SitesBLAST
Comparing 8501639 FitnessBrowser__Miya:8501639 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, 97% coverage: 10:545/550 of query aligns to 38:577/590 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)
32% identity, 97% coverage: 7:541/550 of query aligns to 21:553/561 of P69451
- Y213 (= Y199) mutation to A: Loss of activity.
- T214 (= T200) mutation to A: 10% of wild-type activity.
- G216 (= G202) mutation to A: Decreases activity.
- T217 (= T203) mutation to A: Decreases activity.
- G219 (= G205) mutation to A: Decreases activity.
- K222 (= K208) mutation to A: Decreases activity.
- E361 (= E344) mutation to A: Loss of activity.
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, 92% coverage: 38:542/550 of query aligns to 65:551/556 of Q9S725
- K211 (= K208) mutation to S: Drastically reduces the activity.
- M293 (≠ Y286) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I313) mutation K->L,A: Affects the substrate specificity.
- E401 (= E392) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ V394) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R440) mutation to Q: Drastically reduces the activity.
- K457 (≠ G448) mutation to S: Drastically reduces the activity.
- K540 (= K531) 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)
29% identity, 98% coverage: 9:547/550 of query aligns to 2:503/503 of P9WQ37
- R9 (≠ D16) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D24) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K208) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T231) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ K233) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C245) 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 (≠ G247) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ L250) 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 (≠ K281) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G341) 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 (= W420) 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 (= D425) 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 (= R440) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R447) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G449) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K531) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
29% identity, 92% coverage: 38:545/550 of query aligns to 30:505/506 of 4gxqA
- active site: T163 (= T200), N183 (= N220), H207 (= H244), T303 (= T343), E304 (= E344), I403 (= I446), N408 (= N451), A491 (≠ K531)
- binding adenosine-5'-triphosphate: T163 (= T200), S164 (= S201), G165 (= G202), T166 (= T203), T167 (= T204), H207 (= H244), S277 (= S317), A278 (≠ V318), P279 (≠ C319), E298 (≠ I338), M302 (≠ L342), T303 (= T343), D382 (= D425), R397 (= R440)
- binding carbonate ion: H207 (= H244), S277 (= S317), R299 (≠ C339), G301 (= G341)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
29% identity, 98% coverage: 9:546/550 of query aligns to 5:502/502 of 3r44A
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)
28% identity, 92% coverage: 27:534/550 of query aligns to 18:497/512 of O74976
- S283 (≠ P320) modified: Phosphoserine
- S284 (≠ E321) modified: Phosphoserine
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)
27% identity, 96% coverage: 17:546/550 of query aligns to 33:541/542 of O24146
- S189 (≠ T200) binding
- S190 (= S201) binding
- G191 (= G202) binding
- T192 (= T203) binding
- T193 (= T204) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K208) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H244) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F246) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ L250) binding ; binding ; binding
- K260 (≠ S267) binding
- A309 (≠ G316) binding ; binding ; binding
- Q331 (≠ I338) binding
- G332 (≠ C339) binding ; binding ; binding ; binding ; binding
- T336 (= T343) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V348) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ Q351) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D425) binding ; binding ; binding ; binding ; binding
- R435 (= R440) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K442) binding ; binding ; binding ; binding
- K441 (≠ I446) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G448) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G449) binding
- Q446 (≠ N451) binding
- K526 (= K531) 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)
27% identity, 96% coverage: 17:542/550 of query aligns to 26:530/530 of 5bsmA
- active site: S182 (≠ T200), S202 (≠ N216), H230 (= H244), T329 (= T343), E330 (= E344), K434 (≠ I446), Q439 (≠ N451), K519 (= K531)
- binding adenosine-5'-triphosphate: S182 (≠ T200), S183 (= S201), G184 (= G202), T185 (= T203), T186 (= T204), K190 (= K208), H230 (= H244), A302 (≠ G316), A303 (≠ S317), P304 (≠ V318), Y326 (= Y340), G327 (= G341), M328 (≠ L342), T329 (= T343), D413 (= D425), I425 (= I437), R428 (= R440), K519 (= K531)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
27% identity, 95% coverage: 17:538/550 of query aligns to 25:525/528 of 5bsrA
- active site: S181 (≠ T200), S201 (≠ N216), H229 (= H244), T328 (= T343), E329 (= E344), K433 (≠ I446), Q438 (≠ N451), K518 (= K531)
- binding adenosine monophosphate: A301 (≠ G316), G326 (= G341), T328 (= T343), D412 (= D425), K429 (= K442), K433 (≠ I446), Q438 (≠ N451)
- binding coenzyme a: L102 (≠ N94), P226 (= P241), H229 (= H244), Y231 (≠ F246), F253 (= F268), K435 (≠ G448), G436 (= G449), F437 (≠ E450), F498 (≠ W511)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
27% identity, 95% coverage: 17:538/550 of query aligns to 26:526/529 of 5bsvA
- active site: S182 (≠ T200), S202 (≠ N216), H230 (= H244), T329 (= T343), E330 (= E344), K434 (≠ I446), Q439 (≠ N451), K519 (= K531)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H244), Y232 (≠ F246), S236 (≠ L250), A302 (≠ G316), A303 (≠ S317), P304 (≠ V318), G325 (≠ C339), G327 (= G341), M328 (≠ L342), T329 (= T343), P333 (= P347), V334 (= V348), D413 (= D425), K430 (= K442), K434 (≠ I446), Q439 (≠ N451)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
27% identity, 95% coverage: 17:538/550 of query aligns to 26:526/529 of 5bsuA
- active site: S182 (≠ T200), S202 (≠ N216), H230 (= H244), T329 (= T343), E330 (= E344), K434 (≠ I446), Q439 (≠ N451), K519 (= K531)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H244), Y232 (≠ F246), S236 (≠ L250), M299 (≠ I313), A302 (≠ G316), A303 (≠ S317), P304 (≠ V318), G325 (≠ C339), G327 (= G341), M328 (≠ L342), T329 (= T343), P333 (= P347), D413 (= D425), K430 (= K442), K434 (≠ I446), Q439 (≠ N451)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
27% identity, 95% coverage: 17:538/550 of query aligns to 26:526/529 of 5bstA
- active site: S182 (≠ T200), S202 (≠ N216), H230 (= H244), T329 (= T343), E330 (= E344), K434 (≠ I446), Q439 (≠ N451), K519 (= K531)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H244), Y232 (≠ F246), S236 (≠ L250), A302 (≠ G316), A303 (≠ S317), P304 (≠ V318), G325 (≠ C339), Y326 (= Y340), G327 (= G341), M328 (≠ L342), T329 (= T343), P333 (= P347), V334 (= V348), D413 (= D425), K430 (= K442), K434 (≠ I446), Q439 (≠ N451)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
27% identity, 91% coverage: 38:539/550 of query aligns to 47:527/528 of 3ni2A
- active site: S182 (≠ T200), S202 (≠ N216), H230 (= H244), T329 (= T343), E330 (= E344), K434 (≠ I446), Q439 (≠ N451), K519 (= K531)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F246), S236 (≠ L250), G302 (= G316), A303 (≠ S317), P304 (≠ V318), G325 (≠ C339), G327 (= G341), T329 (= T343), P333 (= P347), V334 (= V348), D413 (= D425), K430 (= K442), K434 (≠ I446), Q439 (≠ N451)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
27% identity, 91% coverage: 38:539/550 of query aligns to 47:527/528 of 3a9vA
- active site: S182 (≠ T200), S202 (≠ N216), H230 (= H244), T329 (= T343), E330 (= E344), K434 (≠ I446), Q439 (≠ N451), K519 (= K531)
- binding adenosine monophosphate: H230 (= H244), G302 (= G316), A303 (≠ S317), P304 (≠ V318), Y326 (= Y340), G327 (= G341), M328 (≠ L342), T329 (= T343), D413 (= D425), K430 (= K442), K434 (≠ I446), Q439 (≠ N451)
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
28% identity, 94% coverage: 10:525/550 of query aligns to 5:493/504 of 6qjzA
- active site: T169 (= T200), S189 (≠ N220), H213 (= H244), T314 (= T343), E315 (= E344), N414 (≠ I446), K419 (≠ N451)
- binding adenosine monophosphate: H213 (= H244), S288 (= S317), A289 (≠ V318), S290 (≠ C319), A312 (≠ G341), M313 (≠ L342), T314 (= T343), D393 (= D425), L405 (≠ I437), K410 (= K442), K419 (≠ N451)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
27% identity, 96% coverage: 17:542/550 of query aligns to 25:526/527 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)
28% identity, 93% coverage: 38:546/550 of query aligns to 61:550/559 of Q67W82
- G395 (= G391) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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, 98% coverage: 1:539/550 of query aligns to 14:532/541 of Q5SKN9
- T184 (= T200) binding
- G302 (= G316) binding
- Q322 (≠ I338) binding
- G323 (≠ C339) binding
- T327 (= T343) binding
- E328 (= E344) binding
- D418 (= D425) binding
- K435 (= K442) binding
- K439 (≠ I446) binding
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)
25% identity, 94% coverage: 28:543/550 of query aligns to 47:542/546 of Q84P21
- K530 (= K531) mutation to N: Lossed enzymatic activity.
Query Sequence
>8501639 FitnessBrowser__Miya:8501639
MDEFAVRERTLGQILDETVAKYPDNDAVIYVDRDYRQTYRQFSQVVDDLAKGLMALGVRH
GEKVAVWATNVPYWVALQFATAKMGAILLTVNTNYREHEIRYLLTQSECENLFIIDGFRD
HDYVQTIYNMIPELKTQPRGQLRCSSLPHLKRVMFLGAEKHRGMYSVPEIISMSAMVSDE
EYAERQRALDPHDVVNMQYTSGTTGFPKGVMLTHVNIGNNGYWIGKNQHFTEKDRVCLPV
PLFHCFGCVLGVLAAINHGAALVILESFSPMHVMASVDQEKCTALYGVPTMFLAVLEHKL
FERFDFSSLRTGIMAGSVCPEPLMRRVVEKMYMREITICYGLTEGSPVMTQSLVTDPFER
RVQTVGRAMPCIEVRIVDPDTNEEVPRGTQGEVVCRGYNVMKGYYNMPEATTAAIDADGW
LHSGDLGVMDEEGYVVITGRIKDMIIRGGENIYPREIEEFLYGMDGVQDVQVVGVNSRKY
GEEVGAFIIPKPGVEMAPEDVRDYCRGRIAWHKVPRYISFIDAYPMTASGKIQKFKLREM
AAELFPEAMK
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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