SitesBLAST
Comparing WP_011383961.1 NCBI__GCF_000009985.1:WP_011383961.1 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)
4zjzA Crystal structure of a benzoate coenzyme a ligase with benzoyl-amp (see paper)
35% identity, 96% coverage: 16:497/500 of query aligns to 21:515/517 of 4zjzA
- active site: S176 (≠ T160), T196 (vs. gap), T324 (= T303), E325 (= E304), K422 (= K402), Y427 (≠ W407), K507 (= K489)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: A222 (= A205), Y223 (= Y206), A297 (= A276), G298 (= G277), E299 (= E278), A300 (≠ N279), G320 (= G299), I321 (= I300), G322 (= G301), S323 (≠ A302), T324 (= T303), H328 (≠ F307), I329 (≠ L308), D401 (= D381), R416 (= R396), K422 (= K402), Y427 (≠ W407)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
35% identity, 96% coverage: 16:497/500 of query aligns to 21:515/518 of 4rmnA
- active site: S176 (≠ T160), T196 (vs. gap), T324 (= T303), E325 (= E304), K422 (= K402), Y427 (≠ W407), K507 (= K489)
- binding thiophene-2-carboxylic acid: A217 (≠ S200), F221 (= F204), Y223 (= Y206), G269 (≠ S248), A270 (≠ V249), A297 (= A276), G298 (= G277), G322 (= G301), S323 (≠ A302), H328 (≠ F307), I329 (≠ L308), K422 (= K402), G425 (= G405)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
35% identity, 96% coverage: 16:497/500 of query aligns to 22:516/518 of 4rm3A
- active site: S177 (≠ T160), T197 (vs. gap), T325 (= T303), E326 (= E304), K423 (= K402), Y428 (≠ W407), K508 (= K489)
- binding 2-furoic acid: A223 (= A205), Y224 (= Y206), A298 (= A276), G323 (= G301), H329 (≠ F307), I330 (≠ L308), K423 (= K402)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
35% identity, 96% coverage: 16:497/500 of query aligns to 21:515/519 of 4rlfB
- active site: S176 (≠ T160), T196 (vs. gap), T324 (= T303), E325 (= E304), K422 (= K402), Y427 (≠ W407), K507 (= K489)
- binding 2-methylbenzoic acid: A222 (= A205), Y223 (= Y206), G298 (= G277), I321 (= I300), G322 (= G301), S323 (≠ A302), H328 (≠ F307)
- binding 4-methylbenzoic acid: A216 (≠ T199), P246 (≠ G227), P248 (= P229), G269 (≠ S248), A270 (≠ V249), G273 (≠ L252)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
35% identity, 96% coverage: 16:497/500 of query aligns to 21:515/516 of 4rm2A
- active site: S176 (≠ T160), T196 (vs. gap), T324 (= T303), E325 (= E304), K422 (= K402), Y427 (≠ W407), K507 (= K489)
- binding 2-fluorobenzoic acid: A216 (≠ T199), A222 (= A205), Y223 (= Y206), P246 (≠ G227), T247 (≠ W228), V251 (≠ T232), F267 (≠ V246), G269 (≠ S248), A270 (≠ V249), G273 (≠ L252), M277 (= M256), A297 (= A276), G298 (= G277), I321 (= I300), G322 (= G301), S323 (≠ A302), H328 (≠ F307), K422 (= K402)
6m2uA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-chloro-1,3-thiazole-5-carboxylate-amp (see paper)
35% identity, 96% coverage: 16:497/500 of query aligns to 21:515/518 of 6m2uA
- active site: S176 (≠ T160), T196 (vs. gap), T324 (= T303), E325 (= E304), K422 (= K402), Y427 (≠ W407), K507 (= K489)
- binding adenosine monophosphate: G298 (= G277), E299 (= E278), A300 (≠ N279), D319 (≠ E298), G320 (= G299), I321 (= I300), G322 (= G301), T324 (= T303), D401 (= D381), R416 (= R396), K422 (= K402), Y427 (≠ W407)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (= Y206), A297 (= A276), G322 (= G301), S323 (≠ A302), A328 (≠ F307)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
35% identity, 96% coverage: 16:497/500 of query aligns to 21:515/518 of 6m2tA
- active site: S176 (≠ T160), T196 (vs. gap), T324 (= T303), E325 (= E304), K422 (= K402), Y427 (≠ W407), K507 (= K489)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (= Y206), G322 (= G301), S323 (≠ A302), A328 (≠ F307)
- binding adenosine monophosphate: G298 (= G277), E299 (= E278), A300 (≠ N279), G320 (= G299), I321 (= I300), S323 (≠ A302), T324 (= T303), D401 (= D381), R416 (= R396), K422 (= K402), Y427 (≠ W407)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
32% identity, 97% coverage: 16:498/500 of query aligns to 23:511/518 of 4wv3B
- active site: S175 (≠ T160), T320 (= T303), E321 (= E304), K418 (= K402), W423 (= W407), K502 (= K489)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (= F204), T221 (≠ A205), F222 (≠ Y206), A293 (= A276), S294 (≠ G277), E295 (= E278), A296 (≠ N279), G316 (= G299), I317 (= I300), G318 (= G301), C319 (≠ A302), T320 (= T303), D397 (= D381), H409 (≠ P393), R412 (= R396), K502 (= K489)
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)
29% identity, 94% coverage: 29:497/500 of query aligns to 30:495/503 of P9WQ37
- K172 (= K168) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ L191) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ G193) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ A205) 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 (≠ P207) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ H210) 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 (= R242) 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 (= W376) 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 (= D381) 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 (= R396) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V403) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G405) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K489) 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.
B2HIL6 p-hydroxybenzoic acid--AMP ligase FadD22; p-HB--AMP ligase FadD22; p-hydroxybenzoic acid-AMP synthetase; p-HB-AMP synthetase; EC 6.2.1.50 from Mycobacterium marinum (strain ATCC BAA-535 / M) (see paper)
32% identity, 94% coverage: 28:496/500 of query aligns to 30:487/702 of B2HIL6
Sites not aligning to the query:
- 576 S→A: Catalyzes pHBA-AMP formation, indicating this residue is not essential for adenylation activity.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
29% identity, 94% coverage: 29:497/500 of query aligns to 33:495/502 of 3r44A
Sites not aligning to the query:
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)
27% identity, 95% coverage: 21:497/500 of query aligns to 41:551/561 of P69451
- Y213 (= Y159) mutation to A: Loss of activity.
- T214 (= T160) mutation to A: 10% of wild-type activity.
- G216 (= G162) mutation to A: Decreases activity.
- T217 (= T163) mutation to A: Decreases activity.
- G219 (= G165) mutation to A: Decreases activity.
- K222 (= K168) mutation to A: Decreases activity.
- E361 (= E304) mutation to A: Loss of activity.
5ie2A Crystal structure of a plant enzyme (see paper)
27% identity, 94% coverage: 23:492/500 of query aligns to 25:498/506 of 5ie2A
- active site: T165 (= T160), S185 (≠ G180), H209 (≠ F204), T310 (= T303), E311 (= E304), N410 (≠ K402), K415 (≠ W407), K495 (= K489)
- binding adenosine-5'-triphosphate: T165 (= T160), S166 (= S161), G167 (= G162), T168 (= T163), T169 (= T164), S284 (≠ G277), A285 (≠ E278), S286 (≠ N279), Y307 (≠ I300), A308 (≠ G301), M309 (≠ A302), T310 (= T303), D389 (= D381), L401 (≠ P393), R404 (= R396), K495 (= K489)
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
26% identity, 90% coverage: 47:497/500 of query aligns to 68:531/535 of 3dayA
- active site: T189 (= T160), T332 (= T303), E333 (= E304), N435 (≠ K402), R440 (≠ W407), K523 (= K489)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T160), S190 (= S161), G191 (= G162), T192 (= T163), S193 (≠ T164), K197 (= K168), G306 (= G277), E307 (= E278), S308 (≠ N279), Y329 (≠ I300), G330 (= G301), Q331 (≠ A302), T332 (= T303), D414 (= D381), F426 (≠ P393), R429 (= R396), K523 (= K489)
- binding magnesium ion: M451 (≠ L418), H453 (≠ V420), V456 (= V423)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
27% identity, 96% coverage: 18:498/500 of query aligns to 16:476/481 of 5busA
- active site: T150 (= T160), S170 (≠ G180), H194 (≠ F204), T287 (= T303), E288 (= E304)
- binding adenosine monophosphate: H194 (≠ F204), G262 (= G277), G263 (≠ E278), S283 (≠ G299), M286 (≠ A302), T287 (= T303), D365 (= D381), V377 (≠ P393), R380 (= R396), K467 (= K489)
5ie3A Crystal structure of a plant enzyme (see paper)
27% identity, 94% coverage: 23:492/500 of query aligns to 25:496/504 of 5ie3A
- active site: T163 (= T160), S183 (≠ G180), H207 (≠ F204), T308 (= T303), E309 (= E304), N408 (≠ K402), K413 (≠ W407), K493 (= K489)
- binding adenosine monophosphate: S164 (= S161), S282 (≠ G277), A283 (≠ E278), S284 (≠ N279), Y305 (≠ I300), A306 (≠ G301), M307 (≠ A302), T308 (= T303), D387 (= D381), L399 (≠ P393), R402 (= R396), K493 (= K489)
- binding oxalic acid: V208 (≠ A205), S282 (≠ G277), A306 (≠ G301), M307 (≠ A302), H312 (≠ F307), K493 (= K489)
Q9SMT7 Oxalate--CoA ligase; 4-coumarate--CoA ligase isoform 8; At4CL8; 4-coumarate--CoA ligase-like 10; Acyl-activating enzyme 3; Adenosine monophosphate binding protein 3; AtMPBP3; Oxalyl-CoA synthetase; EC 6.2.1.8 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
26% identity, 94% coverage: 23:492/500 of query aligns to 25:503/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 160:164) binding
- H214 (≠ F204) binding ; mutation to A: Abolished activity.
- S289 (≠ G277) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ GEN 277:279) binding
- EA 310:311 (≠ EG 298:299) binding
- M314 (≠ A302) binding
- T315 (= T303) binding
- H319 (≠ F307) binding ; mutation to A: Abolished activity.
- D394 (= D381) binding
- R409 (= R396) binding ; mutation to A: Abolished activity.
- K500 (= K489) binding ; binding ; mutation to A: Abolished 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)
28% identity, 96% coverage: 18:498/500 of query aligns to 17:479/485 of 5x8fB
- active site: T151 (= T160), S171 (≠ G180), H195 (≠ F204), T288 (= T303), E289 (= E304), I387 (≠ K402), N392 (≠ W407), K470 (= K489)
- binding magnesium ion: Y23 (≠ C24), E24 (≠ G25), H70 (≠ L71), N178 (= N187), L202 (= L212), L214 (= L224), T296 (≠ A311), L297 (≠ S312), S298 (≠ T313)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R86), L191 (≠ S200), P192 (≠ K201), H195 (≠ F204), I196 (≠ A205), S197 (≠ Y206), A237 (≠ S248), V238 (= V249), L260 (≠ V274), G262 (≠ A276), G286 (= G301), M287 (≠ A302), S292 (≠ F307), Q293 (≠ L308), S388 (≠ V403), G389 (≠ S404), G390 (= G405), E391 (≠ Q406), K420 (≠ D435), W421 (vs. gap), K450 (≠ I469), Y451 (= Y470)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
28% identity, 96% coverage: 18:498/500 of query aligns to 17:479/484 of 5gtdA
- active site: T151 (= T160), S171 (≠ G180), H195 (≠ F204), T288 (= T303), E289 (= E304)
- binding adenosine-5'-monophosphate: G263 (= G277), G264 (≠ E278), Y285 (≠ I300), G286 (= G301), M287 (≠ A302), T288 (= T303), D366 (= D381), V378 (≠ P393)
- binding magnesium ion: F314 (≠ P327), S315 (≠ W328)
- binding 2-succinylbenzoate: H195 (≠ F204), S197 (≠ Y206), A237 (≠ S248), L260 (≠ V274), G262 (≠ A276), G263 (= G277), G286 (= G301), M287 (≠ A302), S292 (≠ F307), Q293 (≠ L308)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
27% identity, 96% coverage: 18:497/500 of query aligns to 16:475/475 of 5burA
- active site: T150 (= T160), S170 (≠ G180), H194 (≠ F204), T287 (= T303), E288 (= E304)
- binding adenosine-5'-triphosphate: T150 (= T160), S151 (= S161), T153 (= T163), T154 (= T164), K158 (= K168), G263 (≠ E278), S283 (≠ G299), T287 (= T303), D365 (= D381), V377 (≠ P393), R380 (= R396)
Query Sequence
>WP_011383961.1 NCBI__GCF_000009985.1:WP_011383961.1
MNAADEILGPSLGSGRGESLAIICGEQTLTYDQLNRLACRFGNAMLAAGVQRQQPVLLLL
DDGPELVAAYLGAMKAGLVAVALNTRLSPKDLSHALGDSGAPLLLAETALKDLAAESLAL
AHASARMVTTDELDAFLEGASDQLVSADMGPEDMALWMYTSGTTGQPKGAVHVHGSIPLG
ERHVRENLGLLPGDRIFSTSKLFFAYPLGHCLIGALRCGGTLVLHRGWPDATAAAEVIAR
TRPKLVLSVPSLYRIMLKDGVGSSPAFREVRTWVSAGENLPADLCRRWMEETGGLMLEGI
GATEALFLFIASTPTAMKPGACGRPLPWAEAQLRSPSGEVIAAPDTPGDLWVRMDSLFRR
YHNRPDVTQRVLKDGWWKTGDVFSFDAEGWWSPQGRSDDMIKVSGQWVSPSEVEEAALMV
PGVADAVAVGIPNEDGLVRLVLYAVAEAGEHEPLLETRIVETLRSKLAIYKCPRNVRFLE
TIPRTATGKVQRFKLREAGA
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