SitesBLAST
Comparing BPHYT_RS35445 FitnessBrowser__BFirm:BPHYT_RS35445 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)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
41% identity, 65% coverage: 191:546/546 of query aligns to 155:512/518 of 4wv3B
- active site: S175 (≠ T211), T320 (= T352), E321 (= E353), K418 (≠ V448), W423 (≠ N453), K502 (= K536)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (= F256), T221 (= T257), F222 (= F258), A293 (= A325), S294 (≠ G326), E295 (= E327), A296 (= A328), G316 (= G348), I317 (= I349), G318 (= G350), C319 (≠ G351), T320 (= T352), D397 (= D427), H409 (≠ Y439), R412 (= R442), K502 (= K536)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
33% identity, 93% coverage: 34:543/546 of query aligns to 6:515/518 of 4rm3A
- active site: S177 (≠ T211), T197 (≠ M231), T325 (= T352), E326 (= E353), K423 (≠ V448), Y428 (≠ N453), K508 (= K536)
- binding 2-furoic acid: A223 (≠ T257), Y224 (≠ F258), A298 (= A325), G323 (= G350), H329 (= H356), I330 (= I357), K423 (≠ V448)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
33% identity, 93% coverage: 34:543/546 of query aligns to 5:514/516 of 4rm2A
- active site: S176 (≠ T211), T196 (≠ M231), T324 (= T352), E325 (= E353), K422 (≠ V448), Y427 (≠ N453), K507 (= K536)
- binding 2-fluorobenzoic acid: A216 (≠ T251), A222 (≠ T257), Y223 (≠ F258), P246 (≠ L280), T247 (= T281), V251 (≠ L285), F267 (≠ M297), G269 (≠ T299), A270 (= A300), G273 (≠ F303), M277 (= M307), A297 (= A325), G298 (= G326), I321 (= I349), G322 (= G350), S323 (≠ G351), H328 (= H356), K422 (≠ V448)
4zjzA Crystal structure of a benzoate coenzyme a ligase with benzoyl-amp (see paper)
33% identity, 93% coverage: 34:543/546 of query aligns to 5:514/517 of 4zjzA
- active site: S176 (≠ T211), T196 (≠ M231), T324 (= T352), E325 (= E353), K422 (≠ V448), Y427 (≠ N453), K507 (= K536)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: A222 (≠ T257), Y223 (≠ F258), A297 (= A325), G298 (= G326), E299 (= E327), A300 (= A328), G320 (= G348), I321 (= I349), G322 (= G350), S323 (≠ G351), T324 (= T352), H328 (= H356), I329 (= I357), D401 (= D427), R416 (= R442), K422 (≠ V448), Y427 (≠ N453)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
33% identity, 93% coverage: 34:543/546 of query aligns to 5:514/518 of 4rmnA
- active site: S176 (≠ T211), T196 (≠ M231), T324 (= T352), E325 (= E353), K422 (≠ V448), Y427 (≠ N453), K507 (= K536)
- binding thiophene-2-carboxylic acid: A217 (≠ P252), F221 (= F256), Y223 (≠ F258), G269 (≠ T299), A270 (= A300), A297 (= A325), G298 (= G326), G322 (= G350), S323 (≠ G351), H328 (= H356), I329 (= I357), K422 (≠ V448), G425 (= G451)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
33% identity, 93% coverage: 34:543/546 of query aligns to 5:514/519 of 4rlfB
- active site: S176 (≠ T211), T196 (≠ M231), T324 (= T352), E325 (= E353), K422 (≠ V448), Y427 (≠ N453), K507 (= K536)
- binding 2-methylbenzoic acid: A222 (≠ T257), Y223 (≠ F258), G298 (= G326), I321 (= I349), G322 (= G350), S323 (≠ G351), H328 (= H356)
- binding 4-methylbenzoic acid: A216 (≠ T251), P246 (≠ L280), P248 (= P282), G269 (≠ T299), A270 (= A300), G273 (≠ F303)
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, 93% coverage: 34:543/546 of query aligns to 5:514/518 of 6m2uA
- active site: S176 (≠ T211), T196 (≠ M231), T324 (= T352), E325 (= E353), K422 (≠ V448), Y427 (≠ N453), K507 (= K536)
- binding adenosine monophosphate: G298 (= G326), E299 (= E327), A300 (= A328), D319 (= D347), G320 (= G348), I321 (= I349), G322 (= G350), T324 (= T352), D401 (= D427), R416 (= R442), K422 (≠ V448), Y427 (≠ N453)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ F258), A297 (= A325), G322 (= G350), S323 (≠ G351), A328 (≠ H356)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
32% identity, 93% coverage: 34:543/546 of query aligns to 5:514/518 of 6m2tA
- active site: S176 (≠ T211), T196 (≠ M231), T324 (= T352), E325 (= E353), K422 (≠ V448), Y427 (≠ N453), K507 (= K536)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ F258), G322 (= G350), S323 (≠ G351), A328 (≠ H356)
- binding adenosine monophosphate: G298 (= G326), E299 (= E327), A300 (= A328), G320 (= G348), I321 (= I349), S323 (≠ G351), T324 (= T352), D401 (= D427), R416 (= R442), K422 (≠ V448), Y427 (≠ N453)
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
31% identity, 93% coverage: 34:543/546 of query aligns to 8:531/536 of 3c5eA
- active site: T188 (= T211), T331 (= T352), E332 (= E353), N434 (≠ V448), R439 (≠ N453), K524 (= K536)
- binding adenosine-5'-triphosphate: T188 (= T211), S189 (= S212), G190 (= G213), T191 (= T214), S192 (≠ T215), G305 (= G326), E306 (= E327), S307 (≠ A328), G329 (= G350), Q330 (≠ G351), T331 (= T352), D413 (= D427), F425 (≠ Y439), R428 (= R442), K524 (= K536)
- binding magnesium ion: M450 (≠ L464), H452 (= H466), V455 (= V469)
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
31% identity, 93% coverage: 34:543/546 of query aligns to 5:528/533 of 3eq6A
- active site: T185 (= T211), T328 (= T352), E329 (= E353), N431 (≠ V448), R436 (≠ N453), K521 (= K536)
- binding adenosine monophosphate: G302 (= G326), E303 (= E327), S304 (≠ A328), E323 (≠ D347), S324 (≠ G348), Y325 (≠ I349), G326 (= G350), Q327 (≠ G351), T328 (= T352), D410 (= D427), F422 (≠ Y439), R425 (= R442), R436 (≠ N453)
- binding Butyryl Coenzyme A: W229 (≠ F256), F255 (≠ L280), I277 (≠ T302), V301 (≠ A325), S433 (≠ A450), G434 (= G451), Y435 (= Y452), P501 (= P516), Y502 (= Y517), Y504 (= Y519), R506 (= R521)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
31% identity, 93% coverage: 34:543/546 of query aligns to 5:528/533 of 2wd9A
- active site: T185 (= T211), T328 (= T352), E329 (= E353), N431 (≠ V448), R436 (≠ N453), K521 (= K536)
- binding ibuprofen: I230 (≠ T257), L231 (≠ F258), G326 (= G350), Q327 (≠ G351), T328 (= T352), R436 (≠ N453)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
31% identity, 93% coverage: 34:543/546 of query aligns to 5:528/533 of 2vzeA
- active site: T185 (= T211), T328 (= T352), E329 (= E353), N431 (≠ V448), R436 (≠ N453), K521 (= K536)
- binding adenosine monophosphate: W229 (≠ F256), G302 (= G326), E303 (= E327), S304 (≠ A328), E323 (≠ D347), Y325 (≠ I349), G326 (= G350), Q327 (≠ G351), T328 (= T352), D410 (= D427), F422 (≠ Y439), R425 (= R442), R436 (≠ N453)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
31% identity, 93% coverage: 34:543/546 of query aligns to 9:532/537 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)
31% identity, 93% coverage: 34:543/546 of query aligns to 41:564/577 of Q08AH3
- Q139 (≠ L127) binding
- 221:229 (vs. 211:219, 78% identical) binding
- ESYGQT 359:364 (≠ DGIGGT 347:352) binding
- T364 (= T352) binding
- D446 (= D427) binding
- R461 (= R442) binding
- SGY 469:471 (≠ AGY 450:452) binding
- R472 (≠ N453) binding
- R501 (= R482) binding
- S513 (≠ P494) to L: in dbSNP:rs1133607
- K532 (= K511) binding
- YPR 540:542 (= YPR 519:521) binding
- K557 (= K536) binding
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
31% identity, 93% coverage: 34:543/546 of query aligns to 9:530/535 of 3dayA
- active site: T189 (= T211), T332 (= T352), E333 (= E353), N435 (≠ V448), R440 (≠ N453), K523 (= K536)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T211), S190 (= S212), G191 (= G213), T192 (= T214), S193 (≠ T215), K197 (= K219), G306 (= G326), E307 (= E327), S308 (≠ A328), Y329 (≠ I349), G330 (= G350), Q331 (≠ G351), T332 (= T352), D414 (= D427), F426 (≠ Y439), R429 (= R442), K523 (= K536)
- binding magnesium ion: M451 (≠ L464), H453 (= H466), V456 (= V469)
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
31% identity, 93% coverage: 34:543/546 of query aligns to 6:527/532 of 3gpcA
- active site: T186 (= T211), T327 (= T352), E328 (= E353), N430 (≠ V448), R435 (≠ N453), K520 (= K536)
- binding coenzyme a: G301 (= G326), E302 (= E327), S303 (≠ A328), E322 (≠ D347), Y324 (≠ I349), G325 (= G350), Q326 (≠ G351), T327 (= T352), D409 (= D427), F421 (≠ Y439), R424 (= R442), T516 (= T532), K520 (= K536), Q522 (≠ K538)
- binding magnesium ion: H448 (= H466), V451 (= V469)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
31% identity, 89% coverage: 58:542/546 of query aligns to 58:542/562 of 8biqA
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
31% identity, 89% coverage: 58:542/546 of query aligns to 59:543/562 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 (≠ G261), G321 (= G326), E322 (= E327), P323 (≠ A328), D342 (= D347), F343 (≠ G348), Y344 (≠ I349), Q346 (≠ G351), T347 (= T352), D428 (= D427), F440 (≠ Y439), K449 (≠ V448), R454 (≠ N453)
- binding coenzyme a: N128 (≠ L127), W247 (≠ F256), K249 (≠ F258), K273 (= K279), L274 (= L280), Q300 (= Q306), D452 (≠ G451), Y453 (= Y452), R483 (= R482), P517 (= P516)
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
31% identity, 89% coverage: 58:542/546 of query aligns to 57:541/561 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 (= G326), E320 (= E327), P321 (≠ A328), D340 (= D347), F341 (≠ G348), Y342 (≠ I349), G343 (= G350), Q344 (≠ G351), T345 (= T352), D426 (= D427), F438 (≠ Y439), K447 (≠ V448), R452 (≠ N453)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 93% coverage: 38:543/546 of query aligns to 4:498/506 of 4gxqA
- active site: T163 (= T211), N183 (≠ C232), H207 (≠ F256), T303 (= T352), E304 (= E353), I403 (≠ V448), N408 (= N453), A491 (≠ K536)
- binding adenosine-5'-triphosphate: T163 (= T211), S164 (= S212), G165 (= G213), T166 (= T214), T167 (= T215), H207 (≠ F256), S277 (≠ G326), A278 (≠ E327), P279 (≠ A328), E298 (≠ D347), M302 (≠ G351), T303 (= T352), D382 (= D427), R397 (= R442)
- binding carbonate ion: H207 (≠ F256), S277 (≠ G326), R299 (≠ G348), G301 (= G350)
Query Sequence
>BPHYT_RS35445 FitnessBrowser__BFirm:BPHYT_RS35445
MEPSAHVDTFARDNLPPQDQWPVFLLDNPDVAYPARLNCASELLDRTIDAGHRDDPAIWS
DVDGAPRATTYGELLALVNRSAHVLVDEMGLQPGNRVLLRGPNTLHMAVTALAALKVGLV
VVPTMPLLRAKELKQIIDKAQVGAALCDARLTAELARCSDPEDEFYCAGLMQTRLFHDDS
PDSLDTLAVNKPDHFTACDTAADDVCLIAFTSGTTGAPKGCMHFHRDVVAMCDLFPRHVL
KPTSSDIFCGTPPLAFTFGLGGLLCFPLRVGASTVLIEKLTPETLLQTVERFHATVMFTA
PTFYRQMAPLVAHHDVSSLKKTVSAGEALPDSTRRLWRDATGIDMIDGIGGTELIHIFIS
AQGDEIRPNAIGRAVPGYAVQAVDDDMQPVAPGTIGKLAVRGPTGCRYLADERQMKFVRD
GWNLPGDSVYLDEDGYVFYQARADDMIVSAGYNISGPEVESVLLQHDAVSECGVIGVPDE
TRGQIVKAFVVVNPGYERDDKLVAQLQEFVKNSVAPYKYPRDIVFVDSLPRTETGKLKRF
ELRTMA
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