SitesBLAST
Comparing Ac3H11_4556 FitnessBrowser__acidovorax_3H11:Ac3H11_4556 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)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
36% identity, 88% coverage: 54:540/553 of query aligns to 24:512/518 of 4wv3B
- active site: S175 (≠ T204), T320 (= T346), E321 (= E347), K418 (≠ I442), W423 (≠ N447), K502 (= K530)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (= F249), T221 (= T250), F222 (= F251), A293 (= A319), S294 (≠ G320), E295 (= E321), A296 (≠ G322), G316 (= G342), I317 (= I343), G318 (= G344), C319 (≠ A345), T320 (= T346), D397 (= D421), H409 (≠ Y433), R412 (= R436), K502 (= K530)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
37% identity, 81% coverage: 92:539/553 of query aligns to 59:516/516 of 4rm2A
- active site: S176 (≠ T204), T196 (≠ G224), T324 (= T346), E325 (= E347), K422 (≠ I442), Y427 (≠ N447), K507 (= K530)
- binding 2-fluorobenzoic acid: A216 (≠ S244), A222 (≠ T250), Y223 (≠ F251), P246 (≠ Y274), T247 (= T275), V251 (≠ M279), F267 (≠ C291), G269 (≠ T293), A270 (= A294), G273 (≠ F297), M277 (= M301), A297 (= A319), G298 (= G320), I321 (= I343), G322 (= G344), S323 (≠ A345), H328 (= H350), K422 (≠ I442)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
37% identity, 81% coverage: 92:539/553 of query aligns to 59:516/519 of 4rlfB
- active site: S176 (≠ T204), T196 (≠ G224), T324 (= T346), E325 (= E347), K422 (≠ I442), Y427 (≠ N447), K507 (= K530)
- binding 2-methylbenzoic acid: A222 (≠ T250), Y223 (≠ F251), G298 (= G320), I321 (= I343), G322 (= G344), S323 (≠ A345), H328 (= H350)
- binding 4-methylbenzoic acid: A216 (≠ S244), P246 (≠ Y274), P248 (= P276), G269 (≠ T293), A270 (= A294), G273 (≠ F297)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
37% identity, 81% coverage: 92:539/553 of query aligns to 60:517/518 of 4rm3A
- active site: S177 (≠ T204), T197 (≠ G224), T325 (= T346), E326 (= E347), K423 (≠ I442), Y428 (≠ N447), K508 (= K530)
- binding 2-furoic acid: A223 (≠ T250), Y224 (≠ F251), A298 (= A319), G323 (= G344), H329 (= H350), I330 (= I351), K423 (≠ I442)
4zjzA Crystal structure of a benzoate coenzyme a ligase with benzoyl-amp (see paper)
37% identity, 81% coverage: 92:539/553 of query aligns to 59:516/517 of 4zjzA
- active site: S176 (≠ T204), T196 (≠ G224), T324 (= T346), E325 (= E347), K422 (≠ I442), Y427 (≠ N447), K507 (= K530)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: A222 (≠ T250), Y223 (≠ F251), A297 (= A319), G298 (= G320), E299 (= E321), A300 (≠ G322), G320 (= G342), I321 (= I343), G322 (= G344), S323 (≠ A345), T324 (= T346), H328 (= H350), I329 (= I351), D401 (= D421), R416 (= R436), K422 (≠ I442), Y427 (≠ N447)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
37% identity, 81% coverage: 92:539/553 of query aligns to 59:516/518 of 4rmnA
- active site: S176 (≠ T204), T196 (≠ G224), T324 (= T346), E325 (= E347), K422 (≠ I442), Y427 (≠ N447), K507 (= K530)
- binding thiophene-2-carboxylic acid: A217 (≠ P245), F221 (= F249), Y223 (≠ F251), G269 (≠ T293), A270 (= A294), A297 (= A319), G298 (= G320), G322 (= G344), S323 (≠ A345), H328 (= H350), I329 (= I351), K422 (≠ I442), G425 (= G445)
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)
36% identity, 81% coverage: 92:539/553 of query aligns to 59:516/518 of 6m2uA
- active site: S176 (≠ T204), T196 (≠ G224), T324 (= T346), E325 (= E347), K422 (≠ I442), Y427 (≠ N447), K507 (= K530)
- binding adenosine monophosphate: G298 (= G320), E299 (= E321), A300 (≠ G322), D319 (= D341), G320 (= G342), I321 (= I343), G322 (= G344), T324 (= T346), D401 (= D421), R416 (= R436), K422 (≠ I442), Y427 (≠ N447)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ F251), A297 (= A319), G322 (= G344), S323 (≠ A345), A328 (≠ H350)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
36% identity, 81% coverage: 92:539/553 of query aligns to 59:516/518 of 6m2tA
- active site: S176 (≠ T204), T196 (≠ G224), T324 (= T346), E325 (= E347), K422 (≠ I442), Y427 (≠ N447), K507 (= K530)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ F251), G322 (= G344), S323 (≠ A345), A328 (≠ H350)
- binding adenosine monophosphate: G298 (= G320), E299 (= E321), A300 (≠ G322), G320 (= G342), I321 (= I343), S323 (≠ A345), T324 (= T346), D401 (= D421), R416 (= R436), K422 (≠ I442), Y427 (≠ N447)
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
30% identity, 86% coverage: 60:537/553 of query aligns to 42:531/536 of 3c5eA
- active site: T188 (= T204), T331 (= T346), E332 (= E347), N434 (≠ I442), R439 (≠ N447), K524 (= K530)
- binding adenosine-5'-triphosphate: T188 (= T204), S189 (= S205), G190 (= G206), T191 (= T207), S192 (≠ T208), G305 (= G320), E306 (= E321), S307 (≠ G322), G329 (= G344), Q330 (≠ A345), T331 (= T346), D413 (= D421), F425 (≠ Y433), R428 (= R436), K524 (= K530)
- binding magnesium ion: M450 (≠ L458), H452 (= H460), V455 (= V463)
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
30% identity, 86% coverage: 60:537/553 of query aligns to 39:528/533 of 3eq6A
- active site: T185 (= T204), T328 (= T346), E329 (= E347), N431 (≠ I442), R436 (≠ N447), K521 (= K530)
- binding adenosine monophosphate: G302 (= G320), E303 (= E321), S304 (≠ G322), E323 (≠ D341), S324 (≠ G342), Y325 (≠ I343), G326 (= G344), Q327 (≠ A345), T328 (= T346), D410 (= D421), F422 (≠ Y433), R425 (= R436), R436 (≠ N447)
- binding Butyryl Coenzyme A: W229 (≠ F249), F255 (≠ Y274), I277 (≠ T296), V301 (≠ A319), S433 (≠ A444), G434 (= G445), Y435 (= Y446), P501 (= P510), Y502 (≠ F511), Y504 (= Y513), R506 (= R515)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
30% identity, 86% coverage: 60:537/553 of query aligns to 43:532/537 of 3b7wA
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
30% identity, 86% coverage: 60:537/553 of query aligns to 39:528/533 of 2wd9A
- active site: T185 (= T204), T328 (= T346), E329 (= E347), N431 (≠ I442), R436 (≠ N447), K521 (= K530)
- binding ibuprofen: I230 (≠ T250), L231 (≠ F251), G326 (= G344), Q327 (≠ A345), T328 (= T346), R436 (≠ N447)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
30% identity, 86% coverage: 60:537/553 of query aligns to 39:528/533 of 2vzeA
- active site: T185 (= T204), T328 (= T346), E329 (= E347), N431 (≠ I442), R436 (≠ N447), K521 (= K530)
- binding adenosine monophosphate: W229 (≠ F249), G302 (= G320), E303 (= E321), S304 (≠ G322), E323 (≠ D341), Y325 (≠ I343), G326 (= G344), Q327 (≠ A345), T328 (= T346), D410 (= D421), F422 (≠ Y433), R425 (= R436), R436 (≠ N447)
Q08AH3 Acyl-coenzyme A synthetase ACSM2A, mitochondrial; Acyl-CoA synthetase medium-chain family member 2A; Benzoate--CoA ligase; Butyrate--CoA ligase 2A; Butyryl-coenzyme A synthetase 2A; Middle-chain acyl-CoA synthetase 2A; EC 6.2.1.2; EC 6.2.1.25 from Homo sapiens (Human) (see 4 papers)
29% identity, 86% coverage: 60:537/553 of query aligns to 75:564/577 of Q08AH3
- Q139 (≠ L124) binding
- 221:229 (vs. 204:212, 78% identical) binding
- ESYGQT 359:364 (≠ DGIGAT 341:346) binding
- T364 (= T346) binding
- D446 (= D421) binding
- R461 (= R436) binding
- SGY 469:471 (≠ AGY 444:446) binding
- R472 (≠ N447) binding
- R501 (= R476) binding
- S513 (≠ P488) to L: in dbSNP:rs1133607
- K532 (= K505) binding
- YPR 540:542 (= YPR 513:515) binding
- K557 (= K530) binding
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
30% identity, 86% coverage: 60:537/553 of query aligns to 43:530/535 of 3dayA
- active site: T189 (= T204), T332 (= T346), E333 (= E347), N435 (≠ I442), R440 (≠ N447), K523 (= K530)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T204), S190 (= S205), G191 (= G206), T192 (= T207), S193 (≠ T208), K197 (= K212), G306 (= G320), E307 (= E321), S308 (≠ G322), Y329 (≠ I343), G330 (= G344), Q331 (≠ A345), T332 (= T346), D414 (= D421), F426 (≠ Y433), R429 (= R436), K523 (= K530)
- binding magnesium ion: M451 (≠ L458), H453 (= H460), V456 (= V463)
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
30% identity, 86% coverage: 60:537/553 of query aligns to 40:527/532 of 3gpcA
- active site: T186 (= T204), T327 (= T346), E328 (= E347), N430 (≠ I442), R435 (≠ N447), K520 (= K530)
- binding coenzyme a: G301 (= G320), E302 (= E321), S303 (≠ G322), E322 (≠ D341), Y324 (≠ I343), G325 (= G344), Q326 (≠ A345), T327 (= T346), D409 (= D421), F421 (≠ Y433), R424 (= R436), T516 (= T526), K520 (= K530), Q522 (= Q532)
- binding magnesium ion: H448 (= H460), V451 (= V463)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 91% coverage: 37:538/553 of query aligns to 2:499/506 of 4gxqA
- active site: T163 (= T204), N183 (≠ C225), H207 (≠ F249), T303 (= T346), E304 (= E347), I403 (= I442), N408 (= N447), A491 (≠ K530)
- binding adenosine-5'-triphosphate: T163 (= T204), S164 (= S205), G165 (= G206), T166 (= T207), T167 (= T208), H207 (≠ F249), S277 (≠ G320), A278 (≠ E321), P279 (≠ G322), E298 (≠ D341), M302 (≠ A345), T303 (= T346), D382 (= D421), R397 (= R436)
- binding carbonate ion: H207 (≠ F249), S277 (≠ G320), R299 (≠ G342), G301 (= G344)
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)
30% identity, 92% coverage: 39:544/553 of query aligns to 5:494/702 of B2HIL6
Sites not aligning to the query:
- 576 S→A: Catalyzes pHBA-AMP formation, indicating this residue is not essential for adenylation activity.
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, 90% coverage: 42:540/553 of query aligns to 23:553/561 of P69451
- Y213 (≠ F203) mutation to A: Loss of activity.
- T214 (= T204) mutation to A: 10% of wild-type activity.
- G216 (= G206) mutation to A: Decreases activity.
- T217 (= T207) mutation to A: Decreases activity.
- G219 (= G209) mutation to A: Decreases activity.
- K222 (= K212) mutation to A: Decreases activity.
- E361 (= E347) mutation to A: Loss of activity.
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
28% identity, 87% coverage: 56:536/553 of query aligns to 60:542/562 of 8biqA
Query Sequence
>Ac3H11_4556 FitnessBrowser__acidovorax_3H11:Ac3H11_4556
MKAPSAQPDHFVHDRLPPPEAWPTLRYDLPELQIADQANLVQALFDQAERAGHSDRPLLR
GPHRTYTYRDARTEAARIAEVLTQDHGLVPGNRVLLRGGNTVEMALAWLGTVYAGLVAVA
TMPLLRAVELGSIIDRAQPTLALCDGRLLAELQAAQTQHPVLTTIVPFHTAPDAADLLQR
AQGKPGTTPPCPTSADDIALMAFTSGTTGAPKAAVHTHRDVLAGCEAWPRHVLKATPDDI
VAGSPPLAFTFGLGGLLVFPMWAGASVYFPDQPYTPETMVRLMREAGVTICYTAPTFYRQ
MAPFARQIGLPQLRTSVSAGEGLPDATRQLWREATGLDMTDGIGATEMFHIFISSAGGES
RAGAVGKVVPGYTAKVVDDDGHEVPRGTVGKLAVIGPTGCKYLDDPRQAKYVKDGWNYPG
DAFTQDADGYFFYQARDDDMIITAGYNVGGPEVEDALLRHPAVAECGVIGVPDEERGMVV
KAICVLKPGHTGDAAMVKTLQDHVKATIAPFKYPRVVEFVAALPRTETGKLQRFKLRQGA
GASPSHSPTKTTT
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