SitesBLAST

Comparing WP_085217524.1 NCBI__GCF_900177405.1:WP_085217524.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 20 (the maximum) hits to proteins with known functional sites

8pppA Amide bond synthetase from streptomyces hindustanus k492h mutant in complex with amp-cpp (see paper)
36% identity, 91% coverage: 43:500/501 of query aligns to 38:500/500 of 8pppA

• binding diphosphomethylphosphonic acid adenosyl ester: T163 (= T169), G272 (= G277), A273 (= A278), P274 (= P279), H294 (≠ Q298), Y296 (= Y300), G297 (= G301), S298 (≠ Q302), Q299 (≠ T303), D381 (= D382)

8pyxA Amide bond synthetase from streptomyces hindustanus k492h mutant in complex with adenosine (see paper)
35% identity, 91% coverage: 43:500/501 of query aligns to 38:499/499 of 8pyxA

• binding adenosine: G273 (= G277), P275 (= P279), H295 (≠ Q298), C296 (= C299), G298 (= G301), D382 (= D382)

6sq8B Structure of amide bond synthetase mcba from marinactinospora thermotolerans (see paper)
35% identity, 91% coverage: 41:498/501 of query aligns to 27:492/494 of 6sq8B

• active site: T160 (= T165), D200 (≠ H210), Q296 (≠ T303), E297 (= E304), I397 (= I403), N402 (= N408), K482 (= K488)
• binding adenosine monophosphate: G270 (= G277), Q291 (= Q298), Q296 (≠ T303), D376 (= D382), R391 (= R397), R406 (≠ K412), K482 (= K488)
• binding 1-ethanoyl-9~{H}-pyrido[3,4-b]indole-3-carboxylic acid: L201 (≠ G211), G294 (= G301), T295 (≠ Q302), A299 (≠ N307), F300 (≠ T308)

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, 98% coverage: 5:495/501 of query aligns to 19:550/561 of P69451

• Y213 (= Y164) mutation to A: Loss of activity.
• T214 (= T165) mutation to A: 10% of wild-type activity.
• G216 (= G167) mutation to A: Decreases activity.
• T217 (= T168) mutation to A: Decreases activity.
• G219 (= G170) mutation to A: Decreases activity.
• K222 (= K173) mutation to A: Decreases activity.
• E361 (= E304) mutation to A: Loss of activity.

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)
30% identity, 94% coverage: 25:497/501 of query aligns to 18:479/485 of 5x8fB

• active site: T151 (= T165), S171 (≠ A183), H195 (= H210), T288 (= T303), E289 (= E304), I387 (= I403), N392 (= N408), K470 (= K488)
• binding magnesium ion: Y23 (≠ E30), E24 (≠ G31), H70 (≠ A77), N178 (≠ L190), L202 (≠ V216), L214 (= L228), T296 (≠ Y311), L297 (= L312), S298 (= S313)
• binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ L92), L191 (≠ A206), P192 (= P207), H195 (= H210), I196 (≠ G211), S197 (≠ A212), A237 (≠ L251), V238 (= V252), L260 (≠ I274), G262 (≠ S276), G286 (= G301), M287 (≠ Q302), S292 (≠ N307), Q293 (≠ T308), S388 (≠ T404), G389 (= G405), G390 (= G406), E391 (≠ F407), K420 (= K436), W421 (= W437), K450 (≠ P468), Y451 (≠ V469)

5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
30% identity, 94% coverage: 25:497/501 of query aligns to 18:479/484 of 5gtdA

• active site: T151 (= T165), S171 (≠ A183), H195 (= H210), T288 (= T303), E289 (= E304)
• binding adenosine-5'-monophosphate: G263 (= G277), G264 (≠ A278), Y285 (= Y300), G286 (= G301), M287 (≠ Q302), T288 (= T303), D366 (= D382), V378 (≠ I394)
• binding magnesium ion: F314 (≠ D329), S315 (≠ G330)
• binding 2-succinylbenzoate: H195 (= H210), S197 (≠ A212), A237 (≠ L251), L260 (≠ I274), G262 (≠ S276), G263 (= G277), G286 (= G301), M287 (≠ Q302), S292 (≠ N307), Q293 (≠ T308)

4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
33% identity, 93% coverage: 32:498/501 of query aligns to 26:501/506 of 4gxqA

• active site: T163 (= T165), N183 (= N185), H207 (= H210), T303 (= T303), E304 (= E304), I403 (= I403), N408 (= N408), A491 (≠ K488)
• binding adenosine-5'-triphosphate: T163 (= T165), S164 (≠ G166), G165 (= G167), T166 (= T168), T167 (= T169), H207 (= H210), S277 (vs. gap), A278 (= A278), P279 (= P279), E298 (≠ Q298), M302 (≠ Q302), T303 (= T303), D382 (= D382), R397 (= R397)
• binding carbonate ion: H207 (= H210), S277 (vs. gap), R299 (≠ C299), G301 (= G301)

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)
31% identity, 93% coverage: 35:500/501 of query aligns to 30:499/503 of P9WQ37

• K172 (= K173) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
• R195 (≠ P196) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
• R197 (≠ G198) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
• V209 (≠ G211) 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 (≠ G213) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
• T214 (≠ V216) 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 (≠ H245) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
• A302 (≠ G301) 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 (= W377) 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 (= D382) 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 (= R397) mutation to A: Reduction of binding affinity for fatty acids.
• S404 (≠ T404) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
• G406 (= G406) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
• K487 (= K488) 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.

5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
29% identity, 94% coverage: 25:497/501 of query aligns to 17:476/481 of 5busA

• active site: T150 (= T165), S170 (≠ A183), H194 (= H210), T287 (= T303), E288 (= E304)
• binding adenosine monophosphate: H194 (= H210), G262 (= G277), G263 (≠ A278), S283 (≠ C299), M286 (≠ Q302), T287 (= T303), D365 (= D382), V377 (≠ I394), R380 (= R397), K467 (= K488)

5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
29% identity, 94% coverage: 25:495/501 of query aligns to 17:474/475 of 5burA