SitesBLAST
Comparing WP_057507944.1 NCBI__GCF_001431535.1:WP_057507944.1 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)
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, 97% coverage: 5:375/382 of query aligns to 34:403/412 of P15651
- 152:161 (vs. 123:132, 70% identical) binding FAD
- S161 (= S132) binding substrate
- WIT 185:187 (= WIT 157:159) binding FAD
- DMGR 269:272 (≠ DAGR 241:244) binding substrate
- R297 (= R269) binding FAD
- QILGG 365:369 (≠ QIHGG 337:341) binding FAD
- E392 (= E364) active site, Proton acceptor
- TSE 394:396 (= TSE 366:368) 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)
50% identity, 97% coverage: 5:375/382 of query aligns to 7:376/384 of 1jqiA
- binding acetoacetyl-coenzyme a: L95 (= L93), F125 (= F123), S134 (= S132), F234 (= F233), M238 (= M237), Q239 (≠ G238), L241 (= L240), D242 (= D241), R245 (= R244), Y364 (= Y363), E365 (= E364), G366 (= G365)
- binding flavin-adenine dinucleotide: F125 (= F123), L127 (= L125), S128 (≠ T126), G133 (= G131), S134 (= S132), W158 (= W157), T160 (= T159), R270 (= R269), F273 (= F272), L280 (≠ F279), Q338 (= Q337), I339 (= I338), G342 (= G341), I360 (= I359), T367 (= T366), E369 (= E368), I370 (= I369)
Sites not aligning to the query:
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
50% identity, 99% coverage: 1:377/382 of query aligns to 2:377/378 of 4n5fA
- active site: L126 (= L125), T127 (= T126), G243 (= G243), E364 (= E364), R376 (= R376)
- binding dihydroflavine-adenine dinucleotide: L126 (= L125), T127 (= T126), G132 (= G131), S133 (= S132), F157 (≠ W157), T159 (= T159), T210 (= T210), Y363 (= Y363), T366 (= T366), E368 (= E368), M372 (≠ L372)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
50% identity, 97% coverage: 5:375/382 of query aligns to 34:403/412 of P16219
- G90 (= G61) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E75) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 123:132, 70% identical) binding in other chain
- R171 (≠ V142) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (= WIT 157:159) binding in other chain
- A192 (= A164) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G181) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R269) binding FAD
- Q308 (= Q280) binding in other chain
- R325 (≠ L297) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (= S325) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QIHGG 337:341) binding FAD
- R380 (= R352) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (= TSE 366:368) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
8sgsA Human liver mitochondrial short-chain specific acyl-coa dehydrogenase (see paper)
50% identity, 97% coverage: 5:375/382 of query aligns to 4:373/381 of 8sgsA
- binding coenzyme a: S131 (= S132), A133 (= A134), N177 (≠ A179), F231 (= F233), M235 (= M237), L238 (= L240), I312 (≠ S314), E362 (= E364), G363 (= G365)
- binding flavin-adenine dinucleotide: F122 (= F123), L124 (= L125), S125 (≠ T126), G130 (= G131), S131 (= S132), W155 (= W157), T157 (= T159), R267 (= R269), F270 (= F272), L274 (≠ I276), L277 (≠ F279), Q335 (= Q337), I336 (= I338), G338 (= G340), G339 (= G341), I357 (= I359), I360 (= I362), Y361 (= Y363), T364 (= T366), E366 (= E368)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
50% identity, 97% coverage: 5:375/382 of query aligns to 7:376/385 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 (= M342), T347 (≠ K346), E348 (= E347)
- binding flavin-adenine dinucleotide: F125 (= F123), L127 (= L125), S128 (≠ T126), G133 (= G131), S134 (= S132), W158 (= W157), T160 (= T159), R270 (= R269), F273 (= F272), L280 (≠ F279), V282 (≠ M281), Q338 (= Q337), I339 (= I338), G342 (= G341), I360 (= I359), Y364 (= Y363), T367 (= T366), E369 (= E368), I370 (= I369), L373 (= L372)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
50% identity, 97% coverage: 5:375/382 of query aligns to 10:379/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (= F123), L130 (= L125), S131 (≠ T126), G136 (= G131), S137 (= S132), W161 (= W157), T163 (= T159), T214 (= T210), R273 (= R269), F276 (= F272), L280 (≠ I276), L283 (≠ F279), V285 (≠ M281), Q341 (= Q337), I342 (= I338), G345 (= G341), I363 (= I359), Y367 (= Y363), T370 (= T366), E372 (= E368), L376 (= L372)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
48% identity, 98% coverage: 1:376/382 of query aligns to 1:375/380 of 4l1fA
- active site: L125 (= L125), T126 (= T126), G242 (= G243), E363 (= E364), R375 (= R376)
- binding coenzyme a persulfide: T132 (≠ S132), H179 (≠ R180), F232 (= F233), M236 (= M237), E237 (≠ G238), L239 (= L240), D240 (= D241), R243 (= R244), Y362 (= Y363), E363 (= E364), G364 (= G365), R375 (= R376)
- binding flavin-adenine dinucleotide: F123 (= F123), L125 (= L125), T126 (= T126), G131 (= G131), T132 (≠ S132), F156 (≠ W157), I157 (= I158), T158 (= T159), R268 (= R269), Q270 (≠ A271), F271 (= F272), I275 (= I276), F278 (= F279), L281 (≠ T282), Q336 (= Q337), I337 (= I338), G340 (= G341), I358 (= I359), Y362 (= Y363), T365 (= T366), Q367 (≠ E368)
- binding 1,3-propandiol: L5 (≠ F5), Q10 (≠ L10)
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
50% identity, 97% coverage: 5:375/382 of query aligns to 1:363/371 of 2vigB
- active site: L121 (= L125), S122 (≠ T126), G231 (= G243), E352 (= E364)
- binding coenzyme a persulfide: S128 (= S132), F221 (= F233), M225 (= M237), Q226 (≠ G238), L228 (= L240), D229 (= D241), R232 (= R244), E352 (= E364), G353 (= G365), I357 (= I369)
- binding flavin-adenine dinucleotide: L121 (= L125), S122 (≠ T126), G127 (= G131), S128 (= S132), W152 (= W157), T154 (= T159), R257 (= R269), F260 (= F272), L264 (≠ I276), L267 (≠ F279), Q325 (= Q337), I326 (= I338), G329 (= G341), I347 (= I359), Y351 (= Y363), T354 (= T366), E356 (= E368)
Sites not aligning to the query:
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
46% identity, 98% coverage: 1:375/382 of query aligns to 1:373/378 of 5ol2F
- active site: L124 (= L125), T125 (= T126), G241 (= G243)
- binding calcium ion: E29 (≠ H30), E33 (≠ T34), R35 (≠ E36)
- binding coenzyme a persulfide: L238 (= L240), R242 (= R244), E362 (= E364), G363 (= G365)
- binding flavin-adenine dinucleotide: F122 (= F123), L124 (= L125), T125 (= T126), P127 (= P128), T131 (≠ S132), F155 (≠ W157), I156 (= I158), T157 (= T159), E198 (= E200), R267 (= R269), F270 (= F272), L274 (≠ I276), F277 (= F279), Q335 (= Q337), L336 (≠ I338), G338 (= G340), G339 (= G341), Y361 (= Y363), T364 (= T366), E366 (= E368)
Sites not aligning to the query:
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
47% identity, 97% coverage: 6:376/382 of query aligns to 3:370/374 of 5lnxD
- active site: L122 (= L125), T123 (= T126), G239 (= G243), E358 (= E364), K370 (≠ R376)
- binding flavin-adenine dinucleotide: L122 (= L125), T123 (= T126), G128 (= G131), S129 (= S132), F153 (≠ W157), T155 (= T159), R265 (= R269), Q267 (≠ A271), F268 (= F272), I272 (= I276), N275 (≠ F279), I278 (≠ T282), Q331 (= Q337), I332 (= I338), G335 (= G341), Y357 (= Y363), T360 (= T366), E362 (= E368)
4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
47% identity, 98% coverage: 2:377/382 of query aligns to 1:375/376 of 4m9aB
- active site: L124 (= L125), T125 (= T126), G241 (= G243), E362 (= E364), R374 (= R376)
- binding dihydroflavine-adenine dinucleotide: F122 (= F123), T125 (= T126), G130 (= G131), S131 (= S132), F155 (≠ W157), T157 (= T159), T208 (= T210), Y361 (= Y363), T364 (= T366), E366 (= E368), M370 (≠ L372)
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
46% identity, 98% coverage: 1:373/382 of query aligns to 1:376/383 of 1bucA
- active site: L128 (= L125), T129 (= T126), G246 (= G243), E367 (= E364)
- binding acetoacetyl-coenzyme a: L96 (= L93), F126 (= F123), G134 (= G131), T135 (≠ S132), T162 (= T159), N182 (≠ A179), H183 (≠ R180), F236 (= F233), M240 (= M237), M241 (≠ G238), L243 (= L240), D244 (= D241), T317 (≠ S314), Y366 (= Y363), E367 (= E364), G368 (= G365)
- binding flavin-adenine dinucleotide: F126 (= F123), L128 (= L125), T129 (= T126), G134 (= G131), T135 (≠ S132), F160 (≠ W157), T162 (= T159), Y366 (= Y363), T369 (= T366), E371 (= E368), M375 (≠ L372)
Sites not aligning to the query:
Q06319 Acyl-CoA dehydrogenase, short-chain specific; Butyryl-CoA dehydrogenase; BCAD; SCAD; EC 1.3.8.1 from Megasphaera elsdenii (see paper)
46% identity, 98% coverage: 1:373/382 of query aligns to 1:376/383 of Q06319
- E367 (= E364) active site, Proton acceptor; mutation to Q: Loss of activity.
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
46% identity, 98% coverage: 5:377/382 of query aligns to 1:367/370 of 2dvlA
- active site: L121 (= L125), T122 (= T126), G233 (= G243), E354 (= E364), R366 (= R376)
- binding flavin-adenine dinucleotide: L121 (= L125), T122 (= T126), G127 (= G131), S128 (= S132), W152 (= W157), I153 (= I158), T154 (= T159), T356 (= T366), E358 (= E368)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
43% identity, 99% coverage: 1:377/382 of query aligns to 1:375/379 of 1ukwB
- active site: L124 (= L125), S125 (≠ T126), T241 (≠ G243), E362 (= E364), R374 (= R376)
- binding cobalt (ii) ion: D145 (= D146), H146 (≠ S148)
- binding flavin-adenine dinucleotide: F122 (= F123), L124 (= L125), S125 (≠ T126), G130 (= G131), S131 (= S132), W155 (= W157), S157 (≠ T159), K200 (= K202), L357 (≠ I359), Y361 (= Y363), E362 (= E364), T364 (= T366), E366 (= E368), L370 (= L372)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
43% identity, 99% coverage: 1:377/382 of query aligns to 1:375/379 of 1ukwA
- active site: L124 (= L125), S125 (≠ T126), T241 (≠ G243), E362 (= E364), R374 (= R376)
- binding flavin-adenine dinucleotide: F122 (= F123), L124 (= L125), S125 (≠ T126), G130 (= G131), S131 (= S132), W155 (= W157), S157 (≠ T159), L357 (≠ I359), Y361 (= Y363), E362 (= E364), T364 (= T366), E366 (= E368), L370 (= L372)
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
42% identity, 98% coverage: 4:377/382 of query aligns to 5:376/381 of 2jifA
- active site: L125 (= L125), S126 (≠ T126), G242 (= G243), E363 (= E364), K375 (≠ R376)
- binding coenzyme a persulfide: S132 (= S132), S134 (≠ A134), Y178 (≠ A179), Y232 (≠ F233), I236 (≠ M237), L239 (= L240), N240 (≠ D241), R243 (= R244), Y362 (= Y363), E363 (= E364), G364 (= G365), I368 (= I369)
- binding flavin-adenine dinucleotide: F123 (= F123), L125 (= L125), S126 (≠ T126), G131 (= G131), S132 (= S132), W156 (= W157), I157 (= I158), S158 (≠ T159), K201 (= K202), T209 (= T210), R268 (= R269), F271 (= F272), L275 (≠ I276), F278 (= F279), L281 (≠ T282), E336 (≠ Q337), W337 (≠ I338), G340 (= G341), N367 (≠ E368), I368 (= I369)
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)
42% identity, 98% coverage: 4:377/382 of query aligns to 56:427/432 of P45954
- V137 (≠ T85) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ I86) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 123:132, 50% identical) binding in other chain
- S183 (= S132) binding substrate
- WIS 207:209 (≠ WIT 157:159) binding in other chain
- S210 (= S160) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ A179) binding substrate
- L255 (≠ I205) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ F233) binding substrate
- NEGR 291:294 (≠ DAGR 241:244) binding substrate
- I316 (≠ V266) to V: in dbSNP:rs1131430
- R319 (= R269) binding FAD
- Q330 (= Q280) binding FAD
- EWMGG 387:391 (≠ QIHGG 337:341) binding FAD
- A416 (≠ T366) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ TSE 366:368) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
42% identity, 97% coverage: 5:375/382 of query aligns to 3:373/379 of 6fahD
- active site: L124 (= L125), T125 (= T126), G241 (= G243)
- binding flavin-adenine dinucleotide: F122 (= F123), L124 (= L125), T125 (= T126), R152 (≠ K154), F155 (≠ W157), T157 (= T159), E198 (= E200), R267 (= R269), Q269 (≠ A271), F270 (= F272), I274 (= I276), F277 (= F279), Q335 (= Q337), I336 (= I338), G339 (= G341), Y361 (= Y363), T364 (= T366), Q366 (≠ E368)
Sites not aligning to the query:
Query Sequence
>WP_057507944.1 NCBI__GCF_001431535.1:WP_057507944.1
MDFSFTEEQLMLQDVARRIAQEKIAPSAEHHDRTGEFPLANIQLLGENGLMGIEVPAEYG
GAGMDPIAYVLAMVEVAAGDAAHSTIMSVNNSLFCNGILTHGNEAQKQKYVRAIAEGTAI
GAFALTEPQSGSDATAMRCRAVKQADGSYVINGKKSWITSGPVAKYIVLFAMTDADKGAR
GISAFLIDTDNAGFGRGKTEPKLGIRASATCEIEFNDYVAQAEDLLGQEGEGFKIAMGVL
DAGRIGIASQAIGIARAAYEATLEYVKERKAFGAAIGTFQMTQAKIADMKCKLDAALLLT
LRAAWVKGEGKRFSNEAAIAKLTASEAAMWITHQAVQIHGGMGYSKEMPLERYFRDAKIT
EIYEGTSEIQRLVIARNETGLR
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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