SitesBLAST
Comparing AZOBR_RS22310 FitnessBrowser__azobra:AZOBR_RS22310 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
79% identity, 97% coverage: 9:388/390 of query aligns to 6:377/377 of 4ktoA
- active site: M130 (= M133), S131 (= S134), E239 (= E250), A360 (= A371), R372 (= R383)
- binding flavin-adenine dinucleotide: L128 (= L131), M130 (= M133), S131 (= S134), M155 (= M163), W156 (= W164), T158 (= T166), R265 (= R276), F268 (= F279), I272 (= I283), F275 (= F286), M278 (= M289), Q333 (= Q344), A334 (≠ T345), G337 (= G348), L355 (= L366), G359 (= G370), T362 (= T373), E364 (= E375)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
68% identity, 95% coverage: 13:383/390 of query aligns to 12:386/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (= S134), G140 (= G139), S141 (= S140), W165 (= W164), T167 (= T166), R279 (= R276), F282 (= F279), I286 (= I283), F289 (= F286), Q347 (= Q344), C348 (≠ T345), G351 (= G348), L369 (= L366), G375 (= G372), T376 (= T373), L382 (≠ M379)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
68% identity, 95% coverage: 13:383/390 of query aligns to 8:382/387 of 1ivhA
- active site: M130 (= M133), S131 (= S134), E249 (= E250), A370 (= A371), R382 (= R383)
- binding coenzyme a persulfide: S137 (= S140), S185 (vs. gap), R186 (= R187), V239 (= V240), Y240 (≠ N241), M243 (= M244), E249 (= E250), R250 (= R251), G369 (= G370), A370 (= A371), G371 (= G372), V375 (≠ I376)
- binding flavin-adenine dinucleotide: L128 (= L131), M130 (= M133), S131 (= S134), G136 (= G139), S137 (= S140), W161 (= W164), T163 (= T166), R275 (= R276), F278 (= F279), F285 (= F286), M288 (= M289), Q343 (= Q344), C344 (≠ T345), G347 (= G348), T372 (= T373), E374 (= E375)
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)
68% identity, 95% coverage: 13:383/390 of query aligns to 45:419/426 of P26440
- 165:174 (vs. 131:140, 100% identical) binding
- S174 (= S140) binding
- WIT 198:200 (= WIT 164:166) binding
- SR 222:223 (≠ -R 187) binding
- G250 (= G214) to A: in IVA; uncertain significance
- Y277 (≠ N241) binding
- DLER 284:287 (≠ DYER 248:251) binding
- E286 (= E250) 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 (= A255) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R276) binding
- Q323 (= Q287) binding
- I379 (= I343) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QTLGG 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
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
44% identity, 94% coverage: 19:386/390 of query aligns to 8:373/374 of 5lnxD
- active site: L122 (≠ M133), T123 (≠ S134), G239 (≠ E250), E358 (≠ A371), K370 (≠ R383)
- binding flavin-adenine dinucleotide: L122 (≠ M133), T123 (≠ S134), G128 (= G139), S129 (= S140), F153 (≠ W164), T155 (= T166), R265 (= R276), Q267 (= Q278), F268 (= F279), I272 (= I283), N275 (≠ F286), I278 (≠ M289), Q331 (= Q344), I332 (≠ T345), G335 (= G348), Y357 (≠ G370), T360 (= T373), E362 (= E375)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
42% identity, 97% coverage: 10:387/390 of query aligns to 4:381/384 of 1jqiA
- active site: G377 (≠ R383)
- binding acetoacetyl-coenzyme a: L95 (= L101), F125 (≠ L131), S134 (= S140), F234 (≠ V240), M238 (= M244), Q239 (≠ S245), L241 (= L247), D242 (= D248), R245 (= R251), Y364 (≠ G370), E365 (≠ A371), G366 (= G372)
- binding flavin-adenine dinucleotide: F125 (≠ L131), L127 (≠ M133), S128 (= S134), G133 (= G139), S134 (= S140), W158 (= W164), T160 (= T166), R270 (= R276), F273 (= F279), L280 (≠ F286), Q338 (= Q344), I339 (≠ T345), 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, 97% coverage: 10:387/390 of query aligns to 31:408/412 of P15651
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)
43% identity, 95% coverage: 19:387/390 of query aligns to 10:378/378 of 5ol2F
- active site: L124 (≠ M133), T125 (≠ S134), G241 (≠ E250), G374 (≠ R383)
- binding calcium ion: E29 (= E38), E33 (≠ T42), R35 (≠ E44)
- binding coenzyme a persulfide: L238 (= L247), R242 (= R251), E362 (≠ A371), G363 (= G372)
- binding flavin-adenine dinucleotide: F122 (≠ L131), L124 (≠ M133), T125 (≠ S134), P127 (= P136), T131 (≠ S140), F155 (≠ W164), I156 (= I165), T157 (= T166), E198 (≠ L207), R267 (= R276), F270 (= F279), L274 (≠ I283), F277 (= F286), Q335 (= Q344), L336 (≠ T345), G338 (= G347), G339 (= G348), Y361 (≠ G370), T364 (= T373), E366 (= E375)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
42% identity, 97% coverage: 10:387/390 of query aligns to 4:381/385 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 (≠ L131), L127 (≠ M133), S128 (= S134), G133 (= G139), S134 (= S140), W158 (= W164), T160 (= T166), R270 (= R276), F273 (= F279), L280 (≠ F286), V282 (≠ L288), Q338 (= Q344), I339 (≠ T345), 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, 97% coverage: 10:387/390 of query aligns to 7:384/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ L131), L130 (≠ M133), S131 (= S134), G136 (= G139), S137 (= S140), W161 (= W164), T163 (= T166), T214 (= T217), R273 (= R276), F276 (= F279), L280 (≠ I283), L283 (≠ F286), V285 (≠ L288), Q341 (= Q344), I342 (≠ T345), 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, 97% coverage: 10:387/390 of query aligns to 31:408/412 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. 131:140, 60% identical) binding in other chain
- R171 (≠ E150) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (= WIT 164:166) binding in other chain
- A192 (= A171) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G188) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R276) binding
- Q308 (= Q287) binding in other chain
- R325 (≠ K304) 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 (≠ QTLGG 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
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
42% identity, 97% coverage: 10:387/390 of query aligns to 1:378/381 of 8sgsA
- binding coenzyme a: S131 (= S140), A133 (≠ V142), N177 (≠ P186), F231 (≠ V240), M235 (= M244), L238 (= L247), I312 (≠ R321), E362 (≠ A371), G363 (= G372)
- binding flavin-adenine dinucleotide: F122 (≠ L131), L124 (≠ M133), S125 (= S134), G130 (= G139), S131 (= S140), W155 (= W164), T157 (= T166), R267 (= R276), F270 (= F279), L274 (≠ I283), L277 (≠ F286), Q335 (= Q344), I336 (≠ T345), G338 (= G347), G339 (= G348), I357 (≠ L366), I360 (= I369), Y361 (≠ G370), T364 (= T373), E366 (= E375)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
39% identity, 97% coverage: 9:388/390 of query aligns to 1:380/380 of 4l1fA
- active site: L125 (≠ M133), T126 (≠ S134), G242 (≠ E250), E363 (≠ A371), R375 (= R383)
- binding coenzyme a persulfide: T132 (≠ S140), H179 (≠ R187), F232 (≠ V240), M236 (= M244), E237 (≠ S245), L239 (= L247), D240 (= D248), R243 (= R251), Y362 (≠ G370), E363 (≠ A371), G364 (= G372), R375 (= R383)
- binding flavin-adenine dinucleotide: F123 (≠ L131), L125 (≠ M133), T126 (≠ S134), G131 (= G139), T132 (≠ S140), F156 (≠ W164), I157 (= I165), T158 (= T166), R268 (= R276), Q270 (= Q278), F271 (= F279), I275 (= I283), F278 (= F286), L281 (≠ M289), Q336 (= Q344), I337 (≠ T345), G340 (= G348), I358 (≠ L366), Y362 (≠ G370), T365 (= T373), Q367 (≠ E375)
- binding 1,3-propandiol: L5 (= L13), Q10 (≠ D18)
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
42% identity, 96% coverage: 13:387/390 of query aligns to 1:368/371 of 2vigB
- active site: L121 (≠ M133), S122 (= S134), G231 (≠ E250), E352 (≠ A371), G364 (≠ R383)
- binding coenzyme a persulfide: S128 (= S140), F221 (≠ V240), M225 (= M244), Q226 (≠ S245), L228 (= L247), D229 (= D248), R232 (= R251), E352 (≠ A371), G353 (= G372), I357 (= I376)
- binding flavin-adenine dinucleotide: L121 (≠ M133), S122 (= S134), G127 (= G139), S128 (= S140), W152 (= W164), T154 (= T166), R257 (= R276), F260 (= F279), L264 (≠ I283), L267 (≠ F286), Q325 (= Q344), I326 (≠ T345), G329 (= G348), I347 (≠ L366), Y351 (≠ G370), T354 (= T373), E356 (= E375)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
39% identity, 95% coverage: 15:385/390 of query aligns to 8:378/378 of 4n5fA
- active site: L126 (≠ M133), T127 (≠ S134), G243 (≠ E250), E364 (≠ A371), R376 (= R383)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ M133), T127 (≠ S134), G132 (= G139), S133 (= S140), F157 (≠ W164), T159 (= T166), T210 (= T217), Y363 (≠ G370), T366 (= T373), E368 (= E375), M372 (= M379)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
39% identity, 97% coverage: 9:386/390 of query aligns to 1:377/379 of 1ukwB
- active site: L124 (≠ M133), S125 (= S134), T241 (≠ E250), E362 (≠ A371), R374 (= R383)
- binding cobalt (ii) ion: D145 (= D154), H146 (≠ R155)
- binding flavin-adenine dinucleotide: F122 (≠ L131), L124 (≠ M133), S125 (= S134), G130 (= G139), S131 (= S140), W155 (= W164), S157 (≠ T166), K200 (= K209), 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: 9:386/390 of query aligns to 1:377/379 of 1ukwA
- active site: L124 (≠ M133), S125 (= S134), T241 (≠ E250), E362 (≠ A371), R374 (= R383)
- binding flavin-adenine dinucleotide: F122 (≠ L131), L124 (≠ M133), S125 (= S134), G130 (= G139), S131 (= S140), W155 (= W164), S157 (≠ T166), L357 (= L366), Y361 (≠ G370), E362 (≠ A371), T364 (= T373), E366 (= E375), L370 (≠ M379)
C3UVB0 Glutaryl-CoA dehydrogenase; GDH(Des); EC 1.3.99.32 from Desulfococcus multivorans (see paper)
40% identity, 96% coverage: 9:381/390 of query aligns to 1:377/389 of C3UVB0
- A80 (≠ S85) mutation to E: Loses the FAD cofactor and dehydrogenase activity.
- R87 (≠ G92) binding
- V88 (≠ L93) mutation to S: A residual dehydrogenase activity is observed.
- N91 (≠ G96) binding
- FGIT 126:129 (≠ LAMS 131:134) binding
- S135 (= S140) binding ; binding
- WIS 159:161 (≠ WIT 164:166) binding
- S181 (≠ P186) binding
- R271 (= R276) binding
- FQMN 281:284 (≠ FQLM 286:289) 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:
3mpiC Structure of the glutaryl-coenzyme a dehydrogenase glutaryl-coa complex (see paper)
40% identity, 96% coverage: 9:381/390 of query aligns to 1:377/395 of 3mpiC
- active site: I128 (≠ M133), T129 (≠ S134), T245 (≠ E250), E367 (≠ A371)
- binding flavin-adenine dinucleotide: I128 (≠ M133), T129 (≠ S134), G134 (= G139), S135 (= S140), W159 (= W164), I160 (= I165), S161 (≠ T166), M365 (≠ I369), V366 (≠ G370), S369 (≠ T373), N371 (≠ E375), M375 (= M379)
- binding glutaryl-coenzyme A: R87 (≠ G92), F126 (≠ L131), S135 (= S140), V137 (= V142), S181 (≠ P186), F239 (≠ M244), R246 (= R251), N315 (≠ A320), V366 (≠ G370), E367 (≠ A371), G368 (= G372), I376 (≠ L380)
Sites not aligning to the query:
3mpjB Structure of the glutaryl-coenzyme a dehydrogenase (see paper)
40% identity, 96% coverage: 9:381/390 of query aligns to 1:377/393 of 3mpjB
- active site: I128 (≠ M133), T129 (≠ S134), T245 (≠ E250), E367 (≠ A371)
- binding flavin-adenine dinucleotide: F126 (≠ L131), I128 (≠ M133), T129 (≠ S134), G134 (= G139), S135 (= S140), W159 (= W164), I160 (= I165), S161 (≠ T166), V366 (≠ G370), S369 (≠ T373), N371 (≠ E375), M375 (= M379)
- binding : H36 (≠ E44), F37 (= F45), Y39 (vs. gap), A164 (≠ P169), Q165 (≠ D170), D167 (= D172), N193 (≠ S197)
Sites not aligning to the query:
Query Sequence
>AZOBR_RS22310 FitnessBrowser__azobra:AZOBR_RS22310
MLSNQYPTLNFDLGESADMLRDTVRSFAADEIAPRAAEIDRTNEFPNELWRKFGDLGVLG
ITAEEEYGGAGMGYLEHVVAMEEISRASASVGLSYGAHSNLCVNQIRKNGTAEQKTRYLP
KLISGEHIGALAMSEPNAGSDVVSMKLRAEKQGDRYVLNGTKMWITNGPDADTLVVYAKT
DVNAGPRGITAFLIEKSFKGFSVAQKLDKLGMRGSNTGELVFEDCEVPEENILGGVGRGV
NVLMSGLDYERAVLAGGPLGIMQACMDVVVPYLHDRKQFGQPIGEFQLMQGKLADMYTIM
NAAKAYVYAVAKACDRGETARKDAAGAILFAAEKATWMALEAIQTLGGNGYINEYPTGRL
LRDAKLYEIGAGTSEIRRMLIGRELFKETA
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