SitesBLAST
Comparing WP_011781244.1 NCBI__GCF_000015305.1:WP_011781244.1 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)
7szvA Crystal structure of acyl-coa dehydrogenase from mycobacterium marinum in complex with fda
80% identity, 98% coverage: 10:386/386 of query aligns to 2:372/372 of 7szvA
- binding dihydroflavine-adenine dinucleotide: L122 (= L130), T123 (= T131), F153 (= F161), I154 (= I162), T155 (= T163), K194 (= K208), R261 (= R275), S263 (≠ A277), Y271 (≠ N285), I274 (= I288), Q329 (= Q343), V330 (≠ I344), G332 (= G346), G333 (= G347), T358 (= T372), E360 (= E374)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
47% identity, 96% coverage: 13:384/386 of query aligns to 7:376/378 of 5ol2F
- active site: L124 (= L130), T125 (= T131), G241 (= G249), G374 (≠ R382)
- binding calcium ion: E29 (≠ K35), E33 (= E39), R35 (≠ S41)
- binding coenzyme a persulfide: L238 (= L246), R242 (= R250), E362 (= E370), G363 (= G371)
- binding flavin-adenine dinucleotide: F122 (= F128), L124 (= L130), T125 (= T131), P127 (≠ A133), T131 (≠ S137), F155 (= F161), I156 (= I162), T157 (= T163), E198 (≠ Y206), R267 (= R275), F270 (= F278), L274 (≠ I282), F277 (≠ N285), Q335 (= Q343), L336 (≠ I344), G338 (= G346), G339 (= G347), Y361 (≠ G369), T364 (= T372), E366 (= E374)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
44% identity, 97% coverage: 10:384/386 of query aligns to 7:379/384 of 1jqiA
- active site: G377 (≠ R382)
- binding acetoacetyl-coenzyme a: L95 (= L98), F125 (= F128), S134 (= S137), F234 (≠ Y239), M238 (≠ L243), Q239 (≠ R244), L241 (= L246), D242 (= D247), R245 (= R250), Y364 (≠ G369), E365 (= E370), G366 (= G371)
- binding flavin-adenine dinucleotide: F125 (= F128), L127 (= L130), S128 (≠ T131), G133 (= G136), S134 (= S137), W158 (≠ F161), T160 (= T163), R270 (= R275), F273 (= F278), L280 (≠ N285), Q338 (= Q343), I339 (= I344), G342 (= G347), I360 (= I365), T367 (= T372), E369 (= E374), I370 (≠ V375)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
44% identity, 97% coverage: 10:384/386 of query aligns to 34:406/412 of P15651
- 152:161 (vs. 128:137, 60% identical) binding FAD
- S161 (= S137) binding substrate
- WIT 185:187 (≠ FIT 161:163) binding FAD
- DMGR 269:272 (≠ DEGR 247:250) binding substrate
- R297 (= R275) binding FAD
- QILGG 365:369 (≠ QIFGG 343:347) binding FAD
- E392 (= E370) active site, Proton acceptor
- TSE 394:396 (≠ TTE 372:374) binding FAD
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
43% identity, 97% coverage: 10:384/386 of query aligns to 5:377/380 of 4l1fA
- active site: L125 (= L130), T126 (= T131), G242 (= G249), E363 (= E370), R375 (= R382)
- binding coenzyme a persulfide: T132 (≠ S137), H179 (≠ K186), F232 (≠ Y239), M236 (≠ L243), E237 (≠ R244), L239 (= L246), D240 (= D247), R243 (= R250), Y362 (≠ G369), E363 (= E370), G364 (= G371), R375 (= R382)
- binding flavin-adenine dinucleotide: F123 (= F128), L125 (= L130), T126 (= T131), G131 (= G136), T132 (≠ S137), F156 (= F161), I157 (= I162), T158 (= T163), R268 (= R275), Q270 (≠ A277), F271 (= F278), I275 (= I282), F278 (≠ N285), L281 (≠ I288), Q336 (= Q343), I337 (= I344), G340 (= G347), I358 (= I365), Y362 (≠ G369), T365 (= T372), Q367 (≠ E374)
- binding 1,3-propandiol: L5 (= L10), Q10 (≠ E15)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
43% identity, 97% coverage: 10:384/386 of query aligns to 7:379/385 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 (≠ Y348), T347 (≠ N352), E348 (= E353)
- binding flavin-adenine dinucleotide: F125 (= F128), L127 (= L130), S128 (≠ T131), G133 (= G136), S134 (= S137), W158 (≠ F161), T160 (= T163), R270 (= R275), F273 (= F278), L280 (≠ N285), V282 (≠ A287), Q338 (= Q343), I339 (= I344), G342 (= G347), I360 (= I365), Y364 (≠ G369), T367 (= T372), E369 (= E374), I370 (≠ V375), L373 (≠ M378)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
43% identity, 97% coverage: 10:384/386 of query aligns to 10:382/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (= F128), L130 (= L130), S131 (≠ T131), G136 (= G136), S137 (= S137), W161 (≠ F161), T163 (= T163), T214 (= T216), R273 (= R275), F276 (= F278), L280 (≠ I282), L283 (≠ N285), V285 (≠ A287), Q341 (= Q343), I342 (= I344), G345 (= G347), I363 (= I365), Y367 (≠ G369), T370 (= T372), E372 (= E374), L376 (≠ M378)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
43% identity, 97% coverage: 10:384/386 of query aligns to 34:406/412 of P16219
- G90 (= G66) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E80) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 128:137, 60% identical) binding in other chain
- R171 (= R147) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ FIT 161:163) binding in other chain
- A192 (≠ T170) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (≠ E187) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R275) binding FAD
- Q308 (= Q286) binding in other chain
- R325 (= R303) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (= S331) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QIFGG 343:347) binding FAD
- R380 (= R358) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ TTE 372:374) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
8sgsA Human liver mitochondrial short-chain specific acyl-coa dehydrogenase (see paper)
43% identity, 97% coverage: 10:384/386 of query aligns to 4:376/381 of 8sgsA
- binding coenzyme a: S131 (= S137), A133 (= A139), N177 (≠ K185), F231 (≠ Y239), M235 (≠ L243), L238 (= L246), I312 (≠ K320), E362 (= E370), G363 (= G371)
- binding flavin-adenine dinucleotide: F122 (= F128), L124 (= L130), S125 (≠ T131), G130 (= G136), S131 (= S137), W155 (≠ F161), T157 (= T163), R267 (= R275), F270 (= F278), L274 (≠ I282), L277 (≠ N285), Q335 (= Q343), I336 (= I344), G338 (= G346), G339 (= G347), I357 (= I365), I360 (= I368), Y361 (≠ G369), T364 (= T372), E366 (= E374)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
43% identity, 96% coverage: 14:384/386 of query aligns to 6:378/378 of 4n5fA
- active site: L126 (= L130), T127 (= T131), G243 (= G249), E364 (= E370), R376 (= R382)
- binding dihydroflavine-adenine dinucleotide: L126 (= L130), T127 (= T131), G132 (= G136), S133 (= S137), F157 (= F161), T159 (= T163), T210 (= T216), Y363 (≠ G369), T366 (= T372), E368 (= E374), M372 (= M378)
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
42% identity, 97% coverage: 10:384/386 of query aligns to 1:366/371 of 2vigB
- active site: L121 (= L130), S122 (≠ T131), G231 (= G249), E352 (= E370), G364 (≠ R382)
- binding coenzyme a persulfide: S128 (= S137), F221 (≠ Y239), M225 (≠ L243), Q226 (≠ R244), L228 (= L246), D229 (= D247), R232 (= R250), E352 (= E370), G353 (= G371), I357 (≠ V375)
- binding flavin-adenine dinucleotide: L121 (= L130), S122 (≠ T131), G127 (= G136), S128 (= S137), W152 (≠ F161), T154 (= T163), R257 (= R275), F260 (= F278), L264 (≠ I282), L267 (≠ N285), Q325 (= Q343), I326 (= I344), G329 (= G347), I347 (= I365), Y351 (≠ G369), T354 (= T372), E356 (= E374)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
43% identity, 95% coverage: 17:384/386 of query aligns to 9:372/374 of 5lnxD
- active site: L122 (= L130), T123 (= T131), G239 (= G249), E358 (= E370), K370 (≠ R382)
- binding flavin-adenine dinucleotide: L122 (= L130), T123 (= T131), G128 (= G136), S129 (= S137), F153 (= F161), T155 (= T163), R265 (= R275), Q267 (≠ A277), F268 (= F278), I272 (= I282), N275 (= N285), I278 (= I288), Q331 (= Q343), I332 (= I344), G335 (= G347), Y357 (≠ G369), T360 (= T372), E362 (= E374)
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
44% identity, 96% coverage: 10:381/386 of query aligns to 5:378/383 of 1bucA
- active site: L128 (= L130), T129 (= T131), G246 (= G249), E367 (= E370)
- binding acetoacetyl-coenzyme a: L96 (= L98), F126 (= F128), G134 (= G136), T135 (≠ S137), T162 (= T163), N182 (≠ K185), H183 (≠ K186), F236 (≠ Y239), M240 (≠ L243), M241 (≠ R244), L243 (= L246), D244 (= D247), T317 (≠ K320), Y366 (≠ G369), E367 (= E370), G368 (= G371)
- binding flavin-adenine dinucleotide: F126 (= F128), L128 (= L130), T129 (= T131), G134 (= G136), T135 (≠ S137), F160 (= F161), T162 (= T163), Y366 (≠ G369), T369 (= T372), E371 (= E374), M375 (= M378)
Sites not aligning to the query:
Q06319 Acyl-CoA dehydrogenase, short-chain specific; Butyryl-CoA dehydrogenase; BCAD; SCAD; EC 1.3.8.1 from Megasphaera elsdenii (see paper)
44% identity, 96% coverage: 10:381/386 of query aligns to 5:378/383 of Q06319
- E367 (= E370) active site, Proton acceptor; mutation to Q: Loss of activity.
4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
46% identity, 94% coverage: 22:384/386 of query aligns to 16:376/376 of 4m9aB
- active site: L124 (= L130), T125 (= T131), G241 (= G249), E362 (= E370), R374 (= R382)
- binding dihydroflavine-adenine dinucleotide: F122 (= F128), T125 (= T131), G130 (= G136), S131 (= S137), F155 (= F161), T157 (= T163), T208 (= T216), Y361 (≠ G369), T364 (= T372), E366 (= E374), M370 (= M378)
P45954 Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial; SBCAD; 2-methyl branched chain acyl-CoA dehydrogenase; 2-MEBCAD; 2-methylbutyryl-coenzyme A dehydrogenase; 2-methylbutyryl-CoA dehydrogenase; EC 1.3.8.5 from Homo sapiens (Human) (see 6 papers)
40% identity, 97% coverage: 12:384/386 of query aligns to 59:428/432 of P45954
- V137 (≠ I90) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ T91) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 128:137, 70% identical) binding in other chain
- S183 (= S137) binding substrate
- WI--S 207:209 (≠ FITNS 161:165) binding in other chain
- S210 (≠ G166) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ K185) binding substrate
- L255 (≠ W211) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (= Y239) binding substrate
- NEGR 291:294 (≠ DEGR 247:250) binding substrate
- I316 (≠ A272) to V: in dbSNP:rs1131430
- R319 (= R275) binding FAD
- Q330 (= Q286) binding FAD
- EWMGG 387:391 (≠ QIFGG 343:347) binding FAD
- A416 (≠ T372) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ TTE 372:374) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
40% identity, 97% coverage: 12:384/386 of query aligns to 8:377/381 of 2jifA
- active site: L125 (= L130), S126 (≠ T131), G242 (= G249), E363 (= E370), K375 (≠ R382)
- binding coenzyme a persulfide: S132 (= S137), S134 (≠ A139), Y178 (≠ K185), Y232 (= Y239), I236 (≠ L243), L239 (= L246), N240 (≠ D247), R243 (= R250), Y362 (≠ G369), E363 (= E370), G364 (= G371), I368 (≠ V375)
- binding flavin-adenine dinucleotide: F123 (= F128), L125 (= L130), S126 (≠ T131), G131 (= G136), S132 (= S137), W156 (≠ F161), I157 (= I162), S158 (= S165), K201 (= K208), T209 (= T216), R268 (= R275), F271 (= F278), L275 (≠ I282), F278 (≠ N285), L281 (≠ I288), E336 (≠ Q343), W337 (≠ I344), G340 (= G347), N367 (≠ E374), I368 (≠ V375)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
41% identity, 97% coverage: 10:384/386 of query aligns to 5:376/379 of 1ukwB
- active site: L124 (= L130), S125 (≠ T131), T241 (≠ G249), E362 (= E370), R374 (= R382)
- binding cobalt (ii) ion: D145 (≠ G151), H146 (= H152)
- binding flavin-adenine dinucleotide: F122 (= F128), L124 (= L130), S125 (≠ T131), G130 (= G136), S131 (= S137), W155 (≠ F161), S157 (≠ T163), K200 (= K208), L357 (≠ I365), Y361 (≠ G369), E362 (= E370), T364 (= T372), E366 (= E374), L370 (≠ M378)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
41% identity, 97% coverage: 10:384/386 of query aligns to 5:376/379 of 1ukwA
- active site: L124 (= L130), S125 (≠ T131), T241 (≠ G249), E362 (= E370), R374 (= R382)
- binding flavin-adenine dinucleotide: F122 (= F128), L124 (= L130), S125 (≠ T131), G130 (= G136), S131 (= S137), W155 (≠ F161), S157 (≠ T163), L357 (≠ I365), Y361 (≠ G369), E362 (= E370), T364 (= T372), E366 (= E374), L370 (≠ M378)
2d29A Structural study on project id tt0172 from thermus thermophilus hb8
42% identity, 96% coverage: 16:384/386 of query aligns to 12:382/386 of 2d29A
- active site: L126 (= L130), T127 (= T131), G247 (= G249), E368 (= E370), R380 (= R382)
- binding flavin-adenine dinucleotide: L126 (= L130), T127 (= T131), G132 (= G136), S133 (= S137), F157 (= F161), I158 (= I162), T159 (= T163), L363 (≠ I365), T370 (= T372), E372 (= E374)
Query Sequence
>WP_011781244.1 NCBI__GCF_000015305.1:WP_011781244.1
MSNNLATGILPDHYEQLAKTVRDFAQSVVAPVAAKHDEEHSFPYEVVAGMADMGLFGLPF
PEEYGGMGGDYFALCLALEELGKVDQSVAITLEAGVSLGAMPVYRFGTEAQKQEWLPLLA
SGKALGAFGLTEAGGGSDAGATKTTARLDDGHWVINGSKQFITNSGTDITKLVTVTAVTG
ETDGKKEISSILVPVPTPGFTAEPAYNKVGWNASDTHPLSFDDVRVPQENLLGERGRGYA
GFLRILDEGRIAIAALSVGAAQGCVDESVKYAKERHAFGRAIGTNQAIAFKIARMEARAH
AARAAYYDAAALMLAGKPFKKAAAVAKLVSSEAAMDNARDATQIFGGYGFMNEYPVARHY
RDSKILEIGEGTTEVQLMLIGRELGL
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