SitesBLAST
Comparing WP_090445290.1 NCBI__GCF_900100495.1:WP_090445290.1 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)
5ez3B Crystal structure acyl-coa dehydrogenase from brucella melitensis in complex with fad
50% identity, 95% coverage: 8:531/549 of query aligns to 1:524/541 of 5ez3B
- active site: M181 (= M185), T182 (= T186), T295 (= T303), E423 (= E430), R435 (= R442)
- binding flavin-adenine dinucleotide: M181 (= M185), T182 (= T186), G186 (= G190), G187 (= G191), T188 (= T192), F213 (= F221), S215 (= S223), R321 (= R329), F324 (≠ G332), L328 (= L336), Q331 (= Q339), M334 (= M342), E396 (= E403), C397 (= C404), G399 (= G406), G400 (= G407), W422 (= W429), E423 (= E430), S425 (= S432), N427 (= N434), L431 (= L438)
3u33A Crystal structure of the e. Coli adaptive response protein aidb in the space group p3(2) (see paper)
48% identity, 87% coverage: 8:483/549 of query aligns to 4:479/540 of 3u33A
- active site: M184 (= M185), T185 (= T186), T298 (= T303), E425 (= E430), R437 (= R442)
- binding flavin-adenine dinucleotide: M182 (= M183), M184 (= M185), T185 (= T186), G190 (= G191), S191 (≠ T192), F216 (= F221), S218 (= S223), R324 (= R329), F327 (≠ G332), L331 (= L336), Q334 (= Q339), M337 (= M342), E398 (= E403), V399 (≠ C404), G401 (= G406), G402 (= G407), W424 (= W429), G426 (= G431), S427 (= S432), N429 (= N434), L433 (= L438)
P33224 Putative acyl-CoA dehydrogenase AidB; EC 1.3.99.- from Escherichia coli (strain K12) (see paper)
48% identity, 87% coverage: 8:483/549 of query aligns to 4:479/541 of P33224
- 182:191 (vs. 183:192, 80% identical) binding FAD
- T185 (= T186) binding FAD
- S191 (≠ T192) binding FAD
- FFS 216:218 (≠ FCS 221:223) binding FAD
- S218 (= S223) binding FAD
- 423:433 (vs. 428:438, 73% identical) binding FAD
- N429 (= N434) binding FAD
- R437 (= R442) mutation to Q: Does not affect DNA binding affinity.
Sites not aligning to the query:
- 518 R→Q: Reduces DNA binding affinity.
6sdaB Bd2924 c10 acyl-coenzymea bound form (see paper)
35% identity, 70% coverage: 65:447/549 of query aligns to 57:444/503 of 6sdaB
- active site: M171 (= M185), T172 (= T186), T296 (= T303), R439 (= R442)
- binding flavin-adenine dinucleotide: Q169 (≠ M183), M171 (= M185), T172 (= T186), G177 (= G191), S178 (≠ T192), F208 (= F221), T209 (≠ C222), R322 (= R329), F325 (≠ G332), L329 (= L336), H332 (≠ Q339), E400 (= E403), M401 (≠ C404), G404 (= G407), Y407 (= Y410), W426 (= W429), T429 (≠ S432), N431 (= N434), L435 (= L438)
- binding decanoyl-CoA: C128 (= C135), G177 (= G191), S178 (≠ T192), S230 (vs. gap), V286 (= V293), A290 (≠ I297), L293 (≠ V300), N294 (≠ A301), R297 (= R304), R377 (= R380), W426 (= W429), E427 (= E430)
6sd8X Bd2924 apo-form (see paper)
35% identity, 70% coverage: 65:447/549 of query aligns to 57:444/503 of 6sd8X
- active site: M171 (= M185), T172 (= T186), T296 (= T303), R439 (= R442)
- binding flavin-adenine dinucleotide: Q169 (≠ M183), M171 (= M185), T172 (= T186), G176 (= G190), G177 (= G191), S178 (≠ T192), F208 (= F221), T209 (≠ C222), R322 (= R329), F325 (≠ G332), L329 (= L336), H332 (≠ Q339), M401 (≠ C404), G404 (= G407), W426 (= W429), T429 (≠ S432), V432 (= V435), L435 (= L438)
4y9jB Crystal structure of caenorhabditis elegans acdh-11 in complex with c11-coa (see paper)
30% identity, 90% coverage: 18:512/549 of query aligns to 32:514/593 of 4y9jB
- active site: M190 (= M185), T191 (= T186), T315 (= T303), E446 (= E430), R458 (= R442)
- binding flavin-adenine dinucleotide: Q188 (≠ M183), M190 (= M185), T191 (= T186), G196 (= G191), S197 (≠ T192), F223 (= F221), S224 (≠ C222), S225 (= S223), R341 (= R329), V343 (= V331), F344 (≠ G332), Q348 (≠ L336), E419 (= E403), C420 (= C404), G422 (= G406), G423 (= G407), Y426 (= Y410), W445 (= W429), T448 (≠ S432), V451 (= V435), L454 (= L438)
- binding S-{(3S,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} undecanethioate: S143 (≠ G134), A147 (≠ T138), Q188 (≠ M183), S197 (≠ T192), S249 (≠ D237), R303 (= R291), V305 (= V293), S309 (≠ I297), L312 (≠ V300), N313 (≠ A301), R316 (= R304), A322 (≠ G310), R396 (= R380), W445 (= W429), E446 (= E430), V451 (= V435), R458 (= R442)
Q9XWZ2 Acyl-CoA dehydrogenase family member 11; EC 1.3.99.- from Caenorhabditis elegans (see paper)
30% identity, 90% coverage: 18:512/549 of query aligns to 50:532/617 of Q9XWZ2
- E91 (≠ N66) mutation to K: In n5655; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- S156 (≠ A129) mutation to F: In n5657; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G158 (≠ A131) mutation to R: In n5661; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G214 (= G191) mutation to E: In n5879; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G443 (= G409) mutation to R: In n5877; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- R455 (= R421) mutation to H: In n5876; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
25% identity, 48% coverage: 183:444/549 of query aligns to 120:375/378 of 7p9xA
- binding 1-monoenoyl-CoA: S129 (≠ T192), L131 (≠ V194), K176 (≠ R238), F229 (≠ V293), M233 (≠ I297), L236 (≠ V300), R240 (= R304), Y360 (≠ W429), T361 (≠ E430), G362 (= G431), R373 (= R442)
- binding flavin-adenine dinucleotide: A122 (≠ M185), T123 (= T186), G128 (= G191), S129 (≠ T192), F153 (= F221), I154 (≠ C222), T155 (≠ S223), N206 (≠ S273), L356 (≠ V425), Y360 (≠ W429), T363 (≠ S432), Q365 (≠ N434), I366 (≠ V435)
Sites not aligning to the query:
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
25% identity, 48% coverage: 183:444/549 of query aligns to 122:377/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (≠ T192), L133 (≠ V194), K178 (≠ R238), F231 (≠ V293), M235 (≠ I297), L238 (≠ V300), N241 (≠ T303), R242 (= R304), Y362 (≠ W429), T363 (≠ E430), G364 (= G431), R375 (= R442)
- binding flavin-adenine dinucleotide: L122 (≠ M183), A124 (≠ M185), T125 (= T186), G130 (= G191), S131 (≠ T192), F155 (= F221), I156 (≠ C222), T157 (≠ S223), K200 (= K265), N208 (≠ S273), L358 (≠ V425), T365 (≠ S432), Q367 (≠ N434), I368 (≠ V435)
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)
24% identity, 53% coverage: 157:449/549 of query aligns to 148:455/591 of A3SI50
- M161 (= M183) mutation to A: Retains 37% of wild-type activity.
- T170 (= T192) mutation to A: Retains 8.8% of wild-type activity.
- F195 (= F221) mutation to A: Almost completely abolishes the activity.
- S197 (= S223) mutation to A: Retains 3.6% of wild-type activity.
- K223 (≠ R238) mutation to A: Retains 9.4% of wild-type activity.
- H280 (≠ G290) mutation to A: Retains 18% of wild-type activity.
- K281 (≠ R291) mutation to A: Retains 54% of wild-type activity.
- R284 (≠ P294) mutation to A: Retains 97% of wild-type activity.
- F287 (≠ I297) mutation to A: Retains 76% of wild-type activity.
- Y434 (≠ W429) mutation to A: Retains 51% of wild-type activity.
- E435 (= E430) mutation to A: Loss of activity.
- R448 (= R442) mutation to A: Retains 44% of wild-type activity.
8sgrA Human liver mitochondrial isovaleryl-coa dehydrogenase (see paper)
25% identity, 53% coverage: 157:447/549 of query aligns to 119:391/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ T186), G140 (= G191), S141 (≠ T192), W165 (= W220), T167 (≠ C222), R279 (= R329), F282 (≠ G332), I286 (≠ L336), F289 (≠ Q339), Q347 (≠ E403), C348 (= C404), G351 (= G407), L369 (≠ V425), G375 (= G431), T376 (≠ S432), L382 (= L438)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
25% identity, 53% coverage: 157:447/549 of query aligns to 115:387/387 of 1ivhA
- active site: M130 (= M185), S131 (≠ T186), E249 (≠ T303), A370 (≠ E430), R382 (= R442)
- binding coenzyme a persulfide: S137 (≠ T192), S185 (vs. gap), R186 (= R238), V239 (= V293), Y240 (≠ P294), M243 (≠ I297), E249 (≠ T303), R250 (= R304), G369 (≠ W429), A370 (≠ E430), G371 (= G431), V375 (= V435)
- binding flavin-adenine dinucleotide: L128 (≠ M183), M130 (= M185), S131 (≠ T186), G136 (= G191), S137 (≠ T192), W161 (= W220), T163 (≠ C222), R275 (= R329), F278 (≠ G332), F285 (≠ Q339), M288 (= M342), Q343 (≠ E403), C344 (= C404), G347 (= G407), T372 (≠ S432), E374 (≠ N434)
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)
25% identity, 53% coverage: 157:447/549 of query aligns to 152:424/426 of P26440
- 165:174 (vs. 183:192, 40% identical) binding FAD
- S174 (≠ T192) binding substrate
- WIT 198:200 (≠ WFC 220:222) binding FAD
- SR 222:223 (≠ -R 238) binding substrate
- G250 (≠ S270) to A: in IVA; uncertain significance
- Y277 (≠ P294) binding substrate
- DLER 284:287 (≠ ALTR 301:304) binding substrate
- E286 (≠ T303) 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 (≠ M308) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R329) binding FAD
- Q323 (≠ P340) binding FAD
- I379 (≠ A402) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ ECMGG 403:407) binding FAD
- R398 (= R421) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ N426) to N: in IVA; uncertain significance
- A407 (≠ E430) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ EG 430:431) binding substrate
- TSE 409:411 (≠ SGN 432:434) binding FAD
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
23% identity, 62% coverage: 107:444/549 of query aligns to 53:378/380 of 2pg0A
- active site: M124 (= M185), T125 (= T186), E243 (≠ T303), A364 (≠ E430), R376 (= R442)
- binding flavin-adenine dinucleotide: I122 (≠ M183), M124 (= M185), T125 (= T186), G130 (= G191), S131 (≠ T192), F155 (= F221), I156 (≠ C222), T157 (≠ S223), R269 (= R329), F272 (≠ G332), F279 (≠ Q339), Q337 (≠ E403), L338 (≠ C404), G340 (= G406), G341 (= G407), V359 (= V425), I362 (≠ T428), Y363 (≠ W429), T366 (≠ S432), E368 (≠ N434), M369 (≠ V435)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
28% identity, 48% coverage: 177:440/549 of query aligns to 118:375/384 of 1jqiA
- binding acetoacetyl-coenzyme a: F125 (≠ M183), S134 (≠ T192), F234 (≠ V293), M238 (≠ I297), Q239 (≠ E298), L241 (≠ V300), D242 (≠ A301), R245 (= R304), Y364 (≠ W429), E365 (= E430), G366 (= G431)
- binding flavin-adenine dinucleotide: F125 (≠ M183), L127 (≠ M185), S128 (≠ T186), G133 (= G191), S134 (≠ T192), W158 (= W220), T160 (≠ C222), R270 (= R334), F273 (≠ S337), L280 (≠ M342), Q338 (≠ E403), I339 (≠ C404), G342 (= G407), I360 (≠ V425), T367 (≠ S432), E369 (≠ N434), I370 (≠ V435)
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)
28% identity, 48% coverage: 177:440/549 of query aligns to 145:402/412 of P15651
- 152:161 (vs. 183:192, 30% identical) binding FAD
- S161 (≠ T192) binding substrate
- WIT 185:187 (≠ WFC 220:222) binding FAD
- DMGR 269:272 (≠ ALTR 301:304) binding substrate
- R297 (= R334) binding FAD
- QILGG 365:369 (≠ ECMGG 403:407) binding FAD
- E392 (= E430) active site, Proton acceptor
- TSE 394:396 (≠ SGN 432:434) binding FAD
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
25% identity, 48% coverage: 183:447/549 of query aligns to 123:380/380 of 4l1fA
- active site: L125 (≠ M185), T126 (= T186), G242 (≠ T303), E363 (= E430), R375 (= R442)
- binding coenzyme a persulfide: T132 (= T192), H179 (vs. gap), F232 (≠ V293), M236 (≠ I297), E237 (= E298), L239 (≠ V300), D240 (≠ A301), R243 (= R304), Y362 (≠ W429), E363 (= E430), G364 (= G431), R375 (= R442)
- binding flavin-adenine dinucleotide: F123 (≠ M183), L125 (≠ M185), T126 (= T186), G131 (= G191), T132 (= T192), F156 (= F221), I157 (≠ C222), T158 (≠ S223), R268 (= R329), Q270 (≠ V331), F271 (≠ G332), I275 (≠ L336), F278 (≠ Q339), L281 (≠ M342), Q336 (≠ E403), I337 (≠ C404), G340 (= G407), I358 (≠ V425), Y362 (≠ W429), T365 (≠ S432), Q367 (≠ N434)
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)
27% identity, 48% coverage: 177:440/549 of query aligns to 145:402/412 of P16219
- 152:161 (vs. 183:192, 30% identical) binding in other chain
- R171 (≠ Y202) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ WFC 220:222) binding in other chain
- A192 (≠ C227) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G239) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R329) binding FAD
- Q308 (≠ P340) binding in other chain
- R325 (≠ L357) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ C391) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ ECMGG 403:407) binding FAD
- R380 (= R418) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ SGN 432:434) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
- 90 G → S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- 104 natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
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)
25% identity, 51% coverage: 163:444/549 of query aligns to 94:367/369 of 3pfdC
- active site: L116 (≠ M185), S117 (≠ T186), T233 (= T303), E353 (= E430), R365 (= R442)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ M183), L116 (≠ M185), S117 (≠ T186), G122 (= G191), S123 (≠ T192), W147 (= W220), I148 (≠ F221), T149 (≠ C222), R259 (= R329), F262 (≠ G332), V266 (≠ L336), N269 (≠ Q339), Q326 (≠ E403), L327 (≠ C404), G330 (= G407), I348 (≠ V425), Y352 (≠ W429), T355 (≠ S432), Q357 (≠ N434)
8sgsA Human liver mitochondrial short-chain specific acyl-coa dehydrogenase (see paper)
27% identity, 48% coverage: 177:440/549 of query aligns to 115:372/381 of 8sgsA
- binding coenzyme a: S131 (≠ T192), A133 (≠ V194), N177 (vs. gap), F231 (≠ V293), M235 (≠ I297), L238 (≠ V300), I312 (≠ Q374), E362 (= E430), G363 (= G431)
- binding flavin-adenine dinucleotide: F122 (≠ M183), L124 (≠ M185), S125 (≠ T186), G130 (= G191), S131 (≠ T192), W155 (= W220), T157 (≠ C222), R267 (= R329), F270 (≠ G332), L274 (= L336), L277 (≠ Q339), Q335 (≠ E403), I336 (≠ C404), G338 (= G406), G339 (= G407), I357 (≠ V425), I360 (≠ T428), Y361 (≠ W429), T364 (≠ S432), E366 (≠ N434)
Query Sequence
>WP_090445290.1 NCBI__GCF_900100495.1:WP_090445290.1
MQPNLLAETHEVFNQVPPLDDVNLYRIDLPLQEWTRRFGGDWAEARIDAYGALAGGELMA
AGFLANENKPVFKSHDRFGHRIDLVEFHPAYHQLMSAAIEHGIPSMPWTAPRPGAQVARA
AMSYLHSQAEAGSGCPLTMTYASVPALKLQPDIAALWLPKILSREYDPRNLPIEQKNGAT
IGMAMTEKQGGTDVRANTTRAYPVGAPGPGQAYELVGHKWFCSAPMCDAFLTLAYTDRGL
TCFLLPRHRPDGTRNQFYIQRLKNKLGNWSNASSEVEYRGALAWMIGEEGRGVPTIIEMV
ALTRFDCMVGSSALMRQALTQAAHHCAYRQVGGRVLSEQPLMQNVLADLALESEAALALT
MRLGQALDNAHEQQEDKFARLVTAVGKYWICKRAPAMINEAAECMGGAGYVEDSILPRLY
REAPVNSTWEGSGNVQCLDVLRALSKEPGVLDALFNELGDGHGDARLKAHIQRLQADFRD
SAEIQYRARQLTEDVALALQAKLLLEAGNATVSDAFIASRLGEGGRVYGTLPRGVDVTAL
VARSMPQLG
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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