SitesBLAST
Comparing 3609616 FitnessBrowser__Dino:3609616 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)
58% identity, 99% coverage: 1:503/506 of query aligns to 1:506/506 of 4gxqA
- active site: T163 (= T163), N183 (= N183), H207 (= H207), T303 (= T303), E304 (= E304), I403 (= I403), N408 (= N408), A491 (≠ K488)
- binding adenosine-5'-triphosphate: T163 (= T163), S164 (= S164), G165 (= G165), T166 (= T166), T167 (= T167), H207 (= H207), S277 (= S277), A278 (= A278), P279 (= P279), E298 (= E298), M302 (= M302), T303 (= T303), D382 (= D382), R397 (= R397)
- binding carbonate ion: H207 (= H207), S277 (= S277), R299 (= R299), G301 (= G301)
3nyrA Malonyl-coa ligase ternary product complex with malonyl-coa and amp bound (see paper)
43% identity, 79% coverage: 82:483/506 of query aligns to 71:460/460 of 3nyrA
- active site: T137 (= T163), T157 (≠ N183), H181 (= H207), T281 (= T303), E282 (= E304), K379 (≠ I403), K384 (≠ N408)
- binding adenosine monophosphate: S255 (= S277), A256 (= A278), A257 (≠ P279), R277 (= R299), Y278 (= Y300), G279 (= G301), M280 (= M302), T281 (= T303), D357 (= D382), K379 (≠ I403), K384 (≠ N408)
- binding malonyl-coenzyme a: P178 (= P204), H181 (= H207), T226 (= T251), R230 (= R255), S255 (= S277), R277 (= R299), G279 (= G301), G381 (= G405), G382 (= G406), Y383 (= Y407)
3nyqA Malonyl-coa ligase ternary product complex with methylmalonyl-coa and amp bound (see paper)
43% identity, 79% coverage: 82:483/506 of query aligns to 71:460/460 of 3nyqA
- active site: T137 (= T163), T157 (≠ N183), H181 (= H207), T281 (= T303), E282 (= E304), K379 (≠ I403), K384 (≠ N408)
- binding adenosine monophosphate: S255 (= S277), A256 (= A278), A257 (≠ P279), R277 (= R299), Y278 (= Y300), G279 (= G301), M280 (= M302), T281 (= T303), D357 (= D382), K379 (≠ I403), K384 (≠ N408)
- binding methylmalonyl-coenzyme a: P178 (= P204), H181 (= H207), H183 (= H209), T226 (= T251), R230 (= R255), S255 (= S277), R277 (= R299), G279 (= G301), M280 (= M302), M285 (= M307), G381 (= G405), G382 (= G406), Y383 (= Y407)
Q4G176 Malonate--CoA ligase ACSF3, mitochondrial; Acyl-CoA synthetase family member 3; EC 6.2.1.76 from Homo sapiens (Human) (see 2 papers)
32% identity, 85% coverage: 67:498/506 of query aligns to 110:573/576 of Q4G176
- R354 (= R299) mutation to A: Impairs malonyl-CoA synthase activity.; mutation to L: Impairs malonyl-CoA synthase activity.
- V372 (vs. gap) 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)
31% identity, 93% coverage: 26:497/506 of query aligns to 46:552/561 of P69451
- Y213 (= Y162) mutation to A: Loss of activity.
- T214 (= T163) mutation to A: 10% of wild-type activity.
- G216 (= G165) mutation to A: Decreases activity.
- T217 (= T166) mutation to A: Decreases activity.
- G219 (= G168) mutation to A: Decreases activity.
- K222 (= K171) mutation to A: Decreases activity.
- E361 (= E304) mutation to A: Loss of activity.
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
32% identity, 92% coverage: 21:488/506 of query aligns to 23:499/504 of 6qjzA
- active site: T169 (= T163), S189 (≠ N183), H213 (= H207), T314 (= T303), E315 (= E304), N414 (≠ I403), K419 (≠ N408)
- binding adenosine monophosphate: H213 (= H207), S288 (= S277), A289 (= A278), S290 (≠ P279), A312 (≠ G301), M313 (= M302), T314 (= T303), D393 (= D382), L405 (≠ I394), K410 (= K399), K419 (≠ N408)
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)
32% identity, 94% coverage: 21:498/506 of query aligns to 23:510/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 163:167) binding
- H214 (= H207) binding ; mutation to A: Abolished activity.
- S289 (= S277) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ SAP 277:279) binding
- EA 310:311 (≠ ER 298:299) binding
- M314 (= M302) binding
- T315 (= T303) binding
- H319 (≠ N306) binding ; mutation to A: Abolished activity.
- D394 (= D382) binding
- R409 (= R397) binding ; mutation to A: Abolished activity.
- K500 (= K488) binding ; binding ; mutation to A: Abolished activity.
5ie2A Crystal structure of a plant enzyme (see paper)
32% identity, 94% coverage: 21:498/506 of query aligns to 23:505/506 of 5ie2A
- active site: T165 (= T163), S185 (≠ N183), H209 (= H207), T310 (= T303), E311 (= E304), N410 (≠ I403), K415 (≠ N408), K495 (= K488)
- binding adenosine-5'-triphosphate: T165 (= T163), S166 (= S164), G167 (= G165), T168 (= T166), T169 (= T167), S284 (= S277), A285 (= A278), S286 (≠ P279), Y307 (= Y300), A308 (≠ G301), M309 (= M302), T310 (= T303), D389 (= D382), L401 (≠ I394), R404 (= R397), K495 (= K488)
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)
31% identity, 96% coverage: 12:499/506 of query aligns to 9:498/503 of P9WQ37
- R9 (= R12) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ F20) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K171) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T194) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ K196) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ T208) 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 (≠ G210) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ G214) 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 (≠ T244) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G301) 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 (≠ F377) 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 (= D382) 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 (= R397) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S404) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G406) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K488) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
5ie3A Crystal structure of a plant enzyme (see paper)
32% identity, 94% coverage: 21:498/506 of query aligns to 23:503/504 of 5ie3A
- active site: T163 (= T163), S183 (≠ N183), H207 (= H207), T308 (= T303), E309 (= E304), N408 (≠ I403), K413 (≠ N408), K493 (= K488)
- binding adenosine monophosphate: S164 (= S164), S282 (= S277), A283 (= A278), S284 (≠ P279), Y305 (= Y300), A306 (≠ G301), M307 (= M302), T308 (= T303), D387 (= D382), L399 (≠ I394), R402 (= R397), K493 (= K488)
- binding oxalic acid: V208 (≠ T208), S282 (= S277), A306 (≠ G301), M307 (= M302), H312 (≠ N306), K493 (= K488)
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)
32% identity, 90% coverage: 45:498/506 of query aligns to 44:504/512 of O74976
- S283 (= S277) modified: Phosphoserine
- S284 (≠ A278) modified: Phosphoserine
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
31% identity, 96% coverage: 12:499/506 of query aligns to 12:498/502 of 3r44A
Sites not aligning to the query:
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, 94% coverage: 26:499/506 of query aligns to 57:546/559 of Q67W82
- G395 (= G348) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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)
27% identity, 99% coverage: 4:502/506 of query aligns to 37:554/556 of Q9S725
- K211 (= K171) mutation to S: Drastically reduces the activity.
- M293 (= M247) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V274) mutation K->L,A: Affects the substrate specificity.
- E401 (≠ Q349) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ E351) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R397) mutation to Q: Drastically reduces the activity.
- K457 (≠ G405) mutation to S: Drastically reduces the activity.
- K540 (= K488) mutation to N: Abolishes the activity.
Q08AH3 Acyl-coenzyme A synthetase ACSM2A, mitochondrial; Acyl-CoA synthetase medium-chain family member 2A; Benzoate--CoA ligase; Butyrate--CoA ligase 2A; Butyryl-coenzyme A synthetase 2A; Middle-chain acyl-CoA synthetase 2A; EC 6.2.1.2; EC 6.2.1.25 from Homo sapiens (Human) (see 4 papers)
31% identity, 91% coverage: 36:497/506 of query aligns to 88:566/577 of Q08AH3
- Q139 (≠ A86) binding
- 221:229 (vs. 163:171, 67% identical) binding
- ESYGQT 359:364 (≠ ERYGMT 298:303) binding
- T364 (= T303) binding
- D446 (= D382) binding
- R461 (= R397) binding
- SGY 469:471 (≠ GGY 405:407) binding
- R472 (≠ N408) binding
- R501 (≠ F437) binding
- S513 (≠ Q448) to L: in dbSNP:rs1133607
- K532 (vs. gap) binding
- YPR 540:542 (≠ QPR 471:473) binding
- K557 (= K488) binding
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
31% identity, 91% coverage: 36:497/506 of query aligns to 55:533/536 of 3c5eA
- active site: T188 (= T163), T331 (= T303), E332 (= E304), N434 (≠ I403), R439 (≠ N408), K524 (= K488)
- binding adenosine-5'-triphosphate: T188 (= T163), S189 (= S164), G190 (= G165), T191 (= T166), S192 (≠ T167), G305 (≠ S277), E306 (≠ A278), S307 (≠ P279), G329 (= G301), Q330 (≠ M302), T331 (= T303), D413 (= D382), F425 (≠ I394), R428 (= R397), K524 (= K488)
- binding magnesium ion: M450 (≠ D419), H452 (≠ A421), V455 (= V424)
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
31% identity, 91% coverage: 36:497/506 of query aligns to 52:530/533 of 3eq6A
- active site: T185 (= T163), T328 (= T303), E329 (= E304), N431 (≠ I403), R436 (≠ N408), K521 (= K488)
- binding adenosine monophosphate: G302 (≠ S277), E303 (≠ A278), S304 (≠ P279), E323 (= E298), S324 (≠ R299), Y325 (= Y300), G326 (= G301), Q327 (≠ M302), T328 (= T303), D410 (= D382), F422 (≠ I394), R425 (= R397), R436 (≠ N408)
- binding Butyryl Coenzyme A: W229 (≠ V198), F255 (= F231), I277 (≠ T251), V301 (≠ G276), S433 (≠ G405), G434 (= G406), Y435 (= Y407), P501 (≠ R468), Y502 (≠ F469), Y504 (≠ Q471), R506 (= R473)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
31% identity, 91% coverage: 36:497/506 of query aligns to 52:530/533 of 2wd9A
- active site: T185 (= T163), T328 (= T303), E329 (= E304), N431 (≠ I403), R436 (≠ N408), K521 (= K488)
- binding ibuprofen: I230 (≠ L199), L231 (= L200), G326 (= G301), Q327 (≠ M302), T328 (= T303), R436 (≠ N408)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
31% identity, 91% coverage: 36:497/506 of query aligns to 52:530/533 of 2vzeA
- active site: T185 (= T163), T328 (= T303), E329 (= E304), N431 (≠ I403), R436 (≠ N408), K521 (= K488)
- binding adenosine monophosphate: W229 (≠ V198), G302 (≠ S277), E303 (≠ A278), S304 (≠ P279), E323 (= E298), Y325 (= Y300), G326 (= G301), Q327 (≠ M302), T328 (= T303), D410 (= D382), F422 (≠ I394), R425 (= R397), R436 (≠ N408)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
31% identity, 91% coverage: 36:497/506 of query aligns to 56:534/537 of 3b7wA
Query Sequence
>3609616 FitnessBrowser__Dino:3609616
MTNPLYDALFGRNAGSDAPFLQLPGGDTLTHGGFVELAARYAATLTGLGLAPGDRLALQV
EKSPEALAVYAGCVQAGIVFLPLNTAYTPAEISYFVGNSGAKLVLCDPRAEAGLTPVAAE
AGAQLLTLAADGTGSFPDAAATAPATFETVARTEDDLAAFLYTSGTTGRSKGAMLSQRNL
LSNAEVLVDYWRFTDKDVLLHALPIFHTHGLFVGTNITLLAGGSMIFLPKFDAEAVLANL
PRATTMMGVPTFYTRLLAEDRFDRDLVAHMRLFVSGSAPLLAETHREFEARTGHRILERY
GMTETNMNTSNPYDGARRAGTVGFPLPGVELKVCDPDTGAELPQGEIGQIEVRGPNVFQG
YWQMPEKTAAELRADGFFITGDLGLIDDQGYVQIVGRGKDLIISGGYNIYPKEVELALDE
APGVLESAVIGAPHPDFGESVVGILVPQPGARIDTEAVAARLAGQLARFKQPRKLVVMDA
LPRNTMGKVQKNVLREQFADAFSEPA
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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