SitesBLAST
Comparing RR42_RS07520 FitnessBrowser__Cup4G11:RR42_RS07520 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)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
61% identity, 91% coverage: 26:541/566 of query aligns to 1:516/518 of 4rm3A
- active site: S177 (= S203), T197 (= T223), T325 (= T347), E326 (= E348), K423 (= K445), Y428 (= Y450), K508 (= K533)
- binding 2-furoic acid: A223 (= A249), Y224 (= Y250), A298 (= A320), G323 (= G345), H329 (= H351), I330 (= I352), K423 (= K445)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
62% identity, 90% coverage: 31:541/566 of query aligns to 5:515/519 of 4rlfB
- active site: S176 (= S203), T196 (= T223), T324 (= T347), E325 (= E348), K422 (= K445), Y427 (= Y450), K507 (= K533)
- binding 2-methylbenzoic acid: A222 (= A249), Y223 (= Y250), G298 (= G321), I321 (= I344), G322 (= G345), S323 (= S346), H328 (= H351)
- binding 4-methylbenzoic acid: A216 (= A243), P246 (= P273), P248 (= P275), G269 (= G292), A270 (≠ V293), G273 (≠ L296)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
62% identity, 90% coverage: 31:541/566 of query aligns to 5:515/518 of 4rmnA
- active site: S176 (= S203), T196 (= T223), T324 (= T347), E325 (= E348), K422 (= K445), Y427 (= Y450), K507 (= K533)
- binding thiophene-2-carboxylic acid: A217 (= A244), F221 (= F248), Y223 (= Y250), G269 (= G292), A270 (≠ V293), A297 (= A320), G298 (= G321), G322 (= G345), S323 (= S346), H328 (= H351), I329 (= I352), K422 (= K445), G425 (= G448)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
62% identity, 90% coverage: 31:541/566 of query aligns to 5:515/516 of 4rm2A
- active site: S176 (= S203), T196 (= T223), T324 (= T347), E325 (= E348), K422 (= K445), Y427 (= Y450), K507 (= K533)
- binding 2-fluorobenzoic acid: A216 (= A243), A222 (= A249), Y223 (= Y250), P246 (= P273), T247 (= T274), V251 (= V278), F267 (= F290), G269 (= G292), A270 (≠ V293), G273 (≠ L296), M277 (= M300), A297 (= A320), G298 (= G321), I321 (= I344), G322 (= G345), S323 (= S346), H328 (= H351), K422 (= K445)
4zjzA Crystal structure of a benzoate coenzyme a ligase with benzoyl-amp (see paper)
62% identity, 90% coverage: 31:541/566 of query aligns to 5:515/517 of 4zjzA
- active site: S176 (= S203), T196 (= T223), T324 (= T347), E325 (= E348), K422 (= K445), Y427 (= Y450), K507 (= K533)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: A222 (= A249), Y223 (= Y250), A297 (= A320), G298 (= G321), E299 (= E322), A300 (= A323), G320 (= G343), I321 (= I344), G322 (= G345), S323 (= S346), T324 (= T347), H328 (= H351), I329 (= I352), D401 (= D424), R416 (= R439), K422 (= K445), Y427 (= Y450)
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)
61% identity, 90% coverage: 31:541/566 of query aligns to 5:515/518 of 6m2uA
- active site: S176 (= S203), T196 (= T223), T324 (= T347), E325 (= E348), K422 (= K445), Y427 (= Y450), K507 (= K533)
- binding adenosine monophosphate: G298 (= G321), E299 (= E322), A300 (= A323), D319 (= D342), G320 (= G343), I321 (= I344), G322 (= G345), T324 (= T347), D401 (= D424), R416 (= R439), K422 (= K445), Y427 (= Y450)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (= Y250), A297 (= A320), G322 (= G345), S323 (= S346), A328 (≠ H351)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
61% identity, 90% coverage: 31:541/566 of query aligns to 5:515/518 of 6m2tA
- active site: S176 (= S203), T196 (= T223), T324 (= T347), E325 (= E348), K422 (= K445), Y427 (= Y450), K507 (= K533)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (= Y250), G322 (= G345), S323 (= S346), A328 (≠ H351)
- binding adenosine monophosphate: G298 (= G321), E299 (= E322), A300 (= A323), G320 (= G343), I321 (= I344), S323 (= S346), T324 (= T347), D401 (= D424), R416 (= R439), K422 (= K445), Y427 (= Y450)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
43% identity, 92% coverage: 28:548/566 of query aligns to 4:517/518 of 4wv3B
- active site: S175 (= S203), T320 (= T347), E321 (= E348), K418 (= K445), W423 (≠ Y450), K502 (= K533)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (= F248), T221 (≠ A249), F222 (≠ Y250), A293 (= A320), S294 (≠ G321), E295 (= E322), A296 (= A323), G316 (= G343), I317 (= I344), G318 (= G345), C319 (≠ S346), T320 (= T347), D397 (= D424), H409 (≠ Y436), R412 (= R439), K502 (= K533)
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)
33% identity, 89% coverage: 35:540/566 of query aligns to 5:487/702 of B2HIL6
Sites not aligning to the query:
- 576 S→A: Catalyzes pHBA-AMP formation, indicating this residue is not essential for adenylation activity.
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
30% identity, 91% coverage: 30:543/566 of query aligns to 8:533/535 of 3dayA
- active site: T189 (≠ S203), T332 (= T347), E333 (= E348), N435 (≠ K445), R440 (≠ Y450), K523 (= K533)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (≠ S203), S190 (= S204), G191 (= G205), T192 (≠ S206), S193 (≠ T207), K197 (= K211), G306 (= G321), E307 (= E322), S308 (≠ A323), Y329 (≠ I344), G330 (= G345), Q331 (≠ S346), T332 (= T347), D414 (= D424), F426 (≠ Y436), R429 (= R439), K523 (= K533)
- binding magnesium ion: M451 (≠ A461), H453 (= H463), V456 (= V466)
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, 91% coverage: 30:543/566 of query aligns to 4:531/533 of 3eq6A
- active site: T185 (≠ S203), T328 (= T347), E329 (= E348), N431 (≠ K445), R436 (≠ Y450), K521 (= K533)
- binding adenosine monophosphate: G302 (= G321), E303 (= E322), S304 (≠ A323), E323 (≠ D342), S324 (≠ G343), Y325 (≠ I344), G326 (= G345), Q327 (≠ S346), T328 (= T347), D410 (= D424), F422 (≠ Y436), R425 (= R439), R436 (≠ Y450)
- binding Butyryl Coenzyme A: W229 (≠ F248), F255 (≠ P273), I277 (≠ T295), V301 (≠ A320), S433 (≠ G447), G434 (= G448), Y435 (≠ I449), P501 (= P513), Y502 (= Y514), Y504 (= Y516), R506 (= R518)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
30% identity, 91% coverage: 30:543/566 of query aligns to 4:531/533 of 2wd9A
- active site: T185 (≠ S203), T328 (= T347), E329 (= E348), N431 (≠ K445), R436 (≠ Y450), K521 (= K533)
- binding ibuprofen: I230 (≠ A249), L231 (≠ Y250), G326 (= G345), Q327 (≠ S346), T328 (= T347), R436 (≠ Y450)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
30% identity, 91% coverage: 30:543/566 of query aligns to 4:531/533 of 2vzeA
- active site: T185 (≠ S203), T328 (= T347), E329 (= E348), N431 (≠ K445), R436 (≠ Y450), K521 (= K533)
- binding adenosine monophosphate: W229 (≠ F248), G302 (= G321), E303 (= E322), S304 (≠ A323), E323 (≠ D342), Y325 (≠ I344), G326 (= G345), Q327 (≠ S346), T328 (= T347), D410 (= D424), F422 (≠ Y436), R425 (= R439), R436 (≠ Y450)
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
30% identity, 91% coverage: 30:543/566 of query aligns to 7:534/536 of 3c5eA
- active site: T188 (≠ S203), T331 (= T347), E332 (= E348), N434 (≠ K445), R439 (≠ Y450), K524 (= K533)
- binding adenosine-5'-triphosphate: T188 (≠ S203), S189 (= S204), G190 (= G205), T191 (≠ S206), S192 (≠ T207), G305 (= G321), E306 (= E322), S307 (≠ A323), G329 (= G345), Q330 (≠ S346), T331 (= T347), D413 (= D424), F425 (≠ Y436), R428 (= R439), K524 (= K533)
- binding magnesium ion: M450 (≠ A461), H452 (= H463), V455 (= V466)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
30% identity, 91% coverage: 30:543/566 of query aligns to 8:535/537 of 3b7wA
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)
30% identity, 92% coverage: 30:550/566 of query aligns to 40:574/577 of Q08AH3
- Q139 (≠ L119) binding
- 221:229 (vs. 203:211, 56% identical) binding
- ESYGQT 359:364 (≠ DGIGST 342:347) binding
- T364 (= T347) binding
- D446 (= D424) binding
- R461 (= R439) binding
- SGY 469:471 (≠ GGI 447:449) binding
- R472 (≠ Y450) binding
- R501 (≠ E479) binding
- S513 (≠ P491) to L: in dbSNP:rs1133607
- K532 (= K508) binding
- YPR 540:542 (= YPR 516:518) binding
- K557 (= K533) binding
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
30% identity, 91% coverage: 30:543/566 of query aligns to 5:530/532 of 3gpcA
- active site: T186 (≠ S203), T327 (= T347), E328 (= E348), N430 (≠ K445), R435 (≠ Y450), K520 (= K533)
- binding coenzyme a: G301 (= G321), E302 (= E322), S303 (≠ A323), E322 (≠ D342), Y324 (≠ I344), G325 (= G345), Q326 (≠ S346), T327 (= T347), D409 (= D424), F421 (≠ Y436), R424 (= R439), T516 (= T529), K520 (= K533), Q522 (= Q535)
- binding magnesium ion: H448 (= H463), V451 (= V466)
Q4G176 Malonate--CoA ligase ACSF3, mitochondrial; Acyl-CoA synthetase family member 3; EC 6.2.1.76 from Homo sapiens (Human) (see 2 papers)
28% identity, 89% coverage: 32:536/566 of query aligns to 38:566/576 of Q4G176
- R354 (≠ G343) mutation to A: Impairs malonyl-CoA synthase activity.; mutation to L: Impairs malonyl-CoA synthase activity.
- V372 (= V361) to M: in dbSNP:rs3743979
Sites not aligning to the query:
- 2 L → P: in dbSNP:rs7188200
- 17 A → P: in dbSNP:rs11547019
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
30% identity, 90% coverage: 33:539/566 of query aligns to 35:542/562 of 8biqA
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
30% identity, 90% coverage: 33:539/566 of query aligns to 36:543/562 of 8bitA
- binding [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] ethanoate: W252 (≠ G253), G321 (= G321), E322 (= E322), P323 (≠ A323), D342 (= D342), F343 (≠ G343), Y344 (≠ I344), Q346 (≠ S346), T347 (= T347), D428 (= D424), F440 (≠ Y436), K449 (= K445), R454 (≠ Y450)
- binding coenzyme a: N128 (≠ L119), W247 (≠ F248), K249 (≠ Y250), K273 (≠ R272), L274 (≠ P273), Q300 (≠ G299), D452 (≠ G448), Y453 (≠ I449), R483 (≠ E479), P517 (= P513)
Query Sequence
>RR42_RS07520 FitnessBrowser__Cup4G11:RR42_RS07520
MTPPIASPSPAADATNAATATTAAAAISVLPARYNAAADLLSRNLAAGRADKVAYVDDAG
QLSFAALDQRCRRFAAALLHAGIRPEERLLLCALDTIDFPTVFLGCLLAGVVPVAVNTLL
TVDDYAYMLDHSAARAAVVSAPLASVMREAIGKAGTAPALILAAPDAGSAGPGPSVAEMA
GQGTALEGAAATRPDDIAFWLYSSGSTGRPKGTVHTHGNLFHTADLYARQVLGLREDDVV
FSAAKLFFAYGLGNALTFPLAVGATTVLMAERPTPQAVFRRLREQRPTVFCGVPTLYAGM
LAASDLPGRPDVALRVCTSAGEALPKDIGERFRAHFGCDILDGIGSTEMLHIFLSNRPGD
VRYGTTGKPVPGYALRLLDEAGQPCAPGEIGDLFIKGPSAALMYWGNRDKTRDTFVGEWT
RSGDKYQQDADGYFIYAGRSDDMLKVGGIYVSPFEVEAVLALHPAVLEAAVIGVADADEL
VKPKAFVVLRPGRSWHEGMAAELQAFVKSRLAPYKYPRQIECVAELPKTATGKIQRFRLR
QREQAAHAAADGVAPPPAIAPAATDR
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