SitesBLAST
Comparing WP_059153145.1 NCBI__GCF_001046635.1:WP_059153145.1 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)
8pppA Amide bond synthetase from streptomyces hindustanus k492h mutant in complex with amp-cpp (see paper)
34% identity, 93% coverage: 31:515/520 of query aligns to 15:500/500 of 8pppA
6sq8B Structure of amide bond synthetase mcba from marinactinospora thermotolerans (see paper)
35% identity, 94% coverage: 26:513/520 of query aligns to 16:492/494 of 6sq8B
- active site: T160 (= T177), D200 (≠ H218), Q296 (≠ A314), E297 (= E315), I397 (≠ V418), N402 (= N423), K482 (= K503)
- binding adenosine monophosphate: G270 (≠ A288), Q291 (= Q309), Q296 (≠ A314), D376 (= D397), R391 (= R412), R406 (= R427), K482 (= K503)
- binding 1-ethanoyl-9~{H}-pyrido[3,4-b]indole-3-carboxylic acid: L201 (≠ S219), G294 (= G312), T295 (≠ Q313), A299 (≠ P317), F300 (≠ M318)
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
36% identity, 93% coverage: 32:512/520 of query aligns to 26:486/486 of 8wevA
Sites not aligning to the query:
8pyxA Amide bond synthetase from streptomyces hindustanus k492h mutant in complex with adenosine (see paper)
34% identity, 93% coverage: 31:515/520 of query aligns to 15:499/499 of 8pyxA
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, 96% coverage: 10:510/520 of query aligns to 24:550/561 of P69451
- Y213 (= Y173) mutation to A: Loss of activity.
- T214 (≠ S174) mutation to A: 10% of wild-type activity.
- G216 (= G176) mutation to A: Decreases activity.
- T217 (= T177) mutation to A: Decreases activity.
- G219 (= G179) mutation to A: Decreases activity.
- K222 (= K182) mutation to A: Decreases activity.
- E361 (= E315) 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)
32% identity, 88% coverage: 61:515/520 of query aligns to 56:499/503 of P9WQ37
- K172 (= K182) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R209) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (vs. gap) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ A221) 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 (≠ V223) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ A226) 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 (= R253) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G312) 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 (= W392) 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 (= D397) 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 (= R412) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ T419) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G421) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K503) 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)
32% identity, 88% coverage: 61:515/520 of query aligns to 59:499/502 of 3r44A
Sites not aligning to the query:
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, 86% coverage: 62:510/520 of query aligns to 55:477/485 of 5x8fB
- active site: T151 (≠ S174), S171 (≠ A191), H195 (= H218), T288 (≠ A314), E289 (= E315), I387 (≠ V418), N392 (= N423), K470 (= K503)
- binding magnesium ion: H70 (≠ N77), N178 (≠ Q198), L202 (= L224), L214 (≠ V236), T296 (≠ L322), L297 (= L323), S298 (≠ R324)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ M92), L191 (≠ A214), P192 (= P215), H195 (= H218), I196 (vs. gap), S197 (= S219), A237 (≠ M259), V238 (= V260), L260 (≠ F285), G262 (= G287), G286 (= G312), M287 (≠ Q313), S292 (≠ M318), Q293 (≠ S319), S388 (≠ T419), G389 (= G420), G390 (= G421), E391 (≠ F422), K420 (= K451), W421 (= W452), K450 (≠ A483), Y451 (≠ V484)
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)
30% identity, 86% coverage: 62:510/520 of query aligns to 55:477/484 of 5gtdA
- active site: T151 (≠ S174), S171 (≠ A191), H195 (= H218), T288 (≠ A314), E289 (= E315)
- binding adenosine-5'-monophosphate: G263 (≠ A288), G264 (≠ S289), Y285 (= Y311), G286 (= G312), M287 (≠ Q313), T288 (≠ A314), D366 (= D397), V378 (≠ I409)
- binding magnesium ion: F314 (≠ P344), S315 (≠ L345)
- binding 2-succinylbenzoate: H195 (= H218), S197 (= S219), A237 (≠ M259), L260 (≠ F285), G262 (= G287), G263 (≠ A288), G286 (= G312), M287 (≠ Q313), S292 (≠ M318), Q293 (≠ S319)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
33% identity, 68% coverage: 166:516/520 of query aligns to 155:504/506 of 4gxqA
- active site: T163 (≠ S174), N183 (≠ S194), H207 (= H218), T303 (≠ A314), E304 (= E315), I403 (≠ V418), N408 (= N423), A491 (≠ K503)
- binding adenosine-5'-triphosphate: T163 (≠ S174), S164 (≠ G175), G165 (= G176), T166 (= T177), T167 (= T178), H207 (= H218), S277 (≠ A288), A278 (≠ S289), P279 (≠ A290), E298 (≠ Q309), M302 (≠ Q313), T303 (≠ A314), D382 (= D397), R397 (= R412)
- binding carbonate ion: H207 (= H218), S277 (≠ A288), R299 (≠ F310), G301 (= G312)
5wm6A Crystal structure of cahj in complex with benzoyl adenylate (see paper)
30% identity, 95% coverage: 22:514/520 of query aligns to 40:535/535 of 5wm6A
- active site: S193 (= S174), N213 (≠ S194), H237 (= H218), A336 (= A314), E337 (= E315), N437 (≠ V418), K442 (≠ N423), K524 (= K503)
- binding magnesium ion: S301 (= S279), L303 (= L281), G326 (= G304)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: F239 (≠ G220), G310 (≠ A288), S311 (= S289), K312 (vs. gap), V332 (≠ F310), F333 (≠ Y311), G334 (= G312), M335 (≠ Q313), A336 (= A314), D416 (= D397), K433 (= K414), K442 (≠ N423)
5wm2A Crystal structure of cahj in complex with salicylic acid and amp (see paper)
30% identity, 95% coverage: 22:514/520 of query aligns to 40:535/536 of 5wm2A
- active site: S193 (= S174), N213 (≠ S194), H237 (= H218), A336 (= A314), E337 (= E315), N437 (≠ V418), K442 (≠ N423), K524 (= K503)
- binding adenosine monophosphate: G310 (≠ A288), S311 (= S289), K312 (vs. gap), V332 (≠ F310), F333 (≠ Y311), G334 (= G312), M335 (≠ Q313), A336 (= A314), E337 (= E315), D416 (= D397), V428 (≠ I409), K433 (= K414), K442 (≠ N423)
5wm3A Crystal structure of cahj in complex with salicyl adenylate (see paper)
30% identity, 95% coverage: 22:514/520 of query aligns to 40:535/537 of 5wm3A
- active site: S193 (= S174), N213 (≠ S194), H237 (= H218), A336 (= A314), E337 (= E315), N437 (≠ V418), K442 (≠ N423), K524 (= K503)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxybenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: N238 (≠ S219), F239 (≠ G220), G310 (≠ A288), S311 (= S289), K312 (vs. gap), V332 (≠ F310), F333 (≠ Y311), G334 (= G312), M335 (≠ Q313), A336 (= A314), D416 (= D397), K433 (= K414), K442 (≠ N423)
- binding magnesium ion: S301 (= S279), L303 (= L281), G326 (= G304)
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)
33% identity, 67% coverage: 170:516/520 of query aligns to 216:576/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
30% identity, 71% coverage: 146:514/520 of query aligns to 174:551/556 of Q9S725
- K211 (= K182) mutation to S: Drastically reduces the activity.
- M293 (≠ L258) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ F285) mutation K->L,A: Affects the substrate specificity.
- E401 (= E365) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C367) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R412) mutation to Q: Drastically reduces the activity.
- K457 (≠ G420) mutation to S: Drastically reduces the activity.
- K540 (= K503) mutation to N: Abolishes the activity.
5wm5A Crystal structure of cahj in complex with 5-methylsalicyl adenylate (see paper)
31% identity, 95% coverage: 22:514/520 of query aligns to 40:533/533 of 5wm5A
- active site: S193 (= S174), N213 (≠ S194), H237 (= H218), A336 (= A314), E337 (= E315), N437 (≠ V418), K442 (≠ N423), K522 (= K503)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxy-5-methylbenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: H237 (= H218), N238 (≠ S219), F239 (≠ G220), G309 (= G287), G310 (≠ A288), S311 (= S289), K312 (vs. gap), V332 (≠ F310), F333 (≠ Y311), G334 (= G312), M335 (≠ Q313), A336 (= A314), L340 (≠ M318), D416 (= D397), K433 (= K414), K442 (≠ N423)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
30% identity, 86% coverage: 62:510/520 of query aligns to 54:474/475 of 5burA
- active site: T150 (≠ S174), S170 (≠ A191), H194 (= H218), T287 (≠ A314), E288 (= E315)
- binding adenosine-5'-triphosphate: T150 (≠ S174), S151 (≠ G175), T153 (= T177), T154 (= T178), K158 (= K182), G263 (≠ S289), S283 (≠ F310), T287 (≠ A314), D365 (= D397), V377 (≠ I409), R380 (= R412)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
30% identity, 86% coverage: 62:510/520 of query aligns to 54:474/481 of 5busA
- active site: T150 (≠ S174), S170 (≠ A191), H194 (= H218), T287 (≠ A314), E288 (= E315)
- binding adenosine monophosphate: H194 (= H218), G262 (≠ A288), G263 (≠ S289), S283 (≠ F310), M286 (≠ Q313), T287 (≠ A314), D365 (= D397), V377 (≠ I409), R380 (= R412), K467 (= K503)
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, 68% coverage: 165:515/520 of query aligns to 180:538/542 of O24146
- S189 (= S174) binding ATP
- S190 (≠ G175) binding ATP
- G191 (= G176) binding ATP
- T192 (= T177) binding ATP
- T193 (= T178) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K182) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H218) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (vs. gap) 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 (≠ A222) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ G239) binding CoA
- A309 (= A288) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E298) binding ATP
- G332 (≠ A299) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (vs. gap) 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 (≠ I306) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ Q309) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D397) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R412) 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 (= K414) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ V418) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G420) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G421) binding CoA
- Q446 (≠ N423) binding AMP
- K526 (= K503) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
29% identity, 89% coverage: 53:514/520 of query aligns to 65:530/530 of 5bsmA
- active site: S182 (= S174), S202 (= S194), H230 (= H218), T329 (vs. gap), E330 (≠ K302), K434 (≠ V418), Q439 (≠ N423), K519 (= K503)
- binding adenosine-5'-triphosphate: S182 (= S174), S183 (≠ G175), G184 (= G176), T185 (= T177), T186 (= T178), K190 (= K182), H230 (= H218), A302 (= A288), A303 (≠ S289), P304 (vs. gap), Y326 (≠ I300), G327 (= G301), M328 (vs. gap), T329 (vs. gap), D413 (= D397), I425 (= I409), R428 (= R412), K519 (= K503)
Query Sequence
>WP_059153145.1 NCBI__GCF_001046635.1:WP_059153145.1
MSALLHQQISTLDMIAQALTRDTDRLVVIGAGGEHVTAQGLADEISRYQQSFEALEPRPR
RAALLSRNRIEVLYASNGLNFAGVVNTALHPMGSVDDYLYVIEDAGIDTLLFDPDHYADI
AAQLKARAPGLLHLLALGQTDVGTDLAEKARSLAPRPLVAPPCDPDALFRIAYSGGTTGK
PKGIMTTHRAAATSTLIQLTSWEWPKEVRHLICAPLSHSGAAVLSAVLVKGGSMVVLPGF
DPVGTMQAIADHRITSVLMVPTMVLAMIDHPRFGEFDLSSLEVIFYGASAFPTARLKEAI
GKLGPIFFQFYGQAEAPMSVTLLRRDEHDVDDMTRLSSCGRPSPLVRVALLDDACNEVPE
GEPGEICVRGPLLMAGYLNKPEETAAAFEGGWLHTGDVAVRSPDGFLRIVDRKKDMIVTG
GFNVYAREVEDVLVEHPGVRQAAVIGVPDEKWGEAVKAVVVLEPGVEVDPQALIARVREK
KGAVQAPKTVEFVDELPLSPLGKPDKKALRVRYAAVTAPA
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