SitesBLAST
Comparing WP_007473537.1 NCBI__GCF_000170735.1:WP_007473537.1 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)
32% identity, 99% coverage: 4:518/519 of query aligns to 21:561/561 of P69451
- Y213 (= Y171) mutation to A: Loss of activity.
- T214 (= T172) mutation to A: 10% of wild-type activity.
- G216 (= G174) mutation to A: Decreases activity.
- T217 (= T175) mutation to A: Decreases activity.
- G219 (= G177) mutation to A: Decreases activity.
- K222 (= K180) mutation to A: Decreases activity.
- E361 (= E318) mutation to A: Loss of 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)
34% identity, 93% coverage: 29:509/519 of query aligns to 27:496/503 of P9WQ37
- K172 (= K180) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T203) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ K205) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ S217) 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 (≠ T219) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V222) 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 (= R254) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G315) 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 (= W389) 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 (= D394) 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 (= R409) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S416) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G418) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K500) 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)
33% identity, 97% coverage: 4:509/519 of query aligns to 3:496/502 of 3r44A
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
32% identity, 92% coverage: 31:509/519 of query aligns to 28:500/506 of 4gxqA
- active site: T163 (= T172), N183 (≠ D192), H207 (= H216), T303 (≠ S317), E304 (= E318), I403 (= I415), N408 (= N420), A491 (≠ K500)
- binding adenosine-5'-triphosphate: T163 (= T172), S164 (= S173), G165 (= G174), T166 (= T175), T167 (= T176), H207 (= H216), S277 (≠ A290), A278 (= A291), P279 (≠ A292), E298 (= E312), M302 (≠ L316), T303 (≠ S317), D382 (= D394), R397 (= R409)
- binding carbonate ion: H207 (= H216), S277 (≠ A290), R299 (≠ G313), G301 (= G315)
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, 93% coverage: 33:516/519 of query aligns to 65:556/556 of Q9S725
- K211 (= K180) mutation to S: Drastically reduces the activity.
- M293 (≠ T259) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V287) mutation K->L,A: Affects the substrate specificity.
- E401 (= E362) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ I364) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R409) mutation to Q: Drastically reduces the activity.
- K457 (= K417) mutation to S: Drastically reduces the activity.
- K540 (= K500) mutation to N: Abolishes the activity.
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
30% identity, 97% coverage: 5:508/519 of query aligns to 9:510/518 of 4wv3B
- active site: S175 (≠ T172), T320 (≠ S317), E321 (= E318), K418 (≠ I415), W423 (≠ N420), K502 (= K500)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H216), T221 (≠ S217), F222 (= F218), A293 (≠ G289), S294 (≠ A290), E295 (≠ A291), A296 (= A292), G316 (= G313), I317 (≠ Y314), G318 (= G315), C319 (≠ L316), T320 (≠ S317), D397 (= D394), H409 (≠ I406), R412 (= R409), K502 (= K500)
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)
30% identity, 92% coverage: 29:506/519 of query aligns to 25:500/512 of O74976
- S283 (≠ A290) modified: Phosphoserine
- S284 (≠ A291) modified: Phosphoserine
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
33% identity, 92% coverage: 33:508/519 of query aligns to 47:527/528 of 3ni2A
- active site: S182 (≠ T172), S202 (≠ D192), H230 (= H216), T329 (≠ S317), E330 (= E318), K434 (≠ I415), Q439 (≠ N420), K519 (= K500)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F218), S236 (≠ V222), G302 (≠ A290), A303 (= A291), P304 (≠ A292), G325 (= G313), G327 (= G315), T329 (≠ S317), P333 (= P321), V334 (= V322), D413 (= D394), K430 (= K411), K434 (≠ I415), Q439 (≠ N420)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
33% identity, 92% coverage: 33:508/519 of query aligns to 47:527/528 of 3a9vA
- active site: S182 (≠ T172), S202 (≠ D192), H230 (= H216), T329 (≠ S317), E330 (= E318), K434 (≠ I415), Q439 (≠ N420), K519 (= K500)
- binding adenosine monophosphate: H230 (= H216), G302 (≠ A290), A303 (= A291), P304 (≠ A292), Y326 (= Y314), G327 (= G315), M328 (≠ L316), T329 (≠ S317), D413 (= D394), K430 (= K411), K434 (≠ I415), Q439 (≠ N420)
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)
31% identity, 96% coverage: 12:508/519 of query aligns to 8:478/485 of 5x8fB
- active site: T151 (= T172), S171 (≠ D192), H195 (= H216), T288 (≠ S317), E289 (= E318), I387 (= I415), N392 (= N420), K470 (= K500)
- binding magnesium ion: Y23 (≠ I27), E24 (≠ D28), H70 (≠ F74), N178 (≠ I199), L202 (≠ N223), L214 (≠ I237), T296 (≠ V325), L297 (≠ N326), S298 (≠ R327)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ F89), L191 (= L212), P192 (= P213), H195 (= H216), I196 (≠ S217), S197 (≠ F218), A237 (≠ G260), V238 (= V261), L260 (≠ V287), G262 (= G289), G286 (= G315), M287 (≠ L316), S292 (≠ P321), Q293 (≠ V322), S388 (= S416), G389 (≠ K417), G390 (= G418), E391 (≠ V419), K420 (≠ N448), W421 (≠ H449), K450 (≠ N480), Y451 (= Y481)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
31% identity, 96% coverage: 12:508/519 of query aligns to 8:478/484 of 5gtdA
- active site: T151 (= T172), S171 (≠ D192), H195 (= H216), T288 (≠ S317), E289 (= E318)
- binding adenosine-5'-monophosphate: G263 (≠ A290), G264 (≠ A291), Y285 (= Y314), G286 (= G315), M287 (≠ L316), T288 (≠ S317), D366 (= D394), V378 (≠ I406)
- binding magnesium ion: F314 (≠ P341), S315 (≠ G342)
- binding 2-succinylbenzoate: H195 (= H216), S197 (≠ F218), A237 (≠ G260), L260 (≠ V287), G262 (= G289), G263 (≠ A290), G286 (= G315), M287 (≠ L316), S292 (≠ P321), Q293 (≠ V322)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
31% identity, 96% coverage: 12:508/519 of query aligns to 7:475/475 of 5burA
- active site: T150 (= T172), S170 (≠ D192), H194 (= H216), T287 (≠ S317), E288 (= E318)
- binding adenosine-5'-triphosphate: T150 (= T172), S151 (= S173), T153 (= T175), T154 (= T176), K158 (= K180), G263 (≠ A291), S283 (≠ G313), T287 (≠ S317), D365 (= D394), V377 (≠ I406), R380 (= R409)
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, 92% coverage: 33:510/519 of query aligns to 61:545/559 of Q67W82
- G395 (= G361) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
30% identity, 96% coverage: 12:508/519 of query aligns to 7:475/481 of 5busA
- active site: T150 (= T172), S170 (≠ D192), H194 (= H216), T287 (≠ S317), E288 (= E318)
- binding adenosine monophosphate: H194 (= H216), G262 (≠ A290), G263 (≠ A291), S283 (≠ G313), M286 (≠ L316), T287 (≠ S317), D365 (= D394), V377 (≠ I406), R380 (= R409), K467 (= K500)
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)
32% identity, 93% coverage: 33:516/519 of query aligns to 54:542/542 of O24146
- S189 (≠ T172) binding ATP
- S190 (= S173) binding ATP
- G191 (= G174) binding ATP
- T192 (= T175) binding ATP
- T193 (= T176) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K180) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H216) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F218) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ V222) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (vs. gap) binding CoA
- A309 (= A290) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E312) binding ATP
- G332 (= G313) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (≠ S317) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V322) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ V325) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D394) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R409) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding ATP; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K411) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ I415) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (= K417) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G418) binding CoA
- Q446 (≠ N420) binding AMP
- K526 (= K500) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
32% identity, 92% coverage: 33:510/519 of query aligns to 47:529/529 of 5bsvA
- active site: S182 (≠ T172), S202 (≠ D192), H230 (= H216), T329 (≠ S317), E330 (= E318), K434 (≠ I415), Q439 (≠ N420), K519 (= K500)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H216), Y232 (≠ F218), S236 (≠ V222), A302 (= A290), A303 (= A291), P304 (≠ A292), G325 (= G313), G327 (= G315), M328 (≠ L316), T329 (≠ S317), P333 (= P321), V334 (= V322), D413 (= D394), K430 (= K411), K434 (≠ I415), Q439 (≠ N420)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
32% identity, 92% coverage: 33:510/519 of query aligns to 47:529/529 of 5bsuA
- active site: S182 (≠ T172), S202 (≠ D192), H230 (= H216), T329 (≠ S317), E330 (= E318), K434 (≠ I415), Q439 (≠ N420), K519 (= K500)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H216), Y232 (≠ F218), S236 (≠ V222), M299 (≠ V287), A302 (= A290), A303 (= A291), P304 (≠ A292), G325 (= G313), G327 (= G315), M328 (≠ L316), T329 (≠ S317), P333 (= P321), D413 (= D394), K430 (= K411), K434 (≠ I415), Q439 (≠ N420)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
32% identity, 92% coverage: 33:510/519 of query aligns to 47:529/529 of 5bstA
- active site: S182 (≠ T172), S202 (≠ D192), H230 (= H216), T329 (≠ S317), E330 (= E318), K434 (≠ I415), Q439 (≠ N420), K519 (= K500)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H216), Y232 (≠ F218), S236 (≠ V222), A302 (= A290), A303 (= A291), P304 (≠ A292), G325 (= G313), Y326 (= Y314), G327 (= G315), M328 (≠ L316), T329 (≠ S317), P333 (= P321), V334 (= V322), D413 (= D394), K430 (= K411), K434 (≠ I415), Q439 (≠ N420)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
32% identity, 92% coverage: 33:510/519 of query aligns to 47:529/530 of 5bsmA
- active site: S182 (≠ T172), S202 (≠ D192), H230 (= H216), T329 (≠ S317), E330 (= E318), K434 (≠ I415), Q439 (≠ N420), K519 (= K500)
- binding adenosine-5'-triphosphate: S182 (≠ T172), S183 (= S173), G184 (= G174), T185 (= T175), T186 (= T176), K190 (= K180), H230 (= H216), A302 (= A290), A303 (= A291), P304 (≠ A292), Y326 (= Y314), G327 (= G315), M328 (≠ L316), T329 (≠ S317), D413 (= D394), I425 (= I406), R428 (= R409), K519 (= K500)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
32% identity, 92% coverage: 33:510/519 of query aligns to 46:528/528 of 5bsrA
- active site: S181 (≠ T172), S201 (≠ D192), H229 (= H216), T328 (≠ S317), E329 (= E318), K433 (≠ I415), Q438 (≠ N420), K518 (= K500)
- binding adenosine monophosphate: A301 (= A290), G326 (= G315), T328 (≠ S317), D412 (= D394), K429 (= K411), K433 (≠ I415), Q438 (≠ N420)
- binding coenzyme a: L102 (≠ F89), P226 (= P213), H229 (= H216), Y231 (≠ F218), F253 (vs. gap), K435 (= K417), G436 (= G418), F437 (≠ V419), F498 (≠ N480)
Query Sequence
>WP_007473537.1 NCBI__GCF_000170735.1:WP_007473537.1
MKYKYNNFYELLEKNAKEIGKKTAYFIDDKKISWQDVKKKVDTFARTLELLGIKKGDKIP
IYVNNSLEFVIALFGIQKIGAVPVPINTFLKEDEISFILNDIEAEFLIASSKFEKNIPNI
REKTSVKKIIWEGEPSIIDEDNISFTEILSNIEPHESIEYPTLDDLAVIIYTSGTTGKPK
GAMLTYKNIFADIWGINEIVKITPKDRFIAYLPMFHSFTMTVNILLPLYTGSAVVIIKSI
MPFSNIIKQTLLKRVTIFTGVPDVYSALSRAKLPFYFHWFNKVRFYVSGAAALPGEVLER
FSKKFKKAKLLEGYGLSETSPVVAVNRPYLQKPGSVGPAIPGVEVKIVNDELIEVPIGEA
GEIIVKGDIVMKGYYNRDEANEECLINGWFLTGDIGKVDEDGFIYILDRKKDLIISKGVN
IYPREIEEIILKFPGIKDCAVVGLKDENHGEIPVAFIEVEEDMEVNEKDLRKYLKSKLAN
YKLPKYIYFVENLPKNATGKVLKRILRENIDKYISNKGK
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