SitesBLAST
Comparing Dsui_2187 FitnessBrowser__PS:Dsui_2187 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)
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
44% identity, 93% coverage: 33:555/565 of query aligns to 34:561/562 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 (= W250), G321 (= G319), E322 (= E320), P323 (= P321), D342 (= D340), F343 (≠ G341), Y344 (≠ F342), Q346 (= Q344), T347 (= T345), D428 (= D423), F440 (≠ Y435), K449 (= K444), R454 (= R449)
- binding coenzyme a: N128 (≠ L124), W247 (= W245), K249 (= K247), K273 (≠ R270), L274 (≠ F271), Q300 (≠ M297), D452 (= D447), Y453 (= Y448), R483 (= R478), P517 (= P512)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
44% identity, 93% coverage: 33:555/565 of query aligns to 33:560/562 of 8biqA
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
44% identity, 93% coverage: 33:555/565 of query aligns to 32:559/561 of 8biqB
- 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: G319 (= G319), E320 (= E320), P321 (= P321), D340 (= D340), F341 (≠ G341), Y342 (≠ F342), G343 (= G343), Q344 (= Q344), T345 (= T345), D426 (= D423), F438 (≠ Y435), K447 (= K444), R452 (= R449)
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
35% identity, 90% coverage: 35:543/565 of query aligns to 7:533/533 of 3eq6A
- active site: T185 (= T201), T328 (= T345), E329 (= E346), N431 (≠ K444), R436 (= R449), K521 (= K531)
- binding adenosine monophosphate: G302 (= G319), E303 (= E320), S304 (≠ P321), E323 (≠ D340), S324 (≠ G341), Y325 (≠ F342), G326 (= G343), Q327 (= Q344), T328 (= T345), D410 (= D423), F422 (≠ Y435), R425 (= R438), R436 (= R449)
- binding Butyryl Coenzyme A: W229 (= W245), F255 (= F271), I277 (≠ T293), V301 (≠ A318), S433 (= S446), G434 (≠ D447), Y435 (= Y448), P501 (= P512), Y502 (= Y513), Y504 (≠ R515), R506 (= R517)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
35% identity, 90% coverage: 35:543/565 of query aligns to 7:533/533 of 2wd9A
- active site: T185 (= T201), T328 (= T345), E329 (= E346), N431 (≠ K444), R436 (= R449), K521 (= K531)
- binding ibuprofen: I230 (≠ A246), L231 (≠ K247), G326 (= G343), Q327 (= Q344), T328 (= T345), R436 (= R449)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
35% identity, 90% coverage: 35:543/565 of query aligns to 7:533/533 of 2vzeA
- active site: T185 (= T201), T328 (= T345), E329 (= E346), N431 (≠ K444), R436 (= R449), K521 (= K531)
- binding adenosine monophosphate: W229 (= W245), G302 (= G319), E303 (= E320), S304 (≠ P321), E323 (≠ D340), Y325 (≠ F342), G326 (= G343), Q327 (= Q344), T328 (= T345), D410 (= D423), F422 (≠ Y435), R425 (= R438), R436 (= R449)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
35% identity, 90% coverage: 35:543/565 of query aligns to 11:537/537 of 3b7wA
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
35% identity, 90% coverage: 35:543/565 of query aligns to 10:536/536 of 3c5eA
- active site: T188 (= T201), T331 (= T345), E332 (= E346), N434 (≠ K444), R439 (= R449), K524 (= K531)
- binding adenosine-5'-triphosphate: T188 (= T201), S189 (= S202), G190 (= G203), T191 (= T204), S192 (≠ T205), G305 (= G319), E306 (= E320), S307 (≠ P321), G329 (= G343), Q330 (= Q344), T331 (= T345), D413 (= D423), F425 (≠ Y435), R428 (= R438), K524 (= K531)
- binding magnesium ion: M450 (≠ I460), H452 (= H462), V455 (= V465)
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)
34% identity, 94% coverage: 15:543/565 of query aligns to 18:569/577 of Q08AH3
- Q139 (≠ L124) binding
- 221:229 (vs. 201:209, 67% identical) binding
- ESYGQT 359:364 (≠ DGFGQT 340:345) binding
- T364 (= T345) binding
- D446 (= D423) binding
- R461 (= R438) binding
- SGY 469:471 (≠ SDY 446:448) binding
- R472 (= R449) binding
- R501 (= R478) binding
- S513 (≠ N490) to L: in dbSNP:rs1133607
- K532 (≠ R507) binding
- YPR 540:542 (≠ RIR 515:517) binding
- K557 (= K531) binding
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
35% identity, 90% coverage: 35:543/565 of query aligns to 8:532/532 of 3gpcA
- active site: T186 (= T201), T327 (= T345), E328 (= E346), N430 (≠ K444), R435 (= R449), K520 (= K531)
- binding coenzyme a: G301 (= G319), E302 (= E320), S303 (≠ P321), E322 (≠ D340), Y324 (≠ F342), G325 (= G343), Q326 (= Q344), T327 (= T345), D409 (= D423), F421 (≠ Y435), R424 (= R438), T516 (= T527), K520 (= K531), Q522 (≠ R533)
- binding magnesium ion: H448 (= H462), V451 (= V465)
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
35% identity, 90% coverage: 35:543/565 of query aligns to 11:535/535 of 3dayA
- active site: T189 (= T201), T332 (= T345), E333 (= E346), N435 (≠ K444), R440 (= R449), K523 (= K531)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T201), S190 (= S202), G191 (= G203), T192 (= T204), S193 (≠ T205), K197 (= K209), G306 (= G319), E307 (= E320), S308 (≠ P321), Y329 (≠ F342), G330 (= G343), Q331 (= Q344), T332 (= T345), D414 (= D423), F426 (≠ Y435), R429 (= R438), K523 (= K531)
- binding magnesium ion: M451 (≠ I460), H453 (= H462), V456 (= V465)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
31% identity, 84% coverage: 64:539/565 of query aligns to 33:510/518 of 4wv3B
- active site: S175 (≠ T201), T320 (= T345), E321 (= E346), K418 (= K444), W423 (≠ R449), K502 (= K531)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ W245), T221 (≠ A246), F222 (≠ K247), A293 (= A318), S294 (≠ G319), E295 (= E320), A296 (≠ P321), G316 (= G341), I317 (≠ F342), G318 (= G343), C319 (≠ Q344), T320 (= T345), D397 (= D423), H409 (≠ Y435), R412 (= R438), K502 (= K531)
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)
32% identity, 84% coverage: 67:538/565 of query aligns to 34:514/518 of 6m2uA
- active site: S176 (≠ T201), T196 (≠ V220), T324 (= T345), E325 (= E346), K422 (= K444), Y427 (≠ R449), K507 (= K531)
- binding adenosine monophosphate: G298 (= G319), E299 (= E320), A300 (≠ P321), D319 (= D340), G320 (= G341), I321 (≠ F342), G322 (= G343), T324 (= T345), D401 (= D423), R416 (= R438), K422 (= K444), Y427 (≠ R449)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ K247), A297 (= A318), G322 (= G343), S323 (≠ Q344), A328 (= A349)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
32% identity, 84% coverage: 67:538/565 of query aligns to 34:514/518 of 6m2tA
- active site: S176 (≠ T201), T196 (≠ V220), T324 (= T345), E325 (= E346), K422 (= K444), Y427 (≠ R449), K507 (= K531)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ K247), G322 (= G343), S323 (≠ Q344), A328 (= A349)
- binding adenosine monophosphate: G298 (= G319), E299 (= E320), A300 (≠ P321), G320 (= G341), I321 (≠ F342), S323 (≠ Q344), T324 (= T345), D401 (= D423), R416 (= R438), K422 (= K444), Y427 (≠ R449)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
32% identity, 84% coverage: 67:538/565 of query aligns to 34:514/516 of 4rm2A
- active site: S176 (≠ T201), T196 (≠ V220), T324 (= T345), E325 (= E346), K422 (= K444), Y427 (≠ R449), K507 (= K531)
- binding 2-fluorobenzoic acid: A216 (≠ I240), A222 (= A246), Y223 (≠ K247), P246 (vs. gap), T247 (≠ Y268), V251 (≠ S272), F267 (≠ M288), G269 (≠ A290), A270 (≠ P291), G273 (≠ V294), M277 (= M298), A297 (= A318), G298 (= G319), I321 (≠ F342), G322 (= G343), S323 (≠ Q344), H328 (vs. gap), K422 (= K444)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
32% identity, 84% coverage: 67:538/565 of query aligns to 34:514/519 of 4rlfB
- active site: S176 (≠ T201), T196 (≠ V220), T324 (= T345), E325 (= E346), K422 (= K444), Y427 (≠ R449), K507 (= K531)
- binding 2-methylbenzoic acid: A222 (= A246), Y223 (≠ K247), G298 (= G319), I321 (≠ F342), G322 (= G343), S323 (≠ Q344), H328 (vs. gap)
- binding 4-methylbenzoic acid: A216 (≠ I240), P246 (vs. gap), P248 (≠ S269), G269 (≠ A290), A270 (≠ P291), G273 (≠ V294)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
32% identity, 84% coverage: 67:538/565 of query aligns to 35:515/518 of 4rm3A
- active site: S177 (≠ T201), T197 (≠ V220), T325 (= T345), E326 (= E346), K423 (= K444), Y428 (≠ R449), K508 (= K531)
- binding 2-furoic acid: A223 (= A246), Y224 (≠ K247), A298 (= A318), G323 (= G343), H329 (vs. gap), I330 (≠ A349), K423 (= K444)
4zjzA Crystal structure of a benzoate coenzyme a ligase with benzoyl-amp (see paper)
32% identity, 84% coverage: 67:538/565 of query aligns to 34:514/517 of 4zjzA
- active site: S176 (≠ T201), T196 (≠ V220), T324 (= T345), E325 (= E346), K422 (= K444), Y427 (≠ R449), K507 (= K531)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: A222 (= A246), Y223 (≠ K247), A297 (= A318), G298 (= G319), E299 (= E320), A300 (≠ P321), G320 (= G341), I321 (≠ F342), G322 (= G343), S323 (≠ Q344), T324 (= T345), H328 (vs. gap), I329 (≠ A349), D401 (= D423), R416 (= R438), K422 (= K444), Y427 (≠ R449)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
32% identity, 84% coverage: 67:538/565 of query aligns to 34:514/518 of 4rmnA
- active site: S176 (≠ T201), T196 (≠ V220), T324 (= T345), E325 (= E346), K422 (= K444), Y427 (≠ R449), K507 (= K531)
- binding thiophene-2-carboxylic acid: A217 (≠ S241), F221 (≠ W245), Y223 (≠ K247), G269 (≠ A290), A270 (≠ P291), A297 (= A318), G298 (= G319), G322 (= G343), S323 (≠ Q344), H328 (vs. gap), I329 (≠ A349), K422 (= K444), G425 (≠ D447)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
30% identity, 92% coverage: 19:538/565 of query aligns to 54:612/640 of 5jrhA
- active site: T260 (= T201), T412 (= T345), E413 (= E346), N517 (≠ K444), R522 (= R449), K605 (= K531)
- binding (r,r)-2,3-butanediol: W93 (= W56), E140 (≠ P103), G169 (≠ D132), K266 (= K207), P267 (= P208)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G319), E384 (= E320), P385 (= P321), T408 (≠ G341), W409 (≠ F342), W410 (≠ G343), Q411 (= Q344), T412 (= T345), D496 (= D423), I508 (≠ Y435), N517 (≠ K444), R522 (= R449)
- binding coenzyme a: F159 (≠ T122), G160 (≠ T123), G161 (≠ L124), R187 (≠ G145), S519 (= S446), R580 (= R507), P585 (= P512)
- binding magnesium ion: V533 (≠ I460), H535 (= H462), I538 (≠ V465)
Query Sequence
>Dsui_2187 FitnessBrowser__PS:Dsui_2187
MSATEAFLKARDFLLAHRTDYTTAYNGFQWPQLTEFNWALDHFDVMAKGNDKPALWIVEE
DGTEHKISFAQMSARSNQVANWLKAQGVKRGDRILMMLGNEVPLWETMLGCIKLGAVLIP
ATTLLTPEDLRDRLDRGQVKHVIIGAAHTDKFTDLAGDYTRICVGGEPAGWKAFKDSHTA
SAEYTPDAATKVSDPLLLYFTSGTTSKPKLVLHTHQSYPVGHLSTMYWIGLQPGDIHLNI
SSPGWAKHAWSCFFAPWNAGACIFLYNYSRFSAKSMLNVLEKYQVTTMCAPPTVWRMMIQ
EDLAAYKGRLKIRELIGAGEPLNPEIIEQLQNAWNITIRDGFGQTETTAEIGNTPGQPLK
PGSMGRPLPGYQVVLVDSEGNEAAEGEISLKLNPRPLGLMVGYSGDAEKTAEVMRDGVYH
TGDVATKDEDGYITYVGRADDVFKASDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLA
VPKAYVILRNGEKPSKELAKDIFAFLRANLAPYKRIRRLEFSDLPKTISGKIRRVELRAN
EAKRRNANEKGEWEFFEEDFPDLKG
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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