SitesBLAST
Comparing H281DRAFT_00369 FitnessBrowser__Burk376:H281DRAFT_00369 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
61% identity, 97% coverage: 16:532/534 of query aligns to 2:516/518 of 4rm3A
- active site: S177 (= S195), T197 (= T215), T325 (= T339), E326 (= E340), K423 (= K437), Y428 (= Y442), K508 (= K524)
- binding 2-furoic acid: A223 (= A241), Y224 (= Y242), A298 (= A312), G323 (= G337), H329 (= H343), I330 (= I344), K423 (= K437)
4zjzA Crystal structure of a benzoate coenzyme a ligase with benzoyl-amp (see paper)
61% identity, 97% coverage: 16:532/534 of query aligns to 1:515/517 of 4zjzA
- active site: S176 (= S195), T196 (= T215), T324 (= T339), E325 (= E340), K422 (= K437), Y427 (= Y442), K507 (= K524)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: A222 (= A241), Y223 (= Y242), A297 (= A312), G298 (= G313), E299 (= E314), A300 (= A315), G320 (= G335), I321 (= I336), G322 (= G337), S323 (= S338), T324 (= T339), H328 (= H343), I329 (= I344), D401 (= D416), R416 (= R431), K422 (= K437), Y427 (= Y442)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
61% identity, 97% coverage: 16:532/534 of query aligns to 1:515/516 of 4rm2A
- active site: S176 (= S195), T196 (= T215), T324 (= T339), E325 (= E340), K422 (= K437), Y427 (= Y442), K507 (= K524)
- binding 2-fluorobenzoic acid: A216 (= A235), A222 (= A241), Y223 (= Y242), P246 (= P265), T247 (= T266), V251 (= V270), F267 (= F282), G269 (= G284), A270 (≠ V285), G273 (≠ L288), M277 (= M292), A297 (= A312), G298 (= G313), I321 (= I336), G322 (= G337), S323 (= S338), H328 (= H343), K422 (= K437)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
61% identity, 97% coverage: 16:532/534 of query aligns to 1:515/519 of 4rlfB
- active site: S176 (= S195), T196 (= T215), T324 (= T339), E325 (= E340), K422 (= K437), Y427 (= Y442), K507 (= K524)
- binding 2-methylbenzoic acid: A222 (= A241), Y223 (= Y242), G298 (= G313), I321 (= I336), G322 (= G337), S323 (= S338), H328 (= H343)
- binding 4-methylbenzoic acid: A216 (= A235), P246 (= P265), P248 (≠ A267), G269 (= G284), A270 (≠ V285), G273 (≠ L288)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
61% identity, 97% coverage: 16:532/534 of query aligns to 1:515/518 of 4rmnA
- active site: S176 (= S195), T196 (= T215), T324 (= T339), E325 (= E340), K422 (= K437), Y427 (= Y442), K507 (= K524)
- binding thiophene-2-carboxylic acid: A217 (= A236), F221 (= F240), Y223 (= Y242), G269 (= G284), A270 (≠ V285), A297 (= A312), G298 (= G313), G322 (= G337), S323 (= S338), H328 (= H343), I329 (= I344), K422 (= K437), G425 (= G440)
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)
60% identity, 97% coverage: 16:532/534 of query aligns to 1:515/518 of 6m2uA
- active site: S176 (= S195), T196 (= T215), T324 (= T339), E325 (= E340), K422 (= K437), Y427 (= Y442), K507 (= K524)
- binding adenosine monophosphate: G298 (= G313), E299 (= E314), A300 (= A315), D319 (= D334), G320 (= G335), I321 (= I336), G322 (= G337), T324 (= T339), D401 (= D416), R416 (= R431), K422 (= K437), Y427 (= Y442)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (= Y242), A297 (= A312), G322 (= G337), S323 (= S338), A328 (≠ H343)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
60% identity, 97% coverage: 16:532/534 of query aligns to 1:515/518 of 6m2tA
- active site: S176 (= S195), T196 (= T215), T324 (= T339), E325 (= E340), K422 (= K437), Y427 (= Y442), K507 (= K524)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (= Y242), G322 (= G337), S323 (= S338), A328 (≠ H343)
- binding adenosine monophosphate: G298 (= G313), E299 (= E314), A300 (= A315), G320 (= G335), I321 (= I336), S323 (= S338), T324 (= T339), D401 (= D416), R416 (= R431), K422 (= K437), Y427 (= Y442)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
42% identity, 96% coverage: 20:531/534 of query aligns to 7:509/518 of 4wv3B
- active site: S175 (= S195), T320 (= T339), E321 (= E340), K418 (= K437), W423 (≠ Y442), K502 (= K524)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (= F240), T221 (≠ A241), F222 (≠ Y242), A293 (= A312), S294 (≠ G313), E295 (= E314), A296 (= A315), G316 (= G335), I317 (= I336), G318 (= G337), C319 (≠ S338), T320 (= T339), D397 (= D416), H409 (≠ Y428), R412 (= R431), K502 (= K524)
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)
31% identity, 95% coverage: 28:534/534 of query aligns to 5:490/702 of B2HIL6
Sites not aligning to the query:
- 576 S→A: Catalyzes pHBA-AMP formation, indicating this residue is not essential for adenylation activity.
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
28% identity, 96% coverage: 20:533/534 of query aligns to 9:532/535 of 3dayA
- active site: T189 (≠ S195), T332 (= T339), E333 (= E340), N435 (≠ K437), R440 (≠ Y442), K523 (= K524)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (≠ S195), S190 (= S196), G191 (= G197), T192 (≠ S198), S193 (≠ T199), K197 (= K203), G306 (= G313), E307 (= E314), S308 (≠ A315), Y329 (≠ I336), G330 (= G337), Q331 (≠ S338), T332 (= T339), D414 (= D416), F426 (≠ Y428), R429 (= R431), K523 (= K524)
- binding magnesium ion: M451 (≠ V453), H453 (= H455), V456 (= V458)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 95% coverage: 24:532/534 of query aligns to 4:499/506 of 4gxqA
- active site: T163 (≠ S195), N183 (≠ A216), H207 (≠ F240), T303 (= T339), E304 (= E340), I403 (≠ K437), N408 (≠ Y442), A491 (≠ K524)
- binding adenosine-5'-triphosphate: T163 (≠ S195), S164 (= S196), G165 (= G197), T166 (≠ S198), T167 (= T199), H207 (≠ F240), S277 (≠ G313), A278 (≠ E314), P279 (≠ A315), E298 (≠ D334), M302 (≠ S338), T303 (= T339), D382 (≠ K417), R397 (= R431)
- binding carbonate ion: H207 (≠ F240), S277 (≠ G313), R299 (≠ G335), G301 (= G337)
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, 96% coverage: 20:533/534 of query aligns to 5:530/533 of 3eq6A
- active site: T185 (≠ S195), T328 (= T339), E329 (= E340), N431 (≠ K437), R436 (≠ Y442), K521 (= K524)
- binding adenosine monophosphate: G302 (= G313), E303 (= E314), S304 (≠ A315), E323 (≠ D334), S324 (≠ G335), Y325 (≠ I336), G326 (= G337), Q327 (≠ S338), T328 (= T339), D410 (= D416), F422 (≠ Y428), R425 (= R431), R436 (≠ Y442)
- binding Butyryl Coenzyme A: W229 (≠ F240), F255 (≠ P265), I277 (≠ T287), V301 (≠ A312), S433 (= S439), G434 (= G440), Y435 (≠ Q441), P501 (= P504), Y502 (≠ H505), Y504 (= Y507), R506 (= R509)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
28% identity, 96% coverage: 20:533/534 of query aligns to 5:530/533 of 2wd9A
- active site: T185 (≠ S195), T328 (= T339), E329 (= E340), N431 (≠ K437), R436 (≠ Y442), K521 (= K524)
- binding ibuprofen: I230 (≠ A241), L231 (≠ Y242), G326 (= G337), Q327 (≠ S338), T328 (= T339), R436 (≠ Y442)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
28% identity, 96% coverage: 20:533/534 of query aligns to 5:530/533 of 2vzeA
- active site: T185 (≠ S195), T328 (= T339), E329 (= E340), N431 (≠ K437), R436 (≠ Y442), K521 (= K524)
- binding adenosine monophosphate: W229 (≠ F240), G302 (= G313), E303 (= E314), S304 (≠ A315), E323 (≠ D334), Y325 (≠ I336), G326 (= G337), Q327 (≠ S338), T328 (= T339), D410 (= D416), F422 (≠ Y428), R425 (= R431), R436 (≠ Y442)
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
28% identity, 96% coverage: 20:533/534 of query aligns to 8:533/536 of 3c5eA
- active site: T188 (≠ S195), T331 (= T339), E332 (= E340), N434 (≠ K437), R439 (≠ Y442), K524 (= K524)
- binding adenosine-5'-triphosphate: T188 (≠ S195), S189 (= S196), G190 (= G197), T191 (≠ S198), S192 (≠ T199), G305 (= G313), E306 (= E314), S307 (≠ A315), G329 (= G337), Q330 (≠ S338), T331 (= T339), D413 (= D416), F425 (≠ Y428), R428 (= R431), K524 (= K524)
- binding magnesium ion: M450 (≠ V453), H452 (= H455), V455 (= V458)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
28% identity, 96% coverage: 20:533/534 of query aligns to 9:534/537 of 3b7wA
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, 98% coverage: 14:534/534 of query aligns to 13:553/561 of P69451
- Y213 (= Y194) mutation to A: Loss of activity.
- T214 (≠ S195) mutation to A: 10% of wild-type activity.
- G216 (= G197) mutation to A: Decreases activity.
- T217 (≠ S198) mutation to A: Decreases activity.
- G219 (= G200) mutation to A: Decreases activity.
- K222 (= K203) mutation to A: Decreases activity.
- E361 (= E340) mutation to A: Loss of activity.
5oe6A Crystal structure of the n-terminal domain of pqsa in complex with 6- fluoroanthraniloyl-amp (crystal form 1) (see paper)
34% identity, 68% coverage: 70:433/534 of query aligns to 48:394/394 of 5oe6A
- active site: T162 (≠ S198), G178 (≠ W214), F204 (= F240), T299 (= T339), E300 (= E340)
- binding 6-fluoroanthraniloyl-AMP: T162 (≠ S198), F204 (= F240), Y206 (= Y242), G274 (= G313), S275 (≠ E314), P276 (≠ A315), G295 (= G335), I296 (= I336), G297 (= G337), A298 (≠ S338), T299 (= T339), H303 (= H343), D377 (= D416)
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)
27% identity, 96% coverage: 20:533/534 of query aligns to 41:566/577 of Q08AH3
- Q139 (≠ L106) binding
- 221:229 (vs. 195:203, 56% identical) binding
- ESYGQT 359:364 (≠ DGIGST 334:339) binding
- T364 (= T339) binding
- D446 (= D416) binding
- R461 (= R431) binding
- SGY 469:471 (≠ SGQ 439:441) binding
- R472 (≠ Y442) binding
- R501 (≠ H468) binding
- S513 (≠ R482) to L: in dbSNP:rs1133607
- K532 (= K499) binding
- YPR 540:542 (= YPR 507:509) binding
- K557 (= K524) 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, 96% coverage: 20:533/534 of query aligns to 6:529/532 of 3gpcA
- active site: T186 (≠ S195), T327 (= T339), E328 (= E340), N430 (≠ K437), R435 (≠ Y442), K520 (= K524)
- binding coenzyme a: G301 (= G313), E302 (= E314), S303 (≠ A315), E322 (≠ D334), Y324 (≠ I336), G325 (= G337), Q326 (≠ S338), T327 (= T339), D409 (= D416), F421 (≠ Y428), R424 (= R431), T516 (= T520), K520 (= K524), Q522 (= Q526)
- binding magnesium ion: H448 (= H455), V451 (= V458)
Query Sequence
>H281DRAFT_00369 FitnessBrowser__Burk376:H281DRAFT_00369
MEALFEPAASQPVVTVEPPPARFNFAAHLFALNAPRAAKTAYIDDSGHMTYGELEDRARR
FSSALRGLGVHPEERVLLVMLDTVSLPIAFLGALYAGVVPVVANTLLTSADYVYMLTHSH
ARAVIASSVLIPNVTQAMETAEHDGCQLIVSNRAAPAPEGEPLAAPVLEDLIDAATPALK
AATTGCDDIAFWLYSSGSTGKPKGTVHTHANLYWTAELYAKPVLGIVESDVVFSAAKLFF
AYGLGNALTFPLSVGATAVLMAERPTADAVFSRLTRHRPTVFYGVPTLYASMLVSPNLPA
RDDVAMRVCTSAGEALPREIGERFTRHFGCEILDGIGSTEMLHIFLSNRAGEVEYGTTGR
PVPGYEVELRDDSGRAVGDGEVGDLFIKGPSAALMYWCNREKTRATFLGEWIRSGDKYSR
LPNGCYVYAGRSDDMLKVSGQYVSPVEVEMVLVQHDAVLEAAVVGIDHGGLVKTRAFVVL
KREFSPSEILVDELKAFVKGRLAPHKYPRDIVFVDDLPKTATGKIQRFKLREQS
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