SitesBLAST
Comparing AO353_15225 FitnessBrowser__pseudo3_N2E3:AO353_15225 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)
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
55% identity, 99% coverage: 4:378/378 of query aligns to 50:426/430 of P51174
- K318 (= K270) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (= K274) modified: N6-acetyllysine; alternate; mutation to R: Reduces activity by 23%; reduces activity by 80% when associated with R-318.
Sites not aligning to the query:
- 42 modified: N6-acetyllysine; K→R: Reduces activity by 90% when associated with R-318 and R-322.
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
56% identity, 98% coverage: 10:378/378 of query aligns to 8:378/380 of 2pg0A
- active site: M124 (= M126), T125 (= T127), E243 (= E243), A364 (= A364), R376 (= R376)
- binding flavin-adenine dinucleotide: I122 (= I124), M124 (= M126), T125 (= T127), G130 (= G132), S131 (= S133), F155 (= F157), I156 (= I158), T157 (= T159), R269 (= R269), F272 (= F272), F279 (= F279), Q337 (= Q337), L338 (= L338), G340 (= G340), G341 (= G341), V359 (= V359), I362 (= I362), Y363 (= Y363), T366 (= T366), E368 (= E368), M369 (≠ I369)
8w0uA Human lcad complexed with acetoacetyl coenzyme a (see paper)
52% identity, 99% coverage: 4:378/378 of query aligns to 18:394/398 of 8w0uA
- binding acetoacetyl-coenzyme a: M140 (= M126), S147 (= S133), Q150 (= Q136), S193 (vs. gap), H196 (≠ K180), Y250 (≠ A234), E259 (= E243), R260 (= R244), Y379 (= Y363), G380 (≠ A364), G381 (= G365), I385 (= I369), L389 (≠ I373), R392 (= R376)
- binding flavin-adenine dinucleotide: I138 (= I124), M140 (= M126), T141 (= T127), G146 (= G132), S147 (= S133), F171 (= F157), S173 (≠ T159), R285 (= R269), F288 (= F272), L295 (≠ F279), Q353 (= Q337), L354 (= L338), G357 (= G341), V375 (= V359), Y379 (= Y363), T382 (= T366), E384 (= E368)
8w0tA Human lcad (see paper)
52% identity, 99% coverage: 4:378/378 of query aligns to 18:394/398 of 8w0tA
- binding flavin-adenine dinucleotide: I138 (= I124), M140 (= M126), T141 (= T127), G146 (= G132), S147 (= S133), F171 (= F157), I172 (= I158), S173 (≠ T159), R285 (= R269), F288 (= F272), L295 (≠ F279), Q353 (= Q337), L354 (= L338), G356 (= G340), G357 (= G341), V375 (= V359), T382 (= T366), E384 (= E368), I385 (= I369)
P28330 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Homo sapiens (Human) (see 2 papers)
52% identity, 99% coverage: 4:378/378 of query aligns to 50:426/430 of P28330
- E291 (= E243) active site, Proton acceptor; mutation to Q: Loss of long-chain-acyl-CoA dehydrogenase activity. No effect on protein abundance. No effect on solubility. No effect on substrate binding.
- S303 (≠ A255) to T: in dbSNP:rs1801204
- K333 (= K285) to Q: in dbSNP:rs2286963
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
40% identity, 99% coverage: 6:378/378 of query aligns to 3:376/378 of 5ol2F
- active site: L124 (≠ M126), T125 (= T127), G241 (≠ E243), G374 (≠ R376)
- binding calcium ion: E29 (≠ Q32), E33 (≠ Q36), R35 (≠ H38)
- binding coenzyme a persulfide: L238 (= L240), R242 (= R244), E362 (≠ A364), G363 (= G365)
- binding flavin-adenine dinucleotide: F122 (≠ I124), L124 (≠ M126), T125 (= T127), P127 (= P129), T131 (≠ S133), F155 (= F157), I156 (= I158), T157 (= T159), E198 (≠ L200), R267 (= R269), F270 (= F272), L274 (≠ I276), F277 (= F279), Q335 (= Q337), L336 (= L338), G338 (= G340), G339 (= G341), Y361 (= Y363), T364 (= T366), E366 (= E368)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
42% identity, 98% coverage: 10:378/378 of query aligns to 5:372/374 of 5lnxD
- active site: L122 (≠ M126), T123 (= T127), G239 (≠ E243), E358 (≠ A364), K370 (≠ R376)
- binding flavin-adenine dinucleotide: L122 (≠ M126), T123 (= T127), G128 (= G132), S129 (= S133), F153 (= F157), T155 (= T159), R265 (= R269), Q267 (≠ A271), F268 (= F272), I272 (= I276), N275 (≠ F279), I278 (≠ T282), Q331 (= Q337), I332 (≠ L338), G335 (= G341), Y357 (= Y363), T360 (= T366), E362 (= E368)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
40% identity, 98% coverage: 7:378/378 of query aligns to 5:377/380 of 4l1fA
- active site: L125 (≠ M126), T126 (= T127), G242 (≠ E243), E363 (≠ A364), R375 (= R376)
- binding coenzyme a persulfide: T132 (≠ S133), H179 (≠ K180), F232 (= F233), M236 (= M237), E237 (≠ Q238), L239 (= L240), D240 (≠ P241), R243 (= R244), Y362 (= Y363), E363 (≠ A364), G364 (= G365), R375 (= R376)
- binding flavin-adenine dinucleotide: F123 (≠ I124), L125 (≠ M126), T126 (= T127), G131 (= G132), T132 (≠ S133), F156 (= F157), I157 (= I158), T158 (= T159), R268 (= R269), Q270 (≠ A271), F271 (= F272), I275 (= I276), F278 (= F279), L281 (≠ T282), Q336 (= Q337), I337 (≠ L338), G340 (= G341), I358 (≠ V359), Y362 (= Y363), T365 (= T366), Q367 (≠ E368)
- binding 1,3-propandiol: L5 (≠ F7), Q10 (≠ E12)
3r7kA Crystal structure of a probable acyl coa dehydrogenase from mycobacterium abscessus atcc 19977 / dsm 44196 (see paper)
38% identity, 99% coverage: 3:378/378 of query aligns to 1:377/378 of 3r7kA
- active site: V126 (≠ M126), T127 (= T127), E242 (= E243), G363 (≠ A364), K375 (≠ R376)
- binding dihydroflavine-adenine dinucleotide: V126 (≠ M126), T127 (= T127), G132 (= G132), S133 (= S133), F157 (= F157), I158 (= I158), T159 (= T159), R268 (= R269), T270 (≠ A271), F271 (= F272), L275 (≠ I276), R278 (≠ F279), I281 (≠ T282), Q336 (= Q337), I337 (≠ L338), G340 (= G341), I358 (≠ V359), T365 (= T366), E367 (= E368)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
37% identity, 97% coverage: 11:375/378 of query aligns to 38:403/412 of P15651
- 152:161 (vs. 124:133, 60% identical) binding FAD
- S161 (= S133) binding substrate
- WIT 185:187 (≠ FIT 157:159) binding FAD
- DMGR 269:272 (≠ PQER 241:244) binding substrate
- R297 (= R269) binding FAD
- QILGG 365:369 (≠ QLHGG 337:341) binding FAD
- E392 (≠ A364) active site, Proton acceptor
- TSE 394:396 (≠ TNE 366:368) binding FAD
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)
37% identity, 97% coverage: 11:378/378 of query aligns to 11:379/384 of 1jqiA
- active site: G377 (≠ R376)
- binding acetoacetyl-coenzyme a: L95 (≠ I94), F125 (≠ I124), S134 (= S133), F234 (= F233), M238 (= M237), Q239 (= Q238), L241 (= L240), D242 (≠ P241), R245 (= R244), Y364 (= Y363), E365 (≠ A364), G366 (= G365)
- binding flavin-adenine dinucleotide: F125 (≠ I124), L127 (≠ M126), S128 (≠ T127), G133 (= G132), S134 (= S133), W158 (≠ F157), T160 (= T159), R270 (= R269), F273 (= F272), L280 (≠ F279), Q338 (= Q337), I339 (≠ L338), G342 (= G341), I360 (≠ V359), T367 (= T366), E369 (= E368), I370 (= I369)
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
39% identity, 98% coverage: 7:378/378 of query aligns to 4:377/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (= S133), L133 (= L135), K178 (= K180), F231 (= F233), M235 (= M237), L238 (= L240), N241 (≠ E243), R242 (= R244), Y362 (= Y363), T363 (≠ A364), G364 (= G365), R375 (= R376)
- binding flavin-adenine dinucleotide: L122 (≠ I124), A124 (≠ M126), T125 (= T127), G130 (= G132), S131 (= S133), F155 (= F157), I156 (= I158), T157 (= T159), K200 (= K202), N208 (≠ T210), L358 (≠ V359), T365 (= T366), Q367 (≠ E368), I368 (= I369)
Q39QF5 Cyclohex-1-ene-1-carbonyl-CoA dehydrogenase; CHeneCoA dehydrogenase; EC 1.3.8.10 from Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15) (see paper)
39% identity, 98% coverage: 7:378/378 of query aligns to 4:377/380 of Q39QF5
- D91 (= D93) mutation to E: Retains minor activity.; mutation to N: Loss of activity. Gains a low but significant C1,C2-dehydrogenation activity, but the C3,C6- and C3,C4-dehydrogenating activities are largely diminished; when associated with D-241.
- L122 (≠ I124) binding FAD
- A124 (≠ M126) binding FAD
- T125 (= T127) binding FAD
- S131 (= S133) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA; binding FAD
- T157 (= T159) binding FAD
- K178 (= K180) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
- N241 (≠ E243) mutation to D: Shows decreased activity, with a shift towards C3,C4- versus C3,C6-dehydrogenation. Gains a low but significant C1,C2-dehydrogenation activity, but the C3,C6- and C3,C4-dehydrogenating activities are largely diminished; when associated with N-91.
- R242 (= R244) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
- T363 (≠ A364) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA; mutation to V: Shows decreased activity, with a shift towards C3,C4- versus C3,C6-dehydrogenation.
- T365 (= T366) binding FAD
- Q367 (≠ E368) binding FAD
- R375 (= R376) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
39% identity, 98% coverage: 7:378/378 of query aligns to 2:375/378 of 7p9xA
- binding 1-monoenoyl-CoA: L82 (≠ I86), D89 (= D93), S129 (= S133), L131 (= L135), K176 (= K180), F229 (= F233), M233 (= M237), L236 (= L240), R240 (= R244), Y360 (= Y363), T361 (≠ A364), G362 (= G365), R373 (= R376)
- binding flavin-adenine dinucleotide: A122 (≠ M126), T123 (= T127), G128 (= G132), S129 (= S133), F153 (= F157), I154 (= I158), T155 (= T159), N206 (≠ T210), L356 (≠ V359), Y360 (= Y363), T363 (= T366), Q365 (≠ E368), I366 (= I369)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
35% identity, 99% coverage: 6:378/378 of query aligns to 5:378/378 of 4n5fA
- active site: L126 (≠ M126), T127 (= T127), G243 (≠ E243), E364 (≠ A364), R376 (= R376)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ M126), T127 (= T127), G132 (= G132), S133 (= S133), F157 (= F157), T159 (= T159), T210 (= T210), Y363 (= Y363), T366 (= T366), E368 (= E368), M372 (≠ E372)
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)
35% identity, 97% coverage: 11:378/378 of query aligns to 1:367/369 of 3pfdC
- active site: L116 (≠ M126), S117 (≠ T127), T233 (≠ E243), E353 (≠ A364), R365 (= R376)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ I124), L116 (≠ M126), S117 (≠ T127), G122 (= G132), S123 (= S133), W147 (≠ F157), I148 (= I158), T149 (= T159), R259 (= R269), F262 (= F272), V266 (≠ I276), N269 (≠ F279), Q326 (= Q337), L327 (= L338), G330 (= G341), I348 (≠ V359), Y352 (= Y363), T355 (= T366), Q357 (≠ E368)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
36% identity, 98% coverage: 7:375/378 of query aligns to 3:373/379 of 6fahD
- active site: L124 (≠ M126), T125 (= T127), G241 (≠ E243)
- binding flavin-adenine dinucleotide: F122 (≠ I124), L124 (≠ M126), T125 (= T127), R152 (≠ S154), F155 (= F157), T157 (= T159), E198 (≠ L200), R267 (= R269), Q269 (≠ A271), F270 (= F272), I274 (= I276), F277 (= F279), Q335 (= Q337), I336 (≠ L338), G339 (= G341), Y361 (= Y363), T364 (= T366), Q366 (≠ E368)
Sites not aligning to the query:
C3UVB0 Glutaryl-CoA dehydrogenase; GDH(Des); EC 1.3.99.32 from Desulfococcus multivorans (see paper)
39% identity, 98% coverage: 7:375/378 of query aligns to 5:378/389 of C3UVB0
- A80 (≠ G79) mutation to E: Loses the FAD cofactor and dehydrogenase activity.
- R87 (≠ G87) binding substrate
- V88 (≠ F88) mutation to S: A residual dehydrogenase activity is observed.
- N91 (≠ H91) binding substrate
- FGIT 126:129 (≠ IAMT 124:127) binding FAD
- S135 (= S133) binding FAD; binding substrate
- WIS 159:161 (≠ FIT 157:159) binding FAD
- S181 (≠ A179) binding substrate
- R271 (= R269) binding FAD
- FQMN 281:284 (≠ FQNT 279:282) binding FAD
- R340 (≠ Q337) binding FAD
- A344 (≠ G341) binding FAD
- V366 (≠ Y363) mutation to Y: Loses the FAD cofactor but a residual dehydrogenase activity is observed.
- EGSAN 367:371 (≠ AGTNE 364:368) binding FAD
Sites not aligning to the query:
3mpjB Structure of the glutaryl-coenzyme a dehydrogenase (see paper)
39% identity, 98% coverage: 7:375/378 of query aligns to 5:378/393 of 3mpjB
- active site: I128 (≠ M126), T129 (= T127), T245 (≠ E243), E367 (≠ A364)
- binding flavin-adenine dinucleotide: F126 (≠ I124), I128 (≠ M126), T129 (= T127), G134 (= G132), S135 (= S133), W159 (≠ F157), I160 (= I158), S161 (≠ T159), V366 (≠ Y363), S369 (≠ T366), N371 (≠ E368), M375 (≠ E372)
- binding : H36 (= H38), F37 (≠ I39), Y39 (vs. gap), A164 (≠ F162), Q165 (≠ L163), D167 (= D165), N193 (= N190)
Sites not aligning to the query:
3mpiC Structure of the glutaryl-coenzyme a dehydrogenase glutaryl-coa complex (see paper)
39% identity, 98% coverage: 7:375/378 of query aligns to 5:378/395 of 3mpiC
- active site: I128 (≠ M126), T129 (= T127), T245 (≠ E243), E367 (≠ A364)
- binding flavin-adenine dinucleotide: I128 (≠ M126), T129 (= T127), G134 (= G132), S135 (= S133), W159 (≠ F157), I160 (= I158), S161 (≠ T159), M365 (≠ I362), V366 (≠ Y363), S369 (≠ T366), N371 (≠ E368), M375 (≠ E372)
- binding glutaryl-coenzyme A: R87 (≠ G87), F126 (≠ I124), S135 (= S133), V137 (≠ L135), S181 (≠ A179), F239 (≠ M237), R246 (= R244), N315 (≠ D313), V366 (≠ Y363), E367 (≠ A364), G368 (= G365), I376 (= I373)
Sites not aligning to the query:
Query Sequence
>AO353_15225 FitnessBrowser__pseudo3_N2E3:AO353_15225
MIPRTLFSSEHELFRDSVRTFLEKEAVPFHAQWEKQGHIDRKLWNKAGEAGMLCSHLPEA
YGGFDADFLYSTVVIEEVGRLGLTGIGFSLHSDIVAPYILHYGSEVLKHKYLPKLVSGEM
VTAIAMTEPGAGSDLQGVKTTALLDGDEYVINGSKTFITNGFLADLVIVVAKTDPKAGAK
GTSLFLVEANTPGFEKGKRLEKVGMKAQDTSELFFQDVRVPKENLLGQAGMGFAYLMQEL
PQERLTVAIGGLASAEAALQWTLDYTRERKAFGKAIADFQNTRFKLAEMATEIQIGRVFV
DRCLELHLQGKLDVPTAAMAKYWGTDLQCKVLDECVQLHGGYGFMWEYPIARAWADARVQ
RIYAGTNEIMKEIIARSL
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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