SitesBLAST
Comparing 201132 FitnessBrowser__MR1:201132 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)
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)
39% identity, 95% coverage: 18:567/578 of query aligns to 19:572/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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: 32:566/578 of query aligns to 27:551/561 of P69451
- Y213 (≠ F226) mutation to A: Loss of activity.
- T214 (= T227) mutation to A: 10% of wild-type activity.
- G216 (= G229) mutation to A: Decreases activity.
- T217 (= T230) mutation to A: Decreases activity.
- G219 (= G232) mutation to A: Decreases activity.
- K222 (= K235) mutation to A: Decreases activity.
- E361 (= E372) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 92% coverage: 42:574/578 of query aligns to 13:506/506 of 4gxqA
- active site: T163 (= T227), N183 (= N247), H207 (= H271), T303 (= T371), E304 (= E372), I403 (= I473), N408 (= N478), A491 (≠ K558)
- binding adenosine-5'-triphosphate: T163 (= T227), S164 (= S228), G165 (= G229), T166 (= T230), T167 (= T231), H207 (= H271), S277 (≠ G344), A278 (= A345), P279 (≠ T346), E298 (≠ I366), M302 (≠ Q370), T303 (= T371), D382 (= D452), R397 (= R467)
- binding carbonate ion: H207 (= H271), S277 (≠ G344), R299 (≠ G367), G301 (= G369)
6e97B Crystal structure of the aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with dhb-adenylate
29% identity, 93% coverage: 36:572/578 of query aligns to 22:536/537 of 6e97B
- active site: S190 (≠ T227), S210 (≠ N247), H234 (= H271), A336 (≠ Q362), E337 (= E363), N437 (≠ I473), K442 (≠ N478), K522 (= K558)
- binding 5'-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine: H234 (= H271), N235 (≠ C272), F236 (= F273), S240 (≠ L277), G310 (= G344), A311 (= A345), K312 (≠ T346), V332 (≠ L358), F333 (≠ M359), G334 (≠ Y360), M335 (= M361), A336 (≠ Q362), D416 (= D452), K433 (= K469), K442 (≠ N478)
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, 85% coverage: 76:565/578 of query aligns to 76:547/556 of Q9S725
- K211 (= K235) mutation to S: Drastically reduces the activity.
- M293 (≠ H314) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V341) mutation K->L,A: Affects the substrate specificity.
- E401 (= E419) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C421) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R467) mutation to Q: Drastically reduces the activity.
- K457 (≠ G475) mutation to S: Drastically reduces the activity.
- K540 (= K558) mutation to N: Abolishes the activity.
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, 92% coverage: 36:566/578 of query aligns to 2:495/503 of P9WQ37
- R9 (≠ D43) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ E51) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K235) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T258) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ D260) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C272) 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 (≠ V276) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ N279) 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 (= R309) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G369) 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 (= W447) 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 (= D452) 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 (= R467) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R474) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G476) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K558) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
6e8oA Crystal structure of aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with amp
29% identity, 93% coverage: 36:572/578 of query aligns to 22:535/536 of 6e8oA
- active site: S190 (≠ T227), S210 (≠ N247), H234 (= H271), A336 (≠ Q362), E337 (= E363), N437 (≠ I473), K442 (≠ N478), K521 (= K558)
- binding adenosine monophosphate: H234 (= H271), G310 (= G344), A311 (= A345), K312 (≠ T346), V332 (≠ L358), F333 (≠ M359), G334 (≠ Y360), M335 (= M361), A336 (≠ Q362), D416 (= D452), V428 (≠ I464), K442 (≠ N478)
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)
30% identity, 88% coverage: 56:565/578 of query aligns to 52:533/542 of O24146
- S189 (≠ T227) binding
- S190 (= S228) binding
- G191 (= G229) binding
- T192 (= T230) binding
- T193 (= T231) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K235) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H271) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F273) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ G278) binding ; binding ; binding
- K260 (≠ S295) binding
- A309 (≠ G344) binding ; binding ; binding
- Q331 (≠ I366) binding
- G332 (= G367) binding ; binding ; binding ; binding ; binding
- T336 (= T371) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ L376) 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 (= D452) binding ; binding ; binding ; binding ; binding
- R435 (= R467) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K469) binding ; binding ; binding ; binding
- K441 (≠ I473) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G475) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G476) binding
- Q446 (≠ N478) binding
- K526 (= K558) 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)
30% identity, 88% coverage: 56:565/578 of query aligns to 45:526/530 of 5bsmA
- active site: S182 (≠ T227), S202 (vs. gap), H230 (= H271), T329 (= T371), E330 (= E372), K434 (≠ I473), Q439 (≠ N478), K519 (= K558)
- binding adenosine-5'-triphosphate: S182 (≠ T227), S183 (= S228), G184 (= G229), T185 (= T230), T186 (= T231), K190 (= K235), H230 (= H271), A302 (≠ G344), A303 (= A345), P304 (≠ T346), Y326 (= Y368), G327 (= G369), M328 (≠ Q370), T329 (= T371), D413 (= D452), I425 (= I464), R428 (= R467), K519 (= K558)
5ie2A Crystal structure of a plant enzyme (see paper)
30% identity, 91% coverage: 37:561/578 of query aligns to 5:498/506 of 5ie2A
- active site: T165 (= T227), S185 (≠ N247), H209 (= H271), T310 (= T371), E311 (= E372), N410 (≠ I473), K415 (≠ N478), K495 (= K558)
- binding adenosine-5'-triphosphate: T165 (= T227), S166 (= S228), G167 (= G229), T168 (= T230), T169 (= T231), S284 (≠ G344), A285 (= A345), S286 (≠ T346), Y307 (= Y368), A308 (≠ G369), M309 (≠ Q370), T310 (= T371), D389 (= D452), L401 (≠ I464), R404 (= R467), K495 (= K558)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 88% coverage: 56:565/578 of query aligns to 45:526/529 of 5bsvA
- active site: S182 (≠ T227), S202 (vs. gap), H230 (= H271), T329 (= T371), E330 (= E372), K434 (≠ I473), Q439 (≠ N478), K519 (= K558)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H271), Y232 (≠ F273), S236 (≠ G278), A302 (≠ G344), A303 (= A345), P304 (≠ T346), G325 (= G367), G327 (= G369), M328 (≠ Q370), T329 (= T371), P333 (= P375), V334 (≠ L376), D413 (= D452), K430 (= K469), K434 (≠ I473), Q439 (≠ N478)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 88% coverage: 56:565/578 of query aligns to 45:526/529 of 5bsuA
- active site: S182 (≠ T227), S202 (vs. gap), H230 (= H271), T329 (= T371), E330 (= E372), K434 (≠ I473), Q439 (≠ N478), K519 (= K558)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H271), Y232 (≠ F273), S236 (≠ G278), M299 (≠ V341), A302 (≠ G344), A303 (= A345), P304 (≠ T346), G325 (= G367), G327 (= G369), M328 (≠ Q370), T329 (= T371), P333 (= P375), D413 (= D452), K430 (= K469), K434 (≠ I473), Q439 (≠ N478)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
30% identity, 88% coverage: 56:565/578 of query aligns to 45:526/529 of 5bstA
- active site: S182 (≠ T227), S202 (vs. gap), H230 (= H271), T329 (= T371), E330 (= E372), K434 (≠ I473), Q439 (≠ N478), K519 (= K558)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H271), Y232 (≠ F273), S236 (≠ G278), A302 (≠ G344), A303 (= A345), P304 (≠ T346), G325 (= G367), Y326 (= Y368), G327 (= G369), M328 (≠ Q370), T329 (= T371), P333 (= P375), V334 (≠ L376), D413 (= D452), K430 (= K469), K434 (≠ I473), Q439 (≠ N478)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 88% coverage: 56:565/578 of query aligns to 44:525/528 of 5bsrA
- active site: S181 (≠ T227), S201 (vs. gap), H229 (= H271), T328 (= T371), E329 (= E372), K433 (≠ I473), Q438 (≠ N478), K518 (= K558)
- binding adenosine monophosphate: A301 (≠ G344), G326 (= G369), T328 (= T371), D412 (= D452), K429 (= K469), K433 (≠ I473), Q438 (≠ N478)
- binding coenzyme a: L102 (≠ A121), P226 (= P268), H229 (= H271), Y231 (≠ F273), F253 (= F296), K435 (≠ G475), G436 (= G476), F437 (≠ E477), F498 (≠ Y538)
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)
29% identity, 85% coverage: 77:565/578 of query aligns to 73:542/559 of Q67W82
- G395 (= G418) 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)
29% identity, 93% coverage: 37:574/578 of query aligns to 5:512/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 227:231) binding
- H214 (= H271) binding ; mutation to A: Abolished activity.
- S289 (≠ G344) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ GAT 344:346) binding
- EA 310:311 (≠ IG 366:367) binding
- M314 (≠ Q370) binding
- T315 (= T371) binding
- H319 (≠ P375) binding ; mutation to A: Abolished activity.
- D394 (= D452) binding
- R409 (= R467) binding ; mutation to A: Abolished activity.
- K500 (= K558) binding ; binding ; mutation to A: Abolished activity.
5ie3A Crystal structure of a plant enzyme (see paper)
30% identity, 91% coverage: 37:561/578 of query aligns to 5:496/504 of 5ie3A
- active site: T163 (= T227), S183 (≠ N247), H207 (= H271), T308 (= T371), E309 (= E372), N408 (≠ I473), K413 (≠ N478), K493 (= K558)
- binding adenosine monophosphate: S164 (= S228), S282 (≠ G344), A283 (= A345), S284 (≠ T346), Y305 (= Y368), A306 (≠ G369), M307 (≠ Q370), T308 (= T371), D387 (= D452), L399 (≠ I464), R402 (= R467), K493 (= K558)
- binding oxalic acid: V208 (≠ C272), S282 (≠ G344), A306 (≠ G369), M307 (≠ Q370), H312 (≠ P375), K493 (= K558)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
29% identity, 92% coverage: 36:566/578 of query aligns to 5:495/502 of 3r44A
Q5SKN9 Long-chain-fatty-acid--CoA ligase; Long-chain fatty acyl-CoA synthetase; LC-FACS; EC 6.2.1.3 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
29% identity, 88% coverage: 63:573/578 of query aligns to 47:538/541 of Q5SKN9
- T184 (= T227) binding
- G302 (= G344) binding
- Q322 (≠ I366) binding
- G323 (= G367) binding
- T327 (= T371) binding
- E328 (= E372) binding
- D418 (= D452) binding
- K435 (= K469) binding
- K439 (≠ I473) binding
5wm6A Crystal structure of cahj in complex with benzoyl adenylate (see paper)
28% identity, 92% coverage: 36:564/578 of query aligns to 27:530/535 of 5wm6A
- active site: S193 (≠ T227), N213 (= N247), H237 (= H271), A336 (≠ Q362), E337 (= E363), N437 (≠ I473), K442 (≠ N478), K524 (= K558)
- binding magnesium ion: S301 (= S335), L303 (= L337), G326 (vs. gap)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: F239 (= F273), G310 (= G344), S311 (≠ A345), K312 (≠ T346), V332 (≠ L358), F333 (≠ M359), G334 (≠ Y360), M335 (= M361), A336 (≠ Q362), D416 (= D452), K433 (= K469), K442 (≠ N478)
Query Sequence
>201132 FitnessBrowser__MR1:201132
MSVSTNQVTNQATNQTISPLKYSEFRGPNAPELVEKTIGQYLDDIANTYPEQLAVVVNHQ
DIRWNYRQYLARIDALAAGLLKLGIGPGDRIGIWSPNNIEWCLTQFATAKIGAIMVCINP
AYRPEELQYALTNVGCRAVICADKFKSSNYLQMLYTLAPELKECAAGQLQAKALPELQFV
IRMGAEKSPGMLNFDDLLVEVSADDKAMLERIANGLSPYDAINIQFTSGTTGSPKGATLS
HHNILNNGYLVAEAMKFTCDDKLCIPVPLYHCFGMVLGNLVCLAKGAAAVFPGDSFDPLT
TLEVVERERCTALHGVPTMFIAELEHPEFTRFDLSSLRTGVMAGATCPEEVMRRVQQLMY
MQEVLIGYGQTECSPLNHITEIDSPVEKRVLTVGRALPHTEVKIVDEFGEVLPINQPGEV
CSRGYCIMQCYWNDPEKTAATIDREGWLHSGDIGQMDEQGYVQIVGRIKDMIIRGGENIY
PREIEEKLYTHKDVQDAAVFGVHSDKYGEEVCAWIKVRSGATIKEEDIRHFLTEKFAYFK
VPRYIKFVDQYPMTVTGKIQKFKMRELMYQELYEDINA
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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