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Comparing Ac3H11_3533 FitnessBrowser__acidovorax_3H11:Ac3H11_3533 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)
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)
81% identity, 99% coverage: 4:396/398 of query aligns to 1:385/385 of 3gqtC
- active site: L135 (= L138), T136 (= T139), A250 (= A255), E365 (= E376), R377 (= R388)
- binding 1-(1,4-dimethyl-1,2,3,4-tetrahydroquinoxalin-6-yl)methanamine: W166 (= W169), K210 (= K215), L213 (= L218), T218 (= T223), Y364 (= Y375)
3eonC 2.55a crystal structure of native glutaryl-coa dehydrogenase from burkholderia pseudomallei in complex with a small molecule (see paper)
81% identity, 98% coverage: 4:395/398 of query aligns to 1:382/382 of 3eonC
3gncA Crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei with fragment 6421 (see paper)
80% identity, 98% coverage: 4:395/398 of query aligns to 2:380/380 of 3gncA
3d6bC 2.2 a crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei (see paper)
80% identity, 98% coverage: 4:395/398 of query aligns to 1:377/377 of 3d6bC
2r0nA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
66% identity, 98% coverage: 6:397/398 of query aligns to 2:389/390 of 2r0nA
- active site: L133 (= L138), T134 (= T139), A247 (= A255), E368 (= E376), R380 (= R388)
- binding flavin-adenine dinucleotide: F131 (= F136), L133 (= L138), T134 (= T139), G139 (= G144), S140 (= S145), W166 (= W169), I167 (= I170), T168 (= T171), Y367 (= Y375), T370 (= T378), D372 (= D380)
- binding 3-thiaglutaryl-CoA: R92 (= R97), S93 (= S98), V97 (= V102), P142 (= P147), G238 (≠ K246), F241 (= F249), L244 (= L252), N245 (= N253), P318 (≠ V326), Y367 (= Y375), E368 (= E376), I377 (= I385)
1sirA The crystal structure and mechanism of human glutaryl-coa dehydrogenase (see paper)
66% identity, 98% coverage: 6:397/398 of query aligns to 2:389/390 of 1sirA
- active site: L133 (= L138), T134 (= T139), A247 (= A255), E368 (= E376), R380 (= R388)
- binding flavin-adenine dinucleotide: F131 (= F136), L133 (= L138), T134 (= T139), G139 (= G144), S140 (= S145), W166 (= W169), I167 (= I170), T168 (= T171), Y367 (= Y375), T370 (= T378)
- binding s-4-nitrobutyryl-coa: S93 (= S98), S140 (= S145), F241 (= F249), G242 (≠ T250), L244 (= L252), N245 (= N253), R248 (= R256), P318 (≠ V326), Y367 (= Y375), E368 (= E376), R380 (= R388)
2r0mA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
66% identity, 98% coverage: 6:397/398 of query aligns to 2:389/390 of 2r0mA
- active site: L133 (= L138), T134 (= T139), A247 (= A255), D368 (≠ E376), R380 (= R388)
- binding 4-nitrobutanoic acid: L101 (= L106), Y367 (= Y375), D368 (≠ E376)
- binding flavin-adenine dinucleotide: F131 (= F136), L133 (= L138), T134 (= T139), G139 (= G144), S140 (= S145), W166 (= W169), I167 (= I170), T168 (= T171), L210 (= L218), Y367 (= Y375), T370 (= T378)
2ebaA Crystal structure of the putative glutaryl-coa dehydrogenase from thermus thermophilus
46% identity, 97% coverage: 10:396/398 of query aligns to 3:380/380 of 2ebaA
- active site: L131 (= L138), T132 (= T139), A239 (= A255), E360 (= E376), R372 (= R388)
- binding flavin-adenine dinucleotide: L131 (= L138), T132 (= T139), G136 (≠ H143), G137 (= G144), S138 (= S145), W161 (= W169), T163 (= T171), R265 (= R281), L272 (= L288), K275 (≠ N291), D333 (= D349), I334 (≠ M350), G337 (= G353), T355 (≠ V371), T358 (= T374), Y359 (= Y375), T362 (= T378)
3sf6A Crystal structure of glutaryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
47% identity, 97% coverage: 9:396/398 of query aligns to 5:386/387 of 3sf6A
- active site: L134 (= L138), T135 (= T139), A245 (= A255), E366 (= E376), Q378 (≠ R388)
- binding dihydroflavine-adenine dinucleotide: F132 (= F136), L134 (= L138), T135 (= T139), G140 (= G144), S141 (= S145), W165 (= W169), I166 (= I170), T167 (= T171), S361 (≠ V371), T364 (= T374), Y365 (= Y375), T368 (= T378), E370 (≠ D380), M371 (≠ V381)
3swoA Crystal structure of a glutaryl-coa dehydrogenase from mycobacterium smegmatis in complex with fadh2 (see paper)
44% identity, 97% coverage: 12:396/398 of query aligns to 10:387/388 of 3swoA
- active site: L135 (= L138), T136 (= T139), A246 (= A255), E367 (= E376), K379 (≠ R388)
- binding dihydroflavine-adenine dinucleotide: F133 (= F136), L135 (= L138), T136 (= T139), G141 (= G144), S142 (= S145), W166 (= W169), I167 (= I170), T168 (= T171), R272 (= R281), V274 (≠ Q283), F275 (= F284), L279 (= L288), Y282 (≠ N291), T340 (≠ D349), L341 (≠ M350), G344 (= G353), I347 (= I356), T365 (= T374), Y366 (= Y375), T369 (= T378), E371 (≠ D380), M372 (≠ V381)
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)
37% identity, 97% coverage: 9:396/398 of query aligns to 46:428/436 of Q96329
2ix5A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 in complex with acetoacetyl-coa (see paper)
37% identity, 97% coverage: 9:396/398 of query aligns to 30:412/415 of 2ix5A
- active site: L158 (= L138), T159 (= T139), S271 (≠ A255), E392 (= E376), R404 (= R388)
- binding acetoacetyl-coenzyme a: S165 (= S145), A167 (≠ P147), S168 (≠ G148), F261 (≠ L245), L268 (= L252), R272 (= R256), E392 (= E376), G393 (= G377), R404 (= R388)
- binding flavin-adenine dinucleotide: L158 (= L138), T159 (= T139), G164 (= G144), S165 (= S145), W189 (= W169), N239 (≠ T223), R297 (= R281), F300 (= F284), L304 (= L288), F307 (≠ N291), L309 (= L293), N310 (≠ I294), E365 (≠ D349), L366 (≠ M350), G368 (= G352), G369 (= G353), Y391 (= Y375), T394 (= T378), D396 (= D380), I397 (≠ V381)
2ix6A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 (see paper)
37% identity, 97% coverage: 9:396/398 of query aligns to 30:412/416 of 2ix6A
- active site: L158 (= L138), T159 (= T139), S271 (≠ A255), E392 (= E376), R404 (= R388)
- binding flavin-adenine dinucleotide: T159 (= T139), G164 (= G144), S165 (= S145), W189 (= W169), N239 (≠ T223), R297 (= R281), F300 (= F284), L304 (= L288), F307 (≠ N291), N310 (≠ I294), E365 (≠ D349), L366 (≠ M350), G369 (= G353), I372 (= I356), Y391 (= Y375), T394 (= T378), D396 (= D380)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
36% identity, 94% coverage: 14:389/398 of query aligns to 1:376/380 of 4l1fA
- active site: L125 (= L138), T126 (= T139), G242 (≠ A255), E363 (= E376), R375 (= R388)
- binding coenzyme a persulfide: T132 (≠ S145), H179 (≠ V192), F232 (≠ L245), M236 (≠ F249), E237 (≠ T250), L239 (= L252), D240 (≠ N253), R243 (= R256), Y362 (= Y375), E363 (= E376), G364 (= G377), R375 (= R388)
- binding flavin-adenine dinucleotide: F123 (= F136), L125 (= L138), T126 (= T139), G131 (= G144), T132 (≠ S145), F156 (≠ W169), I157 (= I170), T158 (= T171), R268 (= R281), Q270 (= Q283), F271 (= F284), I275 (≠ L288), F278 (≠ N291), L281 (≠ I294), Q336 (≠ D349), I337 (≠ M350), G340 (= G353), I358 (≠ V371), Y362 (= Y375), T365 (= T378), Q367 (≠ D380)
- binding 1,3-propandiol: L5 (= L18), Q10 (≠ R23)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
36% identity, 93% coverage: 23:392/398 of query aligns to 11:374/374 of 5lnxD
- active site: L122 (= L138), T123 (= T139), G239 (≠ A255), E358 (= E376), K370 (≠ R388)
- binding flavin-adenine dinucleotide: L122 (= L138), T123 (= T139), G128 (= G144), S129 (= S145), F153 (≠ W169), T155 (= T171), R265 (= R281), Q267 (= Q283), F268 (= F284), I272 (≠ L288), N275 (= N291), I278 (= I294), Q331 (vs. gap), I332 (≠ M350), G335 (= G353), Y357 (= Y375), T360 (= T378), E362 (≠ D380)
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
37% identity, 93% coverage: 18:388/398 of query aligns to 1:366/370 of 2dvlA
- active site: L121 (= L138), T122 (= T139), G233 (≠ A255), E354 (= E376), R366 (= R388)
- binding flavin-adenine dinucleotide: L121 (= L138), T122 (= T139), G127 (= G144), S128 (= S145), W152 (= W169), I153 (= I170), T154 (= T171), T356 (= T378), E358 (≠ D380)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
35% identity, 94% coverage: 14:388/398 of query aligns to 2:376/378 of 4n5fA
- active site: L126 (= L138), T127 (= T139), G243 (≠ A255), E364 (= E376), R376 (= R388)
- binding dihydroflavine-adenine dinucleotide: L126 (= L138), T127 (= T139), G132 (= G144), S133 (= S145), F157 (≠ W169), T159 (= T171), T210 (= T223), Y363 (= Y375), T366 (= T378), E368 (≠ D380), M372 (≠ L384)
P26440 Isovaleryl-CoA dehydrogenase, mitochondrial; IVD; Butyryl-CoA dehydrogenase; EC 1.3.8.4; EC 1.3.8.1 from Homo sapiens (Human) (see 5 papers)
33% identity, 97% coverage: 2:389/398 of query aligns to 32:420/426 of P26440
- 165:174 (vs. 136:145, 40% identical) binding
- S174 (= S145) binding
- WIT 198:200 (= WIT 169:171) binding
- SR 222:223 (≠ IR 195:196) binding
- G250 (≠ A220) to A: in IVA; uncertain significance
- Y277 (≠ K246) binding
- DLER 284:287 (≠ NSAR 253:256) binding
- E286 (≠ A255) active site, Proton acceptor; mutation to D: Residual isovaleryl-CoA dehydrogenase activity.; mutation to G: Loss of isovaleryl-CoA dehydrogenase activity. Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 407-E.; mutation to Q: Loss of isovaleryl-CoA dehydrogenase activity.
- A291 (= A260) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R281) binding
- Q323 (= Q292) binding
- I379 (≠ R348) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ DMMGG 349:353) binding
- R398 (≠ V367) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ V372) to N: in IVA; uncertain significance
- A407 (≠ E376) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ EG 376:377) binding
- TSE 409:411 (≠ THD 378:380) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
36% identity, 94% coverage: 14:389/398 of query aligns to 1:380/383 of 1bucA
- active site: L128 (= L138), T129 (= T139), G246 (≠ A255), E367 (= E376), G379 (≠ R388)
- binding acetoacetyl-coenzyme a: L96 (= L106), F126 (= F136), G134 (= G144), T135 (≠ S145), T162 (= T171), N182 (≠ A191), H183 (≠ V192), F236 (≠ L245), M240 (≠ F249), M241 (≠ T250), L243 (= L252), D244 (≠ N253), T317 (≠ V326), Y366 (= Y375), E367 (= E376), G368 (= G377)
- binding flavin-adenine dinucleotide: F126 (= F136), L128 (= L138), T129 (= T139), G134 (= G144), T135 (≠ S145), F160 (≠ W169), T162 (= T171), Y366 (= Y375), T369 (= T378), E371 (≠ D380), M375 (≠ L384)
Q06319 Acyl-CoA dehydrogenase, short-chain specific; Butyryl-CoA dehydrogenase; BCAD; SCAD; EC 1.3.8.1 from Megasphaera elsdenii (see paper)
36% identity, 94% coverage: 14:389/398 of query aligns to 1:380/383 of Q06319
- E367 (= E376) active site, Proton acceptor; mutation to Q: Loss of activity.
Query Sequence
>Ac3H11_3533 FitnessBrowser__acidovorax_3H11:Ac3H11_3533
MAHAAFQWDDPFLLNQQLTDDERAIRDAAAAYCQDKLAPRVLDAFRHEKMDVSIFREMGE
VGLLGPTIPEQYGGPGLSYVAYGLIAREVERVDSGYRSMASVQSSLVMVPINEFGTEAQK
QKYLPKLATGEWIGCFGLTEPDHGSDPGSMATRAYKVDGGYKLKGSKMWITNSPVADVFV
VWAKEVSEGGAVGPIRGFVLEKGMKGLTAPAIHGKVGLRASITGEIVMDDVFVPEENAFP
EVQGLKGPFTCLNSARYGIAWGALGAAEFCWHTARQYTLDRKQFGRPLAANQLIQKKLAD
MQTEIAIGLQACLQFGRMKDAGTASVEGTSIIKRNSCGKALDIARLARDMMGGNGISDEF
GVARHLVNLEVVNTYEGTHDVHALILGRAQTGIAAFSN
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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