SitesBLAST
Comparing WP_011951516.1 NCBI__GCF_000016765.1:WP_011951516.1 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)
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
40% identity, 92% coverage: 36:550/560 of query aligns to 34:560/561 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 (= G317), E320 (= E318), P321 (= P319), D340 (= D338), F341 (≠ G339), Y342 (= Y340), G343 (= G341), Q344 (= Q342), T345 (= T343), D426 (= D417), F438 (≠ Y429), K447 (= K438), R452 (= R443)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
40% identity, 92% coverage: 36:550/560 of query aligns to 35:561/562 of 8biqA
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
40% identity, 92% coverage: 36:550/560 of query aligns to 36:562/562 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 (= G317), E322 (= E318), P323 (= P319), D342 (= D338), F343 (≠ G339), Y344 (= Y340), Q346 (= Q342), T347 (= T343), D428 (= D417), F440 (≠ Y429), K449 (= K438), R454 (= R443)
- binding coenzyme a: N128 (≠ M124), W247 (= W245), K249 (= K247), K273 (≠ A270), L274 (≠ F271), Q300 (≠ M297), D452 (= D441), Y453 (= Y442), R483 (= R472), P517 (= P506)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
32% identity, 89% coverage: 36:535/560 of query aligns to 11:535/537 of 3b7wA
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
32% identity, 89% coverage: 36:535/560 of query aligns to 10:534/536 of 3c5eA
- active site: T188 (= T201), T331 (= T343), E332 (= E344), N434 (≠ K438), R439 (= R443), K524 (= K525)
- binding adenosine-5'-triphosphate: T188 (= T201), S189 (= S202), G190 (= G203), T191 (= T204), S192 (≠ T205), G305 (= G317), E306 (= E318), S307 (≠ P319), G329 (= G341), Q330 (= Q342), T331 (= T343), D413 (= D417), F425 (≠ Y429), R428 (= R432), K524 (= K525)
- binding magnesium ion: M450 (≠ L454), H452 (= H456), V455 (= V459)
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
32% identity, 89% coverage: 36:535/560 of query aligns to 7:531/533 of 3eq6A
- active site: T185 (= T201), T328 (= T343), E329 (= E344), N431 (≠ K438), R436 (= R443), K521 (= K525)
- binding adenosine monophosphate: G302 (= G317), E303 (= E318), S304 (≠ P319), E323 (≠ D338), S324 (≠ G339), Y325 (= Y340), G326 (= G341), Q327 (= Q342), T328 (= T343), D410 (= D417), F422 (≠ Y429), R425 (= R432), R436 (= R443)
- binding Butyryl Coenzyme A: W229 (= W245), F255 (= F271), I277 (≠ T293), V301 (≠ A316), S433 (= S440), G434 (≠ D441), Y435 (= Y442), P501 (= P506), Y502 (= Y507), Y504 (≠ R509), R506 (= R511)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
32% identity, 89% coverage: 36:535/560 of query aligns to 7:531/533 of 2wd9A
- active site: T185 (= T201), T328 (= T343), E329 (= E344), N431 (≠ K438), R436 (= R443), K521 (= K525)
- binding ibuprofen: I230 (≠ A246), L231 (≠ K247), G326 (= G341), Q327 (= Q342), T328 (= T343), R436 (= R443)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
32% identity, 89% coverage: 36:535/560 of query aligns to 7:531/533 of 2vzeA
- active site: T185 (= T201), T328 (= T343), E329 (= E344), N431 (≠ K438), R436 (= R443), K521 (= K525)
- binding adenosine monophosphate: W229 (= W245), G302 (= G317), E303 (= E318), S304 (≠ P319), E323 (≠ D338), Y325 (= Y340), G326 (= G341), Q327 (= Q342), T328 (= T343), D410 (= D417), F422 (≠ Y429), R425 (= R432), R436 (= R443)
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, 89% coverage: 36:535/560 of query aligns to 43:567/577 of Q08AH3
- Q139 (≠ M124) binding CoA
- 221:229 (vs. 201:209, 67% identical) binding ATP
- ESYGQT 359:364 (≠ DGYGQT 338:343) binding ATP
- T364 (= T343) binding substrate
- D446 (= D417) binding ATP
- R461 (= R432) binding ATP
- SGY 469:471 (≠ SDY 440:442) binding CoA
- R472 (= R443) binding substrate
- R501 (= R472) binding CoA
- S513 (≠ P484) to L: in dbSNP:rs1133607
- K532 (≠ R501) binding CoA
- YPR 540:542 (≠ RIR 509:511) binding CoA
- K557 (= K525) binding ATP
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
31% identity, 89% coverage: 36:535/560 of query aligns to 11:533/535 of 3dayA
- active site: T189 (= T201), T332 (= T343), E333 (= E344), N435 (≠ K438), R440 (= R443), K523 (= K525)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T201), S190 (= S202), G191 (= G203), T192 (= T204), S193 (≠ T205), K197 (= K209), G306 (= G317), E307 (= E318), S308 (≠ P319), Y329 (= Y340), G330 (= G341), Q331 (= Q342), T332 (= T343), D414 (= D417), F426 (≠ Y429), R429 (= R432), K523 (= K525)
- binding magnesium ion: M451 (≠ L454), H453 (= H456), V456 (= V459)
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
31% identity, 89% coverage: 36:535/560 of query aligns to 8:530/532 of 3gpcA
- active site: T186 (= T201), T327 (= T343), E328 (= E344), N430 (≠ K438), R435 (= R443), K520 (= K525)
- binding coenzyme a: G301 (= G317), E302 (= E318), S303 (≠ P319), E322 (≠ D338), Y324 (= Y340), G325 (= G341), Q326 (= Q342), T327 (= T343), D409 (= D417), F421 (≠ Y429), R424 (= R432), T516 (= T521), K520 (= K525), Q522 (≠ R527)
- binding magnesium ion: H448 (= H456), V451 (= V459)
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
30% identity, 91% coverage: 29:537/560 of query aligns to 71:623/630 of 8rplB
- 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: G391 (= G317), E392 (= E318), P393 (= P319), T416 (≠ G339), W417 (≠ Y340), W418 (≠ G341), Q419 (= Q342), T420 (= T343), D502 (= D417), R517 (= R432), K523 (= K438), R528 (= R443)
- binding magnesium ion: V539 (≠ L454), H541 (= H456)
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)
30% identity, 89% coverage: 35:533/560 of query aligns to 6:515/518 of 6m2uA
- active site: S176 (≠ T201), T196 (≠ I229), T324 (= T343), E325 (= E344), K422 (= K438), Y427 (≠ R443), K507 (= K525)
- binding adenosine monophosphate: G298 (= G317), E299 (= E318), A300 (≠ P319), D319 (= D338), G320 (= G339), I321 (≠ Y340), G322 (= G341), T324 (= T343), D401 (= D417), R416 (= R432), K422 (= K438), Y427 (≠ R443)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ P256), A297 (= A316), G322 (= G341), S323 (≠ Q342), A328 (= A347)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
30% identity, 89% coverage: 35:533/560 of query aligns to 6:515/518 of 6m2tA
- active site: S176 (≠ T201), T196 (≠ I229), T324 (= T343), E325 (= E344), K422 (= K438), Y427 (≠ R443), K507 (= K525)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ P256), G322 (= G341), S323 (≠ Q342), A328 (= A347)
- binding adenosine monophosphate: G298 (= G317), E299 (= E318), A300 (≠ P319), G320 (= G339), I321 (≠ Y340), S323 (≠ Q342), T324 (= T343), D401 (= D417), R416 (= R432), K422 (= K438), Y427 (≠ R443)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
30% identity, 89% coverage: 35:533/560 of query aligns to 6:515/519 of 4rlfB
- active site: S176 (≠ T201), T196 (≠ I229), T324 (= T343), E325 (= E344), K422 (= K438), Y427 (≠ R443), K507 (= K525)
- binding 2-methylbenzoic acid: A222 (= A255), Y223 (≠ P256), G298 (= G317), I321 (≠ Y340), G322 (= G341), S323 (≠ Q342), H328 (vs. gap)
- binding 4-methylbenzoic acid: A216 (= A249), P246 (= P269), P248 (≠ F271), G269 (≠ A290), A270 (≠ P291), G273 (≠ V294)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
30% identity, 89% coverage: 35:533/560 of query aligns to 7:516/518 of 4rm3A
- active site: S177 (≠ T201), T197 (≠ I229), T325 (= T343), E326 (= E344), K423 (= K438), Y428 (≠ R443), K508 (= K525)
- binding 2-furoic acid: A223 (= A255), Y224 (≠ P256), A298 (= A316), G323 (= G341), H329 (vs. gap), I330 (≠ A347), K423 (= K438)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
30% identity, 89% coverage: 35:533/560 of query aligns to 6:515/516 of 4rm2A
- active site: S176 (≠ T201), T196 (≠ I229), T324 (= T343), E325 (= E344), K422 (= K438), Y427 (≠ R443), K507 (= K525)
- binding 2-fluorobenzoic acid: A216 (= A249), A222 (= A255), Y223 (≠ P256), P246 (= P269), T247 (≠ A270), V251 (≠ R274), F267 (= F288), G269 (≠ A290), A270 (≠ P291), G273 (≠ V294), M277 (≠ L298), A297 (= A316), G298 (= G317), I321 (≠ Y340), G322 (= G341), S323 (≠ Q342), H328 (vs. gap), K422 (= K438)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
30% identity, 89% coverage: 35:533/560 of query aligns to 6:515/518 of 4rmnA
- active site: S176 (≠ T201), T196 (≠ I229), T324 (= T343), E325 (= E344), K422 (= K438), Y427 (≠ R443), K507 (= K525)
- binding thiophene-2-carboxylic acid: A217 (≠ W250), F221 (≠ Y254), Y223 (≠ P256), G269 (≠ A290), A270 (≠ P291), A297 (= A316), G298 (= G317), G322 (= G341), S323 (≠ Q342), H328 (vs. gap), I329 (≠ A347), K422 (= K438), G425 (≠ D441)
4zjzA Crystal structure of a benzoate coenzyme a ligase with benzoyl-amp (see paper)
30% identity, 89% coverage: 35:533/560 of query aligns to 6:515/517 of 4zjzA
- active site: S176 (≠ T201), T196 (≠ I229), T324 (= T343), E325 (= E344), K422 (= K438), Y427 (≠ R443), K507 (= K525)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: A222 (= A255), Y223 (≠ P256), A297 (= A316), G298 (= G317), E299 (= E318), A300 (≠ P319), G320 (= G339), I321 (≠ Y340), G322 (= G341), S323 (≠ Q342), T324 (= T343), H328 (vs. gap), I329 (≠ A347), D401 (= D417), R416 (= R432), K422 (= K438), Y427 (≠ R443)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
28% identity, 84% coverage: 65:532/560 of query aligns to 34:509/518 of 4wv3B
- active site: S175 (≠ T201), T320 (= T343), E321 (= E344), K418 (= K438), W423 (≠ R443), K502 (= K525)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ W245), T221 (≠ A246), F222 (≠ K247), A293 (= A316), S294 (≠ G317), E295 (= E318), A296 (≠ P319), G316 (= G339), I317 (≠ Y340), G318 (= G341), C319 (≠ Q342), T320 (= T343), D397 (= D417), H409 (≠ Y429), R412 (= R432), K502 (= K525)
Query Sequence
>WP_011951516.1 NCBI__GCF_000016765.1:WP_011951516.1
MLLNGDRLQAARDFLIRHRTDHDAAVAGFAWPRFEQFNFAFDWFDRIAERSDAIALSIAS
PRGLRAWSYRDLSLGSNRVAHFLRRHGIGPGDRLLIALGNRIELWETQLAAMKAGCVMVP
CTVMLGAAELRERMARSGARAIVADDSIAERLGTPDKGWIGFNVDAPRPGWIDYGAAYGE
PAGFAPDQPTRGTDPLLIYFTSGTTAQPKMVTHSHVSYPVGHLSTLYWIGLKPGDTHLNI
SSPGWAKHAWSSFYAPWLAEASILTIDQPAFDARFVLDQIRDRAVDCFCAPPTVWRMLLQ
ERIEQWPVRLREAVSAGEPLNPHVVERVREVWGIDVRDGYGQTETTAQIGNTPGQPLVAG
AMGRPLPGFRIELDGAADHGEIILHAGDMAAGVMLGLQAEAGSAVLPPSGGIHRTGDIAS
AAPDGTLTYIGRADDVFKSSDYRISPFEIESVLLEHPAVAESAVIPSPEPTRLAVPKAII
VLAPGHAPSAETAAEIFAHSRARLAPYKRIRRLEFGELPKTVSGKTRRAELREREDGGRS
EGEYREEDFATTAKSGSRSG
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