SitesBLAST
Comparing SMc01359 FitnessBrowser__Smeli:SMc01359 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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
66% identity, 97% coverage: 15:549/550 of query aligns to 7:541/541 of 5ez3B
- active site: M181 (= M189), T182 (= T190), T295 (= T303), E423 (= E431), R435 (= R443)
- binding flavin-adenine dinucleotide: M181 (= M189), T182 (= T190), G186 (= G194), G187 (= G195), T188 (= T196), F213 (= F221), S215 (= S223), R321 (= R329), F324 (= F332), L328 (= L336), Q331 (= Q339), M334 (= M342), E396 (= E404), C397 (= C405), G399 (= G407), G400 (= G408), W422 (= W430), E423 (= E431), S425 (= S433), N427 (= N435), L431 (= L439)
3u33A Crystal structure of the e. Coli adaptive response protein aidb in the space group p3(2) (see paper)
45% identity, 92% coverage: 14:521/550 of query aligns to 9:515/540 of 3u33A
- active site: M184 (= M189), T185 (= T190), T298 (= T303), E425 (= E431), R437 (= R443)
- binding flavin-adenine dinucleotide: M182 (= M187), M184 (= M189), T185 (= T190), G190 (= G195), S191 (≠ T196), F216 (= F221), S218 (= S223), R324 (= R329), F327 (= F332), L331 (= L336), Q334 (= Q339), M337 (= M342), E398 (= E404), V399 (≠ C405), G401 (= G407), G402 (= G408), W424 (= W430), G426 (= G432), S427 (= S433), N429 (= N435), L433 (= L439)
P33224 Putative acyl-CoA dehydrogenase AidB; EC 1.3.99.- from Escherichia coli (strain K12) (see paper)
45% identity, 92% coverage: 14:521/550 of query aligns to 9:515/541 of P33224
- 182:191 (vs. 187:196, 90% identical) binding
- T185 (= T190) binding
- S191 (≠ T196) binding
- FFS 216:218 (≠ FMS 221:223) binding
- S218 (= S223) binding
- 423:433 (vs. 429:439, 82% identical) binding
- N429 (= N435) binding
- R437 (= R443) mutation to Q: Does not affect DNA binding affinity.
Sites not aligning to the query:
- 518 R→Q: Reduces DNA binding affinity.
4y9jB Crystal structure of caenorhabditis elegans acdh-11 in complex with c11-coa (see paper)
31% identity, 78% coverage: 24:452/550 of query aligns to 26:467/593 of 4y9jB
- active site: M190 (= M189), T191 (= T190), T315 (= T303), E446 (= E431), R458 (= R443)
- binding flavin-adenine dinucleotide: Q188 (≠ M187), M190 (= M189), T191 (= T190), G196 (= G195), S197 (≠ T196), F223 (= F221), S224 (≠ M222), S225 (= S223), R341 (= R329), V343 (= V331), F344 (= F332), Q348 (≠ L336), E419 (= E404), C420 (= C405), G422 (= G407), G423 (= G408), Y426 (= Y411), W445 (= W430), T448 (≠ S433), V451 (= V436), L454 (= L439)
- 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 (≠ C135), A147 (≠ T142), Q188 (≠ M187), S197 (≠ T196), S249 (vs. gap), R303 (≠ A291), V305 (≠ I293), S309 (≠ L297), L312 (≠ V300), N313 (≠ T301), R316 (= R304), A322 (= A310), R396 (= R381), W445 (= W430), E446 (= E431), V451 (= V436), R458 (= R443)
Q9XWZ2 Acyl-CoA dehydrogenase family member 11; EC 1.3.99.- from Caenorhabditis elegans (see paper)
31% identity, 78% coverage: 24:452/550 of query aligns to 44:485/617 of Q9XWZ2
- E91 (≠ N67) mutation to K: In n5655; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- S156 (≠ T130) mutation to F: In n5657; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G158 (≠ Q132) mutation to R: In n5661; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G214 (= G195) mutation to E: In n5879; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G443 (= G410) mutation to R: In n5877; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- R455 (= R422) mutation to H: In n5876; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
6sdaB Bd2924 c10 acyl-coenzymea bound form (see paper)
28% identity, 85% coverage: 24:489/550 of query aligns to 11:483/503 of 6sdaB
- active site: M171 (= M189), T172 (= T190), T296 (= T303), R439 (= R443)
- binding flavin-adenine dinucleotide: Q169 (≠ M187), M171 (= M189), T172 (= T190), G177 (= G195), S178 (≠ T196), F208 (= F221), T209 (≠ M222), R322 (= R329), F325 (= F332), L329 (= L336), H332 (≠ Q339), E400 (= E404), M401 (≠ C405), G404 (= G408), Y407 (= Y411), W426 (= W430), T429 (≠ S433), N431 (= N435), L435 (= L439)
- binding decanoyl-CoA: C128 (= C139), G177 (= G195), S178 (≠ T196), S230 (≠ R237), V286 (≠ I293), A290 (≠ L297), L293 (≠ V300), N294 (≠ T301), R297 (= R304), R377 (= R381), W426 (= W430), E427 (= E431)
6sd8X Bd2924 apo-form (see paper)
28% identity, 85% coverage: 24:489/550 of query aligns to 11:483/503 of 6sd8X
- active site: M171 (= M189), T172 (= T190), T296 (= T303), R439 (= R443)
- binding flavin-adenine dinucleotide: Q169 (≠ M187), M171 (= M189), T172 (= T190), G176 (= G194), G177 (= G195), S178 (≠ T196), F208 (= F221), T209 (≠ M222), R322 (= R329), F325 (= F332), L329 (= L336), H332 (≠ Q339), M401 (≠ C405), G404 (= G408), W426 (= W430), T429 (≠ S433), V432 (= V436), L435 (= L439)
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
28% identity, 45% coverage: 187:436/550 of query aligns to 126:372/383 of 1bucA
- active site: L128 (≠ M189), T129 (= T190), G246 (≠ T303), E367 (= E431)
- binding acetoacetyl-coenzyme a: F126 (≠ M187), G134 (= G195), T135 (= T196), T162 (≠ S223), N182 (≠ C242), H183 (≠ F243), F236 (≠ I293), M240 (≠ L297), M241 (≠ D298), L243 (≠ V300), D244 (≠ T301), T317 (≠ A374), Y366 (≠ W430), E367 (= E431), G368 (= G432)
- binding flavin-adenine dinucleotide: F126 (≠ M187), L128 (≠ M189), T129 (= T190), G134 (= G195), T135 (= T196), F160 (= F221), T162 (≠ S223), Y366 (≠ W430), T369 (≠ S433), E371 (≠ N435)
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)
28% identity, 45% coverage: 187:436/550 of query aligns to 126:372/383 of Q06319
- E367 (= E431) active site, Proton acceptor; mutation to Q: Loss of activity.
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, 55% coverage: 141:442/550 of query aligns to 128:446/591 of A3SI50
- M161 (= M187) mutation to A: Retains 37% of wild-type activity.
- T170 (= T196) 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 (≠ E238) mutation to A: Retains 9.4% of wild-type activity.
- H280 (≠ D290) mutation to A: Retains 18% of wild-type activity.
- K281 (≠ A291) mutation to A: Retains 54% of wild-type activity.
- R284 (= R294) mutation to A: Retains 97% of wild-type activity.
- F287 (≠ L297) mutation to A: Retains 76% of wild-type activity.
- Y434 (≠ W430) mutation to A: Retains 51% of wild-type activity.
- E435 (= E431) mutation to A: Loss of activity.
Sites not aligning to the query:
- 448 R→A: Retains 44% of wild-type activity.
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
28% identity, 47% coverage: 187:447/550 of query aligns to 123:379/380 of 4l1fA
- active site: L125 (≠ M189), T126 (= T190), G242 (≠ T303), E363 (= E431), R375 (= R443)
- binding coenzyme a persulfide: T132 (= T196), H179 (≠ F243), F232 (≠ I293), M236 (≠ L297), E237 (≠ D298), L239 (≠ V300), D240 (≠ T301), R243 (= R304), Y362 (≠ W430), E363 (= E431), G364 (= G432), R375 (= R443)
- binding flavin-adenine dinucleotide: F123 (≠ M187), L125 (≠ M189), T126 (= T190), G131 (= G195), T132 (= T196), F156 (= F221), I157 (≠ M222), T158 (≠ S223), R268 (= R329), Q270 (≠ V331), F271 (= F332), I275 (≠ L336), F278 (≠ Q339), L281 (≠ M342), Q336 (≠ E404), I337 (≠ C405), G340 (= G408), I358 (≠ V426), Y362 (≠ W430), T365 (≠ S433), Q367 (≠ N435)
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)
30% identity, 46% coverage: 189:441/550 of query aligns to 154:402/412 of P16219
- R171 (≠ E206) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ WFM 220:222) binding in other chain
- A192 (≠ S227) 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 (≠ S357) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ P385) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ ECMGG 404:408) binding
- R380 (= R419) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ SGN 433:435) 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)
- 152:161 binding in other chain
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
30% identity, 46% coverage: 189:441/550 of query aligns to 124:372/381 of 8sgsA
- binding coenzyme a: S131 (≠ T196), A133 (≠ V198), N177 (≠ R237), F231 (≠ I293), M235 (≠ L297), L238 (≠ V300), I312 (≠ A374), E362 (= E431), G363 (= G432)
- binding flavin-adenine dinucleotide: L124 (≠ M189), S125 (≠ T190), G130 (= G195), S131 (≠ T196), W155 (= W220), T157 (≠ M222), R267 (= R329), F270 (= F332), L274 (= L336), L277 (≠ Q339), Q335 (≠ E404), I336 (≠ C405), G338 (= G407), G339 (= G408), I357 (≠ V426), I360 (= I429), Y361 (≠ W430), T364 (≠ S433), E366 (≠ N435)
Sites not aligning to the query:
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
30% identity, 46% coverage: 189:441/550 of query aligns to 127:375/385 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 (≠ N409), T347 (≠ E413), E348 (= E414)
- binding flavin-adenine dinucleotide: L127 (≠ M189), S128 (≠ T190), G133 (= G195), S134 (≠ T196), W158 (= W220), T160 (≠ M222), R270 (= R329), F273 (= F332), L280 (≠ Q339), V282 (≠ M341), Q338 (≠ E404), I339 (≠ C405), G342 (= G408), I360 (≠ V426), Y364 (≠ W430), T367 (≠ S433), E369 (≠ N435), I370 (≠ V436), L373 (= L439)
Sites not aligning to the query:
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
30% identity, 46% coverage: 189:441/550 of query aligns to 130:378/387 of 7y0aC
- binding flavin-adenine dinucleotide: L130 (≠ M189), S131 (≠ T190), G136 (= G195), S137 (≠ T196), W161 (= W220), T163 (≠ M222), T214 (≠ S273), R273 (= R329), F276 (= F332), L280 (= L336), L283 (≠ Q339), V285 (≠ M341), Q341 (≠ E404), I342 (≠ C405), G345 (= G408), I363 (≠ V426), Y367 (≠ W430), T370 (≠ S433), E372 (≠ N435), L376 (= L439)
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, 46% coverage: 189:441/550 of query aligns to 154:402/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
- 152:161 binding
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
30% identity, 46% coverage: 189:441/550 of query aligns to 127:375/384 of 1jqiA
- binding acetoacetyl-coenzyme a: S134 (≠ T196), F234 (≠ I293), M238 (≠ L297), Q239 (≠ D298), L241 (≠ V300), D242 (≠ T301), R245 (= R304), Y364 (≠ W430), E365 (= E431), G366 (= G432)
- binding flavin-adenine dinucleotide: L127 (≠ M189), S128 (≠ T190), G133 (= G195), S134 (≠ T196), W158 (= W220), T160 (≠ M222), R270 (= R329), F273 (= F332), L280 (≠ Q339), Q338 (≠ E404), I339 (≠ C405), G342 (= G408), I360 (≠ V426), T367 (≠ S433), E369 (≠ N435), I370 (≠ V436)
Sites not aligning to the query:
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
30% identity, 46% coverage: 189:441/550 of query aligns to 121:362/371 of 2vigB
- active site: L121 (≠ M189), S122 (≠ T190), G231 (≠ T303), E352 (= E431)
- binding coenzyme a persulfide: S128 (≠ T196), F221 (≠ I293), M225 (≠ L297), Q226 (≠ D298), L228 (≠ V300), D229 (≠ T301), R232 (= R304), E352 (= E431), G353 (= G432), I357 (≠ V436)
- binding flavin-adenine dinucleotide: L121 (≠ M189), S122 (≠ T190), G127 (= G195), S128 (≠ T196), W152 (= W220), T154 (≠ M222), R257 (= R329), F260 (= F332), L264 (= L336), L267 (≠ Q339), Q325 (≠ E404), I326 (≠ C405), G329 (= G408), I347 (≠ V426), Y351 (≠ W430), T354 (≠ S433), E356 (≠ N435)
Sites not aligning to the query:
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, 54% coverage: 152:447/550 of query aligns to 143:419/426 of P26440
- 165:174 (vs. 187:196, 30% identical) binding
- S174 (≠ T196) binding
- WIT 198:200 (≠ WFM 220:222) binding
- SR 222:223 (≠ RE 237:238) binding
- G250 (≠ S270) to A: in IVA; uncertain significance
- Y277 (≠ R294) binding
- DLER 284:287 (≠ TLTR 301:304) binding
- 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 (= A308) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R329) binding
- Q323 (≠ P340) binding
- I379 (≠ M403) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ ECMGG 404:408) binding
- R398 (= R422) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ N427) to N: in IVA; uncertain significance
- A407 (≠ E431) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ EG 431:432) binding
- TSE 409:411 (≠ SGN 433:435) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
25% identity, 54% coverage: 152:447/550 of query aligns to 110:386/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ T190), G140 (= G195), S141 (≠ T196), W165 (= W220), T167 (≠ M222), R279 (= R329), F282 (= F332), I286 (≠ L336), F289 (≠ Q339), Q347 (≠ E404), C348 (= C405), G351 (= G408), L369 (≠ V426), G375 (= G432), T376 (≠ S433), L382 (= L439)
Query Sequence
>SMc01359 FitnessBrowser__Smeli:SMc01359
MNQMNRTEQKLAELNQPKPWSGVNAFRSDPLVVDITSSMPKTLRDEFDGLGRYVTSPEAQ
ELARMANEGVPKLKTHGPRGERLDVVEFHPAWHALMRRSMTTGLHSSAWENLPDERGRSH
KVRAIRFYLTAQLECGHLCPLTMTSASVAAITASPAVQKEWAPKILSRKYDSSNRPWMQK
SAVTIGMGMTEKQGGTDVRANTSTAERVGEGIYRLTGHKWFMSAPMSDAFVMLAQTREGL
GCFLVPRLLEDGGANGLRFQRLKDKLGNRSNASSEVEFSDTFGFLLGTPDAGIRTILDMV
TLTRLDCALASAGMMRASLAEAVHHTRGRKVFGKALVSQPMMTRVLADMALDVAAASALS
FRLAEAFDNAHSSAEDAAYARIMTPVAKYWCCKIAPALIYEAMECMGGNGYVEERALARH
YREAPVNAIWEGSGNVMALDVLRVLGRRKELFEQLFATIGRDLGPAGRKTIEVLRAAMSL
CERDEGAARMLVEQLALAAAAAELYRLGAGRIADAFLESRLAAGWRSTYGMLDSRFDSAY
VLDLLYPAAT
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