SitesBLAST
Comparing WP_017178764.1 NCBI__GCF_000295095.1:WP_017178764.1 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)
8sgsA Human liver mitochondrial short-chain specific acyl-coa dehydrogenase (see paper)
32% identity, 96% coverage: 10:386/393 of query aligns to 6:379/381 of 8sgsA
- binding coenzyme a: S131 (= S135), A133 (= A137), N177 (≠ D181), F231 (≠ L235), M235 (= M239), L238 (= L242), I312 (≠ M316), E362 (= E369), G363 (= G370)
- binding flavin-adenine dinucleotide: F122 (= F126), L124 (= L128), S125 (≠ T129), G130 (= G134), S131 (= S135), W155 (≠ L158), T157 (≠ S160), R267 (= R271), F270 (= F274), L274 (= L278), L277 (≠ R281), Q335 (≠ E339), I336 (= I340), G338 (= G342), G339 (= G343), I357 (≠ A364), I360 (≠ L367), Y361 (≠ E368), T364 (≠ P371), E366 (≠ S373)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
32% identity, 96% coverage: 10:386/393 of query aligns to 9:382/385 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 (≠ I344), T347 (≠ E348), E348 (= E349)
- binding flavin-adenine dinucleotide: F125 (= F126), L127 (= L128), S128 (≠ T129), G133 (= G134), S134 (= S135), W158 (≠ L158), T160 (≠ S160), R270 (= R271), F273 (= F274), L280 (≠ R281), V282 (≠ A283), Q338 (≠ E339), I339 (= I340), G342 (= G343), I360 (≠ A364), Y364 (≠ E368), T367 (≠ P371), E369 (≠ S373), I370 (≠ V374), L373 (≠ T377)
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
34% identity, 91% coverage: 33:388/393 of query aligns to 27:380/383 of 4iv6B
- active site: L121 (= L128), T122 (= T129), G240 (≠ S245), E361 (= E369), K373 (≠ R381)
- binding dihydroflavine-adenine dinucleotide: L121 (= L128), T122 (= T129), G126 (≠ S135), G127 (= G136), S128 (≠ A137), W152 (≠ L158), I153 (= I159), S154 (= S160), R266 (= R271), S268 (≠ T273), F269 (= F274), I273 (≠ L278), H276 (≠ R281), V279 (≠ I284), R334 (≠ E339), V335 (≠ I340), G338 (= G343), L356 (≠ A364), G360 (≠ E368), T363 (≠ P371), E365 (≠ S373), I366 (≠ V374)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
32% identity, 96% coverage: 10:386/393 of query aligns to 36:409/412 of P16219
- G90 (= G64) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E78) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 126:135, 60% identical) binding in other chain
- R171 (= R145) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ LIS 158:160) binding in other chain
- A192 (≠ S165) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (≠ R183) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R271) binding FAD
- Q308 (= Q282) binding in other chain
- R325 (= R299) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ I327) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ EILGG 339:343) binding FAD
- R380 (= R357) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ PPS 371:373) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
32% identity, 96% coverage: 10:386/393 of query aligns to 12:385/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (= F126), L130 (= L128), S131 (≠ T129), G136 (= G134), S137 (= S135), W161 (≠ L158), T163 (≠ S160), T214 (≠ H212), R273 (= R271), F276 (= F274), L280 (= L278), L283 (≠ R281), V285 (≠ A283), Q341 (≠ E339), I342 (= I340), G345 (= G343), I363 (≠ A364), Y367 (≠ E368), T370 (≠ P371), E372 (≠ S373), L376 (≠ T377)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
31% identity, 96% coverage: 8:384/393 of query aligns to 4:377/378 of 5ol2F
- active site: L124 (= L128), T125 (= T129), G241 (≠ S245), G374 (≠ R381)
- binding calcium ion: E29 (= E33), E33 (≠ T37), R35 (≠ K39)
- binding coenzyme a persulfide: L238 (= L242), R242 (= R246), E362 (= E369), G363 (= G370)
- binding flavin-adenine dinucleotide: F122 (= F126), L124 (= L128), T125 (= T129), P127 (≠ K131), T131 (≠ S135), F155 (≠ L158), I156 (= I159), T157 (≠ S160), E198 (≠ P202), R267 (= R271), F270 (= F274), L274 (= L278), F277 (≠ R281), Q335 (≠ E339), L336 (≠ I340), G338 (= G342), G339 (= G343), Y361 (≠ E368), T364 (≠ P371), E366 (≠ S373)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
30% identity, 95% coverage: 10:384/393 of query aligns to 8:380/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S135), T134 (vs. gap), R180 (≠ K182), R234 (≠ H236), L237 (≠ M239), R238 (≠ Y240), L240 (= L242), D241 (≠ G243), R244 (= R246), E365 (= E369), G366 (= G370), R377 (= R381)
- binding flavin-adenine dinucleotide: Y123 (≠ F126), L125 (= L128), S126 (≠ T129), G131 (= G134), S132 (= S135), W156 (≠ L158), I157 (= I159), T158 (≠ S160), I360 (≠ A364), T367 (≠ P371), Q369 (≠ S373)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
30% identity, 95% coverage: 10:384/393 of query aligns to 8:380/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ F126), L125 (= L128), S126 (≠ T129), G131 (= G134), S132 (= S135), W156 (≠ L158), I157 (= I159), T158 (≠ S160), I360 (≠ A364), Y364 (≠ E368), T367 (≠ P371), Q369 (≠ S373)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
32% identity, 96% coverage: 10:386/393 of query aligns to 9:382/384 of 1jqiA
- active site: G377 (≠ R381)
- binding acetoacetyl-coenzyme a: L95 (≠ A94), F125 (= F126), S134 (= S135), F234 (≠ L235), M238 (= M239), Q239 (≠ Y240), L241 (= L242), D242 (≠ G243), R245 (= R246), Y364 (≠ E368), E365 (= E369), G366 (= G370)
- binding flavin-adenine dinucleotide: F125 (= F126), L127 (= L128), S128 (≠ T129), G133 (= G134), S134 (= S135), W158 (≠ L158), T160 (≠ S160), R270 (= R271), F273 (= F274), L280 (≠ R281), Q338 (≠ E339), I339 (= I340), G342 (= G343), I360 (≠ A364), T367 (≠ P371), E369 (≠ S373), I370 (≠ V374)
7w0jE Acyl-coa dehydrogenase, tfu_1647
30% identity, 95% coverage: 10:384/393 of query aligns to 9:381/382 of 7w0jE
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3S,4S)-5-azanyl-2,3,4-tris(oxidanyl)pentyl] hydrogen phosphate: S127 (≠ T129), W157 (≠ L158), R270 (= R271), Q272 (≠ T273), F273 (= F274), I277 (≠ L278), F280 (≠ R281), I283 (= I284), Q339 (≠ E339), L340 (≠ I340), G343 (= G343), Y365 (≠ E368), E366 (= E369), T368 (≠ P371), Q370 (≠ S373), I371 (≠ V374)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
32% identity, 96% coverage: 10:386/393 of query aligns to 36:409/412 of P15651
- 152:161 (vs. 126:135, 60% identical) binding FAD
- S161 (= S135) binding substrate
- WIT 185:187 (≠ LIS 158:160) binding FAD
- DMGR 269:272 (≠ GLSR 243:246) binding substrate
- R297 (= R271) binding FAD
- QILGG 365:369 (≠ EILGG 339:343) binding FAD
- E392 (= E369) active site, Proton acceptor
- TSE 394:396 (≠ PPS 371:373) binding FAD
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
32% identity, 96% coverage: 10:386/393 of query aligns to 3:369/371 of 2vigB
- active site: L121 (= L128), S122 (≠ T129), G231 (≠ S245), E352 (= E369), G364 (≠ R381)
- binding coenzyme a persulfide: S128 (= S135), F221 (≠ L235), M225 (= M239), Q226 (≠ Y240), L228 (= L242), D229 (≠ G243), R232 (= R246), E352 (= E369), G353 (= G370), I357 (≠ V374)
- binding flavin-adenine dinucleotide: L121 (= L128), S122 (≠ T129), G127 (= G134), S128 (= S135), W152 (≠ L158), T154 (≠ S160), R257 (= R271), F260 (= F274), L264 (= L278), L267 (≠ R281), Q325 (≠ E339), I326 (= I340), G329 (= G343), I347 (≠ A364), Y351 (≠ E368), T354 (≠ P371), E356 (≠ S373)
3pfdC Crystal structure of an acyl-coa dehydrogenase from mycobacterium thermoresistibile bound to reduced flavin adenine dinucleotide solved by combined iodide ion sad mr (see paper)
29% identity, 93% coverage: 19:384/393 of query aligns to 8:368/369 of 3pfdC
- active site: L116 (= L128), S117 (≠ T129), T233 (≠ S245), E353 (= E369), R365 (= R381)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ F126), L116 (= L128), S117 (≠ T129), G122 (= G134), S123 (= S135), W147 (≠ L158), I148 (= I159), T149 (≠ S160), R259 (= R271), F262 (= F274), V266 (≠ L278), N269 (≠ R281), Q326 (≠ E339), L327 (≠ I340), G330 (= G343), I348 (≠ A364), Y352 (≠ E368), T355 (≠ P371), Q357 (≠ S373)
2a1tC Structure of the human mcad:etf e165betaa complex (see paper)
31% identity, 95% coverage: 10:381/393 of query aligns to 10:380/388 of 2a1tC
- active site: V127 (≠ L128), T128 (= T129), T247 (≠ S245), E368 (= E369), R380 (= R381)
- binding flavin-adenine dinucleotide: Y125 (≠ F126), V127 (≠ L128), T128 (= T129), G133 (= G134), S134 (= S135), Q155 (≠ E155), W158 (≠ L158), W158 (≠ L158), I159 (= I159), T160 (≠ S160), R273 (= R271), T275 (= T273), F276 (= F274), L280 (= L278), H283 (≠ R281), I286 (= I284), Q341 (≠ E339), I342 (= I340), G345 (= G343), I363 (≠ A364), T370 (≠ P371), Q372 (≠ S373)
P11310 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; Medium chain acyl-CoA dehydrogenase; MCADH; EC 1.3.8.7 from Homo sapiens (Human) (see 16 papers)
31% identity, 95% coverage: 10:381/393 of query aligns to 43:413/421 of P11310
- Y67 (≠ I34) to H: in ACADMD; mild; dbSNP:rs121434280
- L86 (= L53) mutation to M: Strongly reduced rate of electron transfer to ETF.
- L98 (≠ W65) mutation to W: Strongly reduced rate of electron transfer to ETF.
- L100 (= L67) mutation to Y: Strongly reduced rate of electron transfer to ETF.
- I108 (≠ V75) mutation to M: Strongly reduced rate of electron transfer to ETF.
- P132 (≠ R99) to R: in a breast cancer sample; somatic mutation; dbSNP:rs875989854
- 158:167 (vs. 126:135, 50% identical) binding in other chain
- S167 (= S135) binding octanoyl-CoA
- W191 (≠ L158) mutation to A: Loss of electron transfer to ETF.; mutation to F: Reduces rate of electron transfer to ETF about six-fold.
- WIT 191:193 (≠ LIS 158:160) binding in other chain
- T193 (≠ S160) to A: in ACADMD; the thermostability is markedly decreased; dbSNP:rs121434279
- E237 (≠ P202) mutation to A: Strongly reduced rate of electron transfer to ETF.
- D278 (≠ G243) binding octanoyl-CoA
- T280 (≠ S245) mutation to E: Narrower substrate specificity. Changed substrate specificity towards longer acyl chains; when associated with G-401. Loss of acyl-CoA dehydrogenase activity; when associated with T-410.
- R281 (= R246) binding octanoyl-CoA; to T: in ACADMD; mild clinical phenotype; dbSNP:rs121434282
- RKT 306:308 (≠ RIT 271:273) binding FAD
- HQ 316:317 (≠ RQ 281:282) binding in other chain
- K329 (≠ W294) to E: in ACADMD; may alter splicing; decreased fatty acid beta-oxidation; dbSNP:rs77931234
- QILGG 374:378 (≠ EILGG 339:343) binding FAD
- E384 (= E351) mutation to A: Reduces rate of electron transfer to ETF three-fold.; mutation to Q: Reduces rate of electron transfer to ETF two-fold.
- E401 (= E369) active site, Proton acceptor; binding octanoyl-CoA; mutation to G: Changed substrate specificity towards longer acyl chains; when associated with E-280.; mutation to Q: Loss of acyl-CoA dehydrogenase activity.; mutation to T: Loss of acyl-CoA dehydrogenase activity; when associated with E-280.
- EGTSQ 401:405 (≠ EGPPS 369:373) binding in other chain
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
32% identity, 88% coverage: 40:383/393 of query aligns to 38:378/378 of 4n5fA
- active site: L126 (= L128), T127 (= T129), G243 (≠ S245), E364 (= E369), R376 (= R381)
- binding dihydroflavine-adenine dinucleotide: L126 (= L128), T127 (= T129), G132 (= G134), S133 (= S135), F157 (≠ L158), T159 (≠ S160), T210 (≠ H212), Y363 (≠ E368), T366 (≠ P371), E368 (≠ S373), M372 (≠ T377)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
30% identity, 95% coverage: 13:384/393 of query aligns to 5:373/374 of 5lnxD
- active site: L122 (= L128), T123 (= T129), G239 (≠ S245), E358 (= E369), K370 (≠ R381)
- binding flavin-adenine dinucleotide: L122 (= L128), T123 (= T129), G128 (= G134), S129 (= S135), F153 (≠ L158), T155 (≠ S160), R265 (= R271), Q267 (≠ T273), F268 (= F274), I272 (≠ L278), N275 (≠ R281), I278 (= I284), Q331 (≠ E339), I332 (= I340), G335 (= G343), Y357 (≠ E368), T360 (≠ P371), E362 (≠ S373)
1egcA Structure of t255e, e376g mutant of human medium chain acyl-coa dehydrogenase complexed with octanoyl-coa (see paper)
31% identity, 95% coverage: 10:381/393 of query aligns to 9:379/387 of 1egcA
- active site: V126 (≠ L128), T127 (= T129), E246 (≠ S245), G367 (≠ E369), R379 (= R381)
- binding octanoyl-coenzyme a: E90 (≠ H91), L94 (≠ G95), Y124 (≠ F126), S133 (= S135), V135 (vs. gap), N182 (≠ D181), F236 (≠ L235), M240 (= M239), F243 (≠ L242), D244 (≠ G243), R247 (= R246), Y366 (≠ E368), G367 (≠ E369), G368 (= G370)
- binding flavin-adenine dinucleotide: Y124 (≠ F126), V126 (≠ L128), T127 (= T129), G132 (= G134), S133 (= S135), W157 (≠ L158), T159 (≠ S160), R272 (= R271), T274 (= T273), F275 (= F274), L279 (= L278), H282 (≠ R281), I285 (= I284), Q340 (≠ E339), I341 (= I340), G344 (= G343), I362 (≠ A364), I365 (≠ L367), Y366 (≠ E368), T369 (≠ P371), Q371 (≠ S373)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
30% identity, 89% coverage: 29:376/393 of query aligns to 25:369/379 of 6fahD
- active site: L124 (= L128), T125 (= T129), G241 (≠ S245)
- binding flavin-adenine dinucleotide: F122 (= F126), L124 (= L128), T125 (= T129), R152 (≠ E155), F155 (≠ L158), T157 (≠ S160), E198 (≠ P202), R267 (= R271), Q269 (≠ T273), F270 (= F274), I274 (≠ L278), F277 (≠ R281), Q335 (≠ E339), I336 (= I340), G339 (= G343), Y361 (≠ E368), T364 (≠ P371), Q366 (≠ S373)
Sites not aligning to the query:
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
30% identity, 95% coverage: 10:381/393 of query aligns to 8:378/385 of 3mdeA
- active site: V125 (≠ L128), T126 (= T129), T245 (≠ S245), E366 (= E369), R378 (= R381)
- binding octanoyl-coenzyme a: T86 (≠ M88), E89 (≠ H91), L93 (≠ A94), S132 (= S135), V134 (vs. gap), S181 (≠ D181), F235 (≠ L235), M239 (= M239), F242 (≠ L242), R314 (≠ D314), Y365 (≠ E368), E366 (= E369), G367 (= G370)
- binding flavin-adenine dinucleotide: Y123 (≠ F126), V125 (≠ L128), T126 (= T129), G131 (= G134), S132 (= S135), W156 (≠ L158), I157 (= I159), T158 (≠ S160), R271 (= R271), T273 (= T273), F274 (= F274), L278 (= L278), H281 (≠ R281), Q339 (≠ E339), V340 (≠ I340), G343 (= G343), I361 (≠ A364), T368 (≠ P371), Q370 (≠ S373)
Query Sequence
>WP_017178764.1 NCBI__GCF_000295095.1:WP_017178764.1
MITSKPKNDEEFQQYLMEIRELAQGPFDELQTEIEVTNKFPDEFYELAKEHNLYRFYMPE
QYGGWGLSTLEIMKVQEEFSRGPGGMRMHLHHAAGLNWRIMDDFAQPELKEWAMPRFQNK
TLFVNFALTEKEAGSGADIKTTAVRDGDEWVINGEKTLISHTDCSDGTYLITLTNPEADK
DKRLTAFFVPTDTPGYEIVDMPHMMGCRGAGHAGLRFTDCRVPDKYRLGEVGEGLHVAMY
SLGLSRLHIADSNLGMAQRMLEMSIARAKERITFGKPLIKRQAIQTMIAESGKWIYLLRS
AIHDAARRYDAGEDPMTQASLCKLASIDAVKIVSDNILEILGGIGYFEECEYGPAERLYR
DCRAMWLEEGPPSVQRTTAARGLITSGGDLWNS
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