SitesBLAST
Comparing WP_084199459.1 NCBI__GCF_002869505.1:WP_084199459.1 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)
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)
37% identity, 96% coverage: 16:507/511 of query aligns to 10:496/503 of P9WQ37
- R17 (≠ D23) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K179) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (vs. gap) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R203) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I216) 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 (≠ G218) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V221) 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 (≠ K252) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G310) 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 (= W387) 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 (= D392) 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 (= R407) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S414) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G416) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K498) 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.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
37% identity, 96% coverage: 16:507/511 of query aligns to 13:496/502 of 3r44A
Sites not aligning to the query:
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
35% identity, 97% coverage: 15:511/511 of query aligns to 9:483/484 of 5gtdA
- active site: T151 (= T171), S171 (≠ N191), H195 (= H215), T288 (= T312), E289 (= E313)
- binding adenosine-5'-monophosphate: G263 (≠ A287), G264 (≠ A288), Y285 (= Y309), G286 (= G310), M287 (≠ L311), T288 (= T312), D366 (= D392), V378 (≠ I404)
- binding magnesium ion: F314 (≠ Y339), S315 (= S340)
- binding 2-succinylbenzoate: H195 (= H215), S197 (≠ G217), A237 (≠ G258), L260 (≠ V284), G262 (= G286), G263 (≠ A287), G286 (= G310), M287 (≠ L311), S292 (≠ P316), Q293 (≠ F317)
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)
34% identity, 97% coverage: 15:511/511 of query aligns to 9:483/485 of 5x8fB
- active site: T151 (= T171), S171 (≠ N191), H195 (= H215), T288 (= T312), E289 (= E313), I387 (= I413), N392 (= N418), K470 (= K498)
- binding magnesium ion: Y23 (≠ F29), E24 (= E30), H70 (≠ F76), N178 (≠ A198), L202 (≠ M222), L214 (= L235), T296 (≠ L320), L297 (= L321), S298 (≠ T322)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R91), L191 (≠ A211), P192 (= P212), H195 (= H215), I196 (= I216), S197 (≠ G217), A237 (≠ G258), V238 (≠ A259), L260 (≠ V284), G262 (= G286), G286 (= G310), M287 (≠ L311), S292 (≠ P316), Q293 (≠ F317), S388 (= S414), G389 (= G415), G390 (= G416), E391 (= E417), K420 (= K446), W421 (= W447), K450 (≠ R478), Y451 (= Y479)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
35% identity, 97% coverage: 15:511/511 of query aligns to 8:480/481 of 5busA
- active site: T150 (= T171), S170 (≠ N191), H194 (= H215), T287 (= T312), E288 (= E313)
- binding adenosine monophosphate: H194 (= H215), G262 (≠ A287), G263 (≠ A288), S283 (≠ G308), M286 (≠ L311), T287 (= T312), D365 (= D392), V377 (≠ I404), R380 (= R407), K467 (= K498)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
35% identity, 96% coverage: 15:506/511 of query aligns to 8:475/475 of 5burA
- active site: T150 (= T171), S170 (≠ N191), H194 (= H215), T287 (= T312), E288 (= E313)
- binding adenosine-5'-triphosphate: T150 (= T171), S151 (= S172), T153 (= T174), T154 (= T175), K158 (= K179), G263 (≠ A288), S283 (≠ G308), T287 (= T312), D365 (= D392), V377 (≠ I404), R380 (= R407)
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)
36% identity, 94% coverage: 30:507/511 of query aligns to 44:533/541 of Q5SKN9
- T184 (= T171) binding Mg(2+)
- G302 (≠ A287) binding tetradecanoyl-AMP
- Q322 (= Q307) binding tetradecanoyl-AMP
- G323 (= G308) binding tetradecanoyl-AMP
- T327 (= T312) binding tetradecanoyl-AMP
- E328 (= E313) binding Mg(2+)
- D418 (= D392) binding tetradecanoyl-AMP
- K435 (= K409) binding tetradecanoyl-AMP
- K439 (≠ I413) binding tetradecanoyl-AMP
5buqB Unliganded form of o-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, solved at 1.98 angstroms (see paper)
34% identity, 97% coverage: 15:511/511 of query aligns to 8:471/473 of 5buqB
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: 35:508/511 of query aligns to 65:550/556 of Q9S725
- K211 (= K179) mutation to S: Drastically reduces the activity.
- M293 (≠ F257) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V284) mutation K->L,A: Affects the substrate specificity.
- E401 (= E359) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C361) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R407) mutation to Q: Drastically reduces the activity.
- K457 (≠ G415) mutation to S: Drastically reduces the activity.
- K540 (= K498) 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)
33% identity, 93% coverage: 35:508/511 of query aligns to 61:545/559 of Q67W82