SitesBLAST
Comparing Ac3H11_3090 FitnessBrowser__acidovorax_3H11:Ac3H11_3090 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)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
67% identity, 98% coverage: 5:511/518 of query aligns to 5:515/518 of 4rmnA
- active site: S176 (= S176), T196 (= T196), T324 (= T320), E325 (= E321), K422 (= K418), Y427 (= Y423), K507 (= K503)
- binding thiophene-2-carboxylic acid: A217 (= A217), F221 (= F221), Y223 (= Y223), G269 (= G265), A270 (= A266), A297 (= A293), G298 (= G294), G322 (= G318), S323 (= S319), H328 (= H324), I329 (= I325), K422 (= K418), G425 (= G421)
4zjzA Crystal structure of a benzoate coenzyme a ligase with benzoyl-amp (see paper)
67% identity, 98% coverage: 5:511/518 of query aligns to 5:515/517 of 4zjzA
- active site: S176 (= S176), T196 (= T196), T324 (= T320), E325 (= E321), K422 (= K418), Y427 (= Y423), K507 (= K503)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: A222 (= A222), Y223 (= Y223), A297 (= A293), G298 (= G294), E299 (= E295), A300 (= A296), G320 (= G316), I321 (= I317), G322 (= G318), S323 (= S319), T324 (= T320), H328 (= H324), I329 (= I325), D401 (= D397), R416 (= R412), K422 (= K418), Y427 (= Y423)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
67% identity, 98% coverage: 5:511/518 of query aligns to 5:515/516 of 4rm2A
- active site: S176 (= S176), T196 (= T196), T324 (= T320), E325 (= E321), K422 (= K418), Y427 (= Y423), K507 (= K503)
- binding 2-fluorobenzoic acid: A216 (= A216), A222 (= A222), Y223 (= Y223), P246 (= P246), T247 (= T247), V251 (≠ T251), F267 (= F263), G269 (= G265), A270 (= A266), G273 (= G269), M277 (= M273), A297 (= A293), G298 (= G294), I321 (= I317), G322 (= G318), S323 (= S319), H328 (= H324), K422 (= K418)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
67% identity, 98% coverage: 5:511/518 of query aligns to 6:516/518 of 4rm3A
- active site: S177 (= S176), T197 (= T196), T325 (= T320), E326 (= E321), K423 (= K418), Y428 (= Y423), K508 (= K503)
- binding 2-furoic acid: A223 (= A222), Y224 (= Y223), A298 (= A293), G323 (= G318), H329 (= H324), I330 (= I325), K423 (= K418)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
67% identity, 98% coverage: 5:511/518 of query aligns to 5:515/519 of 4rlfB
- active site: S176 (= S176), T196 (= T196), T324 (= T320), E325 (= E321), K422 (= K418), Y427 (= Y423), K507 (= K503)
- binding 2-methylbenzoic acid: A222 (= A222), Y223 (= Y223), G298 (= G294), I321 (= I317), G322 (= G318), S323 (= S319), H328 (= H324)
- binding 4-methylbenzoic acid: A216 (= A216), P246 (= P246), P248 (= P248), G269 (= G265), A270 (= A266), G273 (= G269)
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)
67% identity, 98% coverage: 5:511/518 of query aligns to 5:515/518 of 6m2uA
- active site: S176 (= S176), T196 (= T196), T324 (= T320), E325 (= E321), K422 (= K418), Y427 (= Y423), K507 (= K503)
- binding adenosine monophosphate: G298 (= G294), E299 (= E295), A300 (= A296), D319 (= D315), G320 (= G316), I321 (= I317), G322 (= G318), T324 (= T320), D401 (= D397), R416 (= R412), K422 (= K418), Y427 (= Y423)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (= Y223), A297 (= A293), G322 (= G318), S323 (= S319), A328 (≠ H324)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
67% identity, 98% coverage: 5:511/518 of query aligns to 5:515/518 of 6m2tA
- active site: S176 (= S176), T196 (= T196), T324 (= T320), E325 (= E321), K422 (= K418), Y427 (= Y423), K507 (= K503)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (= Y223), G322 (= G318), S323 (= S319), A328 (≠ H324)
- binding adenosine monophosphate: G298 (= G294), E299 (= E295), A300 (= A296), G320 (= G316), I321 (= I317), S323 (= S319), T324 (= T320), D401 (= D397), R416 (= R412), K422 (= K418), Y427 (= Y423)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
45% identity, 98% coverage: 4:510/518 of query aligns to 6:509/518 of 4wv3B
- active site: S175 (= S176), T320 (= T320), E321 (= E321), K418 (= K418), W423 (≠ Y423), K502 (= K503)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (= F221), T221 (≠ A222), F222 (≠ Y223), A293 (= A293), S294 (≠ G294), E295 (= E295), A296 (= A296), G316 (= G316), I317 (= I317), G318 (= G318), C319 (≠ S319), T320 (= T320), D397 (= D397), H409 (≠ Y409), R412 (= R412), K502 (= K503)
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)
34% identity, 92% coverage: 32:510/518 of query aligns to 29:487/702 of B2HIL6
Sites not aligning to the query:
- 576 S→A: Catalyzes pHBA-AMP formation, indicating this residue is not essential for adenylation activity.
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)
30% identity, 99% coverage: 5:515/518 of query aligns to 19:555/561 of P69451
- Y213 (= Y175) mutation to A: Loss of activity.
- T214 (≠ S176) mutation to A: 10% of wild-type activity.
- G216 (= G178) mutation to A: Decreases activity.
- T217 (≠ S179) mutation to A: Decreases activity.
- G219 (= G181) mutation to A: Decreases activity.
- K222 (= K184) mutation to A: Decreases activity.
- E361 (= E321) mutation to A: Loss of activity.
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
28% identity, 99% coverage: 3:513/518 of query aligns to 6:534/536 of 3c5eA
- active site: T188 (≠ S176), T331 (= T320), E332 (= E321), N434 (≠ K418), R439 (≠ Y423), K524 (= K503)
- binding adenosine-5'-triphosphate: T188 (≠ S176), S189 (= S177), G190 (= G178), T191 (≠ S179), S192 (≠ T180), G305 (= G294), E306 (= E295), S307 (≠ A296), G329 (= G318), Q330 (≠ S319), T331 (= T320), D413 (= D397), F425 (≠ Y409), R428 (= R412), K524 (= K503)
- binding magnesium ion: M450 (= M434), H452 (= H436), V455 (= V439)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
28% identity, 99% coverage: 3:513/518 of query aligns to 7:535/537 of 3b7wA
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
28% identity, 99% coverage: 3:513/518 of query aligns to 3:531/533 of 3eq6A
- active site: T185 (≠ S176), T328 (= T320), E329 (= E321), N431 (≠ K418), R436 (≠ Y423), K521 (= K503)
- binding adenosine monophosphate: G302 (= G294), E303 (= E295), S304 (≠ A296), E323 (≠ D315), S324 (≠ G316), Y325 (≠ I317), G326 (= G318), Q327 (≠ S319), T328 (= T320), D410 (= D397), F422 (≠ Y409), R425 (= R412), R436 (≠ Y423)
- binding Butyryl Coenzyme A: W229 (≠ F221), F255 (≠ P246), I277 (≠ T268), V301 (≠ A293), S433 (= S420), G434 (= G421), Y435 (≠ I422), P501 (= P483), Y502 (= Y484), Y504 (= Y486), R506 (= R488)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
28% identity, 99% coverage: 3:513/518 of query aligns to 3:531/533 of 2wd9A
- active site: T185 (≠ S176), T328 (= T320), E329 (= E321), N431 (≠ K418), R436 (≠ Y423), K521 (= K503)
- binding ibuprofen: I230 (≠ A222), L231 (≠ Y223), G326 (= G318), Q327 (≠ S319), T328 (= T320), R436 (≠ Y423)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
28% identity, 99% coverage: 3:513/518 of query aligns to 3:531/533 of 2vzeA
- active site: T185 (≠ S176), T328 (= T320), E329 (= E321), N431 (≠ K418), R436 (≠ Y423), K521 (= K503)
- binding adenosine monophosphate: W229 (≠ F221), G302 (= G294), E303 (= E295), S304 (≠ A296), E323 (≠ D315), Y325 (≠ I317), G326 (= G318), Q327 (≠ S319), T328 (= T320), D410 (= D397), F422 (≠ Y409), R425 (= R412), R436 (≠ Y423)
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
28% identity, 99% coverage: 3:513/518 of query aligns to 7:533/535 of 3dayA
- active site: T189 (≠ S176), T332 (= T320), E333 (= E321), N435 (≠ K418), R440 (≠ Y423), K523 (= K503)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (≠ S176), S190 (= S177), G191 (= G178), T192 (≠ S179), S193 (≠ T180), K197 (= K184), G306 (= G294), E307 (= E295), S308 (≠ A296), Y329 (≠ I317), G330 (= G318), Q331 (≠ S319), T332 (= T320), D414 (= D397), F426 (≠ Y409), R429 (= R412), K523 (= K503)
- binding magnesium ion: M451 (= M434), H453 (= H436), V456 (= V439)
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)
28% identity, 98% coverage: 4:513/518 of query aligns to 40:567/577 of Q08AH3
- Q139 (≠ L91) binding
- 221:229 (vs. 176:184, 56% identical) binding
- ESYGQT 359:364 (≠ DGIGST 315:320) binding
- T364 (= T320) binding
- D446 (= D397) binding
- R461 (= R412) binding
- SGY 469:471 (≠ SGI 420:422) binding
- R472 (≠ Y423) binding
- R501 (≠ G452) binding
- S513 (vs. gap) to L: in dbSNP:rs1133607
- K532 (= K478) binding
- YPR 540:542 (= YPR 486:488) binding
- K557 (= K503) binding
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
28% identity, 99% coverage: 3:513/518 of query aligns to 4:530/532 of 3gpcA
- active site: T186 (≠ S176), T327 (= T320), E328 (= E321), N430 (≠ K418), R435 (≠ Y423), K520 (= K503)
- binding coenzyme a: G301 (= G294), E302 (= E295), S303 (≠ A296), E322 (≠ D315), Y324 (≠ I317), G325 (= G318), Q326 (≠ S319), T327 (= T320), D409 (= D397), F421 (≠ Y409), R424 (= R412), T516 (= T499), K520 (= K503), Q522 (= Q505)
- binding magnesium ion: H448 (= H436), V451 (= V439)
5oe6A Crystal structure of the n-terminal domain of pqsa in complex with 6- fluoroanthraniloyl-amp (crystal form 1) (see paper)
32% identity, 69% coverage: 59:414/518 of query aligns to 52:394/394 of 5oe6A
- active site: T162 (≠ S176), G178 (≠ W195), F204 (= F221), T299 (= T320), E300 (= E321)
- binding 6-fluoroanthraniloyl-AMP: T162 (≠ S176), F204 (= F221), Y206 (= Y223), G274 (= G294), S275 (≠ E295), P276 (≠ A296), G295 (= G316), I296 (= I317), G297 (= G318), A298 (≠ S319), T299 (= T320), H303 (= H324), D377 (= D397)
5oe3A Crystal structure of the n-terminal domain of pqsa in complex with anthraniloyl-amp (crystal form 1) (see paper)
32% identity, 69% coverage: 59:414/518 of query aligns to 53:394/394 of 5oe3A
- active site: T163 (= T180), G178 (≠ W195), F204 (= F221), T299 (= T320), E300 (= E321)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F204 (= F221), Y206 (= Y223), G274 (= G294), S275 (≠ E295), P276 (≠ A296), G295 (= G316), I296 (= I317), G297 (= G318), A298 (≠ S319), T299 (= T320), H303 (= H324), D377 (= D397), H389 (≠ Y409)
Query Sequence
>Ac3H11_3090 FitnessBrowser__acidovorax_3H11:Ac3H11_3090
MTRLPEHFNFAEHLFALNRARGDRMAYIDDHETLSYGALEDRARRLAAVLAAAGVRREER
VLLLMLDTCDWPVAFLGCLYAGVLPVAVNTLLKPEDYAYMLSHARARAVLVSGALLPVLN
DAMERQPHEVALQVVSQPQGPLPAGAVDMRAAIAAAVPLAAPAATGPDAPGFWLYSSGST
GKPKGTVHTHGNLWWTAELYGKPVLGLTEQDRCFSAAKLYFAYGLGNSLTFPLSVGATVV
LMAERPTPDATFERWTRHQPTVFFGAPTGFAGMLASPRLPPRSAVSLRMCSSAGEALPAE
IAQRFKAHFGCDIIDGIGSTEMLHIFLSNRPGDVRYGTTGKPVPGYEVSLRGEDGREVPD
GEIGDLYIQGPSAALLYWNNREKTRETFQGAWTKSGDKYVRDAEGYYTYAGRSDDMLKVS
GIYVSPFEVEATLMQHQAVLEAAVIGAQDADGLTKTKAFVVLKDGQTATPDDLKAFVKER
LAPYKYPRLIEFVPELPKTATGKIQRFRLREREQGPQA
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