SitesBLAST
Comparing Echvi_1073 FitnessBrowser__Cola:Echvi_1073 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)
2z1qB Crystal structure of acyl coa dehydrogenase
47% identity, 98% coverage: 9:596/599 of query aligns to 6:546/549 of 2z1qB
- active site: L144 (= L150), T145 (= T151), G259 (= G266), E394 (= E406), G406 (= G418)
- binding flavin-adenine dinucleotide: Y142 (= Y148), L144 (= L150), T145 (= T151), G150 (= G156), S151 (= S157), W177 (= W183), S179 (= S185), R285 (= R292), F288 (= F295), I292 (= I299), F295 (= F302), I298 (= I305), H369 (≠ Y381), G370 (= G382), F393 (≠ Y405), I399 (= I411), Q448 (= Q490)
3owaC Crystal structure of acyl-coa dehydrogenase complexed with fad from bacillus anthracis
46% identity, 98% coverage: 8:595/599 of query aligns to 2:585/587 of 3owaC
- active site: L143 (= L150), T144 (= T151), G258 (= G266), E398 (= E406), G410 (= G418)
- binding flavin-adenine dinucleotide: Y141 (= Y148), L143 (= L150), T144 (= T151), G149 (= G156), S150 (= S157), W176 (= W183), I177 (= I184), T178 (≠ S185), R284 (= R292), F287 (= F295), I291 (= I299), F294 (= F302), Q371 (= Q379), I372 (= I380), G375 (= G383), I393 (= I401), F397 (≠ Y405), T400 (= T408), E402 (= E410), I403 (= I411), L406 (≠ M414), Q480 (= Q490)
8pheA Acad9-wt in complex with ecsit-cter (see paper)
37% identity, 91% coverage: 52:595/599 of query aligns to 42:541/551 of 8pheA
- binding : L143 (= L150), D151 (= D158), A153 (≠ N160), S154 (= S161), I155 (≠ G162), K202 (= K203), I205 (≠ L205), F256 (= F256), M260 (≠ V260), F295 (= F295), N296 (≠ G296), I394 (= I411), Y398 (≠ L415), L401 (≠ G418), Q405 (≠ K422), K451 (≠ P484), M454 (≠ E487)
8phfA Cryo-em structure of human acad9-s191a (see paper)
37% identity, 91% coverage: 52:595/599 of query aligns to 42:537/547 of 8phfA
- binding flavin-adenine dinucleotide: T144 (= T151), W176 (= W183), K225 (= K225), R292 (= R292), Q294 (= Q294), F295 (= F295), F302 (= F302), L304 (≠ A304), I305 (= I305), I363 (= I380), G365 (= G382), G366 (= G383), F388 (≠ Y405), E393 (= E410), M397 (= M414), 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)
36% identity, 91% coverage: 52:595/599 of query aligns to 79:611/621 of Q9H845
- R193 (≠ K163) to W: in MC1DN20; uncertain significance; dbSNP:rs377547811
- S234 (vs. gap) to F: in MC1DN20; uncertain significance
- G303 (= G266) to S: in MC1DN20; uncertain significance; dbSNP:rs143383023
- A326 (≠ S289) to T: in MC1DN20; uncertain significance; dbSNP:rs115532916
- E413 (= E393) to K: in MC1DN20; uncertain significance; dbSNP:rs149753643
- E426 (= E406) 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
2uxwA Crystal structure of human very long chain acyl-coa dehydrogenase (acadvl)
36% identity, 84% coverage: 73:573/599 of query aligns to 70:552/567 of 2uxwA
- active site: L148 (= L150), T149 (= T151), G272 (= G266), E394 (= E406), L406 (= L421)
- binding flavin-adenine dinucleotide: F146 (≠ Y148), L148 (= L150), T149 (= T151), G154 (= G156), S155 (= S157), W181 (= W183), I182 (= I184), S183 (= S185), F393 (≠ Y405), T396 (= T408), D398 (≠ E410), I399 (= I411), Q474 (= Q490)
- binding trans delta2 palmitenoyl-coenzymea: V96 (≠ A99), G107 (≠ S109), L110 (≠ Y112), F146 (≠ Y148), L269 (= L263), F393 (≠ Y405), E394 (= E406), G395 (= G407)
Sites not aligning to the query:
3b96A Structural basis for substrate fatty-acyl chain specificity: crystal structure of human very-long-chain acyl-coa dehydrogenase (see paper)
36% identity, 84% coverage: 73:573/599 of query aligns to 70:539/554 of 3b96A
- active site: L148 (= L150), T149 (= T151), G272 (= G266), E394 (= E406), L406 (vs. gap)
- binding flavin-adenine dinucleotide: F146 (≠ Y148), L148 (= L150), T149 (= T151), G154 (= G156), S155 (= S157), W181 (= W183), I182 (= I184), S183 (= S185), I389 (= I401), F393 (≠ Y405), T396 (= T408), D398 (≠ E410), I399 (= I411), Q461 (= Q490)
- binding tetradecanoyl-coa: V96 (≠ A99), G107 (≠ S109), F146 (≠ Y148), L269 (= L263), F393 (≠ Y405), E394 (= E406)
P50544 Very long-chain specific acyl-CoA dehydrogenase, mitochondrial; MVLCAD; VLCAD; EC 1.3.8.9 from Mus musculus (Mouse) (see paper)
34% identity, 92% coverage: 26:577/599 of query aligns to 92:645/656 of P50544
- C238 (≠ D171) modified: S-nitrosocysteine
8ca1B Cryo-em structure of the acadvl dimer from mus musculus. (see paper)
34% identity, 92% coverage: 26:577/599 of query aligns to 25:578/589 of 8ca1B
- binding flavin-adenine dinucleotide: F148 (≠ Y148), T151 (= T151), G156 (= G156), S157 (= S157), W183 (= W183), S185 (= S185), R300 (= R292), Q302 (= Q294), F303 (= F295), I307 (= I299), V312 (≠ A304), I313 (= I305), Q369 (= Q379), I370 (= I380), F395 (≠ Y405), D400 (≠ E410), I401 (= I411)
7s7gA Crystal structure analysis of human vlcad
36% identity, 84% coverage: 73:573/599 of query aligns to 70:556/571 of 7s7gA
- binding flavin-adenine dinucleotide: F146 (≠ Y148), L148 (= L150), T149 (= T151), G154 (= G156), S155 (= S157), W181 (= W183), I182 (= I184), S183 (= S185), I389 (= I401), T396 (= T408), D398 (≠ E410), I399 (= I411), Q478 (= Q490)
P49748 Very long-chain specific acyl-CoA dehydrogenase, mitochondrial; VLCAD; EC 1.3.8.9 from Homo sapiens (Human) (see 8 papers)
35% identity, 84% coverage: 73:573/599 of query aligns to 138:640/655 of P49748
- 214:223 (vs. 148:157, 70% identical) binding
- WIS 249:251 (= WIS 183:185) binding
- F458 (≠ S402) 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 (≠ YEG 405:407) binding
- E462 (= E406) 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 408:410) binding
- A490 (= A437) 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 (≠ G449) to P: in ACADVLD; decreased association with mitochondrial inner membrane; decreased specific activity towards several substrates in vitro
- E534 (= E462) to K: in ACADVLD; uncertain significance; dbSNP:rs2230180
- Q562 (= Q490) binding
- S583 (≠ L511) to W: in ACADVLD; Loss of homodimerization; loss of localization to mitochondrial inner membrane; dbSNP:rs1085307648
Sites not aligning to the query:
- 1:40 modified: transit peptide, Mitochondrion
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
40% identity, 65% coverage: 30:421/599 of query aligns to 3:373/374 of 5lnxD
- active site: L122 (= L150), T123 (= T151), G239 (= G266), E358 (= E406), K370 (≠ G418)
- binding flavin-adenine dinucleotide: L122 (= L150), T123 (= T151), G128 (= G156), S129 (= S157), F153 (≠ W183), T155 (≠ S185), R265 (= R292), Q267 (= Q294), F268 (= F295), I272 (= I299), N275 (≠ F302), I278 (= I305), Q331 (= Q379), I332 (= I380), G335 (= G383), Y357 (= Y405), T360 (= T408), E362 (= E410)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
34% identity, 67% coverage: 23:422/599 of query aligns to 28:408/412 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)
34% identity, 67% coverage: 23:422/599 of query aligns to 1:381/384 of 1jqiA
- active site: G377 (= G418)
- binding acetoacetyl-coenzyme a: L95 (≠ I118), F125 (≠ Y148), S134 (= S157), F234 (= F256), M238 (≠ V260), Q239 (≠ N261), L241 (= L263), D242 (≠ N264), R245 (= R267), Y364 (= Y405), E365 (= E406), G366 (= G407)
- binding flavin-adenine dinucleotide: F125 (≠ Y148), L127 (= L150), S128 (≠ T151), G133 (= G156), S134 (= S157), W158 (= W183), T160 (≠ S185), R270 (= R292), F273 (= F295), L280 (≠ F302), Q338 (= Q379), I339 (= I380), G342 (= G383), I360 (= I401), T367 (= T408), E369 (= E410), I370 (= I411)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
37% identity, 66% coverage: 30:422/599 of query aligns to 5:378/378 of 5ol2F
- active site: L124 (= L150), T125 (= T151), G241 (= G266), G374 (= G418)
- binding calcium ion: E29 (= E54), E33 (≠ M58), R35 (≠ N60)
- binding coenzyme a persulfide: L238 (= L263), R242 (= R267), E362 (= E406), G363 (= G407)
- binding flavin-adenine dinucleotide: F122 (≠ Y148), L124 (= L150), T125 (= T151), P127 (= P153), T131 (≠ S157), F155 (≠ W183), I156 (= I184), T157 (≠ S185), E198 (= E223), R267 (= R292), F270 (= F295), L274 (≠ I299), F277 (= F302), Q335 (= Q379), L336 (≠ I380), G338 (= G382), G339 (= G383), Y361 (= Y405), T364 (= T408), E366 (= E410)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
34% identity, 67% coverage: 23:422/599 of query aligns to 28:408/412 of P16219
- G90 (= G87) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (≠ D100) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 148:157, 50% identical) binding in other chain
- R171 (≠ T169) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ WIS 183:185) binding in other chain
- A192 (= A190) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (≠ N204) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R292) binding
- Q308 (≠ G303) binding in other chain
- R325 (≠ E320) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (= S367) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QIYGG 379:383) binding
- R380 (= R394) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ TNE 408:410) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
34% identity, 67% coverage: 23:422/599 of query aligns to 1:381/385 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 (= M384), T347 (≠ A388), E348 (≠ D389)
- binding flavin-adenine dinucleotide: F125 (≠ Y148), L127 (= L150), S128 (≠ T151), G133 (= G156), S134 (= S157), W158 (= W183), T160 (≠ S185), R270 (= R292), F273 (= F295), L280 (≠ F302), V282 (≠ A304), Q338 (= Q379), I339 (= I380), G342 (= G383), I360 (= I401), Y364 (= Y405), T367 (= T408), E369 (= E410), I370 (= I411), L373 (≠ M414)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
34% identity, 67% coverage: 23:422/599 of query aligns to 4:384/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ Y148), L130 (= L150), S131 (≠ T151), G136 (= G156), S137 (= S157), W161 (= W183), T163 (≠ S185), T214 (= T233), R273 (= R292), F276 (= F295), L280 (≠ I299), L283 (≠ F302), V285 (≠ A304), Q341 (= Q379), I342 (= I380), G345 (= G383), I363 (= I401), Y367 (= Y405), T370 (= T408), E372 (= E410), L376 (≠ M414)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
34% identity, 66% coverage: 28:422/599 of query aligns to 3:378/381 of 8sgsA
- binding coenzyme a: S131 (= S157), A133 (= A159), N177 (≠ D202), F231 (= F256), M235 (≠ V260), L238 (= L263), I312 (≠ A356), E362 (= E406), G363 (= G407)
- binding flavin-adenine dinucleotide: F122 (≠ Y148), L124 (= L150), S125 (≠ T151), G130 (= G156), S131 (= S157), W155 (= W183), T157 (≠ S185), R267 (= R292), F270 (= F295), L274 (≠ I299), L277 (≠ F302), Q335 (= Q379), I336 (= I380), G338 (= G382), G339 (= G383), I357 (= I401), I360 (= I404), Y361 (= Y405), T364 (= T408), E366 (= E410)
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
34% identity, 66% coverage: 29:422/599 of query aligns to 1:368/371 of 2vigB
- active site: L121 (= L150), S122 (≠ T151), G231 (= G266), E352 (= E406), G364 (= G418)
- binding coenzyme a persulfide: S128 (= S157), F221 (= F256), M225 (≠ V260), Q226 (≠ N261), L228 (= L263), D229 (≠ N264), R232 (= R267), E352 (= E406), G353 (= G407), I357 (= I411)
- binding flavin-adenine dinucleotide: L121 (= L150), S122 (≠ T151), G127 (= G156), S128 (= S157), W152 (= W183), T154 (≠ S185), R257 (= R292), F260 (= F295), L264 (≠ I299), L267 (≠ F302), Q325 (= Q379), I326 (= I380), G329 (= G383), I347 (= I401), Y351 (= Y405), T354 (= T408), E356 (= E410)
Query Sequence
>Echvi_1073 FitnessBrowser__Cola:Echvi_1073
MTTKNNTINGGEFLIRETAATEIFIPAEFTEEQRMMAQACQDFIDTEILPKSEEIDSMKN
PDLVPAILKKAGELGLLGISVPEEYQGLGMSFNTSMLIADIIGAAGSFSTTYGAHTGIGT
LPILYYGTEEQKKKYLPKLATGEWAACYCLTEPDAGSDANSGKTKATLTEDGKHYLLNGQ
KMWISNGGFADLFIVFAKIGEDKNLTAFIVEKDFGGITMNEEEKKMGIKGSSTRQVFFND
CKVPVENMLSDRQNGFKIAVNILNIGRVKLGAGVLGGCRQVIKNALQYSSERKQFGVSIN
TFGAIKSKLAEMAVKTYVSESLCYRLGQNIEDRIDALMASGMEANQAKLKGVEQFAMECA
IAKIHGSEVLDYVVDQGVQIYGGMGYSADAPMERAYRDARISRIYEGTNEINRMLMIGML
LKRAMKGEVDLFGPAKAVADELTAVPSFGAVDNSQLFAAEKELLKKLKKVFLMIGGKAAM
TFGPKIEEEQEIMMNLADIMIEIYAAESALLRTEKRVTLQGEEACKQQIAMVKVYLTEAV
DIIQAAGKEAIASFTTGDEQKVMLMGLKRFTKADPENTKALRRQIADHMIDKGKYPYFN
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