SitesBLAST
Comparing WP_009123484.1 NCBI__GCF_000195635.1:WP_009123484.1 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)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
32% identity, 65% coverage: 92:462/567 of query aligns to 39:380/380 of 4l1fA
- active site: L125 (= L175), T126 (= T176), G242 (≠ A292), E363 (= E437), R375 (= R449)
- binding coenzyme a persulfide: T132 (≠ S182), H179 (≠ R231), F232 (≠ L281), M236 (= M286), E237 (≠ A287), L239 (≠ M289), D240 (≠ N290), R243 (= R293), Y362 (= Y436), E363 (= E437), G364 (= G438), R375 (= R449)
- binding flavin-adenine dinucleotide: F123 (≠ M173), L125 (= L175), T126 (= T176), G131 (= G181), T132 (≠ S182), F156 (= F208), I157 (= I209), T158 (= T210), R268 (= R318), Q270 (= Q320), F271 (= F321), I275 (= I325), F278 (= F328), L281 (≠ V331), Q336 (= Q410), I337 (= I411), G340 (= G414), I358 (= I432), Y362 (= Y436), T365 (= T439), Q367 (= Q441)
Sites not aligning to the query:
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
34% identity, 63% coverage: 93:451/567 of query aligns to 37:372/374 of 5lnxD
- active site: L122 (= L175), T123 (= T176), G239 (≠ A292), E358 (= E437), K370 (≠ R449)
- binding flavin-adenine dinucleotide: L122 (= L175), T123 (= T176), G128 (= G181), S129 (= S182), F153 (= F208), T155 (= T210), R265 (= R318), Q267 (= Q320), F268 (= F321), I272 (= I325), N275 (≠ F328), I278 (≠ V331), Q331 (= Q410), I332 (= I411), G335 (= G414), Y357 (= Y436), T360 (= T439), E362 (≠ Q441)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
33% identity, 62% coverage: 93:443/567 of query aligns to 39:368/378 of 5ol2F
- active site: L124 (= L175), T125 (= T176), G241 (≠ A292)
- binding coenzyme a persulfide: L238 (≠ M289), R242 (= R293), E362 (= E437), G363 (= G438)
- binding flavin-adenine dinucleotide: F122 (≠ M173), L124 (= L175), T125 (= T176), P127 (= P178), T131 (≠ S182), F155 (= F208), I156 (= I209), T157 (= T210), E198 (= E251), R267 (= R318), F270 (= F321), L274 (≠ I325), F277 (= F328), Q335 (= Q410), L336 (≠ I411), G338 (= G413), G339 (= G414), Y361 (= Y436), T364 (= T439), E366 (≠ Q441)
Sites not aligning to the query:
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
32% identity, 68% coverage: 64:449/567 of query aligns to 23:376/378 of 4n5fA
- active site: L126 (= L175), T127 (= T176), G243 (≠ A292), E364 (= E437), R376 (= R449)
- binding dihydroflavine-adenine dinucleotide: L126 (= L175), T127 (= T176), G132 (= G181), S133 (= S182), F157 (= F208), T159 (= T210), T210 (= T261), Y363 (= Y436), T366 (= T439), E368 (≠ Q441), M372 (≠ V445)
4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
32% identity, 70% coverage: 54:449/567 of query aligns to 11:374/376 of 4m9aB
- active site: L124 (= L175), T125 (= T176), G241 (≠ A292), E362 (= E437), R374 (= R449)
- binding dihydroflavine-adenine dinucleotide: F122 (≠ M173), T125 (= T176), G130 (= G181), S131 (= S182), F155 (= F208), T157 (= T210), T208 (= T261), Y361 (= Y436), T364 (= T439), E366 (≠ Q441), M370 (≠ V445)
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
31% identity, 62% coverage: 92:443/567 of query aligns to 39:373/383 of 1bucA
- active site: L128 (= L175), T129 (= T176), G246 (≠ A292), E367 (= E437)
- binding acetoacetyl-coenzyme a: L96 (≠ D144), F126 (≠ M173), G134 (= G181), T135 (≠ S182), T162 (= T210), N182 (≠ G230), H183 (≠ R231), F236 (≠ L281), M240 (= M286), M241 (≠ A287), L243 (≠ M289), D244 (≠ N290), T317 (≠ S383), Y366 (= Y436), E367 (= E437), G368 (= G438)
- binding flavin-adenine dinucleotide: F126 (≠ M173), L128 (= L175), T129 (= T176), G134 (= G181), T135 (≠ S182), F160 (= F208), T162 (= T210), Y366 (= Y436), T369 (= T439), E371 (≠ Q441)
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)
31% identity, 62% coverage: 92:443/567 of query aligns to 39:373/383 of Q06319
- E367 (= E437) active site, Proton acceptor; mutation to Q: Loss of activity.
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
32% identity, 62% coverage: 95:443/567 of query aligns to 41:368/379 of 6fahD
- active site: L124 (= L175), T125 (= T176), G241 (≠ A292)
- binding flavin-adenine dinucleotide: F122 (≠ M173), L124 (= L175), T125 (= T176), R152 (≠ V205), F155 (= F208), T157 (= T210), E198 (= E251), R267 (= R318), Q269 (= Q320), F270 (= F321), I274 (= I325), F277 (= F328), Q335 (= Q410), I336 (= I411), G339 (= G414), Y361 (= Y436), T364 (= T439), Q366 (= Q441)
Sites not aligning to the query:
A3SI50 3-methylmercaptopropionyl-CoA dehydrogenase; MMPA-CoA dehydrogenase; EC 1.3.99.41 from Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM) (see paper)
30% identity, 70% coverage: 49:445/567 of query aligns to 35:443/591 of A3SI50
- M161 (= M173) mutation to A: Retains 37% of wild-type activity.
- T170 (≠ S182) mutation to A: Retains 8.8% of wild-type activity.
- F195 (= F208) mutation to A: Almost completely abolishes the activity.
- S197 (≠ T210) mutation to A: Retains 3.6% of wild-type activity.
- K223 (≠ R231) mutation to A: Retains 9.4% of wild-type activity.
- H280 (≠ K278) mutation to A: Retains 18% of wild-type activity.
- K281 (≠ L279) mutation to A: Retains 54% of wild-type activity.
- R284 (≠ K283) mutation to A: Retains 97% of wild-type activity.
- F287 (≠ M286) mutation to A: Retains 76% of wild-type activity.
- Y434 (= Y436) mutation to A: Retains 51% of wild-type activity.
- E435 (= E437) mutation to A: Loss of activity.
Sites not aligning to the query:
- 448 R→A: Retains 44% of wild-type activity.
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
33% identity, 63% coverage: 94:449/567 of query aligns to 37:366/370 of 2dvlA
- active site: L121 (= L175), T122 (= T176), G233 (≠ A292), E354 (= E437), R366 (= R449)
- binding flavin-adenine dinucleotide: L121 (= L175), T122 (= T176), G127 (= G181), S128 (= S182), W152 (≠ F208), I153 (= I209), T154 (= T210), T356 (= T439), E358 (≠ Q441)
6es9A Methylsuccinyl-coa dehydrogenase of paracoccus denitrificans with bound flavin adenine dinucleotide (see paper)
32% identity, 62% coverage: 95:443/567 of query aligns to 199:535/545 of 6es9A
- active site: F281 (vs. gap), T282 (= T176), A408 (= A292)
- binding coenzyme a: F467 (≠ Q351), W470 (≠ R354)
- binding flavin-adenine dinucleotide: A279 (≠ D174), F281 (vs. gap), T282 (= T176), G287 (= G181), S288 (= S182), W312 (≠ F208), I313 (= I209), T314 (= T210), E374 (≠ T261), R434 (= R318), Q436 (= Q320), F437 (= F321), L441 (≠ I325), F444 (= F328), Q502 (= Q410), I503 (= I411), G505 (= G413), G506 (= G414), F528 (≠ Y436), A531 (≠ T439), E533 (≠ Q441), I534 (≠ L442)
Sites not aligning to the query:
7w0jE Acyl-coa dehydrogenase, tfu_1647
34% identity, 52% coverage: 153:449/567 of query aligns to 103:378/382 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 (≠ T176), W157 (≠ F208), R270 (= R318), Q272 (= Q320), F273 (= F321), I277 (= I325), F280 (= F328), I283 (≠ V331), Q339 (= Q410), L340 (≠ I411), G343 (= G414), Y365 (= Y436), E366 (= E437), T368 (= T439), Q370 (= Q441), I371 (≠ L442)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
34% identity, 52% coverage: 153:449/567 of query aligns to 102:377/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S182), T134 (≠ L184), R180 (= R231), R234 (≠ K283), L237 (≠ M286), R238 (≠ A287), L240 (≠ M289), D241 (≠ N290), R244 (= R293), E365 (= E437), G366 (= G438), R377 (= R449)
- binding flavin-adenine dinucleotide: Y123 (≠ M173), L125 (= L175), S126 (≠ T176), G131 (= G181), S132 (= S182), W156 (≠ F208), I157 (= I209), T158 (= T210), I360 (= I432), T367 (= T439), Q369 (= Q441)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
34% identity, 52% coverage: 153:449/567 of query aligns to 102:377/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ M173), L125 (= L175), S126 (≠ T176), G131 (= G181), S132 (= S182), W156 (≠ F208), I157 (= I209), T158 (= T210), I360 (= I432), Y364 (= Y436), T367 (= T439), Q369 (= Q441)
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)
31% identity, 68% coverage: 66:449/567 of query aligns to 16:365/369 of 3pfdC
- active site: L116 (= L175), S117 (≠ T176), T233 (≠ A292), E353 (= E437), R365 (= R449)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ M173), L116 (= L175), S117 (≠ T176), G122 (= G181), S123 (= S182), W147 (≠ F208), I148 (= I209), T149 (= T210), R259 (= R318), F262 (= F321), V266 (≠ I325), N269 (≠ F328), Q326 (= Q410), L327 (≠ I411), G330 (= G414), I348 (= I432), Y352 (= Y436), T355 (= T439), Q357 (= Q441)
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
30% identity, 68% coverage: 64:446/567 of query aligns to 23:374/381 of 2jifA
- active site: L125 (= L175), S126 (≠ T176), G242 (≠ A292), E363 (= E437)
- binding coenzyme a persulfide: S132 (= S182), S134 (= S186), Y178 (≠ G230), Y232 (≠ L281), I236 (≠ M286), L239 (≠ M289), N240 (= N290), R243 (= R293), Y362 (= Y436), E363 (= E437), G364 (= G438), I368 (vs. gap)
- binding flavin-adenine dinucleotide: F123 (≠ M173), L125 (= L175), S126 (≠ T176), G131 (= G181), S132 (= S182), W156 (≠ F208), I157 (= I209), S158 (≠ T210), K201 (= K253), T209 (= T261), R268 (= R318), F271 (= F321), L275 (≠ I325), F278 (= F328), L281 (≠ V331), E336 (≠ Q410), W337 (≠ I411), G340 (= G414), N367 (vs. gap), I368 (vs. gap)
Sites not aligning to the query:
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)
30% identity, 68% coverage: 64:446/567 of query aligns to 74:425/432 of P45954
- V137 (≠ N138) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ I139) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 173:182, 50% identical) binding in other chain
- S183 (= S182) binding substrate
- WIS 207:209 (≠ FIT 208:210) binding in other chain
- S210 (≠ N211) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ G230) binding substrate
- L255 (≠ I256) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ L281) binding substrate
- NEGR 291:294 (≠ NGAR 290:293) binding substrate
- I316 (≠ A315) to V: in dbSNP:rs1131430
- R319 (= R318) binding FAD
- Q330 (≠ P329) binding FAD
- EWMGG 387:391 (≠ QIHGG 410:414) binding FAD
- A416 (≠ T439) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ TT- 439:440) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
Q9H845 Complex I assembly factor ACAD9, mitochondrial; Acyl-CoA dehydrogenase family member 9; ACAD-9; EC 1.3.8.- from Homo sapiens (Human) (see 4 papers)
30% identity, 66% coverage: 93:465/567 of query aligns to 96:455/621 of Q9H845
- R193 (≠ M188) to W: in MC1DN20; uncertain significance; dbSNP:rs377547811
- S234 (≠ K228) to F: in MC1DN20; uncertain significance
- G303 (≠ A292) to S: in MC1DN20; uncertain significance; dbSNP:rs143383023
- A326 (= A315) to T: in MC1DN20; uncertain significance; dbSNP:rs115532916
- E413 (≠ Q424) to K: in MC1DN20; uncertain significance; dbSNP:rs149753643
- E426 (= E437) mutation to Q: Loss of long-chain-acyl-CoA dehydrogenase activity. Does not affect mitochondrial complex I assembly.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
O53666 Broad-specificity linear acyl-CoA dehydrogenase FadE5; Long-chain-acyl-CoA dehydrogenase; Medium-chain-acyl-CoA dehydrogenase; Short-chain-acyl-CoA dehydrogenase; EC 1.3.8.8; EC 1.3.8.7; EC 1.3.8.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
31% identity, 62% coverage: 92:443/567 of query aligns to 81:453/611 of O53666
- MVLT 162:165 (≠ MDLT 173:176) binding FAD
- S171 (= S182) binding a 2,3-saturated acyl-CoA; binding FAD; mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- T198 (= T210) binding FAD
- TK 224:225 (≠ GR 230:231) binding a 2,3-saturated acyl-CoA
- K225 (≠ R231) mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- F294 (≠ M286) mutation to A: Increases affinity for eicosanoyl-CoA; when associated with A-447.
- R301 (= R293) binding a 2,3-saturated acyl-CoA; mutation to A: Increases affinity for eicosanoyl-CoA; when associated with A-447.
- R326 (= R318) binding FAD
- K338 (vs. gap) binding a 2,3-saturated acyl-CoA
- QTLGG 420:424 (≠ QIHGG 410:414) binding FAD
- E447 (= E437) binding a 2,3-saturated acyl-CoA; mutation to A: Loss of activity.
- T449 (= T439) binding FAD
Sites not aligning to the query:
- 456 binding a 2,3-saturated acyl-CoA
- 460 R→A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- 460:461 binding a 2,3-saturated acyl-CoA
8pheA Acad9-wt in complex with ecsit-cter (see paper)
31% identity, 62% coverage: 93:442/567 of query aligns to 59:394/551 of 8pheA
- binding : L143 (= L175), D151 (= D183), A153 (≠ Q185), S154 (= S186), I155 (≠ V187), K202 (vs. gap), I205 (≠ L233), F256 (≠ L281), M260 (= M286), F295 (= F321), N296 (≠ G322), I394 (≠ L442)
Sites not aligning to the query:
Query Sequence
>WP_009123484.1 NCBI__GCF_000195635.1:WP_009123484.1
MANFYTEIPELKYHLNNPMMERICELKERGYQDKDKYDYAPQDYADAMDSFDKVLEITGE
ITGEIIAPNAEGVDEEGPHCANGRVEYASGTKQNLDAMVKAGLNGMTMPRRFGGLNFPIT
PYTMCAEIVAAADAGFGNIWSLQDCIETLYEFGNEDQHSRFIPRICQGETMSMDLTEPDA
GSDLQSVMLKATFDEANNCWRLNGVKRFITNGDANLHLVLARSEEGTKDGRGLSMFIYDK
NEGGVDVRRIENKLGIHGSPTCELVYKNAKAELCGDRKLGLIKYVMALMNGARLGIAAQS
VGLSQAAYNEGLAYAKDRKQFGKAIIEFPAVYDMLAIMKAKLDAGRSLLYQTSRYVDIYK
ALDDISRERKLTPEERQEQKKYSKLADAFTPLAKGMNSEYANQNAYDSIQIHGGSGFMLE
YACQRIYRDARITSIYEGTTQLQTVAAIRYVTNGSYVATLRDYEMIPCSAEMQPLMERVK
EMANKLDACTNAVKEAQNQELLDFLSRRLYEMAAVCIMSHLIIQDATRAPELFAKSALVY
VNYAEAEVEKHFNFIRKFKAEELESYR
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