SitesBLAST
Comparing 8499484 FitnessBrowser__Miya:8499484 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)
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)
39% identity, 95% coverage: 12:563/583 of query aligns to 5:557/561 of P69451
- Y213 (= Y218) mutation to A: Loss of activity.
- T214 (= T219) mutation to A: 10% of wild-type activity.
- G216 (= G221) mutation to A: Decreases activity.
- T217 (= T222) mutation to A: Decreases activity.
- G219 (= G224) mutation to A: Decreases activity.
- K222 (= K227) mutation to A: Decreases activity.
- E361 (= E364) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
32% identity, 86% coverage: 54:556/583 of query aligns to 28:498/506 of 4gxqA
- active site: T163 (= T219), N183 (= N239), H207 (= H265), T303 (= T363), E304 (= E364), I403 (≠ L464), N408 (= N469), A491 (≠ K549)
- binding adenosine-5'-triphosphate: T163 (= T219), S164 (≠ G220), G165 (= G221), T166 (= T222), T167 (= T223), H207 (= H265), S277 (= S337), A278 (= A338), P279 (= P339), E298 (= E358), M302 (≠ L362), T303 (= T363), D382 (= D443), R397 (= R458)
- binding carbonate ion: H207 (= H265), S277 (= S337), R299 (≠ G359), G301 (= G361)
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)
31% identity, 86% coverage: 56:556/583 of query aligns to 65:547/556 of Q9S725
- K211 (= K227) mutation to S: Drastically reduces the activity.
- M293 (≠ P307) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I334) mutation K->L,A: Affects the substrate specificity.
- E401 (= E411) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ I413) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R458) mutation to Q: Drastically reduces the activity.
- K457 (≠ G466) mutation to S: Drastically reduces the activity.
- K540 (= K549) mutation to N: Abolishes the activity.
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
30% identity, 92% coverage: 34:567/583 of query aligns to 15:518/518 of 4wv3B
- active site: S175 (≠ T219), T320 (= T363), E321 (= E364), K418 (≠ L464), W423 (≠ N469), K502 (= K549)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H265), T221 (≠ V266), F222 (≠ Y267), A293 (≠ G336), S294 (= S337), E295 (≠ A338), A296 (≠ P339), G316 (= G359), I317 (≠ F360), G318 (= G361), C319 (≠ L362), T320 (= T363), D397 (= D443), H409 (≠ I455), R412 (= R458), K502 (= K549)
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, 86% coverage: 54:555/583 of query aligns to 57:536/546 of Q84P21
- K530 (= K549) mutation to N: Lossed enzymatic activity.
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
31% identity, 90% coverage: 35:558/583 of query aligns to 25:528/529 of 5bsvA
- active site: S182 (≠ T219), S202 (≠ N239), H230 (= H265), T329 (= T363), E330 (= E364), K434 (≠ L464), Q439 (≠ N469), K519 (= K549)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H265), Y232 (= Y267), S236 (≠ T271), A302 (≠ S337), A303 (= A338), P304 (= P339), G325 (= G359), G327 (= G361), M328 (≠ L362), T329 (= T363), P333 (= P367), V334 (= V368), D413 (= D443), K430 (= K460), K434 (≠ L464), Q439 (≠ N469)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
31% identity, 90% coverage: 35:558/583 of query aligns to 25:528/529 of 5bsuA
- active site: S182 (≠ T219), S202 (≠ N239), H230 (= H265), T329 (= T363), E330 (= E364), K434 (≠ L464), Q439 (≠ N469), K519 (= K549)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H265), Y232 (= Y267), S236 (≠ T271), M299 (≠ I334), A302 (≠ S337), A303 (= A338), P304 (= P339), G325 (= G359), G327 (= G361), M328 (≠ L362), T329 (= T363), P333 (= P367), D413 (= D443), K430 (= K460), K434 (≠ L464), Q439 (≠ N469)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
31% identity, 90% coverage: 35:558/583 of query aligns to 25:528/529 of 5bstA
- active site: S182 (≠ T219), S202 (≠ N239), H230 (= H265), T329 (= T363), E330 (= E364), K434 (≠ L464), Q439 (≠ N469), K519 (= K549)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H265), Y232 (= Y267), S236 (≠ T271), A302 (≠ S337), A303 (= A338), P304 (= P339), G325 (= G359), Y326 (≠ F360), G327 (= G361), M328 (≠ L362), T329 (= T363), P333 (= P367), V334 (= V368), D413 (= D443), K430 (= K460), K434 (≠ L464), Q439 (≠ N469)
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)
31% identity, 90% coverage: 35:558/583 of query aligns to 32:535/542 of O24146
- S189 (≠ T219) binding
- S190 (≠ G220) binding
- G191 (= G221) binding
- T192 (= T222) binding
- T193 (= T223) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K227) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H265) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (= Y267) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ T271) binding ; binding ; binding
- K260 (≠ R288) binding
- A309 (≠ S337) binding ; binding ; binding
- Q331 (≠ E358) binding
- G332 (= G359) binding ; binding ; binding ; binding ; binding
- T336 (= T363) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V368) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ L371) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D443) binding ; binding ; binding ; binding ; binding
- R435 (= R458) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K460) binding ; binding ; binding ; binding
- K441 (≠ L464) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G466) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G467) binding
- Q446 (≠ N469) binding
- K526 (= K549) 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)
31% identity, 90% coverage: 35:558/583 of query aligns to 25:528/530 of 5bsmA
- active site: S182 (≠ T219), S202 (≠ N239), H230 (= H265), T329 (= T363), E330 (= E364), K434 (≠ L464), Q439 (≠ N469), K519 (= K549)
- binding adenosine-5'-triphosphate: S182 (≠ T219), S183 (≠ G220), G184 (= G221), T185 (= T222), T186 (= T223), K190 (= K227), H230 (= H265), A302 (≠ S337), A303 (= A338), P304 (= P339), Y326 (≠ F360), G327 (= G361), M328 (≠ L362), T329 (= T363), D413 (= D443), I425 (= I455), R428 (= R458), K519 (= K549)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
31% identity, 90% coverage: 35:558/583 of query aligns to 24:527/528 of 5bsrA
- active site: S181 (≠ T219), S201 (≠ N239), H229 (= H265), T328 (= T363), E329 (= E364), K433 (≠ L464), Q438 (≠ N469), K518 (= K549)
- binding adenosine monophosphate: A301 (≠ S337), G326 (= G361), T328 (= T363), D412 (= D443), K429 (= K460), K433 (≠ L464), Q438 (≠ N469)
- binding coenzyme a: L102 (= L112), P226 (= P262), H229 (= H265), Y231 (= Y267), F253 (≠ Y289), K435 (≠ G466), G436 (= G467), F437 (≠ Y468), F498 (≠ S529)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
31% identity, 90% coverage: 35:558/583 of query aligns to 24:524/527 of 5u95B
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)
31% identity, 86% coverage: 56:558/583 of query aligns to 61:544/559 of Q67W82
- G395 (= G410) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
Q4WR83 Acyl-CoA ligase sidI; Siderophore biosynthesis protein I; EC 6.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
31% identity, 89% coverage: 54:572/583 of query aligns to 64:586/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
30% identity, 90% coverage: 34:558/583 of query aligns to 7:496/503 of P9WQ37
- R9 (≠ D36) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (= R44) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K227) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R251) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ M253) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V266) 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 (≠ G268) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (= T271) 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 (≠ K302) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G361) 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 (= W438) 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 (= D443) 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 (= R458) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V465) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G467) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K549) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
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)
30% identity, 91% coverage: 31:562/583 of query aligns to 6:513/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 219:223) binding
- H214 (= H265) binding ; mutation to A: Abolished activity.
- S289 (= S337) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ SAP 337:339) binding
- EA 310:311 (≠ EG 358:359) binding
- M314 (≠ L362) binding
- T315 (= T363) binding
- H319 (≠ P367) binding ; mutation to A: Abolished activity.
- D394 (= D443) binding
- R409 (= R458) binding ; mutation to A: Abolished activity.
- K500 (= K549) binding ; binding ; mutation to A: Abolished activity.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
28% identity, 93% coverage: 17:556/583 of query aligns to 11:526/528 of 3ni2A
- active site: S182 (≠ T219), S202 (≠ N239), H230 (= H265), T329 (= T363), E330 (= E364), K434 (≠ L464), Q439 (≠ N469), K519 (= K549)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (= Y267), S236 (≠ T271), G302 (≠ S337), A303 (= A338), P304 (= P339), G325 (= G359), G327 (= G361), T329 (= T363), P333 (= P367), V334 (= V368), D413 (= D443), K430 (= K460), K434 (≠ L464), Q439 (≠ N469)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
28% identity, 93% coverage: 17:556/583 of query aligns to 11:526/528 of 3a9vA
- active site: S182 (≠ T219), S202 (≠ N239), H230 (= H265), T329 (= T363), E330 (= E364), K434 (≠ L464), Q439 (≠ N469), K519 (= K549)
- binding adenosine monophosphate: H230 (= H265), G302 (≠ S337), A303 (= A338), P304 (= P339), Y326 (≠ F360), G327 (= G361), M328 (≠ L362), T329 (= T363), D413 (= D443), K430 (= K460), K434 (≠ L464), Q439 (≠ N469)
5ie3A Crystal structure of a plant enzyme (see paper)
30% identity, 90% coverage: 31:555/583 of query aligns to 6:499/504 of 5ie3A
- active site: T163 (= T219), S183 (≠ N239), H207 (= H265), T308 (= T363), E309 (= E364), N408 (≠ L464), K413 (≠ N469), K493 (= K549)
- binding adenosine monophosphate: S164 (≠ G220), S282 (= S337), A283 (= A338), S284 (≠ P339), Y305 (≠ F360), A306 (≠ G361), M307 (≠ L362), T308 (= T363), D387 (= D443), L399 (≠ I455), R402 (= R458), K493 (= K549)
- binding oxalic acid: V208 (= V266), S282 (= S337), A306 (≠ G361), M307 (≠ L362), H312 (≠ P367), K493 (= K549)
5ie2A Crystal structure of a plant enzyme (see paper)
30% identity, 90% coverage: 31:555/583 of query aligns to 6:501/506 of 5ie2A
- active site: T165 (= T219), S185 (≠ N239), H209 (= H265), T310 (= T363), E311 (= E364), N410 (≠ L464), K415 (≠ N469), K495 (= K549)
- binding adenosine-5'-triphosphate: T165 (= T219), S166 (≠ G220), G167 (= G221), T168 (= T222), T169 (= T223), S284 (= S337), A285 (= A338), S286 (≠ P339), Y307 (≠ F360), A308 (≠ G361), M309 (≠ L362), T310 (= T363), D389 (= D443), L401 (≠ I455), R404 (= R458), K495 (= K549)
Query Sequence
>8499484 FitnessBrowser__Miya:8499484
MTEPNTSADFPWLASYDAGVPANISYETFPLFTLLDRAAERTPRRTAIAFRNYRISYAKL
RQLAEVMAANLRAQGVRRGDKVSIMLPNLPQTVIAFWAVLKAGGVVVMTNPLYMEKELVH
QIHDSGARFMIALDLVWPKIEPLREKLGIDKYFLTRIGDGLAFPLNFLYAFKAKREGTWR
ELPFDGRHVLPWKTLLKGKVRHSTTTCNPTEDLAVLQYTGGTTGISKGVMLTHHNMSVNV
QQITTILGDARDMDHCFLGLMPYFHVYGLTTCLTLPTALAATIVPFPRYVPRDVLVGIQK
HKPTIFPGAPSIYISLMQQKEVGDYDLTSIRYCISGSAPMPVEHIKRFRELTGAQVIEGF
GLTEASPVTHLNPIHGVSKTGSIGIPFPDTEARIVDMEVGQVPLPAGKVGELIIRGPQVM
KGYWNRPDETANTLRNGWLYTGDIAIMDEDGYFTIVDRKKDMFLVGGYNVYPREIDEVLH
EHPKIKEAVTVGVPHPTRGEMIKAFVVVKPGEKLTKAEVVAHCREKLASYKVPKQVEFRD
DLPKTVVGKVLRRILRTEEEEKLKAELAASPATAAASDDDGAQ
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