SitesBLAST
Comparing WP_050464459.1 NCBI__GCF_001189915.1:WP_050464459.1 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
42% identity, 90% coverage: 34:536/557 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 (= W251), G321 (= G318), E322 (= E319), P323 (= P320), D342 (= D339), F343 (≠ G340), Y344 (≠ F341), Q346 (= Q343), T347 (= T344), D428 (= D422), F440 (≠ Y434), K449 (= K443), R454 (= R448)
- binding coenzyme a: N128 (≠ L125), W247 (= W246), K249 (= K248), K273 (≠ R271), L274 (≠ F272), Q300 (≠ M298), D452 (= D446), Y453 (= Y447), R483 (= R477), P517 (= P511)
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
42% identity, 90% coverage: 34:536/557 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 (≠ F341), G343 (= G342), Q344 (= Q343), T345 (= T344), D426 (= D422), F438 (≠ Y434), K447 (= K443), R452 (= R448)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
42% identity, 90% coverage: 34:536/557 of query aligns to 33:542/562 of 8biqA
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)
34% identity, 92% coverage: 36:546/557 of query aligns to 43:573/577 of Q08AH3
- Q139 (≠ L125) binding CoA
- 221:229 (vs. 202:210, 67% identical) binding ATP
- ESYGQT 359:364 (≠ DGFGQT 339:344) binding ATP
- T364 (= T344) binding substrate
- D446 (= D422) binding ATP
- R461 (= R437) binding ATP
- SGY 469:471 (≠ SDY 445:447) binding CoA
- R472 (= R448) binding substrate
- R501 (= R477) binding CoA
- S513 (≠ E489) to L: in dbSNP:rs1133607
- K532 (≠ R506) binding CoA
- YPR 540:542 (≠ RVR 514:516) binding CoA
- K557 (= K530) binding ATP
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
34% identity, 91% coverage: 36:542/557 of query aligns to 7:533/533 of 3eq6A
- active site: T185 (= T202), T328 (= T344), E329 (= E345), N431 (≠ K443), R436 (= R448), K521 (= K530)
- binding adenosine monophosphate: G302 (= G318), E303 (= E319), S304 (≠ P320), E323 (≠ D339), S324 (≠ G340), Y325 (≠ F341), G326 (= G342), Q327 (= Q343), T328 (= T344), D410 (= D422), F422 (≠ Y434), R425 (= R437), R436 (= R448)
- binding Butyryl Coenzyme A: W229 (= W246), F255 (= F272), I277 (≠ T294), V301 (≠ A317), S433 (= S445), G434 (≠ D446), Y435 (= Y447), P501 (= P511), Y502 (= Y512), Y504 (≠ R514), R506 (= R516)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
34% identity, 91% coverage: 36:542/557 of query aligns to 7:533/533 of 2wd9A
- active site: T185 (= T202), T328 (= T344), E329 (= E345), N431 (≠ K443), R436 (= R448), K521 (= K530)
- binding ibuprofen: I230 (≠ A247), L231 (≠ K248), G326 (= G342), Q327 (= Q343), T328 (= T344), R436 (= R448)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
34% identity, 91% coverage: 36:542/557 of query aligns to 7:533/533 of 2vzeA
- active site: T185 (= T202), T328 (= T344), E329 (= E345), N431 (≠ K443), R436 (= R448), K521 (= K530)
- binding adenosine monophosphate: W229 (= W246), G302 (= G318), E303 (= E319), S304 (≠ P320), E323 (≠ D339), Y325 (≠ F341), G326 (= G342), Q327 (= Q343), T328 (= T344), D410 (= D422), F422 (≠ Y434), R425 (= R437), R436 (= R448)
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
34% identity, 91% coverage: 36:542/557 of query aligns to 10:536/536 of 3c5eA
- active site: T188 (= T202), T331 (= T344), E332 (= E345), N434 (≠ K443), R439 (= R448), K524 (= K530)
- 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 (= D422), F425 (≠ Y434), R428 (= R437), K524 (= K530)
- binding magnesium ion: M450 (≠ V459), H452 (= H461), V455 (= V464)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
34% identity, 91% coverage: 36:542/557 of query aligns to 11:537/537 of 3b7wA
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
34% identity, 91% coverage: 36:542/557 of query aligns to 11:535/535 of 3dayA
- active site: T189 (= T202), T332 (= T344), E333 (= E345), N435 (≠ K443), R440 (= R448), K523 (= K530)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T202), S190 (= S203), G191 (= G204), T192 (= T205), S193 (≠ T206), K197 (= K210), G306 (= G318), E307 (= E319), S308 (≠ P320), Y329 (≠ F341), G330 (= G342), Q331 (= Q343), T332 (= T344), D414 (= D422), F426 (≠ Y434), R429 (= R437), K523 (= K530)
- binding magnesium ion: M451 (≠ V459), H453 (= H461), V456 (= V464)
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
33% identity, 91% coverage: 36:542/557 of query aligns to 8:532/532 of 3gpcA
- active site: T186 (= T202), T327 (= T344), E328 (= E345), N430 (≠ K443), R435 (= R448), K520 (= K530)
- binding coenzyme a: G301 (= G318), E302 (= E319), S303 (≠ P320), E322 (≠ D339), Y324 (≠ F341), G325 (= G342), Q326 (= Q343), T327 (= T344), D409 (= D422), F421 (≠ Y434), R424 (= R437), T516 (= T526), K520 (= K530), Q522 (≠ R532)
- binding magnesium ion: H448 (= H461), V451 (= V464)
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)
31% identity, 90% coverage: 46:549/557 of query aligns to 85:625/648 of Q89WV5
- G263 (= G204) mutation to I: Loss of activity.
- G266 (≠ S207) mutation to I: Great decrease in activity.
- K269 (= K210) mutation to G: Great decrease in activity.
- E414 (= E345) 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)
31% identity, 85% coverage: 66:537/557 of query aligns to 32:514/518 of 6m2uA
- active site: S176 (≠ T202), T196 (≠ I221), T324 (= T344), E325 (= E345), K422 (= K443), Y427 (≠ R448), K507 (= K530)
- binding adenosine monophosphate: G298 (= G318), E299 (= E319), A300 (≠ P320), D319 (= D339), G320 (= G340), I321 (≠ F341), G322 (= G342), T324 (= T344), D401 (= D422), R416 (= R437), K422 (= K443), Y427 (≠ R448)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ K248), A297 (= A317), G322 (= G342), S323 (≠ Q343), A328 (= A348)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
31% identity, 85% coverage: 66:537/557 of query aligns to 32:514/518 of 6m2tA
- active site: S176 (≠ T202), T196 (≠ I221), T324 (= T344), E325 (= E345), K422 (= K443), Y427 (≠ R448), K507 (= K530)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ K248), G322 (= G342), S323 (≠ Q343), A328 (= A348)
- binding adenosine monophosphate: G298 (= G318), E299 (= E319), A300 (≠ P320), G320 (= G340), I321 (≠ F341), S323 (≠ Q343), T324 (= T344), D401 (= D422), R416 (= R437), K422 (= K443), Y427 (≠ R448)
8w0dA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with an isopropyl amp ester inhibitor
29% identity, 92% coverage: 36:549/557 of query aligns to 86:643/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G318), E399 (= E319), P400 (= P320), T423 (≠ G340), Y424 (≠ F341), W425 (≠ G342), Q426 (= Q343), T427 (= T344), D513 (= D422), I525 (≠ Y434), R528 (= R437), R539 (= R448)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
29% identity, 92% coverage: 36:549/557 of query aligns to 86:643/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G318), E399 (= E319), P400 (= P320), T423 (≠ G340), Y424 (≠ F341), Q426 (= Q343), T427 (= T344), D513 (= D422), I525 (≠ Y434), R528 (= R437), R539 (= R448)
- binding coenzyme a: F175 (≠ T123), R203 (vs. gap), R206 (≠ Q146), G316 (≠ S242), H538 (≠ Y447), R599 (= R506), F605 (≠ Y512)
8w0cA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopentyl ester amp inhibitor
29% identity, 92% coverage: 36:549/557 of query aligns to 87:644/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G318), E400 (= E319), P401 (= P320), T424 (≠ G340), Y425 (≠ F341), W426 (≠ G342), Q427 (= Q343), T428 (= T344), D514 (= D422), R529 (= R437), R540 (= R448)
8w0bA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopropyl amp ester inhibitor
29% identity, 92% coverage: 36:549/557 of query aligns to 87:644/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ A317), G399 (= G318), E400 (= E319), P401 (= P320), T424 (≠ G340), Y425 (≠ F341), W426 (≠ G342), Q427 (= Q343), T428 (= T344), D514 (= D422), I526 (≠ Y434), R529 (= R437), R540 (= R448)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
31% identity, 85% coverage: 66:537/557 of query aligns to 32:514/516 of 4rm2A
- active site: S176 (≠ T202), T196 (≠ I221), T324 (= T344), E325 (= E345), K422 (= K443), Y427 (≠ R448), K507 (= K530)
- binding 2-fluorobenzoic acid: A216 (≠ I241), A222 (= A247), Y223 (≠ K248), P246 (≠ F272), T247 (≠ N273), V251 (vs. gap), F267 (≠ L289), G269 (≠ A291), A270 (≠ P292), G273 (≠ V295), M277 (= M299), A297 (= A317), G298 (= G318), I321 (≠ F341), G322 (= G342), S323 (≠ Q343), H328 (≠ A348), K422 (= K443)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
31% identity, 85% coverage: 66:537/557 of query aligns to 32:514/519 of 4rlfB
- active site: S176 (≠ T202), T196 (≠ I221), T324 (= T344), E325 (= E345), K422 (= K443), Y427 (≠ R448), K507 (= K530)
- binding 2-methylbenzoic acid: A222 (= A247), Y223 (≠ K248), G298 (= G318), I321 (≠ F341), G322 (= G342), S323 (≠ Q343), H328 (≠ A348)
- binding 4-methylbenzoic acid: A216 (≠ I241), P246 (≠ F272), P248 (≠ A274), G269 (≠ A291), A270 (≠ P292), G273 (≠ V295)
Query Sequence
>WP_050464459.1 NCBI__GCF_001189915.1:WP_050464459.1
MTDKYRSFIAARDFLQLHRNDYDTAYRDYRAPVLPEFNWALDFFDVQAKGNTAPALWVVD
ENGKESKISFADMAQRSSQVANYLRSLGVKRGERLLLMLPNRVELWEIMLACIKLGAVIV
PTTMLVSGDDLLDRMERGAIRHVVAQTTELEKFAALGDGFTRIAVGGATPGWHAFEESSF
AATGFSPDARTLATDPLLLYFTSGTTSKPKLVLHSHASYTIGHLSTMYWIGLKAGDIHWN
ISSPGWAKHAWSCFFAPWNAGAAVFVYNYERFNARKSLEVIARCGVTSLCAPPTVWRMMI
QEELSKYKLPLRELVGAGEPLNPEVIEQVERAWGIRIRDGFGQTETTAQIGNTPGQKLKP
GSMGRPLPGYRVALLDPDDQPALEGEISLDLQTRPVGLMIGYEGDAEKNADVMSSGHYHT
GDTASRDADGYYFYVGRNDDVFKSSDYRISPFELESVMVEHEAVLEAAIVPSPDDLRLYV
PKAFITLREGFTPDNALAQSIFAFARARLAPYKRVRIIEFSDLPKTISGKIRRVELRRQE
QKRSGEIGNAMEFREEV
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