SitesBLAST
Comparing CA265_RS17575 CA265_RS17575 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)
3owaC Crystal structure of acyl-coa dehydrogenase complexed with fad from bacillus anthracis
47% identity, 98% coverage: 9:595/597 of query aligns to 2:585/587 of 3owaC
- active site: L143 (= L151), T144 (= T152), G258 (= G267), E398 (= E407), G410 (≠ D419)
- binding flavin-adenine dinucleotide: Y141 (= Y149), L143 (= L151), T144 (= T152), G149 (= G157), S150 (= S158), W176 (= W184), I177 (= I185), T178 (= T186), R284 (= R293), F287 (= F296), I291 (= I300), F294 (≠ Y303), Q371 (= Q380), I372 (= I381), G375 (= G384), I393 (= I402), F397 (= F406), T400 (= T409), E402 (= E411), I403 (= I412), L406 (= L415), Q480 (= Q490)
2z1qB Crystal structure of acyl coa dehydrogenase
47% identity, 98% coverage: 10:595/597 of query aligns to 6:545/549 of 2z1qB
- active site: L144 (= L151), T145 (= T152), G259 (= G267), E394 (= E407), G406 (≠ D419)
- binding flavin-adenine dinucleotide: Y142 (= Y149), L144 (= L151), T145 (= T152), G150 (= G157), S151 (= S158), W177 (= W184), S179 (≠ T186), R285 (= R293), F288 (= F296), I292 (= I300), F295 (≠ Y303), I298 (= I306), H369 (≠ Y382), G370 (= G383), F393 (= F406), I399 (= I412), Q448 (= Q490)
8pheA Acad9-wt in complex with ecsit-cter (see paper)
35% identity, 98% coverage: 13:596/597 of query aligns to 5:542/551 of 8pheA
- binding : L143 (= L151), D151 (= D159), A153 (≠ N161), S154 (= S162), I155 (≠ G163), K202 (vs. gap), I205 (≠ L206), F256 (= F257), M260 (≠ V261), F295 (= F296), N296 (≠ G297), I394 (= I412), Y398 (≠ L416), L401 (≠ D419), Q405 (≠ K423), K451 (vs. gap), M454 (≠ S487)
8phfA Cryo-em structure of human acad9-s191a (see paper)
35% identity, 98% coverage: 13:596/597 of query aligns to 5:538/547 of 8phfA
- binding flavin-adenine dinucleotide: T144 (= T152), W176 (= W184), K225 (= K226), R292 (= R293), Q294 (= Q295), F295 (= F296), F302 (≠ Y303), L304 (≠ A305), I305 (= I306), I363 (= I381), G365 (= G383), G366 (= G384), F388 (= F406), E393 (= E411), M397 (≠ L415), Q453 (= Q490)
Q9H845 Complex I assembly factor ACAD9, mitochondrial; Acyl-CoA dehydrogenase family member 9; ACAD-9; EC 1.3.8.- from Homo sapiens (Human) (see 4 papers)
34% identity, 98% coverage: 13:596/597 of query aligns to 42:612/621 of Q9H845
- R193 (≠ K164) to W: in MC1DN20; uncertain significance; dbSNP:rs377547811
- S234 (≠ D202) to F: in MC1DN20; uncertain significance
- G303 (= G267) to S: in MC1DN20; uncertain significance; dbSNP:rs143383023
- A326 (≠ S290) to T: in MC1DN20; uncertain significance; dbSNP:rs115532916
- E413 (≠ D394) to K: in MC1DN20; uncertain significance; dbSNP:rs149753643
- E426 (= E407) mutation to Q: Loss of long-chain-acyl-CoA dehydrogenase activity. Does not affect mitochondrial complex I assembly.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
41% identity, 65% coverage: 32:422/597 of query aligns to 4:373/374 of 5lnxD
- active site: L122 (= L151), T123 (= T152), G239 (= G267), E358 (= E407), K370 (≠ D419)
- binding flavin-adenine dinucleotide: L122 (= L151), T123 (= T152), G128 (= G157), S129 (= S158), F153 (≠ W184), T155 (= T186), R265 (= R293), Q267 (= Q295), F268 (= F296), I272 (= I300), N275 (≠ Y303), I278 (= I306), Q331 (= Q380), I332 (= I381), G335 (= G384), Y357 (≠ F406), T360 (= T409), E362 (= E411)
3b96A Structural basis for substrate fatty-acyl chain specificity: crystal structure of human very-long-chain acyl-coa dehydrogenase (see paper)
39% identity, 72% coverage: 5:431/597 of query aligns to 1:411/554 of 3b96A
- active site: L148 (= L151), T149 (= T152), G272 (= G267), E394 (= E407), L406 (≠ M426)
- binding flavin-adenine dinucleotide: F146 (≠ Y149), L148 (= L151), T149 (= T152), G154 (= G157), S155 (= S158), W181 (= W184), I182 (= I185), S183 (≠ T186), I389 (= I402), F393 (= F406), T396 (= T409), D398 (≠ E411), I399 (= I412)
- binding tetradecanoyl-coa: V96 (≠ A100), G107 (≠ A112), F146 (≠ Y149), L269 (= L264), F393 (= F406), E394 (= E407)
Sites not aligning to the query:
P49748 Very long-chain specific acyl-CoA dehydrogenase, mitochondrial; VLCAD; EC 1.3.8.9 from Homo sapiens (Human) (see 8 papers)
36% identity, 86% coverage: 5:515/597 of query aligns to 69:556/655 of P49748
- 214:223 (vs. 149:158, 80% identical) binding
- WIS 249:251 (≠ WIT 184:186) binding
- F458 (≠ N403) to L: in ACADVLD; loss of acyl-CoA dehydrogenase activity; Loss of FAD cofactor-binding; dbSNP:rs118204017; mutation to T: Decreased acyl-CoA dehydrogenase activity. Decreased affinity for acyl-CoA. No effect on FAD cofactor-binding.; mutation to V: Loss of acyl-CoA dehydrogenase activity. Loss of FAD cofactor-binding.; mutation to Y: Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. Decreased FAD cofactor-binding.
- FEG 461:463 (= FEG 406:408) binding
- E462 (= E407) active site, Proton acceptor; mutation to D: Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. No effect on FAD cofactor-binding.; mutation to Q: Loss of acyl-CoA dehydrogenase activity. No effect on FAD cofactor-binding.
- TND 464:466 (≠ TNE 409:411) binding
- A490 (≠ E442) to P: in ACADVLD; decreased association with mitochondrial inner membrane; may affect substrate specificity, possibly reducing the affinity for long-chain acyl-CoA substrates; dbSNP:rs759775666; mutation A->G,V,S,D,H: Changed substrate specificity with decreased affinity for tetradecanoyl-CoA and hexadecanoyl-CoA.
- L502 (= L456) to P: in ACADVLD; decreased association with mitochondrial inner membrane; decreased specific activity towards several substrates in vitro
- E534 (= E491) to K: in ACADVLD; uncertain significance; dbSNP:rs2230180
Sites not aligning to the query:
- 1:40 modified: transit peptide, Mitochondrion
- 562 binding
- 583 S → W: in ACADVLD; Loss of homodimerization; loss of localization to mitochondrial inner membrane; dbSNP:rs1085307648
7s7gA Crystal structure analysis of human vlcad
39% identity, 72% coverage: 5:431/597 of query aligns to 1:411/571 of 7s7gA
- binding flavin-adenine dinucleotide: F146 (≠ Y149), L148 (= L151), T149 (= T152), G154 (= G157), S155 (= S158), W181 (= W184), I182 (= I185), S183 (≠ T186), I389 (= I402), T396 (= T409), D398 (≠ E411), I399 (= I412)
Sites not aligning to the query:
2uxwA Crystal structure of human very long chain acyl-coa dehydrogenase (acadvl)
36% identity, 84% coverage: 12:515/597 of query aligns to 8:499/567 of 2uxwA
- active site: P21 (≠ F25), L148 (= L151), T149 (= T152), G272 (= G267), E394 (= E407), L406 (≠ M426)
- binding flavin-adenine dinucleotide: F146 (≠ Y149), L148 (= L151), T149 (= T152), G154 (= G157), S155 (= S158), W181 (= W184), I182 (= I185), S183 (≠ T186), F393 (= F406), T396 (= T409), D398 (≠ E411), I399 (= I412), Q474 (= Q490)
- binding trans delta2 palmitenoyl-coenzymea: V96 (≠ A100), G107 (≠ A112), L110 (= L113), F146 (≠ Y149), L269 (= L264), F393 (= F406), E394 (= E407), G395 (= G408)
P50544 Very long-chain specific acyl-CoA dehydrogenase, mitochondrial; MVLCAD; VLCAD; EC 1.3.8.9 from Mus musculus (Mouse) (see paper)
35% identity, 86% coverage: 5:515/597 of query aligns to 70:557/656 of P50544
- C238 (≠ D172) modified: S-nitrosocysteine
8ca1B Cryo-em structure of the acadvl dimer from mus musculus. (see paper)
35% identity, 86% coverage: 5:515/597 of query aligns to 3:490/589 of 8ca1B
- binding flavin-adenine dinucleotide: F148 (≠ Y149), T151 (= T152), G156 (= G157), S157 (= S158), W183 (= W184), S185 (≠ T186), R300 (= R293), Q302 (= Q295), F303 (= F296), I307 (= I300), V312 (≠ A305), I313 (= I306), Q369 (= Q380), I370 (= I381), F395 (= F406), D400 (≠ E411), I401 (= I412)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
37% identity, 65% coverage: 35:423/597 of query aligns to 9:378/378 of 5ol2F
- active site: L124 (= L151), T125 (= T152), G241 (= G267), G374 (≠ D419)
- binding calcium ion: E29 (≠ K55), E33 (≠ Q59), R35 (≠ E63)
- binding coenzyme a persulfide: L238 (= L264), R242 (= R268), E362 (= E407), G363 (= G408)
- binding flavin-adenine dinucleotide: F122 (≠ Y149), L124 (= L151), T125 (= T152), P127 (= P154), T131 (≠ S158), F155 (≠ W184), I156 (= I185), T157 (= T186), E198 (= E224), R267 (= R293), F270 (= F296), L274 (≠ I300), F277 (≠ Y303), Q335 (= Q380), L336 (≠ I381), G338 (= G383), G339 (= G384), Y361 (≠ F406), T364 (= T409), E366 (= E411)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
36% identity, 68% coverage: 19:423/597 of query aligns to 27:408/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
35% identity, 68% coverage: 19:423/597 of query aligns to 27:408/412 of P16219
- G90 (= G88) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (≠ V102) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 149:158, 50% identical) binding in other chain
- R171 (≠ S170) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (= WIT 184:186) binding in other chain
- A192 (= A191) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (≠ N205) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R293) binding
- Q308 (≠ G304) binding in other chain
- R325 (≠ D321) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (= S368) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QIYGG 380:384) binding
- R380 (= R395) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ TNE 409:411) 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
35% identity, 68% coverage: 19:423/597 of query aligns to 3:384/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ Y149), L130 (= L151), S131 (≠ T152), G136 (= G157), S137 (= S158), W161 (= W184), T163 (= T186), T214 (= T234), R273 (= R293), F276 (= F296), L280 (≠ I300), L283 (≠ Y303), V285 (≠ A305), Q341 (= Q380), I342 (= I381), G345 (= G384), I363 (= I402), Y367 (≠ F406), T370 (= T409), E372 (= E411), L376 (= L415)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
36% identity, 68% coverage: 21:423/597 of query aligns to 2:381/384 of 1jqiA
- active site: G377 (≠ D419)
- binding acetoacetyl-coenzyme a: L95 (≠ I119), F125 (≠ Y149), S134 (= S158), F234 (= F257), M238 (≠ V261), Q239 (≠ N262), L241 (= L264), D242 (≠ N265), R245 (= R268), Y364 (≠ F406), E365 (= E407), G366 (= G408)
- binding flavin-adenine dinucleotide: F125 (≠ Y149), L127 (= L151), S128 (≠ T152), G133 (= G157), S134 (= S158), W158 (= W184), T160 (= T186), R270 (= R293), F273 (= F296), L280 (≠ Y303), Q338 (= Q380), I339 (= I381), G342 (= G384), I360 (= I402), T367 (= T409), E369 (= E411), I370 (= I412)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
35% identity, 68% coverage: 21:423/597 of query aligns to 2:381/385 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 (= M385), T347 (≠ A389), E348 (≠ D390)
- binding flavin-adenine dinucleotide: F125 (≠ Y149), L127 (= L151), S128 (≠ T152), G133 (= G157), S134 (= S158), W158 (= W184), T160 (= T186), R270 (= R293), F273 (= F296), L280 (≠ Y303), V282 (≠ A305), Q338 (= Q380), I339 (= I381), G342 (= G384), I360 (= I402), Y364 (≠ F406), T367 (= T409), E369 (= E411), I370 (= I412), L373 (= L415)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
35% identity, 66% coverage: 29:423/597 of query aligns to 3:378/381 of 8sgsA
- binding coenzyme a: S131 (= S158), A133 (= A160), N177 (≠ D203), F231 (= F257), M235 (≠ V261), L238 (= L264), I312 (≠ A357), E362 (= E407), G363 (= G408)
- binding flavin-adenine dinucleotide: F122 (≠ Y149), L124 (= L151), S125 (≠ T152), G130 (= G157), S131 (= S158), W155 (= W184), T157 (= T186), R267 (= R293), F270 (= F296), L274 (≠ I300), L277 (≠ Y303), Q335 (= Q380), I336 (= I381), G338 (= G383), G339 (= G384), I357 (= I402), I360 (= I405), Y361 (≠ F406), T364 (= T409), E366 (= E411)
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
34% identity, 66% coverage: 30:423/597 of query aligns to 1:368/371 of 2vigB
- active site: L121 (= L151), S122 (≠ T152), G231 (= G267), E352 (= E407), G364 (≠ D419)
- binding coenzyme a persulfide: S128 (= S158), F221 (= F257), M225 (≠ V261), Q226 (≠ N262), L228 (= L264), D229 (≠ N265), R232 (= R268), E352 (= E407), G353 (= G408), I357 (= I412)
- binding flavin-adenine dinucleotide: L121 (= L151), S122 (≠ T152), G127 (= G157), S128 (= S158), W152 (= W184), T154 (= T186), R257 (= R293), F260 (= F296), L264 (≠ I300), L267 (≠ Y303), Q325 (= Q380), I326 (= I381), G329 (= G384), I347 (= I402), Y351 (≠ F406), T354 (= T409), E356 (= E411)
Query Sequence
>CA265_RS17575 CA265_RS17575 acyl-CoA dehydrogenase
METTEKKTIKGGEFLIKDTTYQEVFIPEEFDEEQQMIAQTCRDFLAAEVYPNLDKIDKQE
DPELMPTLLTKAGELGILGVSVPEEYGGFGKNFNTSMLVADVVGAGHSFAVALSAHTGIG
TLPILYYGNEAQKAKYIPKLGSGEWKAAYCLTEPNSGSDANSGKTKATLSEDGKHYIITG
QKMWITNGGFADIFIVFAKIDDDKNLTAFIVEKDFGGITMNPEEHKMGIKGSSTRQVFFN
DCPVPVENMLSDRENGFKIAVNILNIGRIKLSAAAIGASKATLNTAINYSNERIQFGRPI
SKYGAIRFKIAEIASKLYAVDAANYRAGQNIDDTYDQLVAGGMESGKARLKSVEQFAVEC
AILKVWGSEALDYTVDEGVQIYGGMGFSADAPMDRAYRDARINRIFEGTNEINRLLTVDM
MLKRAMKGELDLMTPATAVAAELMSIPDFGEEDTTLFAAEKKVLSNLKKATLMVAGAAVQ
KLMMTLSKEQEILMNIADMASYVYVLESALLRTEKLASTRGEEAIAGQLDLLRIYLVEAV
DGIAKAGKEALWAFAEGDEQRMMLVGLRRFTKVEPFNVKDARQRVAQQLIEANKYIF
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