SitesBLAST
Comparing HSERO_RS04640 FitnessBrowser__HerbieS:HSERO_RS04640 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
57% identity, 98% coverage: 2:375/382 of query aligns to 5:378/378 of 4n5fA
- active site: L126 (= L123), T127 (= T124), G243 (= G240), E364 (= E361), R376 (= R373)
- binding dihydroflavine-adenine dinucleotide: L126 (= L123), T127 (= T124), G132 (= G129), S133 (= S130), F157 (= F154), T159 (= T156), T210 (= T207), Y363 (= Y360), T366 (≠ A363), E368 (≠ D365), M372 (≠ L369)
4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
57% identity, 98% coverage: 2:375/382 of query aligns to 3:376/376 of 4m9aB
- active site: L124 (= L123), T125 (= T124), G241 (= G240), E362 (= E361), R374 (= R373)
- binding dihydroflavine-adenine dinucleotide: F122 (= F121), T125 (= T124), G130 (= G129), S131 (= S130), F155 (= F154), T157 (= T156), T208 (= T207), Y361 (= Y360), T364 (≠ A363), E366 (≠ D365), M370 (≠ L369)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
50% identity, 96% coverage: 5:371/382 of query aligns to 8:375/384 of 1jqiA
- binding acetoacetyl-coenzyme a: L95 (= L91), F125 (= F121), S134 (= S130), F234 (≠ Y230), M238 (≠ L234), Q239 (≠ S235), L241 (= L237), D242 (≠ E238), R245 (= R241), Y364 (= Y360), E365 (= E361), G366 (= G362)
- binding flavin-adenine dinucleotide: F125 (= F121), L127 (= L123), S128 (≠ T124), G133 (= G129), S134 (= S130), W158 (≠ F154), T160 (= T156), R270 (= R266), F273 (= F269), L280 (≠ H276), Q338 (= Q334), I339 (= I335), G342 (= G338), I360 (= I356), T367 (≠ A363), E369 (≠ D365), I370 (= I366)
Sites not aligning to the query:
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
50% identity, 96% coverage: 5:371/382 of query aligns to 35:402/412 of P15651
- 152:161 (vs. 121:130, 60% identical) binding FAD
- S161 (= S130) binding substrate
- WIT 185:187 (≠ FIT 154:156) binding FAD
- DMGR 269:272 (≠ EAGR 238:241) binding substrate
- R297 (= R266) binding FAD
- QILGG 365:369 (≠ QIHGG 334:338) binding FAD
- E392 (= E361) active site, Proton acceptor
- TSE 394:396 (≠ AND 363:365) binding FAD
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
49% identity, 96% coverage: 5:371/382 of query aligns to 8:375/385 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 (≠ V339), T347 (≠ S343), E348 (≠ D344)
- binding flavin-adenine dinucleotide: F125 (= F121), L127 (= L123), S128 (≠ T124), G133 (= G129), S134 (= S130), W158 (≠ F154), T160 (= T156), R270 (= R266), F273 (= F269), L280 (≠ H276), V282 (≠ A278), Q338 (= Q334), I339 (= I335), G342 (= G338), I360 (= I356), Y364 (= Y360), T367 (≠ A363), E369 (≠ D365), I370 (= I366), L373 (= L369)
8sgsA Human liver mitochondrial short-chain specific acyl-coa dehydrogenase (see paper)
49% identity, 97% coverage: 3:371/382 of query aligns to 4:372/381 of 8sgsA
- binding coenzyme a: S131 (= S130), A133 (= A132), N177 (≠ K176), F231 (≠ Y230), M235 (≠ L234), L238 (= L237), I312 (≠ L311), E362 (= E361), G363 (= G362)
- binding flavin-adenine dinucleotide: F122 (= F121), L124 (= L123), S125 (≠ T124), G130 (= G129), S131 (= S130), W155 (≠ F154), T157 (= T156), R267 (= R266), F270 (= F269), L274 (≠ I273), L277 (≠ H276), Q335 (= Q334), I336 (= I335), G338 (= G337), G339 (= G338), I357 (= I356), I360 (= I359), Y361 (= Y360), T364 (≠ A363), E366 (≠ D365)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
49% identity, 97% coverage: 3:371/382 of query aligns to 10:378/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (= F121), L130 (= L123), S131 (≠ T124), G136 (= G129), S137 (= S130), W161 (≠ F154), T163 (= T156), T214 (= T207), R273 (= R266), F276 (= F269), L280 (≠ I273), L283 (≠ H276), V285 (≠ A278), Q341 (= Q334), I342 (= I335), G345 (= G338), I363 (= I356), Y367 (= Y360), T370 (≠ A363), E372 (≠ D365), L376 (= L369)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
49% identity, 97% coverage: 3:371/382 of query aligns to 34:402/412 of P16219
- G90 (= G59) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E73) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 121:130, 60% identical) binding in other chain
- R171 (≠ E140) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ FIT 154:156) binding in other chain
- A192 (= A161) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G178) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R266) binding FAD
- Q308 (= Q277) binding in other chain
- R325 (= R294) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (= S322) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QIHGG 334:338) binding FAD
- R380 (= R349) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ AND 363:365) 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
48% identity, 97% coverage: 3:371/382 of query aligns to 1:362/371 of 2vigB
- active site: L121 (= L123), S122 (≠ T124), G231 (= G240), E352 (= E361)
- binding coenzyme a persulfide: S128 (= S130), F221 (≠ Y230), M225 (≠ L234), Q226 (≠ S235), L228 (= L237), D229 (≠ E238), R232 (= R241), E352 (= E361), G353 (= G362), I357 (= I366)
- binding flavin-adenine dinucleotide: L121 (= L123), S122 (≠ T124), G127 (= G129), S128 (= S130), W152 (≠ F154), T154 (= T156), R257 (= R266), F260 (= F269), L264 (≠ I273), L267 (≠ H276), Q325 (= Q334), I326 (= I335), G329 (= G338), I347 (= I356), Y351 (= Y360), T354 (≠ A363), E356 (≠ D365)
Sites not aligning to the query:
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
48% identity, 97% coverage: 6:375/382 of query aligns to 5:372/374 of 5lnxD
- active site: L122 (= L123), T123 (= T124), G239 (= G240), E358 (= E361), K370 (≠ R373)
- binding flavin-adenine dinucleotide: L122 (= L123), T123 (= T124), G128 (= G129), S129 (= S130), F153 (= F154), T155 (= T156), R265 (= R266), Q267 (≠ S268), F268 (= F269), I272 (= I273), N275 (≠ H276), I278 (≠ V279), Q331 (= Q334), I332 (= I335), G335 (= G338), Y357 (= Y360), T360 (≠ A363), E362 (≠ D365)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
45% identity, 98% coverage: 3:378/382 of query aligns to 5:380/380 of 4l1fA
- active site: L125 (= L123), T126 (= T124), G242 (= G240), E363 (= E361), R375 (= R373)
- binding coenzyme a persulfide: T132 (≠ S130), H179 (≠ K177), F232 (≠ Y230), M236 (≠ L234), E237 (≠ S235), L239 (= L237), D240 (≠ E238), R243 (= R241), Y362 (= Y360), E363 (= E361), G364 (= G362), R375 (= R373)
- binding flavin-adenine dinucleotide: F123 (= F121), L125 (= L123), T126 (= T124), G131 (= G129), T132 (≠ S130), F156 (= F154), I157 (= I155), T158 (= T156), R268 (= R266), Q270 (≠ S268), F271 (= F269), I275 (= I273), F278 (≠ H276), L281 (≠ V279), Q336 (= Q334), I337 (= I335), G340 (= G338), I358 (= I356), Y362 (= Y360), T365 (≠ A363), Q367 (≠ D365)
- binding 1,3-propandiol: L5 (= L3), Q10 (≠ E8)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
45% identity, 97% coverage: 2:371/382 of query aligns to 3:372/378 of 5ol2F
- active site: L124 (= L123), T125 (= T124), G241 (= G240)
- binding calcium ion: E29 (≠ D28), E33 (≠ N32), R35 (≠ T34)
- binding coenzyme a persulfide: L238 (= L237), R242 (= R241), E362 (= E361), G363 (= G362)
- binding flavin-adenine dinucleotide: F122 (= F121), L124 (= L123), T125 (= T124), P127 (= P126), T131 (≠ S130), F155 (= F154), I156 (= I155), T157 (= T156), E198 (= E197), R267 (= R266), F270 (= F269), L274 (≠ I273), F277 (≠ H276), Q335 (= Q334), L336 (≠ I335), G338 (= G337), G339 (= G338), Y361 (= Y360), T364 (≠ A363), E366 (≠ D365)
Sites not aligning to the query:
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
49% identity, 98% coverage: 3:375/382 of query aligns to 1:368/370 of 2dvlA
- active site: L121 (= L123), T122 (= T124), G233 (= G240), E354 (= E361), R366 (= R373)
- binding flavin-adenine dinucleotide: L121 (= L123), T122 (= T124), G127 (= G129), S128 (= S130), W152 (≠ F154), I153 (= I155), T154 (= T156), T356 (≠ A363), E358 (≠ D365)
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
40% identity, 98% coverage: 3:378/382 of query aligns to 6:380/381 of 2jifA
- active site: L125 (= L123), S126 (≠ T124), G242 (= G240), E363 (= E361), K375 (≠ R373)
- binding coenzyme a persulfide: S132 (= S130), S134 (≠ A132), Y178 (≠ K176), Y232 (= Y230), I236 (≠ L234), L239 (= L237), N240 (≠ E238), R243 (= R241), Y362 (= Y360), E363 (= E361), G364 (= G362), I368 (= I366)
- binding flavin-adenine dinucleotide: F123 (= F121), L125 (= L123), S126 (≠ T124), G131 (= G129), S132 (= S130), W156 (≠ F154), I157 (= I155), S158 (≠ T156), K201 (= K199), T209 (= T207), R268 (= R266), F271 (= F269), L275 (≠ I273), F278 (≠ H276), L281 (≠ V279), E336 (≠ Q334), W337 (≠ I335), G340 (= G338), N367 (≠ D365), I368 (= I366)
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)
40% identity, 98% coverage: 3:378/382 of query aligns to 57:431/432 of P45954
- V137 (≠ T83) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ I84) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 121:130, 60% identical) binding in other chain
- S183 (= S130) binding substrate
- WIS 207:209 (≠ FIT 154:156) binding in other chain
- S210 (= S157) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ K176) binding substrate
- L255 (≠ Q202) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (= Y230) binding substrate
- NEGR 291:294 (≠ EAGR 238:241) binding substrate
- I316 (≠ A263) to V: in dbSNP:rs1131430
- R319 (= R266) binding FAD
- Q330 (= Q277) binding FAD
- EWMGG 387:391 (≠ QIHGG 334:338) binding FAD
- A416 (= A363) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ AND 363:365) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
42% identity, 98% coverage: 3:375/382 of query aligns to 5:376/379 of 1ukwB
- active site: L124 (= L123), S125 (≠ T124), T241 (≠ G240), E362 (= E361), R374 (= R373)
- binding cobalt (ii) ion: D145 (= D144), H146 (≠ D145)
- binding flavin-adenine dinucleotide: F122 (= F121), L124 (= L123), S125 (≠ T124), G130 (= G129), S131 (= S130), W155 (≠ F154), S157 (≠ T156), K200 (= K199), L357 (≠ I356), Y361 (= Y360), E362 (= E361), T364 (≠ A363), E366 (≠ D365), L370 (= L369)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
42% identity, 98% coverage: 3:375/382 of query aligns to 5:376/379 of 1ukwA
- active site: L124 (= L123), S125 (≠ T124), T241 (≠ G240), E362 (= E361), R374 (= R373)
- binding flavin-adenine dinucleotide: F122 (= F121), L124 (= L123), S125 (≠ T124), G130 (= G129), S131 (= S130), W155 (≠ F154), S157 (≠ T156), L357 (≠ I356), Y361 (= Y360), E362 (= E361), T364 (≠ A363), E366 (≠ D365), L370 (= L369)
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)
43% identity, 97% coverage: 7:375/382 of query aligns to 1:367/369 of 3pfdC
- active site: L116 (= L123), S117 (≠ T124), T233 (≠ G240), E353 (= E361), R365 (= R373)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ F121), L116 (= L123), S117 (≠ T124), G122 (= G129), S123 (= S130), W147 (≠ F154), I148 (= I155), T149 (= T156), R259 (= R266), F262 (= F269), V266 (≠ I273), N269 (≠ H276), Q326 (= Q334), L327 (≠ I335), G330 (= G338), I348 (= I356), Y352 (= Y360), T355 (≠ A363), Q357 (≠ D365)
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
42% identity, 94% coverage: 17:375/382 of query aligns to 19:381/383 of 1bucA
- active site: L128 (= L123), T129 (= T124), G246 (= G240), E367 (= E361), G379 (≠ R373)
- binding acetoacetyl-coenzyme a: L96 (= L91), F126 (= F121), G134 (= G129), T135 (≠ S130), T162 (= T156), N182 (≠ K176), H183 (≠ K177), F236 (≠ Y230), M240 (≠ L234), M241 (≠ S235), L243 (= L237), D244 (≠ E238), T317 (≠ L311), Y366 (= Y360), E367 (= E361), G368 (= G362)
- binding flavin-adenine dinucleotide: F126 (= F121), L128 (= L123), T129 (= T124), G134 (= G129), T135 (≠ S130), F160 (= F154), T162 (= T156), Y366 (= Y360), T369 (≠ A363), E371 (≠ D365), M375 (≠ L369)
Q06319 Acyl-CoA dehydrogenase, short-chain specific; Butyryl-CoA dehydrogenase; BCAD; SCAD; EC 1.3.8.1 from Megasphaera elsdenii (see paper)
42% identity, 94% coverage: 17:375/382 of query aligns to 19:381/383 of Q06319
- E367 (= E361) active site, Proton acceptor; mutation to Q: Loss of activity.
Query Sequence
>HSERO_RS04640 FitnessBrowser__HerbieS:HSERO_RS04640
MLLSPEHEMIRDAMRHFAQERLLPFAADWDRNHTFPAEALKELAELGAMGMCVPEQWGGA
GMDYMSLVLALEEIAAGDGATSTIVSVQNSLACGITEKYGSPTQKEQWLKPLARGEMLGC
FCLTEPHTGSDAAAIRTRAERDGDDFILNGTKQFITSGKHAGVAIVFAVTDRSAGKKGIS
CFLVPCDTPGFVVGRSEEKMGQHASDTVQIMLDNCRVPATALLGKEGEGYRIALSNLEAG
RIGIAAQSVGMARAAFEAAVSYARQRESFGVPIIEHQAVNFRLADMNTLLDAARLMVWRA
AQLKDQGRPCLKEASMAKMFASEAAEKIASDAIQIHGGVGYTSDFPVERIYRDVRICQIY
EGANDIQRLVIGRAIASDQAHA
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