SitesBLAST
Comparing SMa0150 FitnessBrowser__Smeli:SMa0150 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)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
67% identity, 98% coverage: 5:501/508 of query aligns to 9:505/506 of 4gxqA
- active site: T163 (= T162), N183 (= N182), H207 (= H206), T303 (= T302), E304 (= E303), I403 (= I402), N408 (= N407), A491 (≠ K487)
- binding adenosine-5'-triphosphate: T163 (= T162), S164 (= S163), G165 (= G164), T166 (= T165), T167 (= T166), H207 (= H206), S277 (= S276), A278 (= A277), P279 (= P278), E298 (= E297), M302 (= M301), T303 (= T302), D382 (= D381), R397 (= R396)
- binding carbonate ion: H207 (= H206), S277 (= S276), R299 (= R298), G301 (= G300)
P9WQ37 Long-chain-fatty-acid--CoA ligase FadD13; Fatty acyl-CoA ligase; FACL; FACL13; Fatty acyl-CoA synthetase; ACS; FACS; Very-long-chain fatty-acyl-CoA synthetase; ACSVL; EC 6.2.1.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
35% identity, 93% coverage: 29:498/508 of query aligns to 31:498/503 of P9WQ37
- K172 (= K170) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (vs. gap) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (vs. gap) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ T207) mutation to D: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced. Slight increase of susceptibility to proteolysis.
- A211 (≠ G209) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ N215) mutation to W: Shows a marked decrease in the activity with lauric and palmitic acid (C12 and C16 fatty acid) with a simultaneous increase in the activity with caprylic acid (C8 fatty acid).
- R244 (≠ T243) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G300) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.; mutation to W: Does not show activity with small, medium or long acyl chains.
- W377 (≠ F376) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding. No significant change in the total expression level, however the cytoplasmic expression is low. Slight increase of susceptibility to proteolysis.
- D382 (= D381) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced.
- R397 (= R396) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S403) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G405) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K487) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
Sites not aligning to the query:
- 9 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- 17 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
3nyrA Malonyl-coa ligase ternary product complex with malonyl-coa and amp bound (see paper)
40% identity, 84% coverage: 54:482/508 of query aligns to 44:460/460 of 3nyrA
- active site: T137 (= T162), T157 (≠ N182), H181 (= H206), T281 (= T302), E282 (= E303), K379 (≠ I402), K384 (≠ N407)
- binding adenosine monophosphate: S255 (= S276), A256 (= A277), A257 (≠ P278), R277 (= R298), Y278 (= Y299), G279 (= G300), M280 (= M301), T281 (= T302), D357 (= D381), K379 (≠ I402), K384 (≠ N407)
- binding malonyl-coenzyme a: P178 (= P203), H181 (= H206), T226 (= T250), R230 (= R254), S255 (= S276), R277 (= R298), G279 (= G300), G381 (= G404), G382 (= G405), Y383 (= Y406)
3nyqA Malonyl-coa ligase ternary product complex with methylmalonyl-coa and amp bound (see paper)
40% identity, 84% coverage: 54:482/508 of query aligns to 44:460/460 of 3nyqA
- active site: T137 (= T162), T157 (≠ N182), H181 (= H206), T281 (= T302), E282 (= E303), K379 (≠ I402), K384 (≠ N407)
- binding adenosine monophosphate: S255 (= S276), A256 (= A277), A257 (≠ P278), R277 (= R298), Y278 (= Y299), G279 (= G300), M280 (= M301), T281 (= T302), D357 (= D381), K379 (≠ I402), K384 (≠ N407)
- binding methylmalonyl-coenzyme a: P178 (= P203), H181 (= H206), H183 (= H208), T226 (= T250), R230 (= R254), S255 (= S276), R277 (= R298), G279 (= G300), M280 (= M301), M285 (= M306), G381 (= G404), G382 (= G405), Y383 (= Y406)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
35% identity, 93% coverage: 29:498/508 of query aligns to 34:498/502 of 3r44A
Sites not aligning to the query:
Q4G176 Malonate--CoA ligase ACSF3, mitochondrial; Acyl-CoA synthetase family member 3; EC 6.2.1.76 from Homo sapiens (Human) (see 2 papers)
31% identity, 92% coverage: 29:493/508 of query aligns to 67:569/576 of Q4G176
- R354 (= R298) mutation to A: Impairs malonyl-CoA synthase activity.; mutation to L: Impairs malonyl-CoA synthase activity.
- V372 (≠ E315) to M: in dbSNP:rs3743979
Sites not aligning to the query:
- 2 L → P: in dbSNP:rs7188200
- 17 A → P: in dbSNP:rs11547019
P69451 Long-chain-fatty-acid--CoA ligase; Long-chain acyl-CoA synthetase; Acyl-CoA synthetase; EC 6.2.1.3 from Escherichia coli (strain K12) (see paper)
29% identity, 93% coverage: 25:495/508 of query aligns to 46:551/561 of P69451
- Y213 (= Y161) mutation to A: Loss of activity.
- T214 (= T162) mutation to A: 10% of wild-type activity.
- G216 (= G164) mutation to A: Decreases activity.
- T217 (= T165) mutation to A: Decreases activity.
- G219 (= G167) mutation to A: Decreases activity.
- K222 (= K170) mutation to A: Decreases activity.
- E361 (= E303) mutation to A: Loss of activity.
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
32% identity, 90% coverage: 29:487/508 of query aligns to 32:499/504 of 6qjzA
- active site: T169 (= T162), S189 (≠ N182), H213 (= H206), T314 (= T302), E315 (= E303), N414 (≠ I402), K419 (≠ N407)
- binding adenosine monophosphate: H213 (= H206), S288 (= S276), A289 (= A277), S290 (≠ P278), A312 (≠ G300), M313 (= M301), T314 (= T302), D393 (= D381), L405 (≠ I393), K410 (= K398), K419 (≠ N407)
O74976 Oxalate--CoA ligase; Oxalyl-CoA synthetase; Peroxisomal-coenzyme A synthetase; EC 6.2.1.8 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
30% identity, 89% coverage: 44:497/508 of query aligns to 44:504/512 of O74976
- S283 (= S276) modified: Phosphoserine
- S284 (≠ A277) modified: Phosphoserine
5ie2A Crystal structure of a plant enzyme (see paper)
32% identity, 92% coverage: 32:497/508 of query aligns to 38:505/506 of 5ie2A
- active site: T165 (= T162), S185 (≠ N182), H209 (= H206), T310 (= T302), E311 (= E303), N410 (≠ I402), K415 (≠ N407), K495 (= K487)
- binding adenosine-5'-triphosphate: T165 (= T162), S166 (= S163), G167 (= G164), T168 (= T165), T169 (= T166), S284 (= S276), A285 (= A277), S286 (≠ P278), Y307 (= Y299), A308 (≠ G300), M309 (= M301), T310 (= T302), D389 (= D381), L401 (≠ I393), R404 (= R396), K495 (= K487)
5ie3A Crystal structure of a plant enzyme (see paper)
32% identity, 92% coverage: 32:497/508 of query aligns to 38:503/504 of 5ie3A
- active site: T163 (= T162), S183 (≠ N182), H207 (= H206), T308 (= T302), E309 (= E303), N408 (≠ I402), K413 (≠ N407), K493 (= K487)
- binding adenosine monophosphate: S164 (= S163), S282 (= S276), A283 (= A277), S284 (≠ P278), Y305 (= Y299), A306 (≠ G300), M307 (= M301), T308 (= T302), D387 (= D381), L399 (≠ I393), R402 (= R396), K493 (= K487)
- binding oxalic acid: V208 (≠ T207), S282 (= S276), A306 (≠ G300), M307 (= M301), H312 (≠ N305), K493 (= K487)
Q84P21 Peroxisomal OPC-8:0-CoA ligase 1; 4-coumarate--CoA ligase isoform 9; At4CL9; 4-coumarate--CoA ligase-like 5; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
30% identity, 95% coverage: 11:494/508 of query aligns to 41:538/546 of Q84P21
- K530 (= K487) mutation to N: Lossed enzymatic activity.
Q67W82 4-coumarate--CoA ligase 4; 4CL 4; Os4CL4; (E)-ferulate--CoA ligase; 4-coumaroyl-CoA synthase 4; Protein RESISTANCE TO ALUMINUM 1; EC 6.2.1.12; EC 6.2.1.34 from Oryza sativa subsp. japonica (Rice) (see paper)
30% identity, 97% coverage: 12:503/508 of query aligns to 46:548/559 of Q67W82
- G395 (= G347) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
Q9SMT7 Oxalate--CoA ligase; 4-coumarate--CoA ligase isoform 8; At4CL8; 4-coumarate--CoA ligase-like 10; Acyl-activating enzyme 3; Adenosine monophosphate binding protein 3; AtMPBP3; Oxalyl-CoA synthetase; EC 6.2.1.8 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 92% coverage: 32:497/508 of query aligns to 38:510/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 162:166) binding
- H214 (= H206) binding ; mutation to A: Abolished activity.
- S289 (= S276) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ SAP 276:278) binding
- EA 310:311 (≠ ER 297:298) binding
- M314 (= M301) binding
- T315 (= T302) binding
- H319 (≠ N305) binding ; mutation to A: Abolished activity.
- D394 (= D381) binding
- R409 (= R396) binding ; mutation to A: Abolished activity.
- K500 (= K487) binding ; binding ; mutation to A: Abolished activity.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
29% identity, 97% coverage: 1:495/508 of query aligns to 28:527/528 of 3ni2A
- active site: S182 (≠ T162), S202 (≠ N182), H230 (= H206), T329 (= T302), E330 (= E303), K434 (≠ I402), Q439 (≠ N407), K519 (= K487)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ H208), S236 (≠ V216), G302 (≠ S276), A303 (= A277), P304 (= P278), G325 (≠ R298), G327 (= G300), T329 (= T302), P333 (vs. gap), V334 (vs. gap), D413 (= D381), K430 (= K398), K434 (≠ I402), Q439 (≠ N407)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
29% identity, 97% coverage: 1:495/508 of query aligns to 28:527/528 of 3a9vA
- active site: S182 (≠ T162), S202 (≠ N182), H230 (= H206), T329 (= T302), E330 (= E303), K434 (≠ I402), Q439 (≠ N407), K519 (= K487)
- binding adenosine monophosphate: H230 (= H206), G302 (≠ S276), A303 (= A277), P304 (= P278), Y326 (= Y299), G327 (= G300), M328 (= M301), T329 (= T302), D413 (= D381), K430 (= K398), K434 (≠ I402), Q439 (≠ N407)
O24146 4-coumarate--CoA ligase 2; 4CL 2; Nt4CL-19; Nt4CL-2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; Cinnamate--CoA ligase; Ferulate--CoA ligase; EC 6.2.1.12; EC 6.2.1.-; EC 6.2.1.-; EC 6.2.1.34 from Nicotiana tabacum (Common tobacco) (see paper)
28% identity, 99% coverage: 1:503/508 of query aligns to 27:539/542 of O24146
- S189 (≠ T162) binding
- S190 (= S163) binding
- G191 (= G164) binding
- T192 (= T165) binding
- T193 (= T166) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K170) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H206) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ H208) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ V216) binding ; binding ; binding
- K260 (= K229) binding
- A309 (≠ S276) binding ; binding ; binding
- Q331 (≠ E297) binding
- G332 (≠ R298) binding ; binding ; binding ; binding ; binding
- T336 (= T302) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (vs. gap) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (vs. gap) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D381) binding ; binding ; binding ; binding ; binding
- R435 (= R396) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K398) binding ; binding ; binding ; binding
- K441 (≠ I402) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G404) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G405) binding
- Q446 (≠ N407) binding
- K526 (= K487) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
28% identity, 98% coverage: 1:498/508 of query aligns to 20:530/530 of 5bsmA
- active site: S182 (≠ T162), S202 (≠ N182), H230 (= H206), T329 (= T302), E330 (= E303), K434 (≠ I402), Q439 (≠ N407), K519 (= K487)
- binding adenosine-5'-triphosphate: S182 (≠ T162), S183 (= S163), G184 (= G164), T185 (= T165), T186 (= T166), K190 (= K170), H230 (= H206), A302 (≠ S276), A303 (= A277), P304 (= P278), Y326 (= Y299), G327 (= G300), M328 (= M301), T329 (= T302), D413 (= D381), I425 (= I393), R428 (= R396), K519 (= K487)
Q9S725 4-coumarate--CoA ligase 2; 4CL 2; 4-coumarate--CoA ligase isoform 2; At4CL2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; EC 6.2.1.12; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
29% identity, 99% coverage: 1:503/508 of query aligns to 38:553/556 of Q9S725
- K211 (= K170) mutation to S: Drastically reduces the activity.
- M293 (= M246) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V273) mutation K->L,A: Affects the substrate specificity.
- E401 (≠ M348) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ E350) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R396) mutation to Q: Drastically reduces the activity.
- K457 (≠ G404) mutation to S: Drastically reduces the activity.
- K540 (= K487) mutation to N: Abolishes the activity.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
28% identity, 97% coverage: 1:494/508 of query aligns to 19:525/528 of 5bsrA
- active site: S181 (≠ T162), S201 (≠ N182), H229 (= H206), T328 (= T302), E329 (= E303), K433 (≠ I402), Q438 (≠ N407), K518 (= K487)
- binding adenosine monophosphate: A301 (≠ S276), G326 (= G300), T328 (= T302), D412 (= D381), K429 (= K398), K433 (≠ I402), Q438 (≠ N407)
- binding coenzyme a: L102 (≠ A85), P226 (= P203), H229 (= H206), Y231 (≠ H208), F253 (= F230), K435 (≠ G404), G436 (= G405), F437 (≠ Y406), F498 (≠ R467)
Query Sequence
>SMa0150 FitnessBrowser__Smeli:SMa0150
MSNHLFDAIRRAARPDSAFILTADGRVWTYGDMLEHSGRIASVLDALGVRPGDRVAVQVE
KSPEALMLYLACLRTGAVYLPLNTAYTLAELDYFFGDAEPRLIVCAPGAKEGIAKHAADC
GAEVETLDEKGGGSLIDLARGKAPDFPDADRGPDDLAAILYTSGTTGRSKGAMLTHDNLL
SNATTLREYWRFTADDRLIHALPIFHTHGLFVASNVILLAGASMFFLPKFDANEVLRLMP
QSTSMMGVPTFYVRLVQNPGLTHEATAGMRLFVSGSAPLLAETHRTFAQMTGHAILERYG
MTETNMNTSNPYDGERIAGTVGFPLPGVSLRVADPESGRPLPKGETGMIEVKGPNVFKGY
WRMPEKTQGEFRADGFFITGDLGRIDERGYVHIVGRGKDLVISGGYNIYPKEVETEIDQM
PGVVETAVIGLPHPDFGEGVTAVVVRKPGAAIDERAILDGLEGRLARYKQPKRVIFVDDL
PRNTMGKVQKNVLRETYARLYAGAEARV
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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