SitesBLAST
Comparing GFF1026 FitnessBrowser__Marino:GFF1026 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)
4ktoA Crystal structure of a putative isovaleryl-coa dehydrogenase (psi- nysgrc-012251) from sinorhizobium meliloti 1021
71% identity, 97% coverage: 8:386/389 of query aligns to 6:375/377 of 4ktoA
- active site: M130 (= M132), S131 (= S133), E239 (= E249), A360 (= A371), R372 (= R383)
- binding flavin-adenine dinucleotide: L128 (= L130), M130 (= M132), S131 (= S133), M155 (= M162), W156 (= W163), T158 (= T165), R265 (= R275), F268 (= F278), I272 (= I282), F275 (= F285), M278 (≠ V288), Q333 (= Q344), A334 (≠ L345), G337 (= G348), L355 (= L366), G359 (= G370), T362 (= T373), E364 (= E375)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
64% identity, 96% coverage: 11:383/389 of query aligns to 7:382/387 of 1ivhA
- active site: M130 (= M132), S131 (= S133), E249 (= E249), A370 (= A371), R382 (= R383)
- binding coenzyme a persulfide: S137 (= S139), S185 (= S185), R186 (= R186), V239 (≠ A239), Y240 (≠ K240), M243 (= M243), E249 (= E249), R250 (= R250), G369 (= G370), A370 (= A371), G371 (= G372), V375 (≠ I376)
- binding flavin-adenine dinucleotide: L128 (= L130), M130 (= M132), S131 (= S133), G136 (= G138), S137 (= S139), W161 (= W163), T163 (= T165), R275 (= R275), F278 (= F278), F285 (= F285), M288 (≠ V288), Q343 (= Q344), C344 (≠ L345), G347 (= G348), T372 (= T373), E374 (= E375)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
64% identity, 96% coverage: 11:383/389 of query aligns to 11:386/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (= S133), G140 (= G138), S141 (= S139), W165 (= W163), T167 (= T165), R279 (= R275), F282 (= F278), I286 (= I282), F289 (= F285), Q347 (= Q344), C348 (≠ L345), G351 (= G348), L369 (= L366), G375 (= G372), T376 (= T373), L382 (≠ M379)
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)
64% identity, 96% coverage: 11:383/389 of query aligns to 44:419/426 of P26440
- 165:174 (vs. 130:139, 100% identical) binding
- S174 (= S139) binding
- WIT 198:200 (= WIT 163:165) binding
- SR 222:223 (= SR 185:186) binding
- G250 (= G213) to A: in IVA; uncertain significance
- Y277 (≠ K240) binding
- DLER 284:287 (≠ DYER 247:250) binding
- E286 (= E249) 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 (≠ S254) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R275) binding
- Q323 (≠ E286) binding
- I379 (= I343) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QLLGG 344:348) binding
- R398 (= R362) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (= Y367) to N: in IVA; uncertain significance
- A407 (= A371) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (= AG 371:372) binding
- TSE 409:411 (= TSE 373:375) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
43% identity, 95% coverage: 18:385/389 of query aligns to 10:376/378 of 5ol2F
- active site: L124 (≠ M132), T125 (≠ S133), G241 (≠ E249), G374 (≠ R383)
- binding calcium ion: E29 (= E37), E33 (≠ N41), R35 (≠ E43)
- binding coenzyme a persulfide: L238 (= L246), R242 (= R250), E362 (≠ A371), G363 (= G372)
- binding flavin-adenine dinucleotide: F122 (≠ L130), L124 (≠ M132), T125 (≠ S133), P127 (= P135), T131 (≠ S139), F155 (≠ W163), I156 (= I164), T157 (= T165), E198 (≠ L206), R267 (= R275), F270 (= F278), L274 (≠ I282), F277 (= F285), Q335 (= Q344), L336 (= L345), G338 (= G347), G339 (= G348), Y361 (≠ G370), T364 (= T373), E366 (= E375)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
43% identity, 95% coverage: 18:385/389 of query aligns to 8:372/374 of 5lnxD
- active site: L122 (≠ M132), T123 (≠ S133), G239 (≠ E249), E358 (≠ A371), K370 (≠ R383)
- binding flavin-adenine dinucleotide: L122 (≠ M132), T123 (≠ S133), G128 (= G138), S129 (= S139), F153 (≠ W163), T155 (= T165), R265 (= R275), Q267 (= Q277), F268 (= F278), I272 (= I282), N275 (≠ F285), I278 (≠ V288), Q331 (= Q344), I332 (≠ L345), G335 (= G348), Y357 (≠ G370), T360 (= T373), E362 (= E375)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
40% identity, 97% coverage: 8:385/389 of query aligns to 1:377/380 of 4l1fA
- active site: L125 (≠ M132), T126 (≠ S133), G242 (≠ E249), E363 (≠ A371), R375 (= R383)
- binding coenzyme a persulfide: T132 (≠ S139), H179 (≠ R186), F232 (≠ A239), M236 (= M243), E237 (≠ S244), L239 (= L246), D240 (= D247), R243 (= R250), Y362 (≠ G370), E363 (≠ A371), G364 (= G372), R375 (= R383)
- binding flavin-adenine dinucleotide: F123 (≠ L130), L125 (≠ M132), T126 (≠ S133), G131 (= G138), T132 (≠ S139), F156 (≠ W163), I157 (= I164), T158 (= T165), R268 (= R275), Q270 (= Q277), F271 (= F278), I275 (= I282), F278 (= F285), L281 (≠ V288), Q336 (= Q344), I337 (≠ L345), G340 (= G348), I358 (≠ L366), Y362 (≠ G370), T365 (= T373), Q367 (≠ E375)
- binding 1,3-propandiol: L5 (= L12), Q10 (≠ D17)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
42% identity, 96% coverage: 12:385/389 of query aligns to 7:379/384 of 1jqiA
- active site: G377 (≠ R383)
- binding acetoacetyl-coenzyme a: L95 (= L100), F125 (≠ L130), S134 (= S139), F234 (≠ A239), M238 (= M243), Q239 (≠ S244), L241 (= L246), D242 (= D247), R245 (= R250), Y364 (≠ G370), E365 (≠ A371), G366 (= G372)
- binding flavin-adenine dinucleotide: F125 (≠ L130), L127 (≠ M132), S128 (= S133), G133 (= G138), S134 (= S139), W158 (= W163), T160 (= T165), R270 (= R275), F273 (= F278), L280 (≠ F285), Q338 (= Q344), I339 (≠ L345), G342 (= G348), I360 (≠ L366), T367 (= T373), E369 (= E375), I370 (= I376)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
42% identity, 96% coverage: 12:385/389 of query aligns to 34:406/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
42% identity, 96% coverage: 12:385/389 of query aligns to 4:376/381 of 8sgsA
- binding coenzyme a: S131 (= S139), A133 (≠ V141), N177 (≠ S185), F231 (≠ A239), M235 (= M243), L238 (= L246), I312 (≠ R321), E362 (≠ A371), G363 (= G372)
- binding flavin-adenine dinucleotide: F122 (≠ L130), L124 (≠ M132), S125 (= S133), G130 (= G138), S131 (= S139), W155 (= W163), T157 (= T165), R267 (= R275), F270 (= F278), L274 (≠ I282), L277 (≠ F285), Q335 (= Q344), I336 (≠ L345), G338 (= G347), G339 (= G348), I357 (≠ L366), I360 (= I369), Y361 (≠ G370), T364 (= T373), E366 (= E375)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
42% identity, 96% coverage: 12:385/389 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 (≠ N349), T347 (≠ N353), E348 (= E354)
- binding flavin-adenine dinucleotide: F125 (≠ L130), L127 (≠ M132), S128 (= S133), G133 (= G138), S134 (= S139), W158 (= W163), T160 (= T165), R270 (= R275), F273 (= F278), L280 (≠ F285), V282 (≠ L287), Q338 (= Q344), I339 (≠ L345), G342 (= G348), I360 (≠ L366), Y364 (≠ G370), T367 (= T373), E369 (= E375), I370 (= I376), L373 (≠ M379)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
42% identity, 96% coverage: 12:385/389 of query aligns to 10:382/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ L130), L130 (≠ M132), S131 (= S133), G136 (= G138), S137 (= S139), W161 (= W163), T163 (= T165), T214 (= T216), R273 (= R275), F276 (= F278), L280 (≠ I282), L283 (≠ F285), V285 (≠ L287), Q341 (= Q344), I342 (≠ L345), G345 (= G348), I363 (≠ L366), Y367 (≠ G370), T370 (= T373), E372 (= E375), L376 (≠ M379)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
42% identity, 96% coverage: 12:385/389 of query aligns to 34:406/412 of P16219
- G90 (= G68) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E82) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 130:139, 60% identical) binding in other chain
- R171 (≠ K149) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (= WIT 163:165) binding in other chain
- A192 (= A170) 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 (= R275) binding
- Q308 (≠ E286) binding in other chain
- R325 (≠ K303) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ A332) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QLLGG 344:348) binding
- R380 (= R359) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (= TSE 373:375) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
41% identity, 96% coverage: 12:385/389 of query aligns to 1:366/371 of 2vigB
- active site: L121 (≠ M132), S122 (= S133), G231 (≠ E249), E352 (≠ A371), G364 (≠ R383)
- binding coenzyme a persulfide: S128 (= S139), F221 (≠ A239), M225 (= M243), Q226 (≠ S244), L228 (= L246), D229 (= D247), R232 (= R250), E352 (≠ A371), G353 (= G372), I357 (= I376)
- binding flavin-adenine dinucleotide: L121 (≠ M132), S122 (= S133), G127 (= G138), S128 (= S139), W152 (= W163), T154 (= T165), R257 (= R275), F260 (= F278), L264 (≠ I282), L267 (≠ F285), Q325 (= Q344), I326 (≠ L345), G329 (= G348), I347 (≠ L366), Y351 (≠ G370), T354 (= T373), E356 (= E375)
3mpiC Structure of the glutaryl-coenzyme a dehydrogenase glutaryl-coa complex (see paper)
40% identity, 96% coverage: 8:381/389 of query aligns to 1:377/395 of 3mpiC
- active site: I128 (≠ M132), T129 (≠ S133), T245 (≠ E249), E367 (≠ A371)
- binding flavin-adenine dinucleotide: I128 (≠ M132), T129 (≠ S133), G134 (= G138), S135 (= S139), W159 (= W163), I160 (= I164), S161 (≠ T165), M365 (≠ I369), V366 (≠ G370), S369 (≠ T373), N371 (≠ E375), M375 (= M379)
- binding glutaryl-coenzyme A: R87 (≠ G91), F126 (≠ L130), S135 (= S139), V137 (= V141), S181 (= S185), F239 (≠ M243), R246 (= R250), N315 (≠ T319), V366 (≠ G370), E367 (≠ A371), G368 (= G372), I376 (≠ L380)
Sites not aligning to the query:
C3UVB0 Glutaryl-CoA dehydrogenase; GDH(Des); EC 1.3.99.32 from Desulfococcus multivorans (see paper)
40% identity, 96% coverage: 8:381/389 of query aligns to 1:377/389 of C3UVB0
- A80 (≠ S84) mutation to E: Loses the FAD cofactor and dehydrogenase activity.
- R87 (≠ G91) binding
- V88 (≠ L92) mutation to S: A residual dehydrogenase activity is observed.
- N91 (≠ G95) binding
- FGIT 126:129 (≠ LAMS 130:133) binding
- S135 (= S139) binding ; binding
- WIS 159:161 (≠ WIT 163:165) binding
- S181 (= S185) binding
- R271 (= R275) binding
- FQMN 281:284 (≠ FELV 285:288) binding
- R340 (≠ Q344) binding
- A344 (≠ G348) binding
- V366 (≠ G370) mutation to Y: Loses the FAD cofactor but a residual dehydrogenase activity is observed.
- EGSAN 367:371 (≠ AGTSE 371:375) binding
Sites not aligning to the query:
3mpjB Structure of the glutaryl-coenzyme a dehydrogenase (see paper)
40% identity, 96% coverage: 8:381/389 of query aligns to 1:377/393 of 3mpjB
- active site: I128 (≠ M132), T129 (≠ S133), T245 (≠ E249), E367 (≠ A371)
- binding flavin-adenine dinucleotide: F126 (≠ L130), I128 (≠ M132), T129 (≠ S133), G134 (= G138), S135 (= S139), W159 (= W163), I160 (= I164), S161 (≠ T165), V366 (≠ G370), S369 (≠ T373), N371 (≠ E375), M375 (= M379)
- binding : H36 (≠ E43), F37 (= F44), Y39 (≠ M46), A164 (≠ P168), Q165 (≠ D169), D167 (≠ N171), N193 (≠ D196)
Sites not aligning to the query:
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
39% identity, 97% coverage: 8:385/389 of query aligns to 1:376/379 of 1ukwB
- active site: L124 (≠ M132), S125 (= S133), T241 (≠ E249), E362 (≠ A371), R374 (= R383)
- binding cobalt (ii) ion: D145 (= D153), H146 (= H154)
- binding flavin-adenine dinucleotide: F122 (≠ L130), L124 (≠ M132), S125 (= S133), G130 (= G138), S131 (= S139), W155 (= W163), S157 (≠ T165), K200 (= K208), L357 (= L366), Y361 (≠ G370), E362 (≠ A371), T364 (= T373), E366 (= E375), L370 (≠ M379)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
39% identity, 97% coverage: 8:385/389 of query aligns to 1:376/379 of 1ukwA
- active site: L124 (≠ M132), S125 (= S133), T241 (≠ E249), E362 (≠ A371), R374 (= R383)
- binding flavin-adenine dinucleotide: F122 (≠ L130), L124 (≠ M132), S125 (= S133), G130 (= G138), S131 (= S139), W155 (= W163), S157 (≠ T165), L357 (= L366), Y361 (≠ G370), E362 (≠ A371), T364 (= T373), E366 (= E375), L370 (≠ M379)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
39% identity, 95% coverage: 12:381/389 of query aligns to 3:372/379 of 6fahD
- active site: L124 (≠ M132), T125 (≠ S133), G241 (≠ E249)
- binding flavin-adenine dinucleotide: F122 (≠ L130), L124 (≠ M132), T125 (≠ S133), R152 (≠ N160), F155 (≠ W163), T157 (= T165), E198 (≠ L206), R267 (= R275), Q269 (= Q277), F270 (= F278), I274 (= I282), F277 (= F285), Q335 (= Q344), I336 (≠ L345), G339 (= G348), Y361 (≠ G370), T364 (= T373), Q366 (≠ E375)
Sites not aligning to the query:
Query Sequence
>GFF1026 FitnessBrowser__Marino:GFF1026
MKSQYSELNFGLGETLDMLREQINGFAASEIAPRAEEIDRNNEFPMDLWRKMGDMGLLGI
TVSEEYGGSDMGYLAHVIAMEEISRASASVGLSYGAHSNLCVNQIHRNGTEEQKQKYLPK
LVSGEHIGALAMSEPNAGSDVISMKLTAKDEGDHYLLNGNKMWITNGPDANTYVIYAKTD
TSAGSRGVTAFIVERDAPGFSRHQKLDKLGMRGSNTCELVFQDCKVPKENVLGGVGNGAK
VLMSGLDYERLVLSGGPLGIMQAAMDVVVPYIRERKQFGQAIGEFELVQGKVADMYTWMN
TAKSYVYMVAMSADRGAETTRKDAAGAILYSAEMATKIALDAIQLLGGNGYINEYPTGRL
LRDAKLYEIGAGTSEIRRMLIGRELYLNK
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