SitesBLAST
Comparing Dsui_0975 Dsui_0975 acyl-CoA dehydrogenase 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)
4ktoA Crystal structure of a putative isovaleryl-coa dehydrogenase (psi- nysgrc-012251) from sinorhizobium meliloti 1021
74% identity, 98% coverage: 6:388/390 of query aligns to 6:377/377 of 4ktoA
- active site: M130 (= M130), S131 (= S131), E239 (= E247), A360 (= A371), R372 (= R383)
- binding flavin-adenine dinucleotide: L128 (= L128), M130 (= M130), S131 (= S131), M155 (= M160), W156 (= W161), T158 (= T163), R265 (= R273), F268 (= F276), I272 (= I280), F275 (= F283), M278 (= M286), Q333 (= Q344), A334 (≠ T345), G337 (= G348), L355 (= L366), G359 (= G370), T362 (= T373), E364 (= E375)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
62% identity, 97% coverage: 9:388/390 of query aligns to 7:387/387 of 1ivhA
- active site: M130 (= M130), S131 (= S131), E249 (= E247), A370 (= A371), R382 (= R383)
- binding coenzyme a persulfide: S137 (= S137), S185 (≠ A183), R186 (≠ K184), V239 (≠ A237), Y240 (≠ K238), M243 (= M241), E249 (= E247), R250 (= R248), G369 (= G370), A370 (= A371), G371 (= G372), V375 (≠ I376)
- binding flavin-adenine dinucleotide: L128 (= L128), M130 (= M130), S131 (= S131), G136 (= G136), S137 (= S137), W161 (= W161), T163 (= T163), R275 (= R273), F278 (= F276), F285 (= F283), M288 (= M286), Q343 (= Q344), C344 (≠ T345), G347 (= G348), T372 (= T373), E374 (= E375)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
62% identity, 97% coverage: 9:388/390 of query aligns to 11:391/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (= S131), G140 (= G136), S141 (= S137), W165 (= W161), T167 (= T163), R279 (= R273), F282 (= F276), I286 (= I280), F289 (= F283), Q347 (= Q344), C348 (≠ T345), G351 (= G348), L369 (= L366), G375 (= G372), T376 (= T373), L382 (≠ M379)
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)
62% identity, 97% coverage: 9:388/390 of query aligns to 44:424/426 of P26440
- 165:174 (vs. 128:137, 100% identical) binding
- S174 (= S137) binding
- WIT 198:200 (= WIT 161:163) binding
- SR 222:223 (≠ AK 183:184) binding
- G250 (= G211) to A: in IVA; uncertain significance
- Y277 (≠ K238) binding
- DLER 284:287 (≠ DYER 245:248) binding
- E286 (= E247) 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 (≠ C252) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R273) binding
- Q323 (= Q284) binding
- I379 (= I343) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QTLGG 344:348) binding
- R398 (= R362) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (= Y367) to N: in IVA; uncertain significance
- A407 (= A371) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (= AG 371:372) binding
- TSE 409:411 (= TSE 373:375) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
41% identity, 96% coverage: 12:386/390 of query aligns to 9:380/384 of 1jqiA
- active site: G377 (≠ R383)
- binding acetoacetyl-coenzyme a: L95 (= L98), F125 (≠ L128), S134 (= S137), F234 (≠ A237), M238 (= M241), Q239 (≠ S242), L241 (= L244), D242 (= D245), R245 (= R248), Y364 (≠ G370), E365 (≠ A371), G366 (= G372)
- binding flavin-adenine dinucleotide: F125 (≠ L128), L127 (≠ M130), S128 (= S131), G133 (= G136), S134 (= S137), W158 (= W161), T160 (= T163), R270 (= R273), F273 (= F276), L280 (≠ F283), Q338 (= Q344), I339 (≠ T345), G342 (= G348), I360 (≠ L366), T367 (= T373), E369 (= E375), I370 (= I376)
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, 96% coverage: 12:386/390 of query aligns to 36:407/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
42% identity, 97% coverage: 10:386/390 of query aligns to 2:373/374 of 5lnxD
- active site: L122 (≠ M130), T123 (≠ S131), G239 (≠ E247), E358 (≠ A371), K370 (≠ R383)
- binding flavin-adenine dinucleotide: L122 (≠ M130), T123 (≠ S131), G128 (= G136), S129 (= S137), F153 (≠ W161), T155 (= T163), R265 (= R273), Q267 (= Q275), F268 (= F276), I272 (= I280), N275 (≠ F283), I278 (≠ M286), Q331 (= Q344), I332 (≠ T345), G335 (= G348), Y357 (≠ G370), T360 (= T373), E362 (= E375)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
41% identity, 95% coverage: 15:386/390 of query aligns to 9:377/378 of 5ol2F
- active site: L124 (≠ M130), T125 (≠ S131), G241 (≠ E247), G374 (≠ R383)
- binding calcium ion: E29 (≠ Q35), E33 (≠ D39), R35 (≠ E41)
- binding coenzyme a persulfide: L238 (= L244), R242 (= R248), E362 (≠ A371), G363 (= G372)
- binding flavin-adenine dinucleotide: F122 (≠ L128), L124 (≠ M130), T125 (≠ S131), P127 (= P133), T131 (≠ S137), F155 (≠ W161), I156 (= I162), T157 (= T163), E198 (≠ L204), R267 (= R273), F270 (= F276), L274 (≠ I280), F277 (= F283), Q335 (= Q344), L336 (≠ T345), G338 (= G347), G339 (= G348), Y361 (≠ G370), T364 (= T373), E366 (= E375)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
40% identity, 98% coverage: 6:386/390 of query aligns to 1:378/380 of 4l1fA
- active site: L125 (≠ M130), T126 (≠ S131), G242 (≠ E247), E363 (≠ A371), R375 (= R383)
- binding coenzyme a persulfide: T132 (≠ S137), H179 (≠ K184), F232 (≠ A237), M236 (= M241), E237 (≠ S242), L239 (= L244), D240 (= D245), R243 (= R248), Y362 (≠ G370), E363 (≠ A371), G364 (= G372), R375 (= R383)
- binding flavin-adenine dinucleotide: F123 (≠ L128), L125 (≠ M130), T126 (≠ S131), G131 (= G136), T132 (≠ S137), F156 (≠ W161), I157 (= I162), T158 (= T163), R268 (= R273), Q270 (= Q275), F271 (= F276), I275 (= I280), F278 (= F283), L281 (≠ M286), Q336 (= Q344), I337 (≠ T345), G340 (= G348), I358 (≠ L366), Y362 (≠ G370), T365 (= T373), Q367 (≠ E375)
- binding 1,3-propandiol: L5 (≠ H10), Q10 (≠ E15)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
41% identity, 96% coverage: 12:386/390 of query aligns to 36:407/412 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 (≠ E147) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (= WIT 161:163) binding in other chain
- A192 (= A168) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G185) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R273) binding
- Q308 (= Q284) binding in other chain
- R325 (= R301) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ A332) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QTLGG 344:348) binding
- R380 (= R359) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (= TSE 373:375) 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
41% identity, 96% coverage: 12:386/390 of query aligns to 12:383/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ L128), L130 (≠ M130), S131 (= S131), G136 (= G136), S137 (= S137), W161 (= W161), T163 (= T163), T214 (= T214), R273 (= R273), F276 (= F276), L280 (≠ I280), L283 (≠ F283), V285 (≠ L285), Q341 (= Q344), I342 (≠ T345), G345 (= G348), I363 (≠ L366), Y367 (≠ G370), T370 (= T373), E372 (= E375), L376 (≠ M379)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
41% identity, 96% coverage: 12:386/390 of query aligns to 6:377/381 of 8sgsA
- binding coenzyme a: S131 (= S137), A133 (≠ V139), N177 (≠ A183), F231 (≠ A237), M235 (= M241), L238 (= L244), I312 (≠ R321), E362 (≠ A371), G363 (= G372)
- binding flavin-adenine dinucleotide: F122 (≠ L128), L124 (≠ M130), S125 (= S131), G130 (= G136), S131 (= S137), W155 (= W161), T157 (= T163), R267 (= R273), F270 (= F276), L274 (≠ I280), L277 (≠ F283), Q335 (= Q344), I336 (≠ T345), G338 (= G347), G339 (= G348), I357 (≠ L366), I360 (= I369), Y361 (≠ G370), T364 (= T373), E366 (= E375)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
41% identity, 96% coverage: 12:386/390 of query aligns to 9:380/385 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 (≠ V349), T347 (≠ N353), E348 (= E354)
- binding flavin-adenine dinucleotide: F125 (≠ L128), L127 (≠ M130), S128 (= S131), G133 (= G136), S134 (= S137), W158 (= W161), T160 (= T163), R270 (= R273), F273 (= F276), L280 (≠ F283), V282 (≠ L285), Q338 (= Q344), I339 (≠ T345), G342 (= G348), I360 (≠ L366), Y364 (≠ G370), T367 (= T373), E369 (= E375), I370 (= I376), L373 (≠ M379)
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
40% identity, 96% coverage: 12:386/390 of query aligns to 3:367/371 of 2vigB
- active site: L121 (≠ M130), S122 (= S131), G231 (≠ E247), E352 (≠ A371), G364 (≠ R383)
- binding coenzyme a persulfide: S128 (= S137), F221 (≠ A237), M225 (= M241), Q226 (≠ S242), L228 (= L244), D229 (= D245), R232 (= R248), E352 (≠ A371), G353 (= G372), I357 (= I376)
- binding flavin-adenine dinucleotide: L121 (≠ M130), S122 (= S131), G127 (= G136), S128 (= S137), W152 (= W161), T154 (= T163), R257 (= R273), F260 (= F276), L264 (≠ I280), L267 (≠ F283), Q325 (= Q344), I326 (≠ T345), G329 (= G348), I347 (≠ L366), Y351 (≠ G370), T354 (= T373), E356 (= E375)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
38% identity, 97% coverage: 6:385/390 of query aligns to 2:378/378 of 4n5fA
- active site: L126 (≠ M130), T127 (≠ S131), G243 (≠ E247), E364 (≠ A371), R376 (= R383)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ M130), T127 (≠ S131), G132 (= G136), S133 (= S137), F157 (≠ W161), T159 (= T163), T210 (= T214), Y363 (≠ G370), T366 (= T373), E368 (= E375), M372 (= M379)
3mpjB Structure of the glutaryl-coenzyme a dehydrogenase (see paper)
39% identity, 96% coverage: 6:381/390 of query aligns to 1:377/393 of 3mpjB
- active site: I128 (≠ M130), T129 (≠ S131), T245 (≠ E247), E367 (≠ A371)
- binding flavin-adenine dinucleotide: F126 (≠ L128), I128 (≠ M130), T129 (≠ S131), G134 (= G136), S135 (= S137), W159 (= W161), I160 (= I162), S161 (≠ T163), V366 (≠ G370), S369 (≠ T373), N371 (≠ E375), M375 (= M379)
- binding : H36 (≠ E41), F37 (= F42), Y39 (vs. gap), A164 (≠ G166), Q165 (≠ D167), D167 (= D169), N193 (≠ G194)
Sites not aligning to the query:
C3UVB0 Glutaryl-CoA dehydrogenase; GDH(Des); EC 1.3.99.32 from Desulfococcus multivorans (see paper)
39% identity, 96% coverage: 6:381/390 of query aligns to 1:377/389 of C3UVB0
- A80 (≠ S82) mutation to E: Loses the FAD cofactor and dehydrogenase activity.
- R87 (≠ G89) binding
- V88 (≠ L90) mutation to S: A residual dehydrogenase activity is observed.
- N91 (≠ G93) binding
- FGIT 126:129 (≠ LAMS 128:131) binding
- S135 (= S137) binding ; binding
- WIS 159:161 (≠ WIT 161:163) binding
- S181 (≠ A183) binding
- R271 (= R273) binding
- FQMN 281:284 (≠ FQLM 283:286) binding
- R340 (≠ Q344) binding
- A344 (≠ G348) binding
- V366 (≠ G370) mutation to Y: Loses the FAD cofactor but a residual dehydrogenase activity is observed.
- EGSAN 367:371 (≠ AGTSE 371:375) binding
Sites not aligning to the query:
3mpiC Structure of the glutaryl-coenzyme a dehydrogenase glutaryl-coa complex (see paper)
39% identity, 96% coverage: 6:381/390 of query aligns to 1:377/395 of 3mpiC
- active site: I128 (≠ M130), T129 (≠ S131), T245 (≠ E247), E367 (≠ A371)
- binding flavin-adenine dinucleotide: I128 (≠ M130), T129 (≠ S131), G134 (= G136), S135 (= S137), W159 (= W161), I160 (= I162), S161 (≠ T163), M365 (≠ I369), V366 (≠ G370), S369 (≠ T373), N371 (≠ E375), M375 (= M379)
- binding glutaryl-coenzyme A: R87 (≠ G89), F126 (≠ L128), S135 (= S137), V137 (= V139), S181 (≠ A183), F239 (≠ M241), R246 (= R248), N315 (≠ A317), V366 (≠ G370), E367 (≠ A371), G368 (= G372), I376 (≠ L380)
Sites not aligning to the query:
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
36% identity, 96% coverage: 16:388/390 of query aligns to 12:380/381 of 2jifA
- active site: L125 (≠ M130), S126 (= S131), G242 (≠ E247), E363 (≠ A371), K375 (≠ R383)
- binding coenzyme a persulfide: S132 (= S137), S134 (≠ V139), Y178 (≠ A183), Y232 (≠ A237), I236 (≠ M241), L239 (= L244), N240 (≠ D245), R243 (= R248), Y362 (≠ G370), E363 (≠ A371), G364 (= G372), I368 (= I376)
- binding flavin-adenine dinucleotide: F123 (≠ L128), L125 (≠ M130), S126 (= S131), G131 (= G136), S132 (= S137), W156 (= W161), I157 (= I162), S158 (≠ T163), K201 (= K206), T209 (= T214), R268 (= R273), F271 (= F276), L275 (≠ I280), F278 (= F283), L281 (≠ M286), E336 (≠ Q344), W337 (≠ T345), G340 (= G348), N367 (≠ E375), I368 (= I376)
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)
36% identity, 96% coverage: 16:388/390 of query aligns to 63:431/432 of P45954
- V137 (≠ L90) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ S91) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 128:137, 50% identical) binding in other chain
- S183 (= S137) binding
- WIS 207:209 (≠ WIT 161:163) binding in other chain
- S210 (≠ N164) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ A183) binding
- L255 (≠ M209) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ A237) binding
- NEGR 291:294 (≠ DYER 245:248) binding
- I316 (≠ L270) to V: in dbSNP:rs1131430
- R319 (= R273) binding
- Q330 (= Q284) binding
- EWMGG 387:391 (≠ QTLGG 344:348) binding
- A416 (≠ T373) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ TSE 373:375) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
Query Sequence
>Dsui_0975 Dsui_0975 acyl-CoA dehydrogenase
MHIPSLDFGHGETIEMLRDTVRAFAAKEIAPRAAQIDRDNEFPADLWQKFGDLGLLGMTA
EEEYGGTAMGYLAHIVAMEEISRASASVGLSYGAHSNLCVNQIRRNGTAAQKAKYLPGLI
SGTQVGALAMSEPNAGSDVVSMKLKAEKKGDRYVLNGSKMWITNGGDADTLVVYAKTDLN
AGAKGMTAFIVEKGFKGFSHGTHLDKLGMRGSNTFPLFFDDCEVPEENVLGGVGNGAKVL
MSGLDYERAVLCGGPLGIMAACMDVVLPYLHEREQFGTAIGEFQLMQGKLADMYSTWQAT
RAYVYAVGQACDRADHARSLRKDAAGAILYSAEKATWMAGDAIQTLGGVGYTNEYPTGRL
WRDAKLYEIGAGTSEIRRMLIGRELFAETA
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