SitesBLAST
Comparing WP_022669656.1 NCBI__GCF_000420385.1:WP_022669656.1 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)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
36% identity, 99% coverage: 2:377/379 of query aligns to 1:378/380 of 4l1fA
- active site: L125 (≠ V125), T126 (= T126), G242 (= G241), E363 (≠ A362), R375 (= R374)
- binding coenzyme a persulfide: T132 (≠ S132), H179 (≠ K177), F232 (≠ M230), M236 (= M234), E237 (≠ S235), L239 (≠ I237), D240 (≠ E239), R243 (= R242), Y362 (≠ S361), E363 (≠ A362), G364 (= G363), R375 (= R374)
- binding flavin-adenine dinucleotide: F123 (≠ V123), L125 (≠ V125), T126 (= T126), G131 (= G131), T132 (≠ S132), F156 (≠ M156), I157 (≠ L157), T158 (= T158), R268 (= R267), Q270 (≠ L269), F271 (≠ Y270), I275 (= I274), F278 (≠ L277), L281 (≠ I280), Q336 (≠ D335), I337 (= I336), G340 (= G339), I358 (≠ V357), Y362 (≠ S361), T365 (= T364), Q367 (≠ D366)
- binding 1,3-propandiol: L5 (≠ F6), Q10 (≠ E11)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
36% identity, 97% coverage: 7:373/379 of query aligns to 5:373/378 of 5ol2F
- active site: L124 (≠ V125), T125 (= T126), G241 (= G241)
- binding calcium ion: E29 (= E31), E33 (≠ K35), R35 (≠ V37)
- binding coenzyme a persulfide: L238 (≠ I237), R242 (= R242), E362 (≠ A362), G363 (= G363)
- binding flavin-adenine dinucleotide: F122 (≠ V123), L124 (≠ V125), T125 (= T126), P127 (≠ A128), T131 (≠ S132), F155 (≠ M156), I156 (≠ L157), T157 (= T158), E198 (≠ W197), R267 (= R267), F270 (≠ Y270), L274 (≠ I274), F277 (≠ L277), Q335 (≠ D335), L336 (≠ I336), G338 (= G338), G339 (= G339), Y361 (≠ S361), T364 (= T364), E366 (≠ D366)
Sites not aligning to the query:
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
37% identity, 98% coverage: 8:378/379 of query aligns to 4:374/374 of 5lnxD
- active site: L122 (≠ V125), T123 (= T126), G239 (= G241), E358 (≠ A362), K370 (≠ R374)
- binding flavin-adenine dinucleotide: L122 (≠ V125), T123 (= T126), G128 (= G131), S129 (= S132), F153 (≠ M156), T155 (= T158), R265 (= R267), Q267 (≠ L269), F268 (≠ Y270), I272 (= I274), N275 (≠ L277), I278 (= I280), Q331 (≠ D335), I332 (= I336), G335 (= G339), Y357 (≠ S361), T360 (= T364), E362 (≠ D366)
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
35% identity, 99% coverage: 2:377/379 of query aligns to 1:382/383 of 1bucA
- active site: L128 (≠ V125), T129 (= T126), G246 (= G241), E367 (≠ A362), G379 (≠ R374)
- binding acetoacetyl-coenzyme a: L96 (= L93), F126 (≠ V123), G134 (= G131), T135 (≠ S132), T162 (= T158), N182 (≠ P176), H183 (≠ K177), F236 (≠ M230), M240 (= M234), M241 (≠ S235), L243 (≠ I237), D244 (≠ E239), T317 (≠ D312), Y366 (≠ S361), E367 (≠ A362), G368 (= G363)
- binding flavin-adenine dinucleotide: F126 (≠ V123), L128 (≠ V125), T129 (= T126), G134 (= G131), T135 (≠ S132), F160 (≠ M156), T162 (= T158), Y366 (≠ S361), T369 (= T364), E371 (≠ D366), M375 (≠ V370)
Q06319 Acyl-CoA dehydrogenase, short-chain specific; Butyryl-CoA dehydrogenase; BCAD; SCAD; EC 1.3.8.1 from Megasphaera elsdenii (see paper)
35% identity, 99% coverage: 2:377/379 of query aligns to 1:382/383 of Q06319
- E367 (≠ A362) active site, Proton acceptor; mutation to Q: Loss of activity.
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
34% identity, 97% coverage: 8:373/379 of query aligns to 36:403/412 of P15651
- 152:161 (vs. 123:132, 40% identical) binding FAD
- S161 (= S132) binding substrate
- WIT 185:187 (≠ MLT 156:158) binding FAD
- DMGR 269:272 (≠ EVGR 239:242) binding substrate
- R297 (= R267) binding FAD
- QILGG 365:369 (≠ DIQGG 335:339) binding FAD
- E392 (≠ A362) active site, Proton acceptor
- TSE 394:396 (≠ TSD 364:366) binding FAD
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
34% identity, 97% coverage: 8:373/379 of query aligns to 9:376/384 of 1jqiA
- binding acetoacetyl-coenzyme a: L95 (= L93), F125 (≠ V123), S134 (= S132), F234 (≠ M230), M238 (= M234), Q239 (≠ S235), L241 (≠ I237), D242 (≠ E239), R245 (= R242), Y364 (≠ S361), E365 (≠ A362), G366 (= G363)
- binding flavin-adenine dinucleotide: F125 (≠ V123), L127 (≠ V125), S128 (≠ T126), G133 (= G131), S134 (= S132), W158 (≠ M156), T160 (= T158), R270 (= R267), F273 (≠ Y270), L280 (= L277), Q338 (≠ D335), I339 (= I336), G342 (= G339), I360 (≠ V357), T367 (= T364), E369 (≠ D366), I370 (= I367)
Sites not aligning to the query:
8sgsA Human liver mitochondrial short-chain specific acyl-coa dehydrogenase (see paper)
34% identity, 97% coverage: 8:373/379 of query aligns to 6:373/381 of 8sgsA
- binding coenzyme a: S131 (= S132), A133 (≠ P134), N177 (≠ P176), F231 (≠ M230), M235 (= M234), L238 (≠ I237), I312 (≠ D312), E362 (≠ A362), G363 (= G363)
- binding flavin-adenine dinucleotide: F122 (≠ V123), L124 (≠ V125), S125 (≠ T126), G130 (= G131), S131 (= S132), W155 (≠ M156), T157 (= T158), R267 (= R267), F270 (≠ Y270), L274 (≠ I274), L277 (= L277), Q335 (≠ D335), I336 (= I336), G338 (= G338), G339 (= G339), I357 (≠ V357), I360 (≠ P360), Y361 (≠ S361), T364 (= T364), E366 (≠ D366)
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
34% identity, 97% coverage: 8:373/379 of query aligns to 3:363/371 of 2vigB
- active site: L121 (≠ V125), S122 (≠ T126), G231 (= G241), E352 (≠ A362)
- binding coenzyme a persulfide: S128 (= S132), F221 (≠ M230), M225 (= M234), Q226 (≠ S235), L228 (≠ I237), D229 (≠ E239), R232 (= R242), E352 (≠ A362), G353 (= G363), I357 (= I367)
- binding flavin-adenine dinucleotide: L121 (≠ V125), S122 (≠ T126), G127 (= G131), S128 (= S132), W152 (≠ M156), T154 (= T158), R257 (= R267), F260 (≠ Y270), L264 (≠ I274), L267 (= L277), Q325 (≠ D335), I326 (= I336), G329 (= G339), I347 (≠ V357), Y351 (≠ S361), T354 (= T364), E356 (≠ D366)
Sites not aligning to the query:
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
34% identity, 97% coverage: 8:373/379 of query aligns to 36:403/412 of P16219
- G90 (= G62) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E76) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 123:132, 40% identical) binding in other chain
- R171 (≠ K142) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ MLT 156:158) binding in other chain
- A192 (= A163) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (≠ A178) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R267) binding FAD
- Q308 (= Q278) binding in other chain
- R325 (= R295) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ T323) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ DIQGG 335:339) binding FAD
- R380 (= R350) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ TSD 364:366) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
34% identity, 97% coverage: 6:373/379 of query aligns to 3:373/379 of 6fahD
- active site: L124 (≠ V125), T125 (= T126), G241 (= G241)
- binding flavin-adenine dinucleotide: F122 (≠ V123), L124 (≠ V125), T125 (= T126), R152 (= R153), F155 (≠ M156), T157 (= T158), E198 (≠ W197), R267 (= R267), Q269 (≠ L269), F270 (≠ Y270), I274 (= I274), F277 (≠ L277), Q335 (≠ D335), I336 (= I336), G339 (= G339), Y361 (≠ S361), T364 (= T364), Q366 (≠ D366)
Sites not aligning to the query:
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
34% identity, 97% coverage: 8:373/379 of query aligns to 9:376/385 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 (≠ Y340), T347 (≠ E344), E348 (= E345)
- binding flavin-adenine dinucleotide: F125 (≠ V123), L127 (≠ V125), S128 (≠ T126), G133 (= G131), S134 (= S132), W158 (≠ M156), T160 (= T158), R270 (= R267), F273 (≠ Y270), L280 (= L277), V282 (≠ T279), Q338 (≠ D335), I339 (= I336), G342 (= G339), I360 (≠ V357), Y364 (≠ S361), T367 (= T364), E369 (≠ D366), I370 (= I367), L373 (≠ V370)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
34% identity, 97% coverage: 8:373/379 of query aligns to 12:379/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ V123), L130 (≠ V125), S131 (≠ T126), G136 (= G131), S137 (= S132), W161 (≠ M156), T163 (= T158), T214 (≠ V207), R273 (= R267), F276 (≠ Y270), L280 (≠ I274), L283 (= L277), V285 (≠ T279), Q341 (≠ D335), I342 (= I336), G345 (= G339), I363 (≠ V357), Y367 (≠ S361), T370 (= T364), E372 (≠ D366), L376 (≠ V370)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
32% identity, 98% coverage: 6:375/379 of query aligns to 8:383/387 of 1ivhA
- active site: M130 (≠ V125), S131 (≠ T126), E249 (≠ G241), A370 (= A362), R382 (= R374)
- binding coenzyme a persulfide: S137 (= S132), S185 (≠ P176), R186 (≠ K177), V239 (≠ M230), Y240 (≠ R231), M243 (= M234), E249 (≠ G241), R250 (= R242), G369 (≠ S361), A370 (= A362), G371 (= G363), V375 (≠ I367)
- binding flavin-adenine dinucleotide: L128 (≠ V123), M130 (≠ V125), S131 (≠ T126), G136 (= G131), S137 (= S132), W161 (≠ M156), T163 (= T158), R275 (= R267), F278 (≠ Y270), F285 (≠ L277), M288 (≠ I280), Q343 (≠ D335), C344 (≠ I336), G347 (= G339), T372 (= T364), E374 (≠ D366)
8sgrA Human liver mitochondrial isovaleryl-coa dehydrogenase (see paper)
32% identity, 98% coverage: 6:375/379 of query aligns to 12:387/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ T126), G140 (= G131), S141 (= S132), W165 (≠ M156), T167 (= T158), R279 (= R267), F282 (≠ Y270), I286 (= I274), F289 (≠ L277), Q347 (≠ D335), C348 (≠ I336), G351 (= G339), L369 (≠ V357), G375 (= G363), T376 (= T364), L382 (≠ V370)
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)
32% identity, 98% coverage: 6:375/379 of query aligns to 45:420/426 of P26440
- 165:174 (vs. 123:132, 40% identical) binding FAD
- S174 (= S132) binding substrate
- WIT 198:200 (≠ MLT 156:158) binding FAD
- SR 222:223 (≠ PK 176:177) binding substrate
- G250 (= G204) to A: in IVA; uncertain significance
- Y277 (≠ R231) binding substrate
- DLER 284:287 (≠ EVGR 239:242) binding substrate
- E286 (≠ G241) 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 (≠ V246) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R267) binding FAD
- Q323 (= Q278) binding FAD
- I379 (≠ V334) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ DIQGG 335:339) binding FAD
- R398 (= R353) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ L358) to N: in IVA; uncertain significance
- A407 (= A362) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (= AG 362:363) binding substrate
- TSE 409:411 (≠ TSD 364:366) binding FAD
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
35% identity, 98% coverage: 2:374/379 of query aligns to 1:374/379 of 1ukwB
- active site: L124 (≠ V125), S125 (≠ T126), T241 (≠ V240), E362 (≠ A362), R374 (= R374)
- binding cobalt (ii) ion: D145 (= D146), H146 (≠ F147)
- binding flavin-adenine dinucleotide: F122 (≠ V123), L124 (≠ V125), S125 (≠ T126), G130 (= G131), S131 (= S132), W155 (≠ M156), S157 (≠ T158), K200 (≠ E199), L357 (≠ V357), Y361 (≠ S361), E362 (≠ A362), T364 (= T364), E366 (≠ D366), L370 (≠ V370)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
35% identity, 98% coverage: 2:374/379 of query aligns to 1:374/379 of 1ukwA
- active site: L124 (≠ V125), S125 (≠ T126), T241 (≠ V240), E362 (≠ A362), R374 (= R374)
- binding flavin-adenine dinucleotide: F122 (≠ V123), L124 (≠ V125), S125 (≠ T126), G130 (= G131), S131 (= S132), W155 (≠ M156), S157 (≠ T158), L357 (≠ V357), Y361 (≠ S361), E362 (≠ A362), T364 (= T364), E366 (≠ D366), L370 (≠ V370)
P45954 Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial; SBCAD; 2-methyl branched chain acyl-CoA dehydrogenase; 2-MEBCAD; 2-methylbutyryl-coenzyme A dehydrogenase; 2-methylbutyryl-CoA dehydrogenase; EC 1.3.8.5 from Homo sapiens (Human) (see 6 papers)
33% identity, 98% coverage: 5:374/379 of query aligns to 56:426/432 of P45954
- V137 (≠ M86) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ M87) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 123:132, 40% identical) binding in other chain
- S183 (= S132) binding substrate
- WIS 207:209 (≠ MLT 156:158) binding in other chain
- S210 (≠ N159) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (vs. gap) binding substrate
- L255 (= L202) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ M230) binding substrate
- NE-GR 291:294 (≠ GEVGR 238:242) binding substrate
- I316 (≠ S264) to V: in dbSNP:rs1131430
- R319 (= R267) binding FAD
- Q330 (= Q278) binding FAD
- EWMGG 387:391 (≠ DIQGG 335:339) binding FAD
- A416 (≠ T364) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ TSD 364:366) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
33% identity, 98% coverage: 5:374/379 of query aligns to 5:375/381 of 2jifA
- active site: L125 (≠ V125), S126 (≠ T126), G242 (= G241), E363 (≠ A362), K375 (≠ R374)
- binding coenzyme a persulfide: S132 (= S132), S134 (≠ P134), Y178 (vs. gap), Y232 (≠ M230), I236 (≠ M234), L239 (≠ I237), N240 (≠ G238), R243 (= R242), Y362 (≠ S361), E363 (≠ A362), G364 (= G363), I368 (= I367)
- binding flavin-adenine dinucleotide: F123 (≠ V123), L125 (≠ V125), S126 (≠ T126), G131 (= G131), S132 (= S132), W156 (≠ M156), I157 (≠ L157), S158 (≠ T158), K201 (≠ E199), T209 (≠ V207), R268 (= R267), F271 (≠ Y270), L275 (≠ I274), F278 (≠ L277), L281 (≠ I280), E336 (≠ D335), W337 (≠ I336), G340 (= G339), N367 (≠ D366), I368 (= I367)
Query Sequence
>WP_022669656.1 NCBI__GCF_000420385.1:WP_022669656.1
MIDFTFTEEQEIFRKKVAEFTEKKIKPKVREMEEKKVALPEVVEALKDEKLTGIFIPKEY
NGLGLGYTERLIALEEIAKVSPGVAMMLQIFGLGIEPILKFGNDEQKQKYLPGLAVGEKL
ATVAVTEATGGSDPTGIKTTYKKEGDFYILNGRKIMLTNAPIANTFVVLAKDSENPKAFS
TLIIEDTFEGFRRGKEWHEIGLHGCSVGEILLENCKVPASNLLGQEGKGMRVAMSAIGEV
GRGGMVGVALGIMDTLLKITVNFSKKRILYGKPISNLQTIQNKIAEMRLDLEIGRLLGYR
ATSIQDKGQRSDLEFAMAKYFTTEAAQKAAKMAVDIQGGYGVTEEAVVTRFLRDSFVLGP
SAGTSDIMKVIIARATIGK
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