SitesBLAST
Comparing WP_043458035.1 NCBI__GCF_000430725.1:WP_043458035.1 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)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
43% identity, 88% coverage: 39:544/574 of query aligns to 33:542/562 of 8biqA
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
43% identity, 88% coverage: 39:544/574 of query aligns to 34:543/562 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 (= W256), G321 (= G325), E322 (= E326), P323 (= P327), D342 (= D346), F343 (≠ G347), Y344 (= Y348), Q346 (= Q350), T347 (= T351), D428 (= D429), F440 (= F441), K449 (= K450), R454 (= R455)
- binding coenzyme a: N128 (≠ L130), W247 (= W251), K249 (= K253), K273 (≠ R276), L274 (≠ F277), Q300 (≠ M303), D452 (= D453), Y453 (= Y454), R483 (= R484), P517 (= P518)
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
43% identity, 88% coverage: 39:544/574 of query aligns to 32:541/561 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 (= G325), E320 (= E326), P321 (= P327), D340 (= D346), F341 (≠ G347), Y342 (= Y348), G343 (= G349), Q344 (= Q350), T345 (= T351), D426 (= D429), F438 (= F441), K447 (= K450), R452 (= R455)
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
36% identity, 89% coverage: 41:548/574 of query aligns to 7:531/533 of 3eq6A
- active site: T185 (= T207), T328 (= T351), E329 (= E352), N431 (≠ K450), R436 (= R455), K521 (= K538)
- binding adenosine monophosphate: G302 (= G325), E303 (= E326), S304 (≠ P327), E323 (≠ D346), S324 (≠ G347), Y325 (= Y348), G326 (= G349), Q327 (= Q350), T328 (= T351), D410 (= D429), F422 (= F441), R425 (= R444), R436 (= R455)
- binding Butyryl Coenzyme A: W229 (= W251), F255 (= F277), I277 (≠ T299), V301 (≠ A324), S433 (= S452), G434 (≠ D453), Y435 (= Y454), P501 (= P518), Y502 (= Y519), Y504 (≠ R521), R506 (= R523)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
36% identity, 89% coverage: 41:548/574 of query aligns to 7:531/533 of 2wd9A
- active site: T185 (= T207), T328 (= T351), E329 (= E352), N431 (≠ K450), R436 (= R455), K521 (= K538)
- binding ibuprofen: I230 (≠ A252), L231 (≠ K253), G326 (= G349), Q327 (= Q350), T328 (= T351), R436 (= R455)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
36% identity, 89% coverage: 41:548/574 of query aligns to 7:531/533 of 2vzeA
- active site: T185 (= T207), T328 (= T351), E329 (= E352), N431 (≠ K450), R436 (= R455), K521 (= K538)
- binding adenosine monophosphate: W229 (= W251), G302 (= G325), E303 (= E326), S304 (≠ P327), E323 (≠ D346), Y325 (= Y348), G326 (= G349), Q327 (= Q350), T328 (= T351), D410 (= D429), F422 (= F441), R425 (= R444), R436 (= R455)
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
36% identity, 89% coverage: 41:548/574 of query aligns to 10:534/536 of 3c5eA
- active site: T188 (= T207), T331 (= T351), E332 (= E352), N434 (≠ K450), R439 (= R455), K524 (= K538)
- binding adenosine-5'-triphosphate: T188 (= T207), S189 (= S208), G190 (= G209), T191 (= T210), S192 (≠ T211), G305 (= G325), E306 (= E326), S307 (≠ P327), G329 (= G349), Q330 (= Q350), T331 (= T351), D413 (= D429), F425 (= F441), R428 (= R444), K524 (= K538)
- binding magnesium ion: M450 (= M466), H452 (= H468), V455 (= V471)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
36% identity, 89% coverage: 41:548/574 of query aligns to 11:535/537 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)
36% identity, 89% coverage: 41:548/574 of query aligns to 43:567/577 of Q08AH3
- Q139 (≠ L130) binding CoA
- 221:229 (vs. 207:215, 67% identical) binding ATP
- ESYGQT 359:364 (≠ DGYGQT 346:351) binding ATP
- T364 (= T351) binding substrate
- D446 (= D429) binding ATP
- R461 (= R444) binding ATP
- SGY 469:471 (≠ SDY 452:454) binding CoA
- R472 (= R455) binding substrate
- R501 (= R484) binding CoA
- S513 (vs. gap) to L: in dbSNP:rs1133607
- K532 (≠ R513) binding CoA
- YPR 540:542 (≠ RVR 521:523) binding CoA
- K557 (= K538) binding ATP
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
36% identity, 89% coverage: 41:548/574 of query aligns to 8:530/532 of 3gpcA
- active site: T186 (= T207), T327 (= T351), E328 (= E352), N430 (≠ K450), R435 (= R455), K520 (= K538)
- binding coenzyme a: G301 (= G325), E302 (= E326), S303 (≠ P327), E322 (≠ D346), Y324 (= Y348), G325 (= G349), Q326 (= Q350), T327 (= T351), D409 (= D429), F421 (= F441), R424 (= R444), T516 (= T534), K520 (= K538), Q522 (≠ R540)
- binding magnesium ion: H448 (= H468), V451 (= V471)
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
36% identity, 89% coverage: 41:548/574 of query aligns to 11:533/535 of 3dayA
- active site: T189 (= T207), T332 (= T351), E333 (= E352), N435 (≠ K450), R440 (= R455), K523 (= K538)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T207), S190 (= S208), G191 (= G209), T192 (= T210), S193 (≠ T211), K197 (= K215), G306 (= G325), E307 (= E326), S308 (≠ P327), Y329 (= Y348), G330 (= G349), Q331 (= Q350), T332 (= T351), D414 (= D429), F426 (= F441), R429 (= R444), K523 (= K538)
- binding magnesium ion: M451 (= M466), H453 (= H468), V456 (= V471)
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
29% identity, 90% coverage: 34:548/574 of query aligns to 71:621/630 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 (= G325), E392 (= E326), P393 (= P327), T416 (≠ G347), W417 (≠ Y348), W418 (≠ G349), Q419 (= Q350), T420 (= T351), D502 (= D429), R517 (= R444), K523 (= K450), R528 (= R455)
- binding magnesium ion: V539 (≠ M466), H541 (= H468)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
31% identity, 82% coverage: 74:545/574 of query aligns to 37:509/518 of 4wv3B
- active site: S175 (≠ T207), T320 (= T351), E321 (= E352), K418 (= K450), W423 (≠ R455), K502 (= K538)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ W251), T221 (≠ A252), F222 (≠ K253), A293 (= A324), S294 (≠ G325), E295 (= E326), A296 (≠ P327), G316 (= G347), I317 (≠ Y348), G318 (= G349), C319 (≠ Q350), T320 (= T351), D397 (= D429), H409 (≠ F441), R412 (= R444), K502 (= K538)
Q89WV5 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110) (see paper)
29% identity, 86% coverage: 54:547/574 of query aligns to 88:615/648 of Q89WV5
- G263 (= G209) mutation to I: Loss of activity.
- G266 (≠ S212) mutation to I: Great decrease in activity.
- K269 (= K215) mutation to G: Great decrease in activity.
- E414 (= E352) mutation to Q: Great decrease in activity.
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: 37:545/574 of query aligns to 3:514/518 of 6m2uA
- active site: S176 (≠ T207), T196 (≠ I235), T324 (= T351), E325 (= E352), K422 (= K450), Y427 (≠ R455), K507 (= K538)
- binding adenosine monophosphate: G298 (= G325), E299 (= E326), A300 (≠ P327), D319 (= D346), G320 (= G347), I321 (≠ Y348), G322 (= G349), T324 (= T351), D401 (= D429), R416 (= R444), K422 (= K450), Y427 (≠ R455)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ P262), A297 (= A324), G322 (= G349), S323 (≠ Q350), A328 (= A355)
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: 37:545/574 of query aligns to 3:514/518 of 6m2tA
- active site: S176 (≠ T207), T196 (≠ I235), T324 (= T351), E325 (= E352), K422 (= K450), Y427 (≠ R455), K507 (= K538)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ P262), G322 (= G349), S323 (≠ Q350), A328 (= A355)
- binding adenosine monophosphate: G298 (= G325), E299 (= E326), A300 (≠ P327), G320 (= G347), I321 (≠ Y348), S323 (≠ Q350), T324 (= T351), D401 (= D429), R416 (= R444), K422 (= K450), Y427 (≠ R455)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
30% identity, 89% coverage: 37:545/574 of query aligns to 4:515/518 of 4rm3A
- active site: S177 (≠ T207), T197 (≠ I235), T325 (= T351), E326 (= E352), K423 (= K450), Y428 (≠ R455), K508 (= K538)
- binding 2-furoic acid: A223 (= A261), Y224 (≠ P262), A298 (= A324), G323 (= G349), H329 (≠ A355), I330 (≠ Q356), K423 (= K450)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
30% identity, 89% coverage: 37:545/574 of query aligns to 3:514/516 of 4rm2A
- active site: S176 (≠ T207), T196 (≠ I235), T324 (= T351), E325 (= E352), K422 (= K450), Y427 (≠ R455), K507 (= K538)
- binding 2-fluorobenzoic acid: A216 (= A255), A222 (= A261), Y223 (≠ P262), P246 (vs. gap), T247 (vs. gap), V251 (= V285), F267 (≠ L294), G269 (≠ A296), A270 (≠ P297), G273 (≠ V300), M277 (≠ V304), A297 (= A324), G298 (= G325), I321 (≠ Y348), G322 (= G349), S323 (≠ Q350), H328 (≠ A355), K422 (= K450)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
30% identity, 89% coverage: 37:545/574 of query aligns to 3:514/519 of 4rlfB
- active site: S176 (≠ T207), T196 (≠ I235), T324 (= T351), E325 (= E352), K422 (= K450), Y427 (≠ R455), K507 (= K538)
- binding 2-methylbenzoic acid: A222 (= A261), Y223 (≠ P262), G298 (= G325), I321 (≠ Y348), G322 (= G349), S323 (≠ Q350), H328 (≠ A355)
- binding 4-methylbenzoic acid: A216 (= A255), P246 (vs. gap), P248 (vs. gap), G269 (≠ A296), A270 (≠ P297), G273 (≠ V300)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
30% identity, 89% coverage: 37:545/574 of query aligns to 3:514/518 of 4rmnA
- active site: S176 (≠ T207), T196 (≠ I235), T324 (= T351), E325 (= E352), K422 (= K450), Y427 (≠ R455), K507 (= K538)
- binding thiophene-2-carboxylic acid: A217 (≠ W256), F221 (= F260), Y223 (≠ P262), G269 (≠ A296), A270 (≠ P297), A297 (= A324), G298 (= G325), G322 (= G349), S323 (≠ Q350), H328 (≠ A355), I329 (≠ Q356), K422 (= K450), G425 (≠ D453)
Query Sequence
>WP_043458035.1 NCBI__GCF_000430725.1:WP_043458035.1
MDNTRATAARQAFLAARDQLLALRTDQVAAARDFRWPVLEQFNWALDHFDAMARDNDAPA
LWIVDEHGGELKRSFRQMSERSAQVANFLRRHGVKRGDRVLLMLGNEVALWELMLGAFKL
GAVVIPATALLTPDDLRDRLERGNVRHVVAGSALSAKFEGLADGCTRLCVGAAQPGWLDF
ALSQEESAHFEPDGPTAANDPLLLYFTSGTTSKPKLVLHTHQSYPVGHLSTMYWIGLQPG
DVHLNISSPGWAKHAWSCFFAPWNAGACVFIHNVARFSASALLGVLERHGVTTLCAPPTV
WRMVIQEDMAAWRGRLKLREVIGAGEPLNPEIIEQVREAWGLSLRDGYGQTETTAQVGNA
PGQPLKPGSMGRPLPGYQVALLDMDGNESTEGEVCLKLTPRPLGLMAGYEDSAEKTAEVM
RDGYYRTGDVAMRDAEGYLTFVGRADDVFKASDYRISPFELESVLMEHPAVTEVAVVPSP
DPVRLAVPKAFITLAQGREADAALALDVLGWARRQLAPYKRVRRIEFLTELPKTISGKLR
RVELRRLEAERRNQGVREAGEFFEEDFPGLKSEG
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