SitesBLAST
Comparing WP_011880690.1 NCBI__GCF_000016205.1:WP_011880690.1 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)
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
40% identity, 95% coverage: 1:541/570 of query aligns to 1:543/562 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 (= W251), G321 (= G318), E322 (= E319), P323 (= P320), D342 (= D339), F343 (≠ G340), Y344 (= Y341), Q346 (= Q343), T347 (= T344), D428 (= D427), F440 (≠ Y439), K449 (= K448), R454 (= R453)
- binding coenzyme a: N128 (≠ Q124), W247 (= W246), K249 (= K248), K273 (≠ R271), L274 (≠ F272), Q300 (≠ M298), D452 (= D451), Y453 (= Y452), R483 (= R482), P517 (= P516)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
40% identity, 95% coverage: 2:541/570 of query aligns to 1:542/562 of 8biqA
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
41% identity, 89% coverage: 32:541/570 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 (= G318), E320 (= E319), P321 (= P320), D340 (= D339), F341 (≠ G340), Y342 (= Y341), G343 (= G342), Q344 (= Q343), T345 (= T344), D426 (= D427), F438 (≠ Y439), K447 (= K448), R452 (= R453)
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: 35:545/570 of query aligns to 8:531/533 of 3eq6A
- active site: T185 (= T202), T328 (= T344), E329 (= E345), N431 (≠ K448), R436 (= R453), K521 (= K535)
- binding adenosine monophosphate: G302 (= G318), E303 (= E319), S304 (≠ P320), E323 (≠ D339), S324 (≠ G340), Y325 (= Y341), G326 (= G342), Q327 (= Q343), T328 (= T344), D410 (= D427), F422 (≠ Y439), R425 (= R442), R436 (= R453)
- binding Butyryl Coenzyme A: W229 (= W246), F255 (= F272), I277 (≠ T294), V301 (≠ A317), S433 (= S450), G434 (≠ D451), Y435 (= Y452), P501 (= P516), Y502 (= Y517), Y504 (≠ R519), R506 (= R521)
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: 35:545/570 of query aligns to 8:531/533 of 2wd9A
- active site: T185 (= T202), T328 (= T344), E329 (= E345), N431 (≠ K448), R436 (= R453), K521 (= K535)
- binding ibuprofen: I230 (≠ A247), L231 (≠ K248), G326 (= G342), Q327 (= Q343), T328 (= T344), R436 (= R453)
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: 35:545/570 of query aligns to 8:531/533 of 2vzeA
- active site: T185 (= T202), T328 (= T344), E329 (= E345), N431 (≠ K448), R436 (= R453), K521 (= K535)
- binding adenosine monophosphate: W229 (= W246), G302 (= G318), E303 (= E319), S304 (≠ P320), E323 (≠ D339), Y325 (= Y341), G326 (= G342), Q327 (= Q343), T328 (= T344), D410 (= D427), F422 (≠ Y439), R425 (= R442), R436 (= R453)
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: 35:545/570 of query aligns to 11:534/536 of 3c5eA
- active site: T188 (= T202), T331 (= T344), E332 (= E345), N434 (≠ K448), R439 (= R453), K524 (= K535)
- binding adenosine-5'-triphosphate: T188 (= T202), S189 (= S203), G190 (= G204), T191 (= T205), S192 (≠ T206), G305 (= G318), E306 (= E319), S307 (≠ P320), G329 (= G342), Q330 (= Q343), T331 (= T344), D413 (= D427), F425 (≠ Y439), R428 (= R442), K524 (= K535)
- binding magnesium ion: M450 (≠ I464), H452 (= H466), V455 (≠ I469)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
35% identity, 90% coverage: 35:545/570 of query aligns to 12:535/537 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)
35% identity, 91% coverage: 35:555/570 of query aligns to 44:577/577 of Q08AH3
- Q139 (= Q124) binding CoA
- 221:229 (vs. 202:210, 67% identical) binding ATP
- ESYGQT 359:364 (≠ DGYGQT 339:344) binding ATP
- T364 (= T344) binding substrate
- D446 (= D427) binding ATP
- R461 (= R442) binding ATP
- SGY 469:471 (≠ SDY 450:452) binding CoA
- R472 (= R453) binding substrate
- R501 (= R482) binding CoA
- S513 (≠ D494) to L: in dbSNP:rs1133607
- K532 (≠ R511) binding CoA
- YPR 540:542 (≠ RIR 519:521) binding CoA
- K557 (= K535) binding ATP
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: 35:545/570 of query aligns to 9:530/532 of 3gpcA
- active site: T186 (= T202), T327 (= T344), E328 (= E345), N430 (≠ K448), R435 (= R453), K520 (= K535)
- binding coenzyme a: G301 (= G318), E302 (= E319), S303 (≠ P320), E322 (≠ D339), Y324 (= Y341), G325 (= G342), Q326 (= Q343), T327 (= T344), D409 (= D427), F421 (≠ Y439), R424 (= R442), T516 (= T531), K520 (= K535), Q522 (≠ R537)
- binding magnesium ion: H448 (= H466), V451 (≠ I469)
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: 35:545/570 of query aligns to 12:533/535 of 3dayA
- active site: T189 (= T202), T332 (= T344), E333 (= E345), N435 (≠ K448), R440 (= R453), K523 (= K535)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T202), S190 (= S203), G191 (= G204), T192 (= T205), S193 (≠ T206), K197 (= K210), G306 (= G318), E307 (= E319), S308 (≠ P320), Y329 (= Y341), G330 (= G342), Q331 (= Q343), T332 (= T344), D414 (= D427), F426 (≠ Y439), R429 (= R442), K523 (= K535)
- binding magnesium ion: M451 (≠ I464), H453 (= H466), V456 (≠ I469)
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
30% identity, 91% coverage: 27:546/570 of query aligns to 71:622/630 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 (= G318), E392 (= E319), P393 (= P320), T416 (≠ G340), W417 (≠ Y341), W418 (≠ G342), Q419 (= Q343), T420 (= T344), D502 (= D427), R517 (= R442), K523 (= K448), R528 (= R453)
- binding magnesium ion: V539 (≠ I464), H541 (= H466)
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, 83% coverage: 68:542/570 of query aligns to 35:514/518 of 6m2uA
- active site: S176 (≠ T202), T196 (≠ V221), T324 (= T344), E325 (= E345), K422 (= K448), Y427 (≠ R453), K507 (= K535)
- binding adenosine monophosphate: G298 (= G318), E299 (= E319), A300 (≠ P320), D319 (= D339), G320 (= G340), I321 (≠ Y341), G322 (= G342), T324 (= T344), D401 (= D427), R416 (= R442), K422 (= K448), Y427 (≠ R453)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ K248), A297 (= A317), G322 (= G342), S323 (≠ Q343), A328 (≠ T347)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
32% identity, 83% coverage: 68:542/570 of query aligns to 35:514/518 of 6m2tA
- active site: S176 (≠ T202), T196 (≠ V221), T324 (= T344), E325 (= E345), K422 (= K448), Y427 (≠ R453), K507 (= K535)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ K248), G322 (= G342), S323 (≠ Q343), A328 (≠ T347)
- binding adenosine monophosphate: G298 (= G318), E299 (= E319), A300 (≠ P320), G320 (= G340), I321 (≠ Y341), S323 (≠ Q343), T324 (= T344), D401 (= D427), R416 (= R442), K422 (= K448), Y427 (≠ R453)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
32% identity, 83% coverage: 68:542/570 of query aligns to 35:514/516 of 4rm2A
- active site: S176 (≠ T202), T196 (≠ V221), T324 (= T344), E325 (= E345), K422 (= K448), Y427 (≠ R453), K507 (= K535)
- binding 2-fluorobenzoic acid: A216 (≠ I241), A222 (= A247), Y223 (≠ K248), P246 (≠ F272), T247 (≠ E273), V251 (= V277), F267 (≠ L289), G269 (≠ A291), A270 (≠ P292), G273 (≠ V295), M277 (≠ L299), A297 (= A317), G298 (= G318), I321 (≠ Y341), G322 (= G342), S323 (≠ Q343), H328 (vs. gap), K422 (= K448)
4zjzA Crystal structure of a benzoate coenzyme a ligase with benzoyl-amp (see paper)
32% identity, 83% coverage: 68:542/570 of query aligns to 35:514/517 of 4zjzA
- active site: S176 (≠ T202), T196 (≠ V221), T324 (= T344), E325 (= E345), K422 (= K448), Y427 (≠ R453), K507 (= K535)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: A222 (= A247), Y223 (≠ K248), A297 (= A317), G298 (= G318), E299 (= E319), A300 (≠ P320), G320 (= G340), I321 (≠ Y341), G322 (= G342), S323 (≠ Q343), T324 (= T344), H328 (vs. gap), I329 (≠ C348), D401 (= D427), R416 (= R442), K422 (= K448), Y427 (≠ R453)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
32% identity, 83% coverage: 68:542/570 of query aligns to 35:514/518 of 4rmnA
- active site: S176 (≠ T202), T196 (≠ V221), T324 (= T344), E325 (= E345), K422 (= K448), Y427 (≠ R453), K507 (= K535)
- binding thiophene-2-carboxylic acid: A217 (≠ S242), F221 (≠ W246), Y223 (≠ K248), G269 (≠ A291), A270 (≠ P292), A297 (= A317), G298 (= G318), G322 (= G342), S323 (≠ Q343), H328 (vs. gap), I329 (≠ C348), K422 (= K448), G425 (≠ D451)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
32% identity, 83% coverage: 68:542/570 of query aligns to 36:515/518 of 4rm3A
- active site: S177 (≠ T202), T197 (≠ V221), T325 (= T344), E326 (= E345), K423 (= K448), Y428 (≠ R453), K508 (= K535)
- binding 2-furoic acid: A223 (= A247), Y224 (≠ K248), A298 (= A317), G323 (= G342), H329 (vs. gap), I330 (≠ C348), K423 (= K448)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
32% identity, 83% coverage: 68:542/570 of query aligns to 35:514/519 of 4rlfB
- active site: S176 (≠ T202), T196 (≠ V221), T324 (= T344), E325 (= E345), K422 (= K448), Y427 (≠ R453), K507 (= K535)
- binding 2-methylbenzoic acid: A222 (= A247), Y223 (≠ K248), G298 (= G318), I321 (≠ Y341), G322 (= G342), S323 (≠ Q343), H328 (vs. gap)
- binding 4-methylbenzoic acid: A216 (≠ I241), P246 (≠ F272), P248 (= P274), G269 (≠ A291), A270 (≠ P292), G273 (≠ V295)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
30% identity, 83% coverage: 68:542/570 of query aligns to 37:509/518 of 4wv3B
- active site: S175 (≠ T202), T320 (= T344), E321 (= E345), K418 (= K448), W423 (≠ R453), K502 (= K535)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ W246), T221 (≠ A247), F222 (≠ K248), A293 (= A317), S294 (≠ G318), E295 (= E319), A296 (≠ P320), G316 (= G340), I317 (≠ Y341), G318 (= G342), C319 (≠ Q343), T320 (= T344), D397 (= D427), H409 (≠ Y439), R412 (= R442), K502 (= K535)
Query Sequence
>WP_011880690.1 NCBI__GCF_000016205.1:WP_011880690.1
MTVQAFLDARDFLLRHRTDYETAYRDFEWPVLDAFNWALDYFDPMARGNDAPALWIVDAA
TGTGDPYSFAQMSERSSRIANWLRGIGVVRGDRILLMLPNRVELWDAMLAAMKLGAVVLP
ATTQLSADDVRDRVQIGGATYAIVDEHETAKFEQAGLGLKRKIVAGAPRDGWLAMNDGYA
ASAAFEPDAVTRSNEAMLLYFTSGTTSKPKLVEHTHRTYPVGHLSTMYWIGLQPGDIHWN
ISSPGWAKHAWSCFFAPWNAQACVFVFNYARFEPKAVLDALVKYRVTTLCAPPTVWRMLV
QQPLATFDVQLREIVGAGEPLNPEIIERVKKAWGITIRDGYGQTETTCLIGNTPGQPVVA
GSMGRPLPGYRIALLDPDGAPVGEGEVALPLGGGTGAMRPVGLMNGYANNPDATAYAMRD
GHYRTSDIAMRGDDGYYVYVGRADDVFKSSDYRLSPFELESVLIEHPAIAEAAVVPSPDP
VRLSVPKTFITLRDGFEESPTLALEIFRFSREKLAPYKRIRRLQFAELPKTISGKIRRVE
LRRREIERGDDATARMPGEYWEEDFAAELK
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