SitesBLAST
Comparing WP_052664119.1 NCBI__GCF_000969705.1:WP_052664119.1 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)
Q9VSA3 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; EC 1.3.8.7 from Drosophila melanogaster (Fruit fly) (see paper)
39% identity, 98% coverage: 7:411/412 of query aligns to 37:419/419 of Q9VSA3
- S347 (≠ T335) 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.
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
38% identity, 97% coverage: 3:403/412 of query aligns to 1:376/379 of 1ukwB
- active site: L124 (≠ V135), S125 (= S136), T241 (= T267), E362 (= E389), R374 (= R401)
- binding cobalt (ii) ion: D145 (≠ G156), H146 (≠ G157)
- binding flavin-adenine dinucleotide: F122 (≠ Y133), L124 (≠ V135), S125 (= S136), G130 (= G141), S131 (= S142), W155 (= W166), S157 (≠ T168), K200 (= K211), L357 (≠ I384), Y361 (≠ F388), E362 (= E389), T364 (= T391), E366 (= E393), L370 (= L397)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
38% identity, 97% coverage: 3:403/412 of query aligns to 1:376/379 of 1ukwA
- active site: L124 (≠ V135), S125 (= S136), T241 (= T267), E362 (= E389), R374 (= R401)
- binding flavin-adenine dinucleotide: F122 (≠ Y133), L124 (≠ V135), S125 (= S136), G130 (= G141), S131 (= S142), W155 (= W166), S157 (≠ T168), L357 (≠ I384), Y361 (≠ F388), E362 (= E389), T364 (= T391), E366 (= E393), L370 (= L397)
2a1tC Structure of the human mcad:etf e165betaa complex (see paper)
37% identity, 97% coverage: 3:401/412 of query aligns to 4:380/388 of 2a1tC
- active site: V127 (= V135), T128 (≠ S136), T247 (= T267), E368 (= E389), R380 (= R401)
- binding flavin-adenine dinucleotide: Y125 (= Y133), V127 (= V135), T128 (≠ S136), G133 (= G141), S134 (= S142), Q155 (≠ E163), W158 (= W166), W158 (= W166), I159 (= I167), T160 (= T168), R273 (= R293), T275 (= T295), F276 (= F296), L280 (≠ I300), H283 (= H303), I286 (= I306), Q341 (= Q362), I342 (= I363), G345 (= G366), I363 (= I384), T370 (= T391), Q372 (≠ E393)
P11310 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; Medium chain acyl-CoA dehydrogenase; MCADH; EC 1.3.8.7 from Homo sapiens (Human) (see 16 papers)
37% identity, 97% coverage: 3:401/412 of query aligns to 37:413/421 of P11310
- Y67 (= Y40) to H: in ACADMD; mild; dbSNP:rs121434280
- L86 (= L59) mutation to M: Strongly reduced rate of electron transfer to ETF.
- L98 (≠ D71) mutation to W: Strongly reduced rate of electron transfer to ETF.
- L100 (≠ T73) mutation to Y: Strongly reduced rate of electron transfer to ETF.
- I108 (= I80) mutation to M: Strongly reduced rate of electron transfer to ETF.
- P132 (≠ G104) to R: in a breast cancer sample; somatic mutation; dbSNP:rs875989854
- 158:167 (vs. 133:142, 80% identical) binding in other chain
- S167 (= S142) binding octanoyl-CoA
- W191 (= W166) mutation to A: Loss of electron transfer to ETF.; mutation to F: Reduces rate of electron transfer to ETF about six-fold.
- WIT 191:193 (= WIT 166:168) binding in other chain
- T193 (= T168) to A: in ACADMD; the thermostability is markedly decreased; dbSNP:rs121434279
- E237 (≠ T209) mutation to A: Strongly reduced rate of electron transfer to ETF.
- D278 (≠ E265) binding octanoyl-CoA
- T280 (= T267) mutation to E: Narrower substrate specificity. Changed substrate specificity towards longer acyl chains; when associated with G-401. Loss of acyl-CoA dehydrogenase activity; when associated with T-410.
- R281 (= R268) binding octanoyl-CoA; to T: in ACADMD; mild clinical phenotype; dbSNP:rs121434282
- RKT 306:308 (≠ RET 293:295) binding FAD
- HQ 316:317 (= HQ 303:304) binding in other chain
- K329 (≠ E316) to E: in ACADMD; may alter splicing; decreased fatty acid beta-oxidation; dbSNP:rs77931234
- QILGG 374:378 (≠ QIHGG 362:366) binding FAD
- E384 (= E372) mutation to A: Reduces rate of electron transfer to ETF three-fold.; mutation to Q: Reduces rate of electron transfer to ETF two-fold.
- E401 (= E389) active site, Proton acceptor; binding octanoyl-CoA; mutation to G: Changed substrate specificity towards longer acyl chains; when associated with E-280.; mutation to Q: Loss of acyl-CoA dehydrogenase activity.; mutation to T: Loss of acyl-CoA dehydrogenase activity; when associated with E-280.
- EGTSQ 401:405 (≠ EGTKE 389:393) binding in other chain
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
36% identity, 98% coverage: 4:407/412 of query aligns to 4:383/384 of 1jqiA
- active site: G377 (≠ R401)
- binding acetoacetyl-coenzyme a: L95 (= L100), F125 (≠ Y133), S134 (= S142), F234 (≠ S257), M238 (≠ L261), Q239 (≠ S262), L241 (≠ F264), D242 (≠ E265), R245 (= R268), Y364 (≠ F388), E365 (= E389), G366 (= G390)
- binding flavin-adenine dinucleotide: F125 (≠ Y133), L127 (≠ V135), S128 (= S136), G133 (= G141), S134 (= S142), W158 (= W166), T160 (= T168), R270 (= R293), F273 (= F296), L280 (≠ H303), Q338 (= Q362), I339 (= I363), G342 (= G366), I360 (= I384), T367 (= T391), E369 (= E393), I370 (= I394)
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, 98% coverage: 4:407/412 of query aligns to 31:410/412 of P15651
- 152:161 (vs. 133:142, 70% identical) binding FAD
- S161 (= S142) binding substrate
- WIT 185:187 (= WIT 166:168) binding FAD
- DMGR 269:272 (≠ EATR 265:268) binding substrate
- R297 (= R293) binding FAD
- QILGG 365:369 (≠ QIHGG 362:366) binding FAD
- E392 (= E389) active site, Proton acceptor
- TSE 394:396 (≠ TKE 391:393) binding FAD
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
1egcA Structure of t255e, e376g mutant of human medium chain acyl-coa dehydrogenase complexed with octanoyl-coa (see paper)
36% identity, 97% coverage: 3:401/412 of query aligns to 3:379/387 of 1egcA
- active site: V126 (= V135), T127 (≠ S136), E246 (≠ T267), G367 (≠ E389), R379 (= R401)
- binding octanoyl-coenzyme a: E90 (≠ F96), L94 (= L100), Y124 (= Y133), S133 (= S142), V135 (= V144), N182 (≠ H188), F236 (≠ A243), M240 (≠ L261), F243 (= F264), D244 (≠ E265), R247 (= R268), Y366 (≠ F388), G367 (≠ E389), G368 (= G390)
- binding flavin-adenine dinucleotide: Y124 (= Y133), V126 (= V135), T127 (≠ S136), G132 (= G141), S133 (= S142), W157 (= W166), T159 (= T168), R272 (= R293), T274 (= T295), F275 (= F296), L279 (≠ I300), H282 (= H303), I285 (= I306), Q340 (= Q362), I341 (= I363), G344 (= G366), I362 (= I384), I365 (= I387), Y366 (≠ F388), T369 (= T391), Q371 (≠ E393)
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
37% identity, 97% coverage: 3:401/412 of query aligns to 2:378/385 of 3mdeA
- active site: V125 (= V135), T126 (≠ S136), T245 (= T267), E366 (= E389), R378 (= R401)
- binding octanoyl-coenzyme a: T86 (≠ L93), E89 (≠ F96), L93 (= L100), S132 (= S142), V134 (= V144), S181 (≠ H188), F235 (≠ A243), M239 (≠ L261), F242 (= F264), R314 (≠ T333), Y365 (≠ F388), E366 (= E389), G367 (= G390)
- binding flavin-adenine dinucleotide: Y123 (= Y133), V125 (= V135), T126 (≠ S136), G131 (= G141), S132 (= S142), W156 (= W166), I157 (= I167), T158 (= T168), R271 (= R293), T273 (= T295), F274 (= F296), L278 (≠ I300), H281 (= H303), Q339 (= Q362), V340 (≠ I363), G343 (= G366), I361 (= I384), T368 (= T391), Q370 (≠ E393)
3mddA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
37% identity, 97% coverage: 3:401/412 of query aligns to 2:378/385 of 3mddA
- active site: V125 (= V135), T126 (≠ S136), T245 (= T267), E366 (= E389), R378 (= R401)
- binding flavin-adenine dinucleotide: Y123 (= Y133), T126 (≠ S136), G131 (= G141), S132 (= S142), W156 (= W166), T158 (= T168), R271 (= R293), T273 (= T295), F274 (= F296), H281 (= H303), Q339 (= Q362), V340 (≠ I363), G343 (= G366), I361 (= I384), T368 (= T391), Q370 (≠ E393)
1udyA Medium-chain acyl-coa dehydrogenase with 3-thiaoctanoyl-coa (see paper)
37% identity, 97% coverage: 3:401/412 of query aligns to 2:378/385 of 1udyA
- active site: V125 (= V135), T126 (≠ S136), T245 (= T267), E366 (= E389), R378 (= R401)
- binding 3-thiaoctanoyl-coenzyme a: L93 (= L100), Y123 (= Y133), S132 (= S142), S181 (≠ H188), F235 (≠ A243), M239 (≠ L261), F242 (= F264), V249 (= V271), R314 (≠ T333), Y365 (≠ F388), E366 (= E389), G367 (= G390), I371 (= I394), I375 (≠ V398)
- binding flavin-adenine dinucleotide: Y123 (= Y133), T126 (≠ S136), G131 (= G141), S132 (= S142), W156 (= W166), T158 (= T168), T273 (= T295), F274 (= F296), Q339 (= Q362), V340 (≠ I363), G343 (= G366), T368 (= T391), Q370 (≠ E393)
P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 from Sus scrofa (Pig) (see 2 papers)
37% identity, 97% coverage: 3:401/412 of query aligns to 37:413/421 of P41367
- 158:167 (vs. 133:142, 80% identical) binding in other chain
- S167 (= S142) binding octanoyl-CoA
- WIT 191:193 (= WIT 166:168) binding in other chain
- S216 (≠ H188) binding octanoyl-CoA
- D278 (≠ E265) binding octanoyl-CoA
- R281 (= R268) binding octanoyl-CoA
- RKT 306:308 (≠ RET 293:295) binding FAD
- HQ 316:317 (= HQ 303:304) binding in other chain
- R349 (≠ T333) binding octanoyl-CoA
- T351 (= T335) binding octanoyl-CoA
- QVFGG 374:378 (≠ QIHGG 362:366) binding FAD
- E401 (= E389) active site, Proton acceptor; binding octanoyl-CoA
- GTAQ 402:405 (≠ GTKE 390:393) binding in other chain
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
38% identity, 97% coverage: 3:403/412 of query aligns to 2:378/378 of 4n5fA
- active site: L126 (≠ V135), T127 (≠ S136), G243 (≠ T267), E364 (= E389), R376 (= R401)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ V135), T127 (≠ S136), G132 (= G141), S133 (= S142), F157 (≠ W166), T159 (= T168), T210 (= T219), Y363 (≠ F388), T366 (= T391), E368 (= E393), M372 (≠ L397)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
37% identity, 96% coverage: 8:403/412 of query aligns to 3:372/374 of 5lnxD
- active site: L122 (≠ V135), T123 (≠ S136), G239 (≠ T267), E358 (= E389), K370 (≠ R401)
- binding flavin-adenine dinucleotide: L122 (≠ V135), T123 (≠ S136), G128 (= G141), S129 (= S142), F153 (≠ W166), T155 (= T168), R265 (= R293), Q267 (≠ T295), F268 (= F296), I272 (= I300), N275 (≠ H303), I278 (= I306), Q331 (= Q362), I332 (= I363), G335 (= G366), Y357 (≠ F388), T360 (= T391), E362 (= E393)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
36% identity, 95% coverage: 18:407/412 of query aligns to 18:383/385 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 (≠ F367), T347 (≠ R371), E348 (= E372)
- binding flavin-adenine dinucleotide: F125 (≠ Y133), L127 (≠ V135), S128 (= S136), G133 (= G141), S134 (= S142), W158 (= W166), T160 (= T168), R270 (= R293), F273 (= F296), L280 (≠ H303), V282 (≠ A305), Q338 (= Q362), I339 (= I363), G342 (= G366), I360 (= I384), Y364 (≠ F388), T367 (= T391), E369 (= E393), I370 (= I394), L373 (= L397)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
36% identity, 95% coverage: 18:407/412 of query aligns to 45:410/412 of P16219
- G90 (= G69) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E83) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 133:142, 70% identical) binding in other chain
- R171 (≠ T152) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (= WIT 166:168) binding in other chain
- A192 (= A173) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G190) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R293) binding FAD
- Q308 (= Q304) binding in other chain
- R325 (= R321) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ G350) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QIHGG 362:366) binding FAD
- R380 (≠ K377) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ TKE 391:393) 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)
36% identity, 95% coverage: 18:407/412 of query aligns to 15:380/381 of 8sgsA
- binding coenzyme a: S131 (= S142), A133 (≠ V144), N177 (≠ H188), F231 (≠ S257), M235 (≠ L261), L238 (≠ F264), I312 (≠ K338), E362 (= E389), G363 (= G390)
- binding flavin-adenine dinucleotide: F122 (≠ Y133), L124 (≠ V135), S125 (= S136), G130 (= G141), S131 (= S142), W155 (= W166), T157 (= T168), R267 (= R293), F270 (= F296), L274 (≠ I300), L277 (≠ H303), Q335 (= Q362), I336 (= I363), G338 (= G365), G339 (= G366), I357 (= I384), I360 (= I387), Y361 (≠ F388), T364 (= T391), E366 (= E393)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
36% identity, 95% coverage: 18:407/412 of query aligns to 21:386/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ Y133), L130 (≠ V135), S131 (= S136), G136 (= G141), S137 (= S142), W161 (= W166), T163 (= T168), T214 (= T219), R273 (= R293), F276 (= F296), L280 (≠ I300), L283 (≠ H303), V285 (≠ A305), Q341 (= Q362), I342 (= I363), G345 (= G366), I363 (= I384), Y367 (≠ F388), T370 (= T391), E372 (= E393), L376 (= L397)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
36% identity, 96% coverage: 3:399/412 of query aligns to 1:372/378 of 5ol2F
- active site: L124 (≠ V135), T125 (≠ S136), G241 (≠ T267)
- binding calcium ion: E29 (≠ H39), E33 (≠ V43), R35 (≠ E45)
- binding coenzyme a persulfide: L238 (≠ F264), R242 (= R268), E362 (= E389), G363 (= G390)
- binding flavin-adenine dinucleotide: F122 (≠ Y133), L124 (≠ V135), T125 (≠ S136), P127 (= P138), T131 (≠ S142), F155 (≠ W166), I156 (= I167), T157 (= T168), E198 (≠ T209), R267 (= R293), F270 (= F296), L274 (≠ I300), F277 (≠ H303), Q335 (= Q362), L336 (≠ I363), G338 (= G365), G339 (= G366), Y361 (≠ F388), T364 (= T391), E366 (= E393)
Sites not aligning to the query:
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
35% identity, 96% coverage: 5:399/412 of query aligns to 1:372/379 of 6fahD
- active site: L124 (≠ V135), T125 (≠ S136), G241 (≠ T267)
- binding flavin-adenine dinucleotide: F122 (≠ Y133), L124 (≠ V135), T125 (≠ S136), R152 (≠ E163), F155 (≠ W166), T157 (= T168), E198 (≠ T209), R267 (= R293), Q269 (≠ T295), F270 (= F296), I274 (= I300), F277 (≠ H303), Q335 (= Q362), I336 (= I363), G339 (= G366), Y361 (≠ F388), T364 (= T391), Q366 (≠ E393)
Sites not aligning to the query:
Query Sequence
>WP_052664119.1 NCBI__GCF_000969705.1:WP_052664119.1
MPFDLKLTEEQISAQKWAHDFARKEMREATVDGVPAHRHYDEVEEFPWPIVQKAAEVGLY
GLEYYQMAGQDPTGLTQALIIEELFWGCAGIGLAIFGSGLALAGLASSGTGDQIAEWAPR
IFGTPDDVKVGAYAVSEPGAGSDVSKIRTKATKVEGGWLLNGEKIWITNGGIADVHIVVA
TVDPTIGHRGQASFIVTSDAEGFQETKKTKKLGIRASHTAELSFTDCFVPDEQLLGGQDK
LDAKIDAAHNPDPNRKSSGALSTFEATRPIVGIQAVGVARAAFDASVQYAMERETFGVPI
IRHQAIAFKLADMATEIDAARLLCWRGINMGTTWTPFKHGEGSMAKLHAGRTAVRVTDEA
IQIHGGFGYSREFDVEKFHRDSKIYEIFEGTKEIQQLVIGRAIARSHGGTAA
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