SitesBLAST
Comparing N515DRAFT_0484 N515DRAFT_0484 glutaryl-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)
2ebaA Crystal structure of the putative glutaryl-coa dehydrogenase from thermus thermophilus
60% identity, 98% coverage: 8:389/389 of query aligns to 2:380/380 of 2ebaA
- active site: L131 (= L137), T132 (= T138), A239 (= A248), E360 (= E369), R372 (= R381)
- binding flavin-adenine dinucleotide: L131 (= L137), T132 (= T138), G136 (= G142), G137 (= G143), S138 (= S144), W161 (= W168), T163 (= T170), R265 (= R274), L272 (= L281), K275 (≠ N284), D333 (= D342), I334 (= I343), G337 (= G346), T355 (≠ S364), T358 (= T367), Y359 (= Y368), T362 (= T371)
3swoA Crystal structure of a glutaryl-coa dehydrogenase from mycobacterium smegmatis in complex with fadh2 (see paper)
57% identity, 98% coverage: 7:389/389 of query aligns to 6:387/388 of 3swoA
- active site: L135 (= L137), T136 (= T138), A246 (= A248), E367 (= E369), K379 (≠ R381)
- binding dihydroflavine-adenine dinucleotide: F133 (= F135), L135 (= L137), T136 (= T138), G141 (= G143), S142 (= S144), W166 (= W168), I167 (= I169), T168 (= T170), R272 (= R274), V274 (≠ L276), F275 (= F277), L279 (= L281), Y282 (≠ N284), T340 (≠ D342), L341 (≠ I343), G344 (= G346), I347 (= I349), T365 (= T367), Y366 (= Y368), T369 (= T371), E371 (≠ T373), M372 (≠ V374)
3sf6A Crystal structure of glutaryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
54% identity, 98% coverage: 9:389/389 of query aligns to 6:386/387 of 3sf6A
- active site: L134 (= L137), T135 (= T138), A245 (= A248), E366 (= E369), Q378 (≠ R381)
- binding dihydroflavine-adenine dinucleotide: F132 (= F135), L134 (= L137), T135 (= T138), G140 (= G143), S141 (= S144), W165 (= W168), I166 (= I169), T167 (= T170), S361 (= S364), T364 (= T367), Y365 (= Y368), T368 (= T371), E370 (≠ T373), M371 (≠ V374)
2r0nA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
51% identity, 96% coverage: 17:389/389 of query aligns to 14:388/390 of 2r0nA
- active site: L133 (= L137), T134 (= T138), A247 (= A248), E368 (= E369), R380 (= R381)
- binding flavin-adenine dinucleotide: F131 (= F135), L133 (= L137), T134 (= T138), G139 (= G143), S140 (= S144), W166 (= W168), I167 (= I169), T168 (= T170), Y367 (= Y368), T370 (= T371), D372 (≠ T373)
- binding 3-thiaglutaryl-CoA: R92 (= R96), S93 (= S97), V97 (= V101), P142 (= P146), G238 (≠ K239), F241 (≠ L242), L244 (= L245), N245 (≠ T246), P318 (= P319), Y367 (= Y368), E368 (= E369), I377 (≠ V378)
1sirA The crystal structure and mechanism of human glutaryl-coa dehydrogenase (see paper)
51% identity, 96% coverage: 17:389/389 of query aligns to 14:388/390 of 1sirA
- active site: L133 (= L137), T134 (= T138), A247 (= A248), E368 (= E369), R380 (= R381)
- binding flavin-adenine dinucleotide: F131 (= F135), L133 (= L137), T134 (= T138), G139 (= G143), S140 (= S144), W166 (= W168), I167 (= I169), T168 (= T170), Y367 (= Y368), T370 (= T371)
- binding s-4-nitrobutyryl-coa: S93 (= S97), S140 (= S144), F241 (≠ L242), G242 (= G243), L244 (= L245), N245 (≠ T246), R248 (= R249), P318 (= P319), Y367 (= Y368), E368 (= E369), R380 (= R381)
2r0mA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
51% identity, 96% coverage: 17:389/389 of query aligns to 14:388/390 of 2r0mA
- active site: L133 (= L137), T134 (= T138), A247 (= A248), D368 (≠ E369), R380 (= R381)
- binding 4-nitrobutanoic acid: L101 (= L105), Y367 (= Y368), D368 (≠ E369)
- binding flavin-adenine dinucleotide: F131 (= F135), L133 (= L137), T134 (= T138), G139 (= G143), S140 (= S144), W166 (= W168), I167 (= I169), T168 (= T170), L210 (= L211), Y367 (= Y368), T370 (= T371)
3gqtC Crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei with fragment (1,4-dimethyl-1,2,3,4- tetrahydroquinoxalin-6-yl)methylamine (see paper)
49% identity, 96% coverage: 17:389/389 of query aligns to 15:385/385 of 3gqtC
- active site: L135 (= L137), T136 (= T138), A250 (= A248), E365 (= E369), R377 (= R381)
- binding 1-(1,4-dimethyl-1,2,3,4-tetrahydroquinoxalin-6-yl)methanamine: W166 (= W168), K210 (= K208), L213 (= L211), T218 (= T216), Y364 (= Y368)
3eonC 2.55a crystal structure of native glutaryl-coa dehydrogenase from burkholderia pseudomallei in complex with a small molecule (see paper)
49% identity, 96% coverage: 17:388/389 of query aligns to 15:382/382 of 3eonC
3gncA Crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei with fragment 6421 (see paper)
48% identity, 96% coverage: 17:388/389 of query aligns to 16:380/380 of 3gncA
3d6bC 2.2 a crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei (see paper)
48% identity, 96% coverage: 17:388/389 of query aligns to 15:377/377 of 3d6bC
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
37% identity, 95% coverage: 16:383/389 of query aligns to 5:378/378 of 4n5fA
- active site: L126 (= L137), T127 (= T138), G243 (≠ A248), E364 (= E369), R376 (= R381)
- binding dihydroflavine-adenine dinucleotide: L126 (= L137), T127 (= T138), G132 (= G143), S133 (= S144), F157 (≠ W168), T159 (= T170), T210 (= T216), Y363 (= Y368), T366 (= T371), E368 (≠ T373), M372 (≠ L377)
2ix6A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 (see paper)
35% identity, 98% coverage: 9:389/389 of query aligns to 31:412/416 of 2ix6A
- active site: L158 (= L137), T159 (= T138), S271 (≠ A248), E392 (= E369), R404 (= R381)
- binding flavin-adenine dinucleotide: T159 (= T138), G164 (= G143), S165 (= S144), W189 (= W168), N239 (≠ T216), R297 (= R274), F300 (= F277), L304 (= L281), F307 (≠ N284), N310 (≠ I287), E365 (≠ D342), L366 (≠ I343), G369 (= G346), I372 (= I349), Y391 (= Y368), T394 (= T371), D396 (≠ T373)
2ix5A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 in complex with acetoacetyl-coa (see paper)
35% identity, 98% coverage: 9:389/389 of query aligns to 31:412/415 of 2ix5A
- active site: L158 (= L137), T159 (= T138), S271 (≠ A248), E392 (= E369), R404 (= R381)
- binding acetoacetyl-coenzyme a: S165 (= S144), A167 (≠ P146), S168 (≠ A147), F261 (≠ L238), L268 (= L245), R272 (= R249), E392 (= E369), G393 (= G370), R404 (= R381)
- binding flavin-adenine dinucleotide: L158 (= L137), T159 (= T138), G164 (= G143), S165 (= S144), W189 (= W168), N239 (≠ T216), R297 (= R274), F300 (= F277), L304 (= L281), F307 (≠ N284), L309 (≠ A286), N310 (≠ I287), E365 (≠ D342), L366 (≠ I343), G368 (= G345), G369 (= G346), Y391 (= Y368), T394 (= T371), D396 (≠ T373), I397 (≠ V374)
Q96329 Acyl-coenzyme A oxidase 4, peroxisomal; AOX 4; G6p; Short-chain acyl-CoA oxidase; AtCX4; AtG6; SAOX; EC 1.3.3.6 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
35% identity, 98% coverage: 9:389/389 of query aligns to 47:428/436 of Q96329
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
36% identity, 94% coverage: 20:385/389 of query aligns to 5:374/374 of 5lnxD
- active site: L122 (= L137), T123 (= T138), G239 (≠ A248), E358 (= E369), K370 (≠ R381)
- binding flavin-adenine dinucleotide: L122 (= L137), T123 (= T138), G128 (= G143), S129 (= S144), F153 (≠ W168), T155 (= T170), R265 (= R274), Q267 (≠ L276), F268 (= F277), I272 (≠ L281), N275 (= N284), I278 (= I287), Q331 (≠ D342), I332 (= I343), G335 (= G346), Y357 (= Y368), T360 (= T371), E362 (≠ T373)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
35% identity, 94% coverage: 17:383/389 of query aligns to 4:376/381 of 8sgsA
- binding coenzyme a: S131 (= S144), A133 (≠ P146), N177 (vs. gap), F231 (≠ L238), M235 (≠ L242), L238 (= L245), I312 (vs. gap), E362 (= E369), G363 (= G370)
- binding flavin-adenine dinucleotide: F122 (= F135), L124 (= L137), S125 (≠ T138), G130 (= G143), S131 (= S144), W155 (= W168), T157 (= T170), R267 (= R274), F270 (= F277), L274 (= L281), L277 (≠ N284), Q335 (≠ D342), I336 (= I343), G338 (= G345), G339 (= G346), I357 (≠ S364), I360 (≠ T367), Y361 (= Y368), T364 (= T371), E366 (≠ T373)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
35% identity, 94% coverage: 17:383/389 of query aligns to 7:379/385 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 (≠ A347), T347 (= T351), E348 (= E352)
- binding flavin-adenine dinucleotide: F125 (= F135), L127 (= L137), S128 (≠ T138), G133 (= G143), S134 (= S144), W158 (= W168), T160 (= T170), R270 (= R274), F273 (= F277), L280 (≠ N284), V282 (≠ A286), Q338 (≠ D342), I339 (= I343), G342 (= G346), I360 (≠ S364), Y364 (= Y368), T367 (= T371), E369 (≠ T373), I370 (≠ V374), L373 (= L377)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
35% identity, 94% coverage: 17:383/389 of query aligns to 10:382/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (= F135), L130 (= L137), S131 (≠ T138), G136 (= G143), S137 (= S144), W161 (= W168), T163 (= T170), T214 (= T216), R273 (= R274), F276 (= F277), L280 (= L281), L283 (≠ N284), V285 (≠ A286), Q341 (≠ D342), I342 (= I343), G345 (= G346), I363 (≠ S364), Y367 (= Y368), T370 (= T371), E372 (≠ T373), L376 (= L377)
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, 94% coverage: 17:383/389 of query aligns to 34:406/412 of P16219
- G90 (≠ C73) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E87) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 135:144, 60% identical) binding in other chain
- R171 (= R154) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (= WIT 168:170) binding in other chain
- A192 (= A175) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G187) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R274) binding
- Q308 (= Q285) binding in other chain
- R325 (≠ Q302) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ C330) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ DILGG 342:346) binding
- R380 (= R357) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ TET 371:373) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
34% identity, 95% coverage: 16:383/389 of query aligns to 3:376/378 of 5ol2F
- active site: L124 (= L137), T125 (= T138), G241 (≠ A248), G374 (≠ R381)
- binding calcium ion: E29 (≠ D42), E33 (≠ Q46), R35 (= R48)
- binding coenzyme a persulfide: L238 (= L245), R242 (= R249), E362 (= E369), G363 (= G370)
- binding flavin-adenine dinucleotide: F122 (= F135), L124 (= L137), T125 (= T138), P127 (= P140), T131 (≠ S144), F155 (≠ W168), I156 (= I169), T157 (= T170), E198 (≠ H206), R267 (= R274), F270 (= F277), L274 (= L281), F277 (≠ N284), Q335 (≠ D342), L336 (≠ I343), G338 (= G345), G339 (= G346), Y361 (= Y368), T364 (= T371), E366 (≠ T373)
Query Sequence
>N515DRAFT_0484 N515DRAFT_0484 glutaryl-CoA dehydrogenase
MSARLNPLDLYDVRSLLTDEERMVQDTVGRFVDERVLPIIGDAFDQGRFPKELIPEIAGL
GLLGATLPEQYGCAGMNGVSYGLICQELERGDSGLRSFASVQSSLCMYPIYAYGTEEQKL
HYLPKMAAGEIIGCFGLTEPHGGSDPANMKTNARKDGGDWIINGAKMWITNGNLAHIAIV
WAQTEDGIQGFIVPTDSQGFTAQEVHKKMSLRASVTSALFFDSVRVPEANRLPNVKGLKG
PLGCLTQARYGITWGPIGAAQACLKEVLDYTQERVLFGRPLASNQAIQLKLAEMARRITM
AQLLSLQLGRLKDAGNMQPTQVSLAKWNNCRIAIDIARECRDILGGAGITTEHVAIRHAL
NLESVITYEGTETVHQLVVGRELTGINAF
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