SitesBLAST
Comparing AO353_24835 FitnessBrowser__pseudo3_N2E3:AO353_24835 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
41% identity, 99% coverage: 2:382/386 of query aligns to 7:384/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (= F122), L130 (= L124), S131 (≠ T125), G136 (= G130), S137 (= S131), W161 (≠ F155), T163 (≠ S157), T214 (= T212), R273 (= R271), F276 (= F274), L280 (≠ I278), L283 (≠ Y281), V285 (≠ G283), Q341 (= Q339), I342 (= I340), G345 (= G343), I363 (= I361), Y367 (≠ W365), T370 (= T368), E372 (= E370), L376 (≠ H374)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
41% identity, 99% coverage: 2:382/386 of query aligns to 4:381/385 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 (= M344), T347 (≠ D348), E348 (= E349)
- binding flavin-adenine dinucleotide: F125 (= F122), L127 (= L124), S128 (≠ T125), G133 (= G130), S134 (= S131), W158 (≠ F155), T160 (≠ S157), R270 (= R271), F273 (= F274), L280 (≠ Y281), V282 (≠ G283), Q338 (= Q339), I339 (= I340), G342 (= G343), I360 (= I361), Y364 (≠ W365), T367 (= T368), E369 (= E370), I370 (= I371), L373 (≠ H374)
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, 99% coverage: 2:382/386 of query aligns to 31:408/412 of P16219
- G90 (= G65) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E79) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 122:131, 80% identical) binding in other chain
- R171 (≠ V141) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ FIS 155:157) binding in other chain
- A192 (= A162) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (≠ A183) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R271) binding FAD
- Q308 (= Q282) binding in other chain
- R325 (≠ E299) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (= S327) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QIFGG 339:343) binding FAD
- R380 (= R354) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (= TSE 368:370) 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)
41% identity, 99% coverage: 2:382/386 of query aligns to 1:378/381 of 8sgsA
- binding coenzyme a: S131 (= S131), A133 (= A133), N177 (= N177), F231 (≠ W235), M235 (≠ N239), L238 (= L242), I312 (≠ D316), E362 (= E366), G363 (= G367)
- binding flavin-adenine dinucleotide: F122 (= F122), L124 (= L124), S125 (≠ T125), G130 (= G130), S131 (= S131), W155 (≠ F155), T157 (≠ S157), R267 (= R271), F270 (= F274), L274 (≠ I278), L277 (≠ Y281), Q335 (= Q339), I336 (= I340), G338 (= G342), G339 (= G343), I357 (= I361), I360 (= I364), Y361 (≠ W365), T364 (= T368), E366 (= E370)
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
40% identity, 98% coverage: 5:382/386 of query aligns to 1:368/371 of 2vigB
- active site: L121 (= L124), S122 (≠ T125), G231 (= G245), E352 (= E366), G364 (≠ R378)
- binding coenzyme a persulfide: S128 (= S131), F221 (≠ W235), M225 (≠ N239), Q226 (≠ A240), L228 (= L242), D229 (≠ T243), R232 (= R246), E352 (= E366), G353 (= G367), I357 (= I371)
- binding flavin-adenine dinucleotide: L121 (= L124), S122 (≠ T125), G127 (= G130), S128 (= S131), W152 (≠ F155), T154 (≠ S157), R257 (= R271), F260 (= F274), L264 (≠ I278), L267 (≠ Y281), Q325 (= Q339), I326 (= I340), G329 (= G343), I347 (= I361), Y351 (≠ W365), T354 (= T368), E356 (= E370)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
38% identity, 99% coverage: 2:382/386 of query aligns to 4:381/384 of 1jqiA
- active site: G377 (≠ R378)
- binding acetoacetyl-coenzyme a: L95 (vs. gap), F125 (= F122), S134 (= S131), F234 (≠ W235), M238 (≠ N239), Q239 (≠ A240), L241 (= L242), D242 (≠ T243), R245 (= R246), Y364 (≠ W365), E365 (= E366), G366 (= G367)
- binding flavin-adenine dinucleotide: F125 (= F122), L127 (= L124), S128 (≠ T125), G133 (= G130), S134 (= S131), W158 (≠ F155), T160 (≠ S157), R270 (= R271), F273 (= F274), L280 (≠ Y281), Q338 (= Q339), I339 (= I340), G342 (= G343), I360 (= I361), T367 (= T368), E369 (= E370), I370 (= I371)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
38% identity, 99% coverage: 2:382/386 of query aligns to 31:408/412 of P15651
- 152:161 (vs. 122:131, 80% identical) binding FAD
- S161 (= S131) binding substrate
- WIT 185:187 (≠ FIS 155:157) binding FAD
- DMGR 269:272 (≠ TAGR 243:246) binding substrate
- R297 (= R271) binding FAD
- QILGG 365:369 (≠ QIFGG 339:343) binding FAD
- E392 (= E366) active site, Proton acceptor
- TSE 394:396 (= TSE 368:370) binding FAD
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
39% identity, 97% coverage: 6:381/386 of query aligns to 3:373/374 of 5lnxD
- active site: L122 (= L124), T123 (= T125), G239 (= G245), E358 (= E366), K370 (≠ R378)
- binding flavin-adenine dinucleotide: L122 (= L124), T123 (= T125), G128 (= G130), S129 (= S131), F153 (= F155), T155 (≠ S157), R265 (= R271), Q267 (= Q273), F268 (= F274), I272 (= I278), N275 (≠ Y281), I278 (≠ V284), Q331 (= Q339), I332 (= I340), G335 (= G343), Y357 (≠ W365), T360 (= T368), E362 (= E370)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
37% identity, 99% coverage: 1:381/386 of query aligns to 1:377/379 of 1ukwB
- active site: L124 (= L124), S125 (≠ T125), T241 (≠ G245), E362 (= E366), R374 (= R378)
- binding cobalt (ii) ion: D145 (= D145), H146 (≠ D146)
- binding flavin-adenine dinucleotide: F122 (= F122), L124 (= L124), S125 (≠ T125), G130 (= G130), S131 (= S131), W155 (≠ F155), S157 (= S157), K200 (≠ C204), L357 (≠ I361), Y361 (≠ W365), E362 (= E366), T364 (= T368), E366 (= E370), L370 (≠ H374)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
37% identity, 99% coverage: 1:381/386 of query aligns to 1:377/379 of 1ukwA
- active site: L124 (= L124), S125 (≠ T125), T241 (≠ G245), E362 (= E366), R374 (= R378)
- binding flavin-adenine dinucleotide: F122 (= F122), L124 (= L124), S125 (≠ T125), G130 (= G130), S131 (= S131), W155 (≠ F155), S157 (= S157), L357 (≠ I361), Y361 (≠ W365), E362 (= E366), T364 (= T368), E366 (= E370), L370 (≠ H374)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
38% identity, 98% coverage: 5:382/386 of query aligns to 3:378/379 of 6fahD
- active site: L124 (= L124), T125 (= T125), G241 (= G245), G374 (≠ R378)
- binding flavin-adenine dinucleotide: F122 (= F122), L124 (= L124), T125 (= T125), R152 (≠ S152), F155 (= F155), T157 (≠ S157), E198 (≠ P202), R267 (= R271), Q269 (= Q273), F270 (= F274), I274 (= I278), F277 (≠ Y281), Q335 (= Q339), I336 (= I340), G339 (= G343), Y361 (≠ W365), T364 (= T368), Q366 (≠ E370)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
39% identity, 99% coverage: 1:382/386 of query aligns to 1:379/380 of 4l1fA
- active site: L125 (= L124), T126 (= T125), G242 (= G245), E363 (= E366), R375 (= R378)
- binding coenzyme a persulfide: T132 (≠ S131), H179 (≠ N182), F232 (≠ W235), M236 (≠ N239), E237 (≠ A240), L239 (= L242), D240 (≠ T243), R243 (= R246), Y362 (≠ W365), E363 (= E366), G364 (= G367), R375 (= R378)
- binding flavin-adenine dinucleotide: F123 (= F122), L125 (= L124), T126 (= T125), G131 (= G130), T132 (≠ S131), F156 (= F155), I157 (= I156), T158 (≠ S157), R268 (= R271), Q270 (= Q273), F271 (= F274), I275 (= I278), F278 (≠ Y281), L281 (≠ V284), Q336 (= Q339), I337 (= I340), G340 (= G343), I358 (= I361), Y362 (≠ W365), T365 (= T368), Q367 (≠ E370)
- binding 1,3-propandiol: L5 (= L5), Q10 (≠ E10)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
37% identity, 98% coverage: 6:382/386 of query aligns to 5:378/378 of 5ol2F
- active site: L124 (= L124), T125 (= T125), G241 (= G245), G374 (≠ R378)
- binding calcium ion: E29 (≠ A30), E33 (≠ A34), R35 (≠ E36)
- binding coenzyme a persulfide: L238 (= L242), R242 (= R246), E362 (= E366), G363 (= G367)
- binding flavin-adenine dinucleotide: F122 (= F122), L124 (= L124), T125 (= T125), P127 (= P127), T131 (≠ S131), F155 (= F155), I156 (= I156), T157 (≠ S157), E198 (≠ P202), R267 (= R271), F270 (= F274), L274 (≠ I278), F277 (≠ Y281), Q335 (= Q339), L336 (≠ I340), G338 (= G342), G339 (= G343), Y361 (≠ W365), T364 (= T368), E366 (= E370)
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)
37% identity, 96% coverage: 12:382/386 of query aligns to 4:369/369 of 3pfdC
- active site: L116 (= L124), S117 (≠ T125), T233 (≠ G245), E353 (= E366), R365 (= R378)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ F122), L116 (= L124), S117 (≠ T125), G122 (= G130), S123 (= S131), W147 (≠ F155), I148 (= I156), T149 (≠ S157), R259 (= R271), F262 (= F274), V266 (≠ I278), N269 (≠ Y281), Q326 (= Q339), L327 (≠ I340), G330 (= G343), I348 (= I361), Y352 (≠ W365), T355 (= T368), Q357 (≠ E370)
2z1qB Crystal structure of acyl coa dehydrogenase
39% identity, 95% coverage: 17:382/386 of query aligns to 36:410/549 of 2z1qB
- active site: L144 (= L124), T145 (= T125), G259 (= G245), E394 (= E366), G406 (≠ R378)
- binding flavin-adenine dinucleotide: Y142 (≠ F122), L144 (= L124), T145 (= T125), G150 (= G130), S151 (= S131), W177 (≠ F155), S179 (= S157), R285 (= R271), F288 (= F274), I292 (= I278), F295 (≠ Y281), I298 (≠ V284), H369 (≠ F341), G370 (= G342), F393 (≠ W365), I399 (= I371)
Sites not aligning to the query:
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
38% identity, 98% coverage: 1:380/386 of query aligns to 2:378/378 of 4n5fA
- active site: L126 (= L124), T127 (= T125), G243 (= G245), E364 (= E366), R376 (= R378)
- binding dihydroflavine-adenine dinucleotide: L126 (= L124), T127 (= T125), G132 (= G130), S133 (= S131), F157 (= F155), T159 (≠ S157), T210 (= T212), Y363 (≠ W365), T366 (= T368), E368 (= E370), M372 (≠ H374)
Q9VSA3 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; EC 1.3.8.7 from Drosophila melanogaster (Fruit fly) (see paper)
37% identity, 98% coverage: 2:380/386 of query aligns to 34:411/419 of Q9VSA3
- S347 (≠ D316) modified: Phosphoserine; by Pink1; mutation to A: Prevents phosphorylation by Pink1. Does not rescue climbing and flight defects in Pink1 mutants.; mutation to D: Phosphomimetic mutant that fully rescues climbing defects and significantly improves flight defects, and thorax and wing posture phenotypes in Pink1 mutants. No effect on acyl-CoA dehydrogenase activity.; mutation to DD: Phosphomimetic mutant that fully rescues climbing defects and significantly improves flight defects, and thorax and wing posture phenotypes in Pink1 mutants. No effect on acyl-CoA dehydrogenase activity.
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
36% identity, 98% coverage: 1:379/386 of query aligns to 2:379/385 of 3mdeA
- active site: V125 (≠ L124), T126 (= T125), T245 (≠ G245), E366 (= E366), R378 (= R378)
- binding octanoyl-coenzyme a: T86 (≠ W85), E89 (≠ H88), L93 (≠ A92), S132 (= S131), V134 (≠ A133), S181 (≠ R181), F235 (≠ W235), M239 (≠ N239), F242 (≠ L242), R314 (≠ M314), Y365 (≠ W365), E366 (= E366), G367 (= G367)
- binding flavin-adenine dinucleotide: Y123 (≠ F122), V125 (≠ L124), T126 (= T125), G131 (= G130), S132 (= S131), W156 (≠ F155), I157 (= I156), T158 (≠ S157), R271 (= R271), T273 (≠ Q273), F274 (= F274), L278 (≠ I278), H281 (≠ Y281), Q339 (= Q339), V340 (≠ I340), G343 (= G343), I361 (= I361), T368 (= T368), Q370 (≠ E370)
3mddA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
36% identity, 98% coverage: 1:379/386 of query aligns to 2:379/385 of 3mddA
- active site: V125 (≠ L124), T126 (= T125), T245 (≠ G245), E366 (= E366), R378 (= R378)
- binding flavin-adenine dinucleotide: Y123 (≠ F122), T126 (= T125), G131 (= G130), S132 (= S131), W156 (≠ F155), T158 (≠ S157), R271 (= R271), T273 (≠ Q273), F274 (= F274), H281 (≠ Y281), Q339 (= Q339), V340 (≠ I340), G343 (= G343), I361 (= I361), T368 (= T368), Q370 (≠ E370)
1udyA Medium-chain acyl-coa dehydrogenase with 3-thiaoctanoyl-coa (see paper)
36% identity, 98% coverage: 1:379/386 of query aligns to 2:379/385 of 1udyA
- active site: V125 (≠ L124), T126 (= T125), T245 (≠ G245), E366 (= E366), R378 (= R378)
- binding 3-thiaoctanoyl-coenzyme a: L93 (≠ A92), Y123 (≠ F122), S132 (= S131), S181 (≠ R181), F235 (≠ W235), M239 (≠ N239), F242 (≠ L242), V249 (= V249), R314 (≠ M314), Y365 (≠ W365), E366 (= E366), G367 (= G367), I371 (= I371), I375 (= I375)
- binding flavin-adenine dinucleotide: Y123 (≠ F122), T126 (= T125), G131 (= G130), S132 (= S131), W156 (≠ F155), T158 (≠ S157), T273 (≠ Q273), F274 (= F274), Q339 (= Q339), V340 (≠ I340), G343 (= G343), T368 (= T368), Q370 (≠ E370)
Query Sequence
>AO353_24835 FitnessBrowser__pseudo3_N2E3:AO353_24835
MNFQLTQEQEMLVDAVRSFVAKELLPHEEAVDRADEVSPELAAQIRGKAIAAGFYAFNMP
EEVGGGGLDYLSQALIERELSKVSWALHVFVARPSKILMACTGQQINDYLLPCIQGEKID
CFALTEPGAGSDANAIKTRAVRDGDDFVLNGSKHFISHAGHADFAIVFAVTDTYEHNGRK
RNAVTSFLVDRDTPGMTIRRGPKCVSNRGYHTFEMFFDDCRVPASKVLGEVGKGWEVANA
WLTAGRVMVAANCVGQAQRALDVSLQWAADRKQFGQPIGTYQGVSFKLADMATQIRAAEL
LTLHTAWKMDQGTMTDGEAGMAKLFASEVLGRAADEAVQIFGGMGLMDEGPVERIWRNAR
IERIWEGTSEIQRHIISRELLRPLLR
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