SitesBLAST
Comparing CA265_RS09630 FitnessBrowser__Pedo557:CA265_RS09630 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)
2r0nA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
53% identity, 97% coverage: 10:395/396 of query aligns to 2:388/390 of 2r0nA
- active site: L133 (= L142), T134 (= T143), A247 (= A254), E368 (= E375), R380 (≠ M387)
- binding flavin-adenine dinucleotide: F131 (= F140), L133 (= L142), T134 (= T143), G139 (= G148), S140 (= S149), W166 (= W173), I167 (= I174), T168 (≠ S175), Y367 (= Y374), T370 (= T377), D372 (= D379)
- binding 3-thiaglutaryl-CoA: R92 (= R101), S93 (= S102), V97 (= V106), P142 (= P151), G238 (≠ K245), F241 (≠ L248), L244 (= L251), N245 (= N252), P318 (≠ A325), Y367 (= Y374), E368 (= E375), I377 (= I384)
1sirA The crystal structure and mechanism of human glutaryl-coa dehydrogenase (see paper)
53% identity, 97% coverage: 10:395/396 of query aligns to 2:388/390 of 1sirA
- active site: L133 (= L142), T134 (= T143), A247 (= A254), E368 (= E375), R380 (≠ M387)
- binding flavin-adenine dinucleotide: F131 (= F140), L133 (= L142), T134 (= T143), G139 (= G148), S140 (= S149), W166 (= W173), I167 (= I174), T168 (≠ S175), Y367 (= Y374), T370 (= T377)
- binding s-4-nitrobutyryl-coa: S93 (= S102), S140 (= S149), F241 (≠ L248), G242 (= G249), L244 (= L251), N245 (= N252), R248 (= R255), P318 (≠ A325), Y367 (= Y374), E368 (= E375), R380 (≠ M387)
2r0mA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
53% identity, 97% coverage: 10:395/396 of query aligns to 2:388/390 of 2r0mA
- active site: L133 (= L142), T134 (= T143), A247 (= A254), D368 (≠ E375), R380 (≠ M387)
- binding 4-nitrobutanoic acid: L101 (= L110), Y367 (= Y374), D368 (≠ E375)
- binding flavin-adenine dinucleotide: F131 (= F140), L133 (= L142), T134 (= T143), G139 (= G148), S140 (= S149), W166 (= W173), I167 (= I174), T168 (≠ S175), L210 (= L217), Y367 (= Y374), T370 (= T377)
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)
53% identity, 96% coverage: 14:395/396 of query aligns to 7:385/385 of 3gqtC
- active site: L135 (= L142), T136 (= T143), A250 (= A254), E365 (= E375), R377 (≠ M387)
- binding 1-(1,4-dimethyl-1,2,3,4-tetrahydroquinoxalin-6-yl)methanamine: W166 (= W173), K210 (= K214), L213 (= L217), T218 (= T222), Y364 (= Y374)
2ebaA Crystal structure of the putative glutaryl-coa dehydrogenase from thermus thermophilus
54% identity, 96% coverage: 14:395/396 of query aligns to 3:380/380 of 2ebaA
- active site: L131 (= L142), T132 (= T143), A239 (= A254), E360 (= E375), R372 (≠ M387)
- binding flavin-adenine dinucleotide: L131 (= L142), T132 (= T143), G136 (≠ H147), G137 (= G148), S138 (= S149), W161 (= W173), T163 (≠ S175), R265 (= R280), L272 (≠ I287), K275 (≠ F290), D333 (≠ Q348), I334 (≠ M349), G337 (= G352), T355 (≠ S370), T358 (= T373), Y359 (= Y374), T362 (= T377)
3eonC 2.55a crystal structure of native glutaryl-coa dehydrogenase from burkholderia pseudomallei in complex with a small molecule (see paper)
52% identity, 96% coverage: 14:394/396 of query aligns to 7:382/382 of 3eonC
3gncA Crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei with fragment 6421 (see paper)
51% identity, 96% coverage: 14:394/396 of query aligns to 8:380/380 of 3gncA
3d6bC 2.2 a crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei (see paper)
51% identity, 96% coverage: 14:394/396 of query aligns to 7:377/377 of 3d6bC
3sf6A Crystal structure of glutaryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
49% identity, 97% coverage: 12:396/396 of query aligns to 4:387/387 of 3sf6A
- active site: L134 (= L142), T135 (= T143), A245 (= A254), E366 (= E375), Q378 (≠ M387)
- binding dihydroflavine-adenine dinucleotide: F132 (= F140), L134 (= L142), T135 (= T143), G140 (= G148), S141 (= S149), W165 (= W173), I166 (= I174), T167 (≠ S175), S361 (= S370), T364 (= T373), Y365 (= Y374), T368 (= T377), E370 (≠ D379), M371 (≠ I380)
3swoA Crystal structure of a glutaryl-coa dehydrogenase from mycobacterium smegmatis in complex with fadh2 (see paper)
48% identity, 98% coverage: 7:396/396 of query aligns to 1:388/388 of 3swoA
- active site: L135 (= L142), T136 (= T143), A246 (= A254), E367 (= E375), K379 (≠ M387)
- binding dihydroflavine-adenine dinucleotide: F133 (= F140), L135 (= L142), T136 (= T143), G141 (= G148), S142 (= S149), W166 (= W173), I167 (= I174), T168 (≠ S175), R272 (= R280), V274 (≠ Q282), F275 (= F283), L279 (≠ I287), Y282 (≠ F290), T340 (≠ Q348), L341 (≠ M349), G344 (= G352), I347 (= I355), T365 (= T373), Y366 (= Y374), T369 (= T377), E371 (≠ D379), M372 (≠ I380)
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)
38% identity, 97% coverage: 14:396/396 of query aligns to 47:429/436 of Q96329
2ix6A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 (see paper)
38% identity, 97% coverage: 14:396/396 of query aligns to 31:413/416 of 2ix6A
- active site: L158 (= L142), T159 (= T143), S271 (≠ A254), E392 (= E375), R404 (≠ M387)
- binding flavin-adenine dinucleotide: T159 (= T143), G164 (= G148), S165 (= S149), W189 (= W173), N239 (≠ T222), R297 (= R280), F300 (= F283), L304 (≠ I287), F307 (= F290), N310 (≠ Q293), E365 (≠ Q348), L366 (≠ M349), G369 (= G352), I372 (= I355), Y391 (= Y374), T394 (= T377), D396 (= D379)
2ix5A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 in complex with acetoacetyl-coa (see paper)
38% identity, 97% coverage: 14:396/396 of query aligns to 31:413/415 of 2ix5A
- active site: L158 (= L142), T159 (= T143), S271 (≠ A254), E392 (= E375), R404 (≠ M387)
- binding acetoacetyl-coenzyme a: S165 (= S149), A167 (≠ P151), S168 (≠ G152), F261 (≠ L244), L268 (= L251), R272 (= R255), E392 (= E375), G393 (= G376), R404 (≠ M387)
- binding flavin-adenine dinucleotide: L158 (= L142), T159 (= T143), G164 (= G148), S165 (= S149), W189 (= W173), N239 (≠ T222), R297 (= R280), F300 (= F283), L304 (≠ I287), F307 (= F290), L309 (= L292), N310 (≠ Q293), E365 (≠ Q348), L366 (≠ M349), G368 (= G351), G369 (= G352), Y391 (= Y374), T394 (= T377), D396 (= D379), I397 (= I380)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
36% identity, 93% coverage: 18:385/396 of query aligns to 1:373/380 of 4l1fA
- active site: L125 (= L142), T126 (= T143), G242 (≠ A254), E363 (= E375)
- binding coenzyme a persulfide: T132 (≠ S149), H179 (≠ R195), F232 (≠ L244), M236 (≠ L248), E237 (≠ G249), L239 (= L251), D240 (≠ N252), R243 (= R255), Y362 (= Y374), E363 (= E375), G364 (= G376)
- binding flavin-adenine dinucleotide: F123 (= F140), L125 (= L142), T126 (= T143), G131 (= G148), T132 (≠ S149), F156 (≠ W173), I157 (= I174), T158 (≠ S175), R268 (= R280), Q270 (= Q282), F271 (= F283), I275 (= I287), F278 (= F290), L281 (≠ Q293), Q336 (= Q348), I337 (≠ M349), G340 (= G352), I358 (≠ S370), Y362 (= Y374), T365 (= T377), Q367 (≠ D379)
- binding 1,3-propandiol: L5 (= L22), Q10 (≠ K27)
Sites not aligning to the query:
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
36% identity, 92% coverage: 22:384/396 of query aligns to 1:361/371 of 2vigB
- active site: L121 (= L142), S122 (≠ T143), G231 (≠ A254), E352 (= E375)
- binding coenzyme a persulfide: S128 (= S149), F221 (≠ L244), M225 (≠ L248), Q226 (≠ G249), L228 (= L251), D229 (≠ N252), R232 (= R255), E352 (= E375), G353 (= G376), I357 (= I380)
- binding flavin-adenine dinucleotide: L121 (= L142), S122 (≠ T143), G127 (= G148), S128 (= S149), W152 (= W173), T154 (≠ S175), R257 (= R280), F260 (= F283), L264 (≠ I287), L267 (≠ F290), Q325 (= Q348), I326 (≠ M349), G329 (= G352), I347 (≠ S370), Y351 (= Y374), T354 (= T377), E356 (≠ D379)
Sites not aligning to the query:
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
36% identity, 92% coverage: 22:384/396 of query aligns to 4:371/381 of 8sgsA
- binding coenzyme a: S131 (= S149), A133 (≠ P151), N177 (vs. gap), F231 (≠ L244), M235 (≠ L248), L238 (= L251), I312 (≠ A325), E362 (= E375), G363 (= G376)
- binding flavin-adenine dinucleotide: F122 (= F140), L124 (= L142), S125 (≠ T143), G130 (= G148), S131 (= S149), W155 (= W173), T157 (≠ S175), R267 (= R280), F270 (= F283), L274 (≠ I287), L277 (≠ F290), Q335 (= Q348), I336 (≠ M349), G338 (= G351), G339 (= G352), I357 (≠ S370), I360 (≠ T373), Y361 (= Y374), T364 (= T377), E366 (≠ D379)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
36% identity, 92% coverage: 22:384/396 of query aligns to 10:377/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (= F140), L130 (= L142), S131 (≠ T143), G136 (= G148), S137 (= S149), W161 (= W173), T163 (≠ S175), T214 (= T222), R273 (= R280), F276 (= F283), L280 (≠ I287), L283 (≠ F290), V285 (≠ L292), Q341 (= Q348), I342 (≠ M349), G345 (= G352), I363 (≠ S370), Y367 (= Y374), T370 (= T377), E372 (≠ D379), L376 (= L383)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
36% identity, 92% coverage: 22:384/396 of query aligns to 7:374/385 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 (= M353), T347 (≠ G357), E348 (= E358)
- binding flavin-adenine dinucleotide: F125 (= F140), L127 (= L142), S128 (≠ T143), G133 (= G148), S134 (= S149), W158 (= W173), T160 (≠ S175), R270 (= R280), F273 (= F283), L280 (≠ F290), V282 (≠ L292), Q338 (= Q348), I339 (≠ M349), G342 (= G352), I360 (≠ S370), Y364 (= Y374), T367 (= T377), E369 (≠ D379), I370 (= I380), L373 (= L383)
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, 92% coverage: 22:384/396 of query aligns to 34:401/412 of P16219
- G90 (= G78) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E92) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 140:149, 60% identical) binding in other chain
- R171 (≠ K159) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ WIS 173:175) binding in other chain
- A192 (= A180) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (≠ K193) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R280) binding
- Q308 (= Q291) binding in other chain
- R325 (≠ Q308) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ V336) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QMLGG 348:352) binding
- R380 (= R363) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ THD 377:379) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
35% identity, 92% coverage: 22:384/396 of query aligns to 34:401/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
Query Sequence
>CA265_RS09630 FitnessBrowser__Pedo557:CA265_RS09630
MSKSAKKDLYEAPDYYLLDELLTDEHKLIRATARDWVKKEVSPIIEDYAQKAEFPKHLIK
GLADIGAFGPTIPVEYGGAGLDYTAYGILMQEIERGDSGIRSTASVQGSLVMYPIYAYGS
EEQRKKYLPKLASGEMMGCFGLTEPDHGSNPGGMVTNIKDAGSHYILNGAKMWISNAPFA
DIAVVWAKDESGKIRGLIVERGMEGFSTPETHHKWSLRASATGELVFDNVKVPKENIFPE
ISGLKGPLGCLNQARYGIAWGALGAAMDCYDTALRYSKERVQFGKPIGGFQLQQKKLAEM
VTEITKGQLLVWRLGVLKSENRASAEQISMAKRNSVEIALDIARNARQMLGGMGITGEYS
IMRHMMNLESVVTYEGTHDIHLLITGMDVTGLNAFK
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