E362 (= E389), G363 (= G390)
- binding flavin-adenine dinucleotide: F122 (= F132), L124 (≠ S134), T125 (≠ S135), P127 (= P137), T131 (≠ S141), F155 (≠ W167), I156 (≠ A168), T157 (= T169), E198 (≠ F210), R267 (= R293), F270 (= F296), L274 (≠ I300), F277 (≠ N303), Q335 (≠ R362), L336 (≠ I363), G338 (= G365), G339 (= G366), Y361 (≠ F388), T364 (≠ A391), E366 (= E393)
Sites not aligning to the query:
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
36% identity, 97% coverage: 9:405/409 of query aligns to 2:382/385 of 3mdeA
- active site: V125 (≠ S134), T126 (≠ S135), T245 (≠ S267), E366 (= E389), R378 (= R401)
- binding octanoyl-coenzyme a: T86 (≠ L92), E89 (≠ T95), L93 (= L99), S132 (= S141), V134 (= V143), S181 (= S189), F235 (≠ S255), M239 (= M261), F242 (= F264), R314 (≠ D336), Y365 (≠ F388), E366 (= E389), G367 (= G390)
- binding flavin-adenine dinucleotide: Y123 (≠ F132), V125 (≠ S134), T126 (≠ S135), G131 (= G140), S132 (= S141), W156 (= W167), I157 (≠ A168), T158 (= T169), R271 (= R293), T273 (≠ Q295), F274 (= F296), L278 (≠ I300), H281 (≠ N303), Q339 (≠ R362), V340 (≠ I363), G343 (= G366), I361 (= I384), T368 (≠ A391), Q370 (≠ E393)
3mddA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
36% identity, 97% coverage: 9:405/409 of query aligns to 2:382/385 of 3mddA
- active site: V125 (≠ S134), T126 (≠ S135), T245 (≠ S267), E366 (= E389), R378 (= R401)
- binding flavin-adenine dinucleotide: Y123 (≠ F132), T126 (≠ S135), G131 (= G140), S132 (= S141), W156 (= W167), T158 (= T169), R271 (= R293), T273 (≠ Q295), F274 (= F296), H281 (≠ N303), Q339 (≠ R362), V340 (≠ I363), G343 (= G366), I361 (= I384), T368 (≠ A391), Q370 (≠ E393)
1udyA Medium-chain acyl-coa dehydrogenase with 3-thiaoctanoyl-coa (see paper)
36% identity, 97% coverage: 9:405/409 of query aligns to 2:382/385 of 1udyA
- active site: V125 (≠ S134), T126 (≠ S135), T245 (≠ S267), E366 (= E389), R378 (= R401)
- binding 3-thiaoctanoyl-coenzyme a: L93 (= L99), Y123 (≠ F132), S132 (= S141), S181 (= S189), F235 (≠ S255), M239 (= M261), F242 (= F264), V249 (= V271), R314 (≠ D336), Y365 (≠ F388), E366 (= E389), G367 (= G390), I371 (= I394), I375 (= I398)
- binding flavin-adenine dinucleotide: Y123 (≠ F132), T126 (≠ S135), G131 (= G140), S132 (= S141), W156 (= W167), T158 (= T169), T273 (≠ Q295), F274 (= F296), Q339 (≠ R362), V340 (≠ I363), G343 (= G366), T368 (≠ A391), Q370 (≠ E393)
P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 from Sus scrofa (Pig) (see 2 papers)
36% identity, 97% coverage: 9:405/409 of query aligns to 37:417/421 of P41367
- 158:167 (vs. 132:141, 60% identical) binding in other chain
- S167 (= S141) binding octanoyl-CoA
- WIT 191:193 (≠ WAT 167:169) binding in other chain
- S216 (= S189) binding octanoyl-CoA
- D278 (≠ E265) binding octanoyl-CoA
- R281 (= R268) binding octanoyl-CoA
- RKT 306:308 (≠ REQ 293:295) binding FAD
- HQ 316:317 (≠ NQ 303:304) binding in other chain
- R349 (≠ D336) binding octanoyl-CoA
- T351 (≠ D338) binding octanoyl-CoA
- QVFGG 374:378 (≠ RILGG 362:366) binding FAD
- E401 (= E389) active site, Proton acceptor; binding octanoyl-CoA
- GTAQ 402:405 (≠ GASE 390:393) binding in other chain
2a1tC Structure of the human mcad:etf e165betaa complex (see paper)
35% identity, 96% coverage: 9:401/409 of query aligns to 4:380/388 of 2a1tC
- active site: V127 (≠ S134), T128 (≠ S135), T247 (≠ S267), E368 (= E389), R380 (= R401)
- binding flavin-adenine dinucleotide: Y125 (≠ F132), V127 (≠ S134), T128 (≠ S135), G133 (= G140), S134 (= S141), Q155 (≠ T164), W158 (= W167), W158 (= W167), I159 (≠ A168), T160 (= T169), R273 (= R293), T275 (≠ Q295), F276 (= F296), L280 (≠ I300), H283 (≠ N303), I286 (≠ V306), Q341 (≠ R362), I342 (= I363), G345 (= G366), I363 (= I384), T370 (≠ A391), Q372 (≠ E393)
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)
35% identity, 96% coverage: 9:401/409 of query aligns to 37:413/421 of P11310
- Y67 (≠ W39) to H: in ACADMD; mild; dbSNP:rs121434280
- L86 (= L58) mutation to M: Strongly reduced rate of electron transfer to ETF.
- L98 (= L74) mutation to W: Strongly reduced rate of electron transfer to ETF.
- L100 (≠ V76) mutation to Y: Strongly reduced rate of electron transfer to ETF.
- I108 (≠ A79) mutation to M: Strongly reduced rate of electron transfer to ETF.
- P132 (≠ S103) to R: in a breast cancer sample; somatic mutation; dbSNP:rs875989854
- 158:167 (vs. 132:141, 60% identical) binding in other chain
- S167 (= S141) binding octanoyl-CoA
- W191 (= W167) 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 (≠ WAT 167:169) binding in other chain
- T193 (= T169) to A: in ACADMD; the thermostability is markedly decreased; dbSNP:rs121434279
- E237 (≠ F210) mutation to A: Strongly reduced rate of electron transfer to ETF.
- D278 (≠ E265) binding octanoyl-CoA
- T280 (≠ S267) 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 (= R268) binding octanoyl-CoA; to T: in ACADMD; mild clinical phenotype; dbSNP:rs121434282
- RKT 306:308 (≠ REQ 293:295) binding FAD
- HQ 316:317 (≠ NQ 303:304) binding in other chain
- K329 (≠ R316) to E: in ACADMD; may alter splicing; decreased fatty acid beta-oxidation; dbSNP:rs77931234
- QILGG 374:378 (≠ RILGG 362:366) binding FAD
- E384 (≠ D372) 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 (= E389) 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 (≠ EGASE 389:393) binding in other chain
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
38% identity, 95% coverage: 14:403/409 of query aligns to 7:378/378 of 4n5fA
- active site: L126 (≠ S134), T127 (≠ S135), G243 (≠ S267), E364 (= E389), R376 (= R401)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ S134), T127 (≠ S135), G132 (= G140), S133 (= S141), F157 (≠ W167), T159 (= T169), T210 (= T220), Y363 (≠ F388), T366 (≠ A391), E368 (= E393), M372 (≠ L397)
1egcA Structure of t255e, e376g mutant of human medium chain acyl-coa dehydrogenase complexed with octanoyl-coa (see paper)
35% identity, 96% coverage: 9:401/409 of query aligns to 3:379/387 of 1egcA
- active site: V126 (≠ S134), T127 (≠ S135), E246 (≠ S267), G367 (≠ E389), R379 (= R401)
- binding octanoyl-coenzyme a: E90 (≠ T95), L94 (= L99), Y124 (≠ F132), S133 (= S141), V135 (= V143), N182 (≠ S189), F236 (≠ S255), M240 (= M261), F243 (= F264), D244 (≠ E265), R247 (= R268), Y366 (≠ F388), G367 (≠ E389), G368 (= G390)
- binding flavin-adenine dinucleotide: Y124 (≠ F132), V126 (≠ S134), T127 (≠ S135), G132 (= G140), S133 (= S141), W157 (= W167), T159 (= T169), R272 (= R293), T274 (≠ Q295), F275 (= F296), L279 (≠ I300), H282 (≠ N303), I285 (≠ V306), Q340 (≠ R362), I341 (= I363), G344 (= G366), I362 (= I384), I365 (= I387), Y366 (≠ F388), T369 (≠ A391), Q371 (≠ E393)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
37% identity, 95% coverage: 14:403/409 of query aligns to 7:379/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S141), T134 (≠ V143), R180 (≠ Q192), R234 (= R254), L237 (≠ M261), R238 (≠ K262), L240 (≠ F264), D241 (≠ E265), R244 (= R268), E365 (= E389), G366 (= G390), R377 (= R401)
- binding flavin-adenine dinucleotide: Y123 (≠ F132), L125 (≠ S134), S126 (= S135), G131 (= G140), S132 (= S141), W156 (= W167), I157 (≠ A168), T158 (= T169), I360 (= I384), T367 (≠ A391), Q369 (≠ E393)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
37% identity, 95% coverage: 14:403/409 of query aligns to 7:379/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ F132), L125 (≠ S134), S126 (= S135), G131 (= G140), S132 (= S141), W156 (= W167), I157 (≠ A168), T158 (= T169), I360 (= I384), Y364 (≠ F388), T367 (≠ A391), Q369 (≠ E393)
7w0jE Acyl-coa dehydrogenase, tfu_1647
37% identity, 95% coverage: 14:403/409 of query aligns to 8:380/382 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 (= S135), W157 (= W167), R270 (= R293), Q272 (= Q295), F273 (= F296), I277 (= I300), F280 (≠ N303), I283 (≠ V306), Q339 (≠ R362), L340 (≠ I363), G343 (= G366), Y365 (≠ F388), E366 (= E389), T368 (≠ A391), Q370 (≠ E393), I371 (= I394)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
37% identity, 95% coverage: 10:399/409 of query aligns to 4:375/384 of 1jqiA
- binding acetoacetyl-coenzyme a: L95 (= L99), F125 (= F132), S134 (= S141), F234 (≠ E244), M238 (= M261), Q239 (≠ K262), L241 (≠ F264), D242 (≠ E265), R245 (= R268), Y364 (≠ F388), E365 (= E389), G366 (= G390)
- binding flavin-adenine dinucleotide: F125 (= F132), L127 (≠ S134), S128 (= S135), G133 (= G140), S134 (= S141), W158 (= W167), T160 (= T169), R270 (= R293), F273 (= F296), L280 (≠ N303), Q338 (≠ R362), I339 (= I363), G342 (= G366), I360 (= I384), T367 (≠ A391), E369 (= E393), I370 (= I394)
Sites not aligning to the query:
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
37% identity, 95% coverage: 10:399/409 of query aligns to 31:402/412 of P15651
- 152:161 (vs. 132:141, 60% identical) binding FAD
- S161 (= S141) binding substrate
- WIT 185:187 (≠ WAT 167:169) binding FAD
- DMGR 269:272 (≠ EASR 265:268) binding substrate
- R297 (= R293) binding FAD
- QILGG 365:369 (≠ RILGG 362:366) binding FAD
- E392 (= E389) active site, Proton acceptor
- TSE 394:396 (≠ ASE 391:393) binding FAD
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
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)
37% identity, 94% coverage: 20:403/409 of query aligns to 4:367/369 of 3pfdC
- active site: L116 (≠ S134), S117 (= S135), T233 (≠ S267), E353 (= E389), R365 (= R401)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ F132), L116 (≠ S134), S117 (= S135), G122 (= G140), S123 (= S141), W147 (= W167), I148 (≠ A168), T149 (= T169), R259 (= R293), F262 (= F296), V266 (≠ I300), N269 (= N303), Q326 (≠ R362), L327 (≠ I363), G330 (= G366), I348 (= I384), Y352 (≠ F388), T355 (≠ A391), Q357 (≠ E393)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
37% identity, 94% coverage: 20:405/409 of query aligns to 9:374/374 of 5lnxD
- active site: L122 (≠ S134), T123 (≠ S135), G239 (≠ S267), E358 (= E389), K370 (≠ R401)
- binding flavin-adenine dinucleotide: L122 (≠ S134), T123 (≠ S135), G128 (= G140), S129 (= S141), F153 (≠ W167), T155 (= T169), R265 (= R293), Q267 (= Q295), F268 (= F296), I272 (= I300), N275 (= N303), I278 (≠ V306), Q331 (≠ R362), I332 (= I363), G335 (= G366), Y357 (≠ F388), T360 (≠ A391), E362 (= E393)
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
36% identity, 95% coverage: 11:400/409 of query aligns to 3:378/383 of 1bucA
- active site: L128 (≠ S134), T129 (≠ S135), G246 (≠ S267), E367 (= E389)
- binding acetoacetyl-coenzyme a: L96 (≠ V104), F126 (= F132), G134 (= G140), T135 (≠ S141), T162 (= T169), N182 (≠ S189), H183 (≠ R190), F236 (≠ S255), M240 (= M261), M241 (≠ K262), L243 (≠ F264), D244 (≠ E265), T317 (≠ D338), Y366 (≠ F388), E367 (= E389), G368 (= G390)
- binding flavin-adenine dinucleotide: F126 (= F132), L128 (≠ S134), T129 (≠ S135), G134 (= G140), T135 (≠ S141), F160 (≠ W167), T162 (= T169), Y366 (≠ F388), T369 (≠ A391), E371 (= E393), M375 (≠ L397)
Sites not aligning to the query:
Query Sequence
>WP_017597307.1 NCBI__GCF_000341125.1:WP_017597307.1
MSEATAPAFSLELSEDVRDVRDWAHGFAADVIRPAAAEWDEREETPWPIIQEAAKIGLYS
LDFFANQWLEPSGLGVPVAFEELYWGDPGIALAITGTGLAAVSVAANGTQDQLLEWTPQM
FGTADDVKLAAFCSSEPDAGSDVSAIRTRAVYDQAKDEWVLNGTKTWATNGGIADVHVVV
ASVEPEFGSRGQATFIVPPGTPGLSQGQKFAKHGIRASHTAEVVLDDVRIPGSCLLGGKE
KLDERIARAREGRRSKGQAAMKTFEASRPTVGAMAVGCARAAYEYALEYSTQREQFGRPI
GDNQGVAFTLAEMATRIDAARLLVWRAAWMARNGKDFDHAQGSMSKLYASETATFVTQNA
VRILGGNGYTRDYPVERWHRDATIFTIFEGASEIQKLIIGRTITGLPIR
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