SitesBLAST
Comparing Ga0059261_1004 FitnessBrowser__Korea:Ga0059261_1004 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
36% identity, 97% coverage: 10:561/571 of query aligns to 2:549/561 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.
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, 90% coverage: 53:566/571 of query aligns to 61:551/556 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 (≠ V413) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R463) mutation to Q: Drastically reduces the activity.
- K457 (≠ G471) mutation to S: Drastically reduces the activity.
- K540 (= K555) mutation to N: Abolishes the 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)
32% identity, 90% coverage: 53:567/571 of query aligns to 57:547/559 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)
30% identity, 95% coverage: 21:561/571 of query aligns to 28:569/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
33% identity, 90% coverage: 56:567/571 of query aligns to 53:538/542 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 (≠ F267) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ C271) binding ; binding ; binding
- K260 (≠ R288) binding
- A309 (≠ G337) binding ; binding ; binding
- Q331 (≠ E358) binding
- G332 (= G359) binding ; binding ; binding ; binding ; binding
- T336 (≠ S363) 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 (≠ A371) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D448) binding ; binding ; binding ; binding ; binding
- R435 (= R463) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K465) binding ; binding ; binding ; binding
- K441 (≠ A469) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G471) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G472) binding
- Q446 (≠ K474) binding
- K526 (= K555) binding ; mutation to A: Abolished activity against 4-coumarate.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
33% identity, 89% coverage: 53:561/571 of query aligns to 43:525/528 of 3ni2A
- active site: S182 (≠ T219), S202 (≠ A238), H230 (= H265), T329 (≠ S363), E330 (= E364), K434 (≠ A469), Q439 (≠ K474), K519 (= K555)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F267), S236 (≠ C271), G302 (= G337), A303 (= A338), P304 (= P339), G325 (= G359), G327 (= G361), T329 (≠ S363), P333 (≠ G367), V334 (= V368), D413 (= D448), K430 (= K465), K434 (≠ A469), Q439 (≠ K474)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
33% identity, 89% coverage: 53:561/571 of query aligns to 43:525/528 of 3a9vA
- active site: S182 (≠ T219), S202 (≠ A238), H230 (= H265), T329 (≠ S363), E330 (= E364), K434 (≠ A469), Q439 (≠ K474), K519 (= K555)
- binding adenosine monophosphate: H230 (= H265), G302 (= G337), A303 (= A338), P304 (= P339), Y326 (= Y360), G327 (= G361), M328 (≠ L362), T329 (≠ S363), D413 (= D448), K430 (= K465), K434 (≠ A469), Q439 (≠ K474)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
33% identity, 89% coverage: 56:566/571 of query aligns to 46:530/530 of 5bsmA
- active site: S182 (≠ T219), S202 (≠ A238), H230 (= H265), T329 (≠ S363), E330 (= E364), K434 (≠ A469), Q439 (≠ K474), K519 (= K555)
- binding adenosine-5'-triphosphate: S182 (≠ T219), S183 (≠ G220), G184 (= G221), T185 (= T222), T186 (= T223), K190 (= K227), H230 (= H265), A302 (≠ G337), A303 (= A338), P304 (= P339), Y326 (= Y360), G327 (= G361), M328 (≠ L362), T329 (≠ S363), D413 (= D448), I425 (= I460), R428 (= R463), K519 (= K555)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
33% identity, 89% coverage: 56:561/571 of query aligns to 46:525/529 of 5bsvA
- active site: S182 (≠ T219), S202 (≠ A238), H230 (= H265), T329 (≠ S363), E330 (= E364), K434 (≠ A469), Q439 (≠ K474), K519 (= K555)
- 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 (≠ F267), S236 (≠ C271), A302 (≠ G337), A303 (= A338), P304 (= P339), G325 (= G359), G327 (= G361), M328 (≠ L362), T329 (≠ S363), P333 (≠ G367), V334 (= V368), D413 (= D448), K430 (= K465), K434 (≠ A469), Q439 (≠ K474)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
33% identity, 89% coverage: 56:561/571 of query aligns to 46:525/529 of 5bsuA
- active site: S182 (≠ T219), S202 (≠ A238), H230 (= H265), T329 (≠ S363), E330 (= E364), K434 (≠ A469), Q439 (≠ K474), K519 (= K555)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H265), Y232 (≠ F267), S236 (≠ C271), M299 (≠ I334), A302 (≠ G337), A303 (= A338), P304 (= P339), G325 (= G359), G327 (= G361), M328 (≠ L362), T329 (≠ S363), P333 (≠ G367), D413 (= D448), K430 (= K465), K434 (≠ A469), Q439 (≠ K474)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
33% identity, 89% coverage: 56:561/571 of query aligns to 46:525/529 of 5bstA
- active site: S182 (≠ T219), S202 (≠ A238), H230 (= H265), T329 (≠ S363), E330 (= E364), K434 (≠ A469), Q439 (≠ K474), K519 (= K555)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H265), Y232 (≠ F267), S236 (≠ C271), A302 (≠ G337), A303 (= A338), P304 (= P339), G325 (= G359), Y326 (= Y360), G327 (= G361), M328 (≠ L362), T329 (≠ S363), P333 (≠ G367), V334 (= V368), D413 (= D448), K430 (= K465), K434 (≠ A469), Q439 (≠ K474)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
33% identity, 89% coverage: 56:561/571 of query aligns to 45:524/528 of 5bsrA
- active site: S181 (≠ T219), S201 (≠ A238), H229 (= H265), T328 (≠ S363), E329 (= E364), K433 (≠ A469), Q438 (≠ K474), K518 (= K555)
- binding adenosine monophosphate: A301 (≠ G337), G326 (= G361), T328 (≠ S363), D412 (= D448), K429 (= K465), K433 (≠ A469), Q438 (≠ K474)
- binding coenzyme a: L102 (= L113), P226 (= P262), H229 (= H265), Y231 (≠ F267), F253 (= F289), K435 (≠ G471), G436 (= G472), F437 (= F473), F498 (≠ K535)
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: 26:570/571 of query aligns to 25:544/546 of Q84P21
- K530 (= K555) mutation to N: Lossed enzymatic activity.
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
33% identity, 90% coverage: 56:567/571 of query aligns to 45:527/527 of 5u95B
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, 88% coverage: 57:561/571 of query aligns to 31:493/503 of P9WQ37
- K172 (= K227) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ E249) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ K254) 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 (= A268) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ C271) 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 (= R302) 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 (= W443) 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 (= D448) 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 (= R463) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V470) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G472) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K555) 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.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
30% identity, 88% coverage: 57:561/571 of query aligns to 34:493/502 of 3r44A
Sites not aligning to the query:
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
34% identity, 61% coverage: 213:561/571 of query aligns to 157:497/506 of 4gxqA
- active site: T163 (= T219), N183 (= N239), H207 (= H265), T303 (≠ S363), E304 (= E364), I403 (≠ A469), N408 (≠ K474), A491 (≠ K555)
- binding adenosine-5'-triphosphate: T163 (= T219), S164 (≠ G220), G165 (= G221), T166 (= T222), T167 (= T223), H207 (= H265), S277 (≠ G337), A278 (= A338), P279 (= P339), E298 (= E358), M302 (≠ L362), T303 (≠ S363), D382 (= D448), R397 (= R463)
- binding carbonate ion: H207 (= H265), S277 (≠ G337), R299 (≠ G359), G301 (= G361)
5ie3A Crystal structure of a plant enzyme (see paper)
29% identity, 93% coverage: 31:559/571 of query aligns to 5:497/504 of 5ie3A
- active site: T163 (= T219), S183 (vs. gap), H207 (= H265), T308 (≠ S363), E309 (= E364), N408 (≠ A469), K413 (= K474), K493 (= K555)
- binding adenosine monophosphate: S164 (≠ G220), S282 (≠ G337), A283 (= A338), S284 (≠ P339), Y305 (= Y360), A306 (≠ G361), M307 (≠ L362), T308 (≠ S363), D387 (= D448), L399 (≠ I460), R402 (= R463), K493 (= K555)
- binding oxalic acid: V208 (= V266), S282 (≠ G337), A306 (≠ G361), M307 (≠ L362), H312 (≠ G367), K493 (= K555)
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)
30% identity, 88% coverage: 57:561/571 of query aligns to 49:530/541 of Q5SKN9
- T184 (= T219) binding
- G302 (= G337) binding
- Q322 (≠ E358) binding
- G323 (= G359) binding
- T327 (≠ S363) binding
- E328 (= E364) binding
- D418 (= D448) binding
- K435 (= K465) binding
- K439 (≠ A469) binding
5x8fB Ternary complex structure of a double mutant i454ra456k of o- succinylbenzoate coa synthetase (mene) from bacillus subtilis bound with amp and its product analogue osb-ncoa at 1.76 angstrom (see paper)
33% identity, 61% coverage: 214:561/571 of query aligns to 146:476/485 of 5x8fB
- active site: T151 (= T219), S171 (≠ N239), H195 (= H265), T288 (≠ S363), E289 (= E364), I387 (≠ A469), N392 (≠ K474), K470 (= K555)
- binding magnesium ion: N178 (≠ E249), L202 (= L273), L214 (≠ M285), T296 (≠ S370), L297 (≠ A371), S298 (≠ N372)
- binding o-succinylbenzoyl-N-coenzyme A: L191 (= L261), P192 (= P262), H195 (= H265), I196 (≠ V266), S197 (≠ A268), A237 (≠ G308), V238 (= V309), L260 (≠ I334), G262 (= G336), G286 (= G361), M287 (≠ L362), S292 (= S366), Q293 (≠ G367), S388 (≠ V470), G389 (= G471), G390 (= G472), E391 (≠ F473), K420 (≠ Y502), W421 (≠ R503), K450 (= K535), Y451 (≠ H536)
Sites not aligning to the query:
Query Sequence
>Ga0059261_1004 FitnessBrowser__Korea:Ga0059261_1004
MSVPEQVWPEQVWRTAYRHPGPWDQPLPPLSMAAAFDDSAQRMGNAPLLDFMGRHYSYAE
TLDGANRVACGLRALGYGPGDRIGLFLPNVPHYVAAYYGILKLGATVVNFSPLYSVEELE
AQVADSGTRLLFTISATALLPTALKVLEASSLERLVVGSVAGALPAAKSLLYRWFKAKEV
AEKPDDPRIIAFSKLIANDGACTTAAIDPETHLALIQYTGGTTGVPKGAMLTHQNLTANA
RQVARLDPELGTTKDKVLGVLPFFHVFANTCVLNRTVITGGEIVMLPRFDAAQALAAITR
TRPLALPGVPTMFQALLDHPNSASTDWSSLKYCISGGAPLPAELKTRFEAATGAKLIEGY
GLSESSGVVSANPYVAEGKSGTIGQPIIATRVRLVDKEDPSKPAPEGEPGEIVVAGPQIM
GGYWDRPETDDSTFCTDATGQKWLRTGDVGQIDEDGFIKIVDRLKDMIAVGGFKVFPKHI
EDVLYRHPAVKEALVVGMPDSYRGETPRAYVALNDDADPVTGNALRDWLNPQLGKHERVD
AVVIRDKLPKTMIGKLSRKDLLIEIAAEASV
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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