SitesBLAST
Comparing GFF3397 FitnessBrowser__Marino:GFF3397 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)
3u33A Crystal structure of the e. Coli adaptive response protein aidb in the space group p3(2) (see paper)
46% identity, 92% coverage: 23:543/566 of query aligns to 5:521/540 of 3u33A
- active site: M184 (= M200), T185 (= T201), T298 (= T318), E425 (= E445), R437 (= R457)
- binding flavin-adenine dinucleotide: M182 (= M198), M184 (= M200), T185 (= T201), G190 (= G206), S191 (= S207), F216 (= F236), S218 (= S238), R324 (= R344), F327 (= F347), L331 (= L351), Q334 (= Q354), M337 (= M357), E398 (= E418), V399 (≠ C419), G401 (= G421), G402 (= G422), W424 (= W444), G426 (= G446), S427 (= S447), N429 (= N449), L433 (= L453)
P33224 Putative acyl-CoA dehydrogenase AidB; EC 1.3.99.- from Escherichia coli (strain K12) (see paper)
46% identity, 92% coverage: 23:543/566 of query aligns to 5:521/541 of P33224
- 182:191 (vs. 198:207, 90% identical) binding
- T185 (= T201) binding
- S191 (= S207) binding
- FFS 216:218 (≠ FVS 236:238) binding
- S218 (= S238) binding
- 423:433 (vs. 443:453, 82% identical) binding
- N429 (= N449) binding
- R437 (= R457) mutation to Q: Does not affect DNA binding affinity.
- R518 (≠ S540) mutation to Q: Reduces DNA binding affinity.
5ez3B Crystal structure acyl-coa dehydrogenase from brucella melitensis in complex with fad
45% identity, 96% coverage: 23:563/566 of query aligns to 2:539/541 of 5ez3B
- active site: M181 (= M200), T182 (= T201), T295 (= T318), E423 (= E445), R435 (= R457)
- binding flavin-adenine dinucleotide: M181 (= M200), T182 (= T201), G186 (= G205), G187 (= G206), T188 (≠ S207), F213 (= F236), S215 (= S238), R321 (= R344), F324 (= F347), L328 (= L351), Q331 (= Q354), M334 (= M357), E396 (= E418), C397 (= C419), G399 (= G421), G400 (= G422), W422 (= W444), E423 (= E445), S425 (= S447), N427 (= N449), L431 (= L453)
6sdaB Bd2924 c10 acyl-coenzymea bound form (see paper)
33% identity, 70% coverage: 80:473/566 of query aligns to 57:459/503 of 6sdaB
- active site: M171 (= M200), T172 (= T201), T296 (= T318), R439 (= R457)
- binding flavin-adenine dinucleotide: Q169 (≠ M198), M171 (= M200), T172 (= T201), G177 (= G206), S178 (= S207), F208 (= F236), T209 (≠ V237), R322 (= R344), F325 (= F347), L329 (= L351), H332 (≠ Q354), E400 (= E418), M401 (≠ C419), G404 (= G422), Y407 (≠ V425), W426 (= W444), T429 (≠ S447), N431 (= N449), L435 (= L453)
- binding decanoyl-CoA: C128 (= C150), G177 (= G206), S178 (= S207), S230 (vs. gap), V286 (= V308), A290 (≠ I312), L293 (≠ V315), N294 (≠ A316), R297 (= R319), R377 (= R395), W426 (= W444), E427 (= E445)
6sd8X Bd2924 apo-form (see paper)
33% identity, 70% coverage: 80:473/566 of query aligns to 57:459/503 of 6sd8X
- active site: M171 (= M200), T172 (= T201), T296 (= T318), R439 (= R457)
- binding flavin-adenine dinucleotide: Q169 (≠ M198), M171 (= M200), T172 (= T201), G176 (= G205), G177 (= G206), S178 (= S207), F208 (= F236), T209 (≠ V237), R322 (= R344), F325 (= F347), L329 (= L351), H332 (≠ Q354), M401 (≠ C419), G404 (= G422), W426 (= W444), T429 (≠ S447), V432 (= V450), L435 (= L453)
Q9XWZ2 Acyl-CoA dehydrogenase family member 11; EC 1.3.99.- from Caenorhabditis elegans (see paper)
29% identity, 84% coverage: 56:530/566 of query aligns to 67:569/617 of Q9XWZ2
- E91 (≠ N81) mutation to K: In n5655; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- S156 (≠ V144) mutation to F: In n5657; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G158 (≠ A146) mutation to R: In n5661; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G214 (= G206) mutation to E: In n5879; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G443 (= G424) mutation to R: In n5877; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- R455 (= R436) mutation to H: In n5876; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
4y9jB Crystal structure of caenorhabditis elegans acdh-11 in complex with c11-coa (see paper)
29% identity, 84% coverage: 56:530/566 of query aligns to 49:551/593 of 4y9jB
- active site: M190 (= M200), T191 (= T201), T315 (= T318), E446 (= E445), R458 (= R457)
- binding flavin-adenine dinucleotide: Q188 (≠ M198), M190 (= M200), T191 (= T201), G196 (= G206), S197 (= S207), F223 (= F236), S224 (≠ V237), S225 (= S238), R341 (= R344), V343 (≠ A346), F344 (= F347), Q348 (≠ L351), E419 (= E418), C420 (= C419), G422 (= G421), G423 (= G422), Y426 (≠ V425), W445 (= W444), T448 (≠ S447), V451 (= V450), L454 (= L453)
- 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 (≠ C149), A147 (≠ T153), Q188 (≠ M198), S197 (= S207), S249 (≠ Q252), R303 (= R306), V305 (= V308), S309 (≠ I312), L312 (≠ V315), N313 (≠ A316), R316 (= R319), A322 (≠ G325), R396 (= R395), W445 (= W444), E446 (= E445), V451 (= V450), R458 (= R457)
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)
25% identity, 52% coverage: 179:471/566 of query aligns to 146:463/591 of A3SI50
- M161 (= M198) mutation to A: Retains 37% of wild-type activity.
- T170 (≠ S207) mutation to A: Retains 8.8% of wild-type activity.
- F195 (= F236) mutation to A: Almost completely abolishes the activity.
- S197 (= S238) mutation to A: Retains 3.6% of wild-type activity.
- K223 (vs. gap) mutation to A: Retains 9.4% of wild-type activity.
- H280 (≠ G305) mutation to A: Retains 18% of wild-type activity.
- K281 (≠ R306) mutation to A: Retains 54% of wild-type activity.
- R284 (≠ P309) mutation to A: Retains 97% of wild-type activity.
- F287 (≠ I312) mutation to A: Retains 76% of wild-type activity.
- Y434 (≠ W444) mutation to A: Retains 51% of wild-type activity.
- E435 (= E445) mutation to A: Loss of activity.
- R448 (vs. gap) mutation to A: Retains 44% of wild-type activity.
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
27% identity, 49% coverage: 186:460/566 of query aligns to 110:377/380 of 2pg0A
- active site: M124 (= M200), T125 (= T201), E243 (≠ T318), A364 (≠ E445), R376 (≠ L459)
- binding flavin-adenine dinucleotide: I122 (≠ M198), M124 (= M200), T125 (= T201), G130 (= G206), S131 (= S207), F155 (= F236), I156 (≠ V237), T157 (≠ S238), R269 (= R344), F272 (= F347), F279 (≠ Q354), Q337 (≠ E418), L338 (≠ C419), G340 (= G421), G341 (= G422), V359 (= V440), I362 (= I443), Y363 (≠ W444), T366 (≠ S447), E368 (≠ Q451), M369 (≠ C452)
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
26% identity, 48% coverage: 191:459/566 of query aligns to 113:375/378 of 7p9xA
- binding 1-monoenoyl-CoA: S129 (= S207), L131 (≠ V209), K176 (≠ S253), F229 (≠ V308), M233 (≠ I312), L236 (≠ V315), R240 (= R319), Y360 (≠ W444), T361 (≠ E445), G362 (= G446), R373 (= R457)
- binding flavin-adenine dinucleotide: A122 (≠ M200), T123 (= T201), G128 (= G206), S129 (= S207), F153 (= F236), I154 (≠ V237), T155 (≠ S238), N206 (≠ S288), L356 (≠ V440), Y360 (≠ W444), T363 (≠ S447), Q365 (≠ N449), I366 (≠ V450)
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)
26% identity, 48% coverage: 191:459/566 of query aligns to 115:377/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (= S207), L133 (≠ V209), K178 (≠ S253), F231 (≠ V308), M235 (≠ I312), L238 (≠ V315), N241 (≠ T318), R242 (= R319), Y362 (≠ W444), T363 (≠ E445), G364 (= G446), R375 (= R457)
- binding flavin-adenine dinucleotide: L122 (≠ M198), A124 (≠ M200), T125 (= T201), G130 (= G206), S131 (= S207), F155 (= F236), I156 (≠ V237), T157 (≠ S238), K200 (= K280), N208 (≠ S288), L358 (≠ V440), T365 (≠ S447), Q367 (≠ N449), I368 (≠ V450)
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
26% identity, 46% coverage: 200:461/566 of query aligns to 121:370/370 of 2dvlA
- active site: L121 (≠ M200), T122 (= T201), G233 (≠ T318), E354 (= E445), R366 (= R457)
- binding flavin-adenine dinucleotide: L121 (≠ M200), T122 (= T201), G127 (= G206), S128 (= S207), W152 (= W235), I153 (≠ F236), T154 (≠ V237), T356 (≠ S447), E358 (≠ N449)
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)
23% identity, 66% coverage: 83:454/566 of query aligns to 63:456/611 of Q3L887
- MVLT 162:165 (≠ MAMT 198:201) binding
- S171 (= S207) binding ; binding
- T198 (≠ S238) binding
- TK 224:225 (≠ -S 253) binding
- R301 (= R319) binding
- R326 (≠ H340) binding
- K338 (≠ R344) binding
- QTLGG 420:424 (≠ ECIGG 418:422) binding
- E447 (= E445) binding ; mutation to A: Loss of activity.
- T449 (≠ S447) binding
- D456 (= D454) binding
Sites not aligning to the query:
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
25% identity, 45% coverage: 196:451/566 of query aligns to 120:368/379 of 6fahD
- active site: L124 (≠ M200), T125 (= T201), G241 (≠ T318)
- binding flavin-adenine dinucleotide: F122 (≠ M198), L124 (≠ M200), T125 (= T201), R152 (≠ H233), F155 (= F236), T157 (≠ S238), E198 (≠ K278), R267 (= R344), Q269 (≠ A346), F270 (= F347), I274 (≠ L351), F277 (≠ Q354), Q335 (≠ E418), I336 (≠ C419), G339 (= G422), Y361 (≠ W444), T364 (≠ S447), Q366 (≠ N449)
Sites not aligning to the query:
6ksbA Crystal structure of e447a m130g acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c16coa (see paper)
23% identity, 66% coverage: 83:454/566 of query aligns to 63:456/608 of 6ksbA
- binding coenzyme a: M162 (= M198), S171 (= S207), V173 (= V209), T224 (vs. gap), K225 (≠ S253), I290 (≠ V308), F294 (≠ I312), E298 (≠ A316), R301 (= R319), A447 (≠ E445), G448 (= G446), I452 (≠ V450), D456 (= D454)
- binding flavin-adenine dinucleotide: L164 (≠ M200), T165 (= T201), G170 (= G206), S171 (= S207), F196 (= F236), I197 (≠ V237), T198 (≠ S238), T266 (≠ S288), R326 (≠ H340), I345 (≠ L351), H348 (≠ Q354), Q420 (≠ E418), T421 (≠ C419), G423 (= G421), G424 (= G422), I442 (≠ V440), Y446 (≠ W444), T449 (≠ S447), Q455 (≠ L453)
Sites not aligning to the query:
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
30% identity, 45% coverage: 198:453/566 of query aligns to 125:373/384 of 1jqiA
- binding acetoacetyl-coenzyme a: F125 (≠ M198), S134 (= S207), F234 (≠ V308), M238 (≠ I312), Q239 (≠ E313), L241 (≠ V315), D242 (≠ A316), R245 (= R319), Y364 (≠ W444), E365 (= E445), G366 (= G446)
- binding flavin-adenine dinucleotide: F125 (≠ M198), L127 (≠ M200), S128 (≠ T201), G133 (= G206), S134 (= S207), W158 (= W235), T160 (≠ V237), R270 (= R344), F273 (= F347), L280 (≠ Q354), Q338 (≠ E418), I339 (≠ C419), G342 (= G422), I360 (≠ V440), T367 (≠ S447), E369 (≠ N449), I370 (≠ V450)
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)
30% identity, 45% coverage: 198:453/566 of query aligns to 152:400/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
6ksaB Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c18coa (see paper)
23% identity, 66% coverage: 83:454/566 of query aligns to 66:459/611 of 6ksaB
- binding flavin-adenine dinucleotide: M165 (= M198), L167 (≠ M200), T168 (= T201), G173 (= G206), S174 (= S207), F199 (= F236), I200 (≠ V237), T201 (≠ S238), R329 (≠ H340), I348 (≠ L351), H351 (≠ Q354), Q423 (≠ E418), T424 (≠ C419), G426 (= G421), G427 (= G422), I445 (≠ V440), Y449 (≠ W444), T452 (≠ S447)
- binding magnesium ion: H388 (≠ D383)
- binding stearoyl-coenzyme a: W115 (≠ Y138), M133 (≠ A158), M137 (≠ I162), A163 (vs. gap), M165 (= M198), L167 (≠ M200), S174 (= S207), V176 (= V209), T227 (vs. gap), K228 (≠ S253), I293 (≠ V308), F297 (≠ I312), Q302 (≠ M317), R304 (= R319), Y449 (≠ W444), A450 (≠ E445), I455 (≠ V450), D459 (= D454)
Sites not aligning to the query:
6lq8A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c22coa (see paper)
23% identity, 66% coverage: 83:454/566 of query aligns to 63:456/607 of 6lq8A
- binding coenzyme a: M162 (= M198), L164 (≠ M200), S171 (= S207), V173 (= V209), T224 (vs. gap), K225 (≠ S253), I290 (≠ V308), F294 (≠ I312), R301 (= R319), A447 (≠ E445), G448 (= G446), I452 (≠ V450), D456 (= D454)
- binding docosanoic acid: G96 (= G127), L97 (≠ Q128), Q111 (≠ K137), M130 (≠ A158), G133 (≠ S161), M134 (≠ I162), E136 (≠ R175), I137 (= I176), M162 (= M198), T198 (≠ S238), Q299 (≠ M317), A300 (≠ T318), Y446 (≠ W444), A447 (≠ E445)
- binding flavin-adenine dinucleotide: M162 (= M198), L164 (≠ M200), T165 (= T201), G170 (= G206), S171 (= S207), F196 (= F236), I197 (≠ V237), T198 (≠ S238), R326 (≠ H340), I345 (≠ L351), H348 (≠ Q354), Q420 (≠ E418), T421 (≠ C419), G423 (= G421), G424 (= G422), I442 (≠ V440), Y446 (≠ W444), T449 (≠ S447)
Sites not aligning to the query:
6lq7A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c17coa (see paper)
23% identity, 66% coverage: 83:454/566 of query aligns to 63:456/607 of 6lq7A
- binding coenzyme a: M162 (= M198), L164 (≠ M200), S171 (= S207), V173 (= V209), T224 (vs. gap), K225 (≠ S253), I290 (≠ V308), F294 (≠ I312), R301 (= R319), A447 (≠ E445), G448 (= G446), I452 (≠ V450), D456 (= D454)
- binding flavin-adenine dinucleotide: M162 (= M198), L164 (≠ M200), T165 (= T201), G170 (= G206), S171 (= S207), F196 (= F236), I197 (≠ V237), T198 (≠ S238), R326 (≠ H340), I345 (≠ L351), H348 (≠ Q354), Q420 (≠ E418), T421 (≠ C419), G423 (= G421), G424 (= G422), I442 (≠ V440), Y446 (≠ W444), T449 (≠ S447)
- binding heptadecanoic acid: M130 (≠ A158), A160 (vs. gap), Q299 (≠ M317), Y446 (≠ W444), A447 (≠ E445)
Sites not aligning to the query:
Query Sequence
>GFF3397 FitnessBrowser__Marino:GFF3397
MNARQPRPETPSNDQEDRYLASTHEVFNQPPALENYNLFEQDIALQEAALREGAGKAAED
LKAFGALAGAAQTIDLGFRANANKPVFNTHDRFGHRIDEVDFHPAYHELMRIAFDNGLHS
SPWSHPGQGAHVARAAKYYMHSQVEAAHCCPVTMTFAAIPSIRKQPELAADWEARILADS
YDPRNLPDSQKSSVTIGMAMTEKQGGSDVRANSTRAYPIGAGGPGQAYELVGHKWFVSAP
MCDAFLVLAQTQSGLSCFLMPRWRPDGTKNPWQVQRLKNKMGNVANASSEAELRGALAWM
VGEEGRGVPTIIEMVAMTRFDCMIGSSAGMRQAIAQASHHCRHRSAFGARLIDQPLMQNV
LADLALESEAALAYTMRIARALDNQDKEHERLLARLATPVGKYWICKRTPNHAYEAMECI
GGSGVMEDCIMPRLFRESPVNAIWEGSGNVQCLDTLRALQKEPETLDAFFNEAAEAKGAD
RRFDQFLAQLQHDFADISDFQYRARNLVDRMALALQGSLLLRHSDAAVADAFCASRLEAS
GGMNYGNLPSGTDPAAIIKRATPVVG
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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