SitesBLAST
Comparing AZOBR_RS19340 FitnessBrowser__azobra:AZOBR_RS19340 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)
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: 5:519/519 of query aligns to 25:553/561 of P69451
- Y213 (= Y175) mutation to A: Loss of activity.
- T214 (= T176) mutation to A: 10% of wild-type activity.
- G216 (= G178) mutation to A: Decreases activity.
- T217 (= T179) mutation to A: Decreases activity.
- G219 (= G181) mutation to A: Decreases activity.
- K222 (= K184) mutation to A: Decreases activity.
- E361 (= E320) mutation to A: Loss of activity.
O30409 Tyrocidine synthase 3; Tyrocidine synthase III from Brevibacillus parabrevis (see paper)
30% identity, 98% coverage: 5:515/519 of query aligns to 5658:6147/6486 of O30409
Sites not aligning to the query:
- 3075 modified: O-(pantetheine 4'-phosphoryl)serine
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
33% identity, 97% coverage: 17:518/519 of query aligns to 16:500/506 of 4gxqA
- active site: T163 (= T176), N183 (≠ T196), H207 (≠ F220), T303 (= T319), E304 (= E320), I403 (≠ K424), N408 (≠ K429), A491 (≠ K509)
- binding adenosine-5'-triphosphate: T163 (= T176), S164 (= S177), G165 (= G178), T166 (= T179), T167 (= T180), H207 (≠ F220), S277 (≠ A292), A278 (= A293), P279 (= P294), E298 (≠ S314), M302 (= M318), T303 (= T319), D382 (= D403), R397 (= R418)
- binding carbonate ion: H207 (≠ F220), S277 (≠ A292), R299 (≠ M315), G301 (= G317)
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)
30% identity, 98% coverage: 7:517/519 of query aligns to 12:515/518 of 6m2uA
- active site: S176 (≠ T176), T196 (≠ S199), T324 (= T319), E325 (= E320), K422 (= K424), Y427 (≠ K429), K507 (= K509)
- binding adenosine monophosphate: G298 (≠ A292), E299 (≠ A293), A300 (≠ P294), D319 (≠ S314), G320 (≠ M315), I321 (≠ Y316), G322 (= G317), T324 (= T319), D401 (= D403), R416 (= R418), K422 (= K424), Y427 (≠ K429)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (= Y222), A297 (= A291), G322 (= G317), S323 (≠ M318), A328 (≠ T323)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
30% identity, 98% coverage: 7:517/519 of query aligns to 12:515/518 of 6m2tA
- active site: S176 (≠ T176), T196 (≠ S199), T324 (= T319), E325 (= E320), K422 (= K424), Y427 (≠ K429), K507 (= K509)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (= Y222), G322 (= G317), S323 (≠ M318), A328 (≠ T323)
- binding adenosine monophosphate: G298 (≠ A292), E299 (≠ A293), A300 (≠ P294), G320 (≠ M315), I321 (≠ Y316), S323 (≠ M318), T324 (= T319), D401 (= D403), R416 (= R418), K422 (= K424), Y427 (≠ K429)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
30% identity, 98% coverage: 7:517/519 of query aligns to 12:515/518 of 4rmnA
- active site: S176 (≠ T176), T196 (≠ S199), T324 (= T319), E325 (= E320), K422 (= K424), Y427 (≠ K429), K507 (= K509)
- binding thiophene-2-carboxylic acid: A217 (≠ L216), F221 (= F220), Y223 (= Y222), G269 (= G263), A270 (≠ V264), A297 (= A291), G298 (≠ A292), G322 (= G317), S323 (≠ M318), H328 (≠ T323), I329 (≠ C326), K422 (= K424), G425 (= G427)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
30% identity, 98% coverage: 7:517/519 of query aligns to 12:515/519 of 4rlfB
- active site: S176 (≠ T176), T196 (≠ S199), T324 (= T319), E325 (= E320), K422 (= K424), Y427 (≠ K429), K507 (= K509)
- binding 2-methylbenzoic acid: A222 (≠ G221), Y223 (= Y222), G298 (≠ A292), I321 (≠ Y316), G322 (= G317), S323 (≠ M318), H328 (≠ T323)
- binding 4-methylbenzoic acid: A216 (≠ V215), P246 (≠ A244), P248 (= P246), G269 (= G263), A270 (≠ V264), G273 (≠ F267)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
30% identity, 98% coverage: 7:517/519 of query aligns to 12:515/516 of 4rm2A
- active site: S176 (≠ T176), T196 (≠ S199), T324 (= T319), E325 (= E320), K422 (= K424), Y427 (≠ K429), K507 (= K509)
- binding 2-fluorobenzoic acid: A216 (≠ V215), A222 (≠ G221), Y223 (= Y222), P246 (≠ A244), T247 (≠ F245), V251 (≠ T249), F267 (≠ L261), G269 (= G263), A270 (≠ V264), G273 (≠ F267), M277 (≠ L271), A297 (= A291), G298 (≠ A292), I321 (≠ Y316), G322 (= G317), S323 (≠ M318), H328 (≠ T323), K422 (= K424)
4zjzA Crystal structure of a benzoate coenzyme a ligase with benzoyl-amp (see paper)
30% identity, 98% coverage: 7:517/519 of query aligns to 12:515/517 of 4zjzA
- active site: S176 (≠ T176), T196 (≠ S199), T324 (= T319), E325 (= E320), K422 (= K424), Y427 (≠ K429), K507 (= K509)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: A222 (≠ G221), Y223 (= Y222), A297 (= A291), G298 (≠ A292), E299 (≠ A293), A300 (≠ P294), G320 (≠ M315), I321 (≠ Y316), G322 (= G317), S323 (≠ M318), T324 (= T319), H328 (≠ T323), I329 (≠ C326), D401 (= D403), R416 (= R418), K422 (= K424), Y427 (≠ K429)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
30% identity, 98% coverage: 7:517/519 of query aligns to 13:516/518 of 4rm3A
- active site: S177 (≠ T176), T197 (≠ S199), T325 (= T319), E326 (= E320), K423 (= K424), Y428 (≠ K429), K508 (= K509)
- binding 2-furoic acid: A223 (≠ G221), Y224 (= Y222), A298 (= A291), G323 (= G317), H329 (≠ T323), I330 (≠ C326), K423 (= K424)
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)
28% identity, 94% coverage: 30:519/519 of query aligns to 66:573/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
7thqB Crystal structure of pltf trapped with pigg using a proline adenosine vinylsulfonamide inhibitor (see paper)
32% identity, 99% coverage: 4:516/519 of query aligns to 3:493/505 of 7thqB
- binding azide ion: Y377 (≠ Q394), T379 (= T401)
- binding 5'-deoxy-5'-({(2S)-2-({2-[(N-{(2R)-4-[(dioxo-lambda~5~-phosphanyl)oxy]-2-hydroxy-3,3-dimethylbutanoyl}-beta-alanyl)amino]ethyl}sulfanyl)-2-[(2S)-pyrrolidin-2-yl]ethanesulfonyl}amino)adenosine: F205 (= F220), D206 (≠ G221), V251 (= V264), A278 (= A291), G279 (≠ A292), E280 (≠ A293), P281 (= P294), L302 (≠ M315), F303 (≠ Y316), G304 (= G317), T306 (= T319), N309 (vs. gap), D381 (= D403), Y393 (≠ F415), K402 (= K424), R404 (= R426), G405 (= G427), N406 (≠ E428), R407 (≠ K429)
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, 98% coverage: 7:517/519 of query aligns to 6:478/485 of 5x8fB
- active site: T151 (= T176), S171 (≠ T196), H195 (≠ F220), T288 (= T319), E289 (= E320), I387 (≠ K424), N392 (≠ K429), K470 (= K509)
- binding magnesium ion: Y23 (≠ A24), E24 (≠ G25), H70 (≠ F71), N178 (≠ Y203), L202 (≠ I227), L214 (= L239), T296 (≠ Y327), L297 (= L328), S298 (≠ D329)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ S86), L191 (= L216), P192 (= P217), H195 (≠ F220), I196 (≠ G221), S197 (≠ Y222), A237 (≠ G263), V238 (= V264), L260 (≠ T289), G262 (≠ A291), G286 (= G317), M287 (= M318), S292 (≠ T323), Q293 (≠ R324), S388 (≠ C425), G389 (≠ R426), G390 (= G427), E391 (= E428), K420 (≠ A457), W421 (≠ D458), K450 (≠ S489), Y451 (≠ H490)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
30% identity, 98% coverage: 7:517/519 of query aligns to 6:478/484 of 5gtdA
- active site: T151 (= T176), S171 (≠ T196), H195 (≠ F220), T288 (= T319), E289 (= E320)
- binding adenosine-5'-monophosphate: G263 (≠ A292), G264 (≠ A293), Y285 (= Y316), G286 (= G317), M287 (= M318), T288 (= T319), D366 (= D403), V378 (≠ F415)
- binding magnesium ion: F314 (≠ P345), S315 (≠ N346)
- binding 2-succinylbenzoate: H195 (≠ F220), S197 (≠ Y222), A237 (≠ G263), L260 (≠ T289), G262 (≠ A291), G263 (≠ A292), G286 (= G317), M287 (= M318), S292 (≠ T323), Q293 (≠ R324)
6mfzA Crystal structure of dimodular lgra in a condensation state (see paper)
27% identity, 99% coverage: 4:519/519 of query aligns to 1214:1706/1789 of 6mfzA
Sites not aligning to the query:
- active site: 351, 371, 484, 485, 589, 594, 672
- binding 4'-phosphopantetheine: 721, 740, 1007, 1098, 1741
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
30% identity, 97% coverage: 16:519/519 of query aligns to 23:512/518 of 4wv3B
- active site: S175 (≠ T176), T320 (≠ C322), E321 (≠ T323), K418 (= K424), W423 (≠ K429), K502 (= K509)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ L218), T221 (= T219), F222 (= F220), A293 (= A291), S294 (≠ A292), E295 (≠ A293), A296 (≠ P294), G316 (≠ M318), I317 (≠ T319), G318 (≠ E320), C319 (= C321), T320 (≠ C322), D397 (= D403), H409 (≠ F415), R412 (= R418), K502 (= K509)
P27206 Surfactin synthase subunit 1 from Bacillus subtilis (strain 168) (see paper)
29% identity, 98% coverage: 7:515/519 of query aligns to 465:956/3587 of P27206
Sites not aligning to the query:
- 1006 modified: O-(pantetheine 4'-phosphoryl)serine
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: 29:517/519 of query aligns to 30:495/503 of P9WQ37
- K172 (= K184) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T207) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ D209) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ G221) 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 (≠ G223) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ Q226) 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 (= R257) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G317) 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 (≠ L398) 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 (= D403) 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 (= R418) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ C425) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G427) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K509) 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.
5n9xA Structure of adenylation domain thr1 involved in the biosynthesis of 4-chlorothreonine in streptomyces sp.Oh-5093, ligand bound structure (see paper)
31% identity, 99% coverage: 5:516/519 of query aligns to 4:482/489 of 5n9xA
- active site: T142 (= T176), L162 (≠ T196), T289 (= T319), E290 (= E320), K395 (= K424), R400 (≠ K429), K475 (= K509)
- binding adenosine-5'-triphosphate: T142 (= T176), S143 (= S177), K150 (= K184), G260 (≠ A292), E261 (≠ A293), K262 (≠ P294), N284 (≠ S314), M285 (= M315), Y286 (= Y316), G287 (= G317), I288 (≠ M318), T289 (= T319), D374 (= D403), Y386 (≠ F415), R389 (= R418), K475 (= K509)
- binding threonine: F186 (= F220), D187 (≠ G221), F188 (≠ Y222), G260 (≠ A292), G287 (= G317), V293 (≠ T323), K475 (= K509)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
30% identity, 98% coverage: 7:517/519 of query aligns to 5:475/475 of 5burA
- active site: T150 (= T176), S170 (≠ T196), H194 (≠ F220), T287 (= T319), E288 (= E320)
- binding adenosine-5'-triphosphate: T150 (= T176), S151 (= S177), T153 (= T179), T154 (= T180), K158 (= K184), G263 (≠ A293), S283 (≠ M315), T287 (= T319), D365 (= D403), V377 (≠ F415), R380 (= R418)
Query Sequence
>AZOBR_RS19340 FitnessBrowser__azobra:AZOBR_RS19340
MAHLLHQFLSETAARRPHHTALIAGENAVTFAELDRQSDAVACALQSAGVVRGDRVAVML
ENSIEYVAGLFGALKAGAVYVPVNPSTKADKLAYILTDAGVRALIAPSALARQVVPAAGE
ASHLATTLWVGPAVPAGAGGLSFTDIVATHPDPQSGGTKPQSRGLIDQDLAAILYTSGTT
GRPKGVMLSHAALVNTTWSISTYLENTPDDVVMCVLPLTFGYGLSQILTGARVGFTVVLE
RSFAFPAETLARMVKHRITGLPGVPTFFSTLLGMEALKTADLSSLRYLTNAAAPLPTAHI
DRLRERFPDAAFYSMYGMTECCTRICYLDPRDLGTKTASVGRAIPNCEAYVVDELGNRAA
PGEVGELVVRGANVMRGYWNRPEETAKRLRSGPQGETLLYTGDLFTMDADGCLYFVSRKD
DVFKCRGEKVSPKEVENALYELEAVVEAAVLGVPDSADGMAVKAYLVVRPGATLTEMAIR
QHCRGRLESHLVPKFIEIRDELPKTESGKIKRAMLAETA
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