SitesBLAST
Comparing GFF534 FitnessBrowser__psRCH2:GFF534 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
51% identity, 96% coverage: 8:531/548 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)
49% identity, 84% coverage: 8:466/548 of query aligns to 4:461/540 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)
49% identity, 84% coverage: 8:466/548 of query aligns to 4:461/541 of P33224
- 182:191 (vs. 183:192, 80% identical) binding
- T185 (= T186) binding
- S191 (≠ T192) binding
- FFS 216:218 (≠ FCS 221:223) binding
- S218 (= S223) binding
- 423:433 (vs. 428:438, 82% identical) binding
- N429 (= N434) binding
- 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)
33% identity, 78% coverage: 22:447/548 of query aligns to 10:444/503 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 (≠ S301), R297 (= R304), R377 (= R380), W426 (= W429), E427 (= E430)
6sd8X Bd2924 apo-form (see paper)
33% identity, 78% coverage: 22:447/548 of query aligns to 10:444/503 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, 85% coverage: 47:512/548 of query aligns to 54:514/593 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 (= S134), A147 (≠ T138), Q188 (≠ M183), S197 (≠ T192), S249 (≠ D237), R303 (= R291), V305 (= V293), S309 (≠ I297), L312 (≠ V300), N313 (≠ S301), 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, 85% coverage: 47:512/548 of query aligns to 72:532/617 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.
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)
26% identity, 56% coverage: 155:461/548 of query aligns to 146:467/591 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 (= K238) 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.
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
25% identity, 62% coverage: 107:444/548 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 (= I428), Y363 (≠ W429), T366 (≠ S432), E368 (≠ N434), M369 (≠ V435)
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
25% identity, 54% coverage: 151:444/548 of query aligns to 102:377/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (≠ T192), L133 (≠ V194), K178 (= K238), 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)
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
25% identity, 54% coverage: 151:444/548 of query aligns to 100:375/378 of 7p9xA
- binding 1-monoenoyl-CoA: S129 (≠ T192), L131 (≠ V194), K176 (= K238), 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:
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
28% identity, 48% coverage: 185:446/548 of query aligns to 121:370/370 of 2dvlA
- active site: L121 (≠ M185), T122 (= T186), G233 (≠ T303), E354 (= E430), R366 (= R442)
- binding flavin-adenine dinucleotide: L121 (≠ M185), T122 (= T186), G127 (= G191), S128 (≠ T192), W152 (= W220), I153 (≠ F221), T154 (≠ C222), T356 (≠ S432), E358 (≠ N434)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
28% identity, 48% coverage: 177:440/548 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
- 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 (≠ ECLGG 403:407) binding
- 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)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
28% identity, 48% coverage: 177:440/548 of query aligns to 118:375/385 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 (≠ A408), T347 (≠ E412), E348 (= E413)
- binding flavin-adenine dinucleotide: F125 (≠ M183), L127 (≠ M185), S128 (≠ T186), G133 (= G191), S134 (≠ T192), W158 (= W220), T160 (≠ C222), R270 (= R329), F273 (≠ G332), L280 (≠ Q339), V282 (≠ L341), Q338 (≠ E403), I339 (≠ C404), G342 (= G407), I360 (≠ V425), Y364 (≠ W429), T367 (≠ S432), E369 (≠ N434), I370 (≠ V435), L373 (= L438)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
28% identity, 48% coverage: 177:440/548 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 (≠ H374), 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 (= I428), Y361 (≠ W429), T364 (≠ S432), E366 (≠ N434)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
28% identity, 48% coverage: 177:440/548 of query aligns to 121:378/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ M183), L130 (≠ M185), S131 (≠ T186), G136 (= G191), S137 (≠ T192), W161 (= W220), T163 (≠ C222), T214 (≠ S273), R273 (= R329), F276 (≠ G332), L280 (= L336), L283 (≠ Q339), V285 (≠ L341), Q341 (≠ E403), I342 (≠ C404), G345 (= G407), I363 (≠ V425), Y367 (≠ W429), T370 (≠ S432), E372 (≠ N434), L376 (= L438)
Q3L887 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 Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
22% identity, 81% coverage: 40:482/548 of query aligns to 35:505/611 of Q3L887
- MVLT 162:165 (≠ MAMT 183:186) binding
- S171 (≠ T192) binding ; binding
- T198 (≠ S223) binding
- TK 224:225 (≠ -K 238) binding
- R301 (= R304) binding
- R326 (= R329) binding
- K338 (vs. gap) binding
- QTLGG 420:424 (≠ ECLGG 403:407) binding
- E447 (= E430) binding ; mutation to A: Loss of activity.
- T449 (≠ S432) binding
- D456 (= D439) binding
- RK 460:461 (vs. gap) binding
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
29% identity, 48% coverage: 178:440/548 of query aligns to 119:375/384 of 1jqiA
- binding acetoacetyl-coenzyme a: F125 (≠ M183), S134 (≠ T192), F234 (≠ V293), M238 (≠ I297), Q239 (≠ E298), L241 (≠ V300), D242 (≠ S301), 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 (≠ L337), 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)
29% identity, 48% coverage: 178:440/548 of query aligns to 146:402/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
25% identity, 47% coverage: 181:436/548 of query aligns to 120:368/379 of 6fahD
- active site: L124 (≠ M185), T125 (= T186), G241 (≠ T303)
- binding flavin-adenine dinucleotide: F122 (≠ M183), L124 (≠ M185), T125 (= T186), R152 (≠ H218), F155 (= F221), T157 (≠ S223), E198 (≠ K263), R267 (= R329), Q269 (≠ V331), F270 (≠ G332), I274 (≠ L336), F277 (≠ Q339), Q335 (≠ E403), I336 (≠ C404), G339 (= G407), Y361 (≠ W429), T364 (≠ S432), Q366 (≠ N434)
Sites not aligning to the query:
Query Sequence
>GFF534 FitnessBrowser__psRCH2:GFF534
MNLQTCAETHEVTNQVPPLDGANLYRIDLPLQQWVQRYHAGWAEDRLDRYGALAGGPLMQ
AGFLANENRPLFKSHDRYGHRIDLVEFHPAYHELMRAAVEHGIPSLPWSEPQPGAQVARA
ALMYLHNQAEAGSSCPLTMTYASVPALRLQPDLAERWLPKILAREYDPRNLPMEQKAGVT
IGMAMTEKQGGTDVRANSTRAYPVGAGGPGQAYELIGHKWFCSAPMCDAFLTLAQTDKGL
SCFLLPRHRPDGTRNQFYIQRLKNKLGNWANASSEVEYRGALAWMVGEDGRGVPTIIEMV
SSTRFDCMIGSSSLMRQALTQAMHHCAHRLVGGRVLLEQPLMQNVLADLALESEAALALT
LRMGRAQDNRHDEHEDKFARLVTAVGKYWICKRAPNMIAEASECLGGAGYVEETILPRLY
REAPVNSIWEGSGNVQCLDVLRALSKEPGVLEVLFTELGDGHGDARLKAHIQRLKVAFGD
TEDIQYRARQLTEDVAIGLQAKLLLEAGNAAVSDAFIASRLEGQGRVYGTLPRGLDIDAL
LARSAPQL
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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