SitesBLAST
Comparing SMa1400 FitnessBrowser__Smeli:SMa1400 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)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
43% identity, 99% coverage: 1:376/380 of query aligns to 1:379/379 of 6fahD
- active site: L124 (≠ I121), T125 (= T122), G241 (= G238), G374 (≠ R371)
- binding flavin-adenine dinucleotide: F122 (≠ Y119), L124 (≠ I121), T125 (= T122), R152 (≠ G149), F155 (≠ W152), T157 (≠ H154), E198 (= E195), R267 (= R264), Q269 (= Q266), F270 (= F267), I274 (= I271), F277 (= F274), Q335 (= Q332), I336 (≠ V333), G339 (= G336), Y361 (= Y358), T364 (= T361), Q366 (= Q363)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
46% identity, 96% coverage: 10:375/380 of query aligns to 11:378/378 of 5ol2F
- active site: L124 (≠ I121), T125 (= T122), G241 (= G238), G374 (≠ R371)
- binding calcium ion: E29 (≠ S28), E33 (= E32), R35 (= R34)
- binding coenzyme a persulfide: L238 (= L235), R242 (= R239), E362 (= E359), G363 (= G360)
- binding flavin-adenine dinucleotide: F122 (≠ Y119), L124 (≠ I121), T125 (= T122), P127 (= P124), T131 (= T128), F155 (≠ W152), I156 (= I153), T157 (≠ H154), E198 (= E195), R267 (= R264), F270 (= F267), L274 (≠ I271), F277 (= F274), Q335 (= Q332), L336 (≠ V333), G338 (= G335), G339 (= G336), Y361 (= Y358), T364 (= T361), E366 (≠ Q363)
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)
45% identity, 96% coverage: 10:375/380 of query aligns to 4:369/369 of 3pfdC
- active site: L116 (≠ I121), S117 (≠ T122), T233 (≠ G238), E353 (= E359), R365 (= R371)
- binding dihydroflavine-adenine dinucleotide: Y114 (= Y119), L116 (≠ I121), S117 (≠ T122), G122 (= G127), S123 (≠ T128), W147 (= W152), I148 (= I153), T149 (≠ H154), R259 (= R264), F262 (= F267), V266 (≠ I271), N269 (≠ F274), Q326 (= Q332), L327 (≠ V333), G330 (= G336), I348 (= I354), Y352 (= Y358), T355 (= T361), Q357 (= Q363)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
45% identity, 98% coverage: 3:375/380 of query aligns to 5:379/380 of 4l1fA
- active site: L125 (≠ I121), T126 (= T122), G242 (= G238), E363 (= E359), R375 (= R371)
- binding coenzyme a persulfide: T132 (= T128), H179 (≠ R175), F232 (= F228), M236 (= M232), E237 (≠ S233), L239 (= L235), D240 (= D236), R243 (= R239), Y362 (= Y358), E363 (= E359), G364 (= G360), R375 (= R371)
- binding flavin-adenine dinucleotide: F123 (≠ Y119), L125 (≠ I121), T126 (= T122), G131 (= G127), T132 (= T128), F156 (≠ W152), I157 (= I153), T158 (≠ H154), R268 (= R264), Q270 (= Q266), F271 (= F267), I275 (= I271), F278 (= F274), L281 (≠ V277), Q336 (= Q332), I337 (≠ V333), G340 (= G336), I358 (= I354), Y362 (= Y358), T365 (= T361), Q367 (= Q363)
- binding 1,3-propandiol: L5 (= L3), Q10 (≠ G8)
7w0jE Acyl-coa dehydrogenase, tfu_1647
45% identity, 98% coverage: 4:375/380 of query aligns to 8:382/382 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 (≠ T122), W157 (= W152), R270 (= R264), Q272 (= Q266), F273 (= F267), I277 (= I271), F280 (= F274), I283 (≠ V277), Q339 (= Q332), L340 (≠ V333), G343 (= G336), Y365 (= Y358), E366 (= E359), T368 (= T361), Q370 (= Q363), I371 (= I364)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
45% identity, 98% coverage: 4:375/380 of query aligns to 7:381/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (≠ T128), T134 (≠ V130), R180 (= R175), R234 (≠ H229), L237 (≠ M232), R238 (≠ S233), L240 (= L235), D241 (= D236), R244 (= R239), E365 (= E359), G366 (= G360), R377 (= R371)
- binding flavin-adenine dinucleotide: Y123 (= Y119), L125 (≠ I121), S126 (≠ T122), G131 (= G127), S132 (≠ T128), W156 (= W152), I157 (= I153), T158 (≠ H154), I360 (= I354), T367 (= T361), Q369 (= Q363)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
45% identity, 98% coverage: 4:375/380 of query aligns to 7:381/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (= Y119), L125 (≠ I121), S126 (≠ T122), G131 (= G127), S132 (≠ T128), W156 (= W152), I157 (= I153), T158 (≠ H154), I360 (= I354), Y364 (= Y358), T367 (= T361), Q369 (= Q363)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
45% identity, 97% coverage: 4:373/380 of query aligns to 7:378/378 of 4n5fA
- active site: L126 (≠ I121), T127 (= T122), G243 (= G238), E364 (= E359), R376 (= R371)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ I121), T127 (= T122), G132 (= G127), S133 (≠ T128), F157 (≠ W152), T159 (≠ H154), T210 (≠ V205), Y363 (= Y358), T366 (= T361), E368 (≠ Q363), M372 (= M367)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
44% identity, 98% coverage: 1:374/380 of query aligns to 1:373/374 of 5lnxD
- active site: L122 (≠ I121), T123 (= T122), G239 (= G238), E358 (= E359), K370 (≠ R371)
- binding flavin-adenine dinucleotide: L122 (≠ I121), T123 (= T122), G128 (= G127), S129 (≠ T128), F153 (≠ W152), T155 (≠ H154), R265 (= R264), Q267 (= Q266), F268 (= F267), I272 (= I271), N275 (≠ F274), I278 (≠ V277), Q331 (= Q332), I332 (≠ V333), G335 (= G336), Y357 (= Y358), T360 (= T361), E362 (≠ Q363)
Q9VSA3 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; EC 1.3.8.7 from Drosophila melanogaster (Fruit fly) (see paper)
44% identity, 98% coverage: 3:375/380 of query aligns to 37:413/419 of Q9VSA3
- S347 (≠ T309) 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.
P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 from Sus scrofa (Pig) (see 2 papers)
44% identity, 97% coverage: 3:372/380 of query aligns to 41:414/421 of P41367
- 158:167 (vs. 119:128, 70% identical) binding in other chain
- S167 (≠ T128) binding
- WIT 191:193 (≠ WIH 152:154) binding in other chain
- S216 (≠ N174) binding
- D278 (= D236) binding
- R281 (= R239) binding
- RKT 306:308 (≠ RKQ 264:266) binding
- HQ 316:317 (≠ FQ 274:275) binding in other chain
- R349 (≠ D307) binding
- T351 (= T309) binding
- QVFGG 374:378 (= QVFGG 332:336) binding
- E401 (= E359) active site, Proton acceptor; binding
- GTAQ 402:405 (≠ GTNQ 360:363) binding in other chain
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
44% identity, 97% coverage: 3:372/380 of query aligns to 6:379/385 of 3mdeA
- active site: V125 (≠ I121), T126 (= T122), T245 (≠ G238), E366 (= E359), R378 (= R371)
- binding octanoyl-coenzyme a: T86 (vs. gap), E89 (vs. gap), L93 (≠ C85), S132 (≠ T128), V134 (= V130), S181 (≠ N174), F235 (= F228), M239 (= M232), F242 (≠ L235), R314 (≠ D307), Y365 (= Y358), E366 (= E359), G367 (= G360)
- binding flavin-adenine dinucleotide: Y123 (= Y119), V125 (≠ I121), T126 (= T122), G131 (= G127), S132 (≠ T128), W156 (= W152), I157 (= I153), T158 (≠ H154), R271 (= R264), T273 (≠ Q266), F274 (= F267), L278 (≠ I271), H281 (≠ F274), Q339 (= Q332), V340 (= V333), G343 (= G336), I361 (= I354), T368 (= T361), Q370 (= Q363)
3mddA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
44% identity, 97% coverage: 3:372/380 of query aligns to 6:379/385 of 3mddA
- active site: V125 (≠ I121), T126 (= T122), T245 (≠ G238), E366 (= E359), R378 (= R371)
- binding flavin-adenine dinucleotide: Y123 (= Y119), T126 (= T122), G131 (= G127), S132 (≠ T128), W156 (= W152), T158 (≠ H154), R271 (= R264), T273 (≠ Q266), F274 (= F267), H281 (≠ F274), Q339 (= Q332), V340 (= V333), G343 (= G336), I361 (= I354), T368 (= T361), Q370 (= Q363)
1udyA Medium-chain acyl-coa dehydrogenase with 3-thiaoctanoyl-coa (see paper)
44% identity, 97% coverage: 3:372/380 of query aligns to 6:379/385 of 1udyA
- active site: V125 (≠ I121), T126 (= T122), T245 (≠ G238), E366 (= E359), R378 (= R371)
- binding 3-thiaoctanoyl-coenzyme a: L93 (≠ C85), Y123 (= Y119), S132 (≠ T128), S181 (≠ N174), F235 (= F228), M239 (= M232), F242 (≠ L235), V249 (≠ I242), R314 (≠ D307), Y365 (= Y358), E366 (= E359), G367 (= G360), I371 (= I364), I375 (= I368)
- binding flavin-adenine dinucleotide: Y123 (= Y119), T126 (= T122), G131 (= G127), S132 (≠ T128), W156 (= W152), T158 (≠ H154), T273 (≠ Q266), F274 (= F267), Q339 (= Q332), V340 (= V333), G343 (= G336), T368 (= T361), Q370 (= Q363)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
41% identity, 98% coverage: 3:375/380 of query aligns to 34:408/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
41% identity, 98% coverage: 3:375/380 of query aligns to 7:381/384 of 1jqiA
- active site: G377 (≠ R371)
- binding acetoacetyl-coenzyme a: L95 (= L95), F125 (≠ Y119), S134 (≠ T128), F234 (= F228), M238 (= M232), Q239 (≠ S233), L241 (= L235), D242 (= D236), R245 (= R239), Y364 (= Y358), E365 (= E359), G366 (= G360)
- binding flavin-adenine dinucleotide: F125 (≠ Y119), L127 (≠ I121), S128 (≠ T122), G133 (= G127), S134 (≠ T128), W158 (= W152), T160 (≠ H154), R270 (= R264), F273 (= F267), L280 (≠ F274), Q338 (= Q332), I339 (≠ V333), G342 (= G336), I360 (= I354), T367 (= T361), E369 (≠ Q363), I370 (= I364)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
40% identity, 98% coverage: 3:375/380 of query aligns to 7:381/385 of 7y0bA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[[4-[(3S)-oxolan-3-yl]oxyphenyl]methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: M343 (≠ S337), T347 (≠ R341), E348 (≠ G342)
- binding flavin-adenine dinucleotide: F125 (≠ Y119), L127 (≠ I121), S128 (≠ T122), G133 (= G127), S134 (≠ T128), W158 (= W152), T160 (≠ H154), R270 (= R264), F273 (= F267), L280 (≠ F274), V282 (≠ G276), Q338 (= Q332), I339 (≠ V333), G342 (= G336), I360 (= I354), Y364 (= Y358), T367 (= T361), E369 (≠ Q363), I370 (= I364), L373 (≠ M367)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
40% identity, 98% coverage: 3:375/380 of query aligns to 34:408/412 of P16219
- G90 (= G59) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E73) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 119:128, 30% identical) binding in other chain
- R171 (≠ E138) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ WIH 152:154) binding in other chain
- A192 (= A159) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G176) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R264) binding
- Q308 (= Q275) binding in other chain
- R325 (= R292) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ G320) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QVFGG 332:336) binding
- R380 (= R347) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ TNQ 361:363) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
40% identity, 98% coverage: 3:375/380 of query aligns to 10:384/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ Y119), L130 (≠ I121), S131 (≠ T122), G136 (= G127), S137 (≠ T128), W161 (= W152), T163 (≠ H154), T214 (≠ V205), R273 (= R264), F276 (= F267), L280 (≠ I271), L283 (≠ F274), V285 (≠ G276), Q341 (= Q332), I342 (≠ V333), G345 (= G336), I363 (= I354), Y367 (= Y358), T370 (= T361), E372 (≠ Q363), L376 (≠ M367)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
40% identity, 98% coverage: 3:375/380 of query aligns to 4:378/381 of 8sgsA
- binding coenzyme a: S131 (≠ T128), A133 (≠ V130), N177 (= N174), F231 (= F228), M235 (= M232), L238 (= L235), I312 (≠ T309), E362 (= E359), G363 (= G360)
- binding flavin-adenine dinucleotide: F122 (≠ Y119), L124 (≠ I121), S125 (≠ T122), G130 (= G127), S131 (≠ T128), W155 (= W152), T157 (≠ H154), R267 (= R264), F270 (= F267), L274 (≠ I271), L277 (≠ F274), Q335 (= Q332), I336 (≠ V333), G338 (= G335), G339 (= G336), I357 (= I354), I360 (= I357), Y361 (= Y358), T364 (= T361), E366 (≠ Q363)
Query Sequence
>SMa1400 FitnessBrowser__Smeli:SMa1400
MYLTEIQGQVRDMARAFADEVIRPMAESLDREERFPAELYGEMAKLGLFGIGVPEHLGGP
GFDTLTYAVVMEELSRGYASVADQCGLVELISTLLVRHGTEGQQRMLPDVLNMSAKVAYC
ITEPEAGTDVSGIRTTAERDGDGWMLNGGKIWIHNAPVADVGFVLARTDKEAGNRGMSIF
IVDLNSAGVERGPKEHKMGQRASQVGALTFTDVRLPGGALLGQEGRGFHMMMSVLDKGRV
GIAALAVGIAQAGLEAAVDYAGTRKQFGKAISDFQGVQWLLADMAKDIEAARLLVHSAAS
KIDRGLDATKACSIAKCFAGDMAVQRTADAVQVFGGSGYIRGFEVERLYRDAKITQIYEG
TNQIQRMIIARELLKKGARA
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