SitesBLAST
Comparing BPHYT_RS23260 FitnessBrowser__BFirm:BPHYT_RS23260 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
70% identity, 98% coverage: 6:391/393 of query aligns to 5:377/377 of 4ktoA
- active site: M130 (= M131), S131 (= S132), E239 (= E248), A360 (= A374), R372 (= R386)
- binding flavin-adenine dinucleotide: L128 (= L129), M130 (= M131), S131 (= S132), M155 (= M161), W156 (= W162), T158 (= T164), R265 (= R274), F268 (= F277), I272 (= I281), F275 (= F284), M278 (≠ I287), Q333 (= Q347), A334 (≠ I348), G337 (= G351), L355 (= L369), G359 (= G373), T362 (= T376), E364 (= E378)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
64% identity, 97% coverage: 11:391/393 of query aligns to 8:387/387 of 1ivhA
- active site: M130 (= M131), S131 (= S132), E249 (= E248), A370 (= A374), R382 (= R386)
- binding coenzyme a persulfide: S137 (= S138), S185 (= S184), R186 (= R185), V239 (≠ A238), Y240 (≠ K239), M243 (= M242), E249 (= E248), R250 (= R249), G369 (= G373), A370 (= A374), G371 (= G375), V375 (≠ I379)
- binding flavin-adenine dinucleotide: L128 (= L129), M130 (= M131), S131 (= S132), G136 (= G137), S137 (= S138), W161 (= W162), T163 (= T164), R275 (= R274), F278 (= F277), F285 (= F284), M288 (≠ I287), Q343 (= Q347), C344 (≠ I348), G347 (= G351), T372 (= T376), E374 (= E378)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
64% identity, 97% coverage: 11:391/393 of query aligns to 12:391/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (= S132), G140 (= G137), S141 (= S138), W165 (= W162), T167 (= T164), R279 (= R274), F282 (= F277), I286 (= I281), F289 (= F284), Q347 (= Q347), C348 (≠ I348), G351 (= G351), L369 (= L369), G375 (= G375), T376 (= T376), L382 (≠ M382)
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, 97% coverage: 11:391/393 of query aligns to 45:424/426 of P26440
- 165:174 (vs. 129:138, 100% identical) binding
- S174 (= S138) binding
- WIT 198:200 (= WIT 162:164) binding
- SR 222:223 (= SR 184:185) binding
- G250 (= G212) to A: in IVA; uncertain significance
- Y277 (≠ K239) binding
- DLER 284:287 (≠ DYER 246:249) binding
- E286 (= E248) 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 (= A253) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R274) binding
- Q323 (= Q285) binding
- I379 (= I346) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QILGG 347:351) binding
- R398 (= R365) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (= Y370) to N: in IVA; uncertain significance
- A407 (= A374) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (= AG 374:375) binding
- TSE 409:411 (= TSE 376:378) 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.
42% identity, 96% coverage: 13:389/393 of query aligns to 4:373/374 of 5lnxD
- active site: L122 (≠ M131), T123 (≠ S132), G239 (≠ E248), E358 (≠ A374), K370 (≠ R386)
- binding flavin-adenine dinucleotide: L122 (≠ M131), T123 (≠ S132), G128 (= G137), S129 (= S138), F153 (≠ W162), T155 (= T164), R265 (= R274), Q267 (= Q276), F268 (= F277), I272 (= I281), N275 (≠ F284), I278 (= I287), Q331 (= Q347), I332 (= I348), G335 (= G351), Y357 (≠ G373), T360 (= T376), E362 (= E378)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
39% identity, 96% coverage: 11:389/393 of query aligns to 7:380/384 of 1jqiA
- active site: G377 (≠ R386)
- binding acetoacetyl-coenzyme a: L95 (= L99), F125 (≠ L129), S134 (= S138), F234 (≠ A238), M238 (= M242), Q239 (≠ S243), L241 (= L245), D242 (= D246), R245 (= R249), Y364 (≠ G373), E365 (≠ A374), G366 (= G375)
- binding flavin-adenine dinucleotide: F125 (≠ L129), L127 (≠ M131), S128 (= S132), G133 (= G137), S134 (= S138), W158 (= W162), T160 (= T164), R270 (= R274), F273 (= F277), L280 (≠ F284), Q338 (= Q347), I339 (= I348), G342 (= G351), I360 (≠ L369), T367 (= T376), E369 (= E378), I370 (= I379)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
39% identity, 96% coverage: 11:389/393 of query aligns to 34:407/412 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)
40% identity, 95% coverage: 16:389/393 of query aligns to 9:377/378 of 5ol2F
- active site: L124 (≠ M131), T125 (≠ S132), G241 (≠ E248), G374 (≠ R386)
- binding calcium ion: E29 (= E36), E33 (≠ T40), R35 (≠ Q42)
- binding coenzyme a persulfide: L238 (= L245), R242 (= R249), E362 (≠ A374), G363 (= G375)
- binding flavin-adenine dinucleotide: F122 (≠ L129), L124 (≠ M131), T125 (≠ S132), P127 (= P134), T131 (≠ S138), F155 (≠ W162), I156 (= I163), T157 (= T164), E198 (≠ L205), R267 (= R274), F270 (= F277), L274 (≠ I281), F277 (= F284), Q335 (= Q347), L336 (≠ I348), G338 (= G350), G339 (= G351), Y361 (≠ G373), T364 (= T376), E366 (= E378)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
39% identity, 97% coverage: 7:389/393 of query aligns to 1:378/380 of 4l1fA
- active site: L125 (≠ M131), T126 (≠ S132), G242 (≠ E248), E363 (≠ A374), R375 (= R386)
- binding coenzyme a persulfide: T132 (≠ S138), H179 (≠ R185), F232 (≠ A238), M236 (= M242), E237 (≠ S243), L239 (= L245), D240 (= D246), R243 (= R249), Y362 (≠ G373), E363 (≠ A374), G364 (= G375), R375 (= R386)
- binding flavin-adenine dinucleotide: F123 (≠ L129), L125 (≠ M131), T126 (≠ S132), G131 (= G137), T132 (≠ S138), F156 (≠ W162), I157 (= I163), T158 (= T164), R268 (= R274), Q270 (= Q276), F271 (= F277), I275 (= I281), F278 (= F284), L281 (≠ I287), Q336 (= Q347), I337 (= I348), G340 (= G351), I358 (≠ L369), Y362 (≠ G373), T365 (= T376), Q367 (≠ E378)
- binding 1,3-propandiol: L5 (= L11), Q10 (≠ E16)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
40% identity, 96% coverage: 11:389/393 of query aligns to 34:407/412 of P16219
- G90 (= G67) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E81) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 129:138, 60% identical) binding in other chain
- R171 (≠ E148) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (= WIT 162:164) binding in other chain
- A192 (≠ C169) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G186) 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 (= R302) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ A335) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (= QILGG 347:351) binding
- R380 (= R362) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (= TSE 376:378) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
40% identity, 96% coverage: 11:389/393 of query aligns to 7:380/385 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 (≠ N352), T347 (≠ N356), E348 (= E357)
- binding flavin-adenine dinucleotide: F125 (≠ L129), L127 (≠ M131), S128 (= S132), G133 (= G137), S134 (= S138), W158 (= W162), T160 (= T164), R270 (= R274), F273 (= F277), L280 (≠ F284), V282 (≠ L286), Q338 (= Q347), I339 (= I348), G342 (= G351), I360 (≠ L369), Y364 (≠ G373), T367 (= T376), E369 (= E378), I370 (= I379), L373 (≠ M382)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
40% identity, 96% coverage: 11:389/393 of query aligns to 4:377/381 of 8sgsA
- binding coenzyme a: S131 (= S138), A133 (≠ V140), N177 (≠ S184), F231 (≠ A238), M235 (= M242), L238 (= L245), I312 (≠ R324), E362 (≠ A374), G363 (= G375)
- binding flavin-adenine dinucleotide: F122 (≠ L129), L124 (≠ M131), S125 (= S132), G130 (= G137), S131 (= S138), W155 (= W162), T157 (= T164), R267 (= R274), F270 (= F277), L274 (≠ I281), L277 (≠ F284), Q335 (= Q347), I336 (= I348), G338 (= G350), G339 (= G351), I357 (≠ L369), I360 (= I372), Y361 (≠ G373), T364 (= T376), E366 (= E378)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
40% identity, 96% coverage: 11:389/393 of query aligns to 10:383/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ L129), L130 (≠ M131), S131 (= S132), G136 (= G137), S137 (= S138), W161 (= W162), T163 (= T164), T214 (= T215), R273 (= R274), F276 (= F277), L280 (≠ I281), L283 (≠ F284), V285 (≠ L286), Q341 (= Q347), I342 (= I348), G345 (= G351), I363 (≠ L369), Y367 (≠ G373), T370 (= T376), E372 (= E378), L376 (≠ M382)
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
39% identity, 96% coverage: 11:389/393 of query aligns to 1:367/371 of 2vigB
- active site: L121 (≠ M131), S122 (= S132), G231 (≠ E248), E352 (≠ A374), G364 (≠ R386)
- binding coenzyme a persulfide: S128 (= S138), F221 (≠ A238), M225 (= M242), Q226 (≠ S243), L228 (= L245), D229 (= D246), R232 (= R249), E352 (≠ A374), G353 (= G375), I357 (= I379)
- binding flavin-adenine dinucleotide: L121 (≠ M131), S122 (= S132), G127 (= G137), S128 (= S138), W152 (= W162), T154 (= T164), R257 (= R274), F260 (= F277), L264 (≠ I281), L267 (≠ F284), Q325 (= Q347), I326 (= I348), G329 (= G351), I347 (≠ L369), Y351 (≠ G373), T354 (= T376), E356 (= E378)
C3UVB0 Glutaryl-CoA dehydrogenase; GDH(Des); EC 1.3.99.32 from Desulfococcus multivorans (see paper)
39% identity, 96% coverage: 7:384/393 of query aligns to 1:377/389 of C3UVB0
- A80 (≠ S83) mutation to E: Loses the FAD cofactor and dehydrogenase activity.
- R87 (≠ G90) binding
- V88 (≠ L91) mutation to S: A residual dehydrogenase activity is observed.
- N91 (≠ G94) binding
- FGIT 126:129 (≠ LAMS 129:132) binding
- S135 (= S138) binding ; binding
- WIS 159:161 (≠ WIT 162:164) binding
- S181 (= S184) binding
- R271 (= R274) binding
- FQMN 281:284 (≠ FQLI 284:287) binding
- R340 (≠ Q347) binding
- A344 (≠ G351) binding
- V366 (≠ G373) mutation to Y: Loses the FAD cofactor but a residual dehydrogenase activity is observed.
- EGSAN 367:371 (≠ AGTSE 374:378) binding
Sites not aligning to the query:
3mpjB Structure of the glutaryl-coenzyme a dehydrogenase (see paper)
39% identity, 96% coverage: 7:384/393 of query aligns to 1:377/393 of 3mpjB
- active site: I128 (≠ M131), T129 (≠ S132), T245 (≠ E248), E367 (≠ A374)
- binding flavin-adenine dinucleotide: F126 (≠ L129), I128 (≠ M131), T129 (≠ S132), G134 (= G137), S135 (= S138), W159 (= W162), I160 (= I163), S161 (≠ T164), V366 (≠ G373), S369 (≠ T376), N371 (≠ E378), M375 (= M382)
- binding : H36 (≠ Q42), F37 (= F43), Y39 (≠ M45), A164 (≠ P167), Q165 (≠ D168), D167 (= D170), N193 (≠ G195)
Sites not aligning to the query:
3mpiC Structure of the glutaryl-coenzyme a dehydrogenase glutaryl-coa complex (see paper)
39% identity, 96% coverage: 7:384/393 of query aligns to 1:377/395 of 3mpiC
- active site: I128 (≠ M131), T129 (≠ S132), T245 (≠ E248), E367 (≠ A374)
- binding flavin-adenine dinucleotide: I128 (≠ M131), T129 (≠ S132), G134 (= G137), S135 (= S138), W159 (= W162), I160 (= I163), S161 (≠ T164), M365 (≠ I372), V366 (≠ G373), S369 (≠ T376), N371 (≠ E378), M375 (= M382)
- binding glutaryl-coenzyme A: R87 (≠ G90), F126 (≠ L129), S135 (= S138), V137 (= V140), S181 (= S184), F239 (≠ M242), R246 (= R249), N315 (≠ Q322), V366 (≠ G373), E367 (≠ A374), G368 (= G375), I376 (≠ L383)
Sites not aligning to the query:
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
38% identity, 98% coverage: 7:390/393 of query aligns to 1:378/379 of 1ukwB
- active site: L124 (≠ M131), S125 (= S132), T241 (≠ E248), E362 (≠ A374), R374 (= R386)
- binding cobalt (ii) ion: D145 (= D152), H146 (= H153)
- binding flavin-adenine dinucleotide: F122 (≠ L129), L124 (≠ M131), S125 (= S132), G130 (= G137), S131 (= S138), W155 (= W162), S157 (≠ T164), K200 (= K207), L357 (= L369), Y361 (≠ G373), E362 (≠ A374), T364 (= T376), E366 (= E378), L370 (≠ M382)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
38% identity, 98% coverage: 7:390/393 of query aligns to 1:378/379 of 1ukwA
- active site: L124 (≠ M131), S125 (= S132), T241 (≠ E248), E362 (≠ A374), R374 (= R386)
- binding flavin-adenine dinucleotide: F122 (≠ L129), L124 (≠ M131), S125 (= S132), G130 (= G137), S131 (= S138), W155 (= W162), S157 (≠ T164), L357 (= L369), Y361 (≠ G373), E362 (≠ A374), T364 (= T376), E366 (= E378), L370 (≠ M382)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
37% identity, 96% coverage: 13:388/393 of query aligns to 8:378/378 of 4n5fA
- active site: L126 (≠ M131), T127 (≠ S132), G243 (≠ E248), E364 (≠ A374), R376 (= R386)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ M131), T127 (≠ S132), G132 (= G137), S133 (= S138), F157 (≠ W162), T159 (= T164), T210 (= T215), Y363 (≠ G373), T366 (= T376), E368 (= E378), M372 (= M382)
Query Sequence
>BPHYT_RS23260 FitnessBrowser__BFirm:BPHYT_RS23260
MSNLPGLQFPLGEEIEMLRDSIAGFAAKEIAPRAAEIDRTDQFPMDLWRKFGDLGVLGMT
VSEEYGGANMGYTAHMIAMEEISRASASVGLSYGAHSNLCVNQIHRNGTEAQKQKYLPKL
VSGEHVGALAMSEPNAGSDVVSMKLRAEKKGDHYVLNGTKMWITNGPDCDTLVVYAKTDP
EANSRGITAFIVEKGMKGFSVAQKLDKLGMRGSHTGELVFQDVEVPEENILGQLNGGAKV
LMSGLDYERAVLAGGPTGIMVAVMDAVVPYIHDRKQFGQSIGEFQLIQGKVADLYTTLQA
CRAYLYAVGRQLDTLGKEHVRQVRKDCAGVILYTAEKATWMAGEAIQILGGNGYINEYPV
GRLWRDAKLYEIGAGTSEIRRMLIGRELFAETA
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