SitesBLAST
Comparing WP_086509453.1 NCBI__GCF_002151265.1:WP_086509453.1 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)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
35% identity, 93% coverage: 31:537/543 of query aligns to 5:510/518 of 4wv3B
- active site: S175 (≠ T203), T320 (= T345), E321 (= E346), K418 (≠ V441), W423 (≠ N446), K502 (= K529)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (= F248), T221 (= T249), F222 (= F250), A293 (= A318), S294 (≠ G319), E295 (= E320), A296 (≠ T321), G316 (= G341), I317 (= I342), G318 (= G343), C319 (≠ A344), T320 (= T345), D397 (= D420), H409 (≠ F432), R412 (= R435), K502 (= K529)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
34% identity, 93% coverage: 33:537/543 of query aligns to 5:515/519 of 4rlfB
- active site: S176 (≠ T203), T196 (≠ I223), T324 (= T345), E325 (= E346), K422 (≠ V441), Y427 (≠ N446), K507 (= K529)
- binding 2-methylbenzoic acid: A222 (≠ T249), Y223 (≠ F250), G298 (= G319), I321 (= I342), G322 (= G343), S323 (≠ A344), H328 (= H349)
- binding 4-methylbenzoic acid: A216 (≠ S243), P246 (≠ A272), P248 (= P274), G269 (≠ T291), A270 (= A292), G273 (≠ A295)
4zjzA Crystal structure of a benzoate coenzyme a ligase with benzoyl-amp (see paper)
34% identity, 93% coverage: 33:537/543 of query aligns to 5:515/517 of 4zjzA
- active site: S176 (≠ T203), T196 (≠ I223), T324 (= T345), E325 (= E346), K422 (≠ V441), Y427 (≠ N446), K507 (= K529)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: A222 (≠ T249), Y223 (≠ F250), A297 (= A318), G298 (= G319), E299 (= E320), A300 (≠ T321), G320 (= G341), I321 (= I342), G322 (= G343), S323 (≠ A344), T324 (= T345), H328 (= H349), I329 (= I350), D401 (= D420), R416 (= R435), K422 (≠ V441), Y427 (≠ N446)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
34% identity, 93% coverage: 33:537/543 of query aligns to 6:516/518 of 4rm3A
- active site: S177 (≠ T203), T197 (≠ I223), T325 (= T345), E326 (= E346), K423 (≠ V441), Y428 (≠ N446), K508 (= K529)
- binding 2-furoic acid: A223 (≠ T249), Y224 (≠ F250), A298 (= A318), G323 (= G343), H329 (= H349), I330 (= I350), K423 (≠ V441)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
34% identity, 93% coverage: 33:537/543 of query aligns to 5:515/518 of 4rmnA
- active site: S176 (≠ T203), T196 (≠ I223), T324 (= T345), E325 (= E346), K422 (≠ V441), Y427 (≠ N446), K507 (= K529)
- binding thiophene-2-carboxylic acid: A217 (≠ P244), F221 (= F248), Y223 (≠ F250), G269 (≠ T291), A270 (= A292), A297 (= A318), G298 (= G319), G322 (= G343), S323 (≠ A344), H328 (= H349), I329 (= I350), K422 (≠ V441), G425 (= G444)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
34% identity, 93% coverage: 33:537/543 of query aligns to 5:515/516 of 4rm2A
- active site: S176 (≠ T203), T196 (≠ I223), T324 (= T345), E325 (= E346), K422 (≠ V441), Y427 (≠ N446), K507 (= K529)
- binding 2-fluorobenzoic acid: A216 (≠ S243), A222 (≠ T249), Y223 (≠ F250), P246 (≠ A272), T247 (= T273), V251 (≠ M277), F267 (≠ V289), G269 (≠ T291), A270 (= A292), G273 (≠ A295), M277 (= M299), A297 (= A318), G298 (= G319), I321 (= I342), G322 (= G343), S323 (≠ A344), H328 (= H349), K422 (≠ V441)
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)
33% identity, 93% coverage: 33:537/543 of query aligns to 5:515/518 of 6m2uA
- active site: S176 (≠ T203), T196 (≠ I223), T324 (= T345), E325 (= E346), K422 (≠ V441), Y427 (≠ N446), K507 (= K529)
- binding adenosine monophosphate: G298 (= G319), E299 (= E320), A300 (≠ T321), D319 (= D340), G320 (= G341), I321 (= I342), G322 (= G343), T324 (= T345), D401 (= D420), R416 (= R435), K422 (≠ V441), Y427 (≠ N446)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ F250), A297 (= A318), G322 (= G343), S323 (≠ A344), A328 (≠ H349)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
33% identity, 93% coverage: 33:537/543 of query aligns to 5:515/518 of 6m2tA
- active site: S176 (≠ T203), T196 (≠ I223), T324 (= T345), E325 (= E346), K422 (≠ V441), Y427 (≠ N446), K507 (= K529)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ F250), G322 (= G343), S323 (≠ A344), A328 (≠ H349)
- binding adenosine monophosphate: G298 (= G319), E299 (= E320), A300 (≠ T321), G320 (= G341), I321 (= I342), S323 (≠ A344), T324 (= T345), D401 (= D420), R416 (= R435), K422 (≠ V441), Y427 (≠ N446)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
32% identity, 88% coverage: 61:539/543 of query aligns to 26:501/506 of 4gxqA
- active site: T163 (= T203), N183 (vs. gap), H207 (≠ F248), T303 (= T345), E304 (= E346), I403 (≠ V441), N408 (= N446), A491 (≠ K529)
- binding adenosine-5'-triphosphate: T163 (= T203), S164 (= S204), G165 (= G205), T166 (= T206), T167 (= T207), H207 (≠ F248), S277 (≠ G319), A278 (≠ E320), P279 (≠ T321), E298 (≠ D340), M302 (≠ A344), T303 (= T345), D382 (= D420), R397 (= R435)
- binding carbonate ion: H207 (≠ F248), S277 (≠ G319), R299 (≠ G341), G301 (= G343)
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
29% identity, 94% coverage: 31:540/543 of query aligns to 6:535/536 of 3c5eA
- active site: T188 (= T203), T331 (= T345), E332 (= E346), N434 (≠ V441), R439 (≠ N446), K524 (= K529)
- binding adenosine-5'-triphosphate: T188 (= T203), S189 (= S204), G190 (= G205), T191 (= T206), S192 (≠ T207), G305 (= G319), E306 (= E320), S307 (≠ T321), G329 (= G343), Q330 (≠ A344), T331 (= T345), D413 (= D420), F425 (= F432), R428 (= R435), K524 (= K529)
- binding magnesium ion: M450 (≠ L457), H452 (= H459), V455 (= V462)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
29% identity, 94% coverage: 31:540/543 of query aligns to 7:536/537 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)
29% identity, 94% coverage: 31:540/543 of query aligns to 3:532/533 of 3eq6A
- active site: T185 (= T203), T328 (= T345), E329 (= E346), N431 (≠ V441), R436 (≠ N446), K521 (= K529)
- binding adenosine monophosphate: G302 (= G319), E303 (= E320), S304 (≠ T321), E323 (≠ D340), S324 (≠ G341), Y325 (≠ I342), G326 (= G343), Q327 (≠ A344), T328 (= T345), D410 (= D420), F422 (= F432), R425 (= R435), R436 (≠ N446)
- binding Butyryl Coenzyme A: W229 (≠ F248), F255 (≠ A272), I277 (≠ T294), V301 (≠ A318), S433 (≠ A443), G434 (= G444), Y435 (= Y445), P501 (= P509), Y502 (= Y510), Y504 (= Y512), R506 (= R514)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
29% identity, 94% coverage: 31:540/543 of query aligns to 3:532/533 of 2wd9A
- active site: T185 (= T203), T328 (= T345), E329 (= E346), N431 (≠ V441), R436 (≠ N446), K521 (= K529)
- binding ibuprofen: I230 (≠ T249), L231 (≠ F250), G326 (= G343), Q327 (≠ A344), T328 (= T345), R436 (≠ N446)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
29% identity, 94% coverage: 31:540/543 of query aligns to 3:532/533 of 2vzeA
- active site: T185 (= T203), T328 (= T345), E329 (= E346), N431 (≠ V441), R436 (≠ N446), K521 (= K529)
- binding adenosine monophosphate: W229 (≠ F248), G302 (= G319), E303 (= E320), S304 (≠ T321), E323 (≠ D340), Y325 (≠ I342), G326 (= G343), Q327 (≠ A344), T328 (= T345), D410 (= D420), F422 (= F432), R425 (= R435), R436 (≠ N446)
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)
29% identity, 94% coverage: 31:540/543 of query aligns to 39:568/577 of Q08AH3
- Q139 (≠ M122) binding
- 221:229 (vs. 203:211, 78% identical) binding
- ESYGQT 359:364 (≠ DGIGAT 340:345) binding
- T364 (= T345) binding
- D446 (= D420) binding
- R461 (= R435) binding
- SGY 469:471 (≠ AGY 443:445) binding
- R472 (≠ N446) binding
- R501 (= R475) binding
- S513 (= S486) to L: in dbSNP:rs1133607
- K532 (= K504) binding
- YPR 540:542 (= YPR 512:514) binding
- K557 (= K529) binding
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
29% identity, 94% coverage: 31:540/543 of query aligns to 7:534/535 of 3dayA
- active site: T189 (= T203), T332 (= T345), E333 (= E346), N435 (≠ V441), R440 (≠ N446), K523 (= K529)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T203), S190 (= S204), G191 (= G205), T192 (= T206), S193 (≠ T207), K197 (= K211), G306 (= G319), E307 (= E320), S308 (≠ T321), Y329 (≠ I342), G330 (= G343), Q331 (≠ A344), T332 (= T345), D414 (= D420), F426 (= F432), R429 (= R435), K523 (= K529)
- binding magnesium ion: M451 (≠ L457), H453 (= H459), V456 (= V462)
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
28% identity, 94% coverage: 31:540/543 of query aligns to 4:531/532 of 3gpcA
- active site: T186 (= T203), T327 (= T345), E328 (= E346), N430 (≠ V441), R435 (≠ N446), K520 (= K529)
- binding coenzyme a: G301 (= G319), E302 (= E320), S303 (≠ T321), E322 (≠ D340), Y324 (≠ I342), G325 (= G343), Q326 (≠ A344), T327 (= T345), D409 (= D420), F421 (= F432), R424 (= R435), T516 (= T525), K520 (= K529), Q522 (= Q531)
- binding magnesium ion: H448 (= H459), V451 (= V462)
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)
29% identity, 93% coverage: 33:538/543 of query aligns to 19:552/561 of P69451
- Y213 (≠ F202) mutation to A: Loss of activity.
- T214 (= T203) mutation to A: 10% of wild-type activity.
- G216 (= G205) mutation to A: Decreases activity.
- T217 (= T206) mutation to A: Decreases activity.
- G219 (= G208) mutation to A: Decreases activity.
- K222 (= K211) mutation to A: Decreases activity.
- E361 (= E346) mutation to A: Loss of activity.
5gxdA Structure of acryloyl-coa lyase prpe from dinoroseobacter shibae dfl 12
29% identity, 92% coverage: 34:532/543 of query aligns to 48:590/627 of 5gxdA
- active site: T238 (= T203), T390 (= T345), E391 (= E346), N498 (≠ V441), R503 (≠ N446), K587 (= K529)
- binding adenosine monophosphate: G364 (= G319), E365 (= E320), R366 (≠ T321), H386 (≠ G341), W387 (≠ I342), W388 (≠ G343), Q389 (≠ A344), T390 (= T345), D477 (= D420), I489 (≠ F432), R492 (= R435), N498 (≠ V441), R503 (≠ N446)
- binding coenzyme a: F139 (≠ M120), G140 (≠ P121), G141 (≠ M122), E167 (≠ R145), R170 (vs. gap), S279 (≠ P244), K307 (vs. gap), P308 (vs. gap), A332 (= A292), T334 (= T294), A363 (= A318), A500 (= A443), H502 (≠ Y445), K532 (≠ R475), R562 (≠ K504), P567 (= P509), V568 (≠ Y510)
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
30% identity, 92% coverage: 35:535/543 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 (vs. gap), G321 (= G319), E322 (= E320), P323 (≠ T321), D342 (= D340), F343 (≠ G341), Y344 (≠ I342), Q346 (≠ A344), T347 (= T345), D428 (= D420), F440 (= F432), K449 (≠ V441), R454 (≠ N446)
- binding coenzyme a: N128 (≠ M122), W247 (≠ L255), K249 (≠ I257), K273 (≠ P274), L274 (≠ P275), Q300 (≠ T298), D452 (≠ G444), Y453 (= Y445), R483 (= R475), P517 (= P509)
Query Sequence
>WP_086509453.1 NCBI__GCF_002151265.1:WP_086509453.1
MNAPSAHADTFARDNLPPVHEWPELRLDGFDYPARLNAAVELCDRWLERGHGERVALIGN
GRRRSYRELAEWSNRLAHALVEELGVRPGNRVLIRSANNPAMVACWLAATKAGAVVVNTM
PMLRASELAQIVDKAEIALALCDTRLLEELETCAAESALLKRVVGFDGTANHDAELDRLA
LDKPTEFKAVATAADDVALLGFTSGTTGQPKATMHFHRDLLIIADGYAREVLQVSADDVF
VGSPPLAFTFGLGGLAIFPLRFGASAVLLEKATPPNMMEIIREHRATVVFTAPTAYRTML
ASLENGEELDSLRLAVSAGETLPAPIYHEWIEKTGKPILDGIGATEMLHIFISNHLDDHR
PACTGKPVAGYEAKVVDAEMNELPRGEVGRLAVRGPTGCRYLNDVRQLKYVRDGWNITGD
AFYQDEEDYFHFAARNDDMIVSAGYNIAGPEVEAALLAHEAVAECAVIGAPNGERGQIVE
AFVVLSPGVEPDAECVKRLQTFVKQRIAPYKYPRSVRFVEALPKTATGKVQRFRLRQEHY
PDD
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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