SitesBLAST
Comparing WP_011385246.1 NCBI__GCF_000009985.1:WP_011385246.1 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)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
52% identity, 93% coverage: 33:522/528 of query aligns to 22:515/518 of 4rm3A
- active site: S177 (= S184), T197 (= T204), T325 (= T329), E326 (= E330), K423 (= K427), Y428 (≠ W432), K508 (= K515)
- binding 2-furoic acid: A223 (= A230), Y224 (= Y231), A298 (= A302), G323 (= G327), H329 (= H333), I330 (= I334), K423 (= K427)
4zjzA Crystal structure of a benzoate coenzyme a ligase with benzoyl-amp (see paper)
52% identity, 93% coverage: 33:522/528 of query aligns to 21:514/517 of 4zjzA
- active site: S176 (= S184), T196 (= T204), T324 (= T329), E325 (= E330), K422 (= K427), Y427 (≠ W432), K507 (= K515)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: A222 (= A230), Y223 (= Y231), A297 (= A302), G298 (= G303), E299 (= E304), A300 (= A305), G320 (= G325), I321 (≠ L326), G322 (= G327), S323 (= S328), T324 (= T329), H328 (= H333), I329 (= I334), D401 (= D406), R416 (= R421), K422 (= K427), Y427 (≠ W432)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
52% identity, 93% coverage: 33:522/528 of query aligns to 21:514/516 of 4rm2A
- active site: S176 (= S184), T196 (= T204), T324 (= T329), E325 (= E330), K422 (= K427), Y427 (≠ W432), K507 (= K515)
- binding 2-fluorobenzoic acid: A216 (= A224), A222 (= A230), Y223 (= Y231), P246 (= P254), T247 (= T255), V251 (= V259), F267 (= F271), G269 (= G273), A270 (≠ V274), G273 (≠ L277), M277 (≠ I281), A297 (= A302), G298 (= G303), I321 (≠ L326), G322 (= G327), S323 (= S328), H328 (= H333), K422 (= K427)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
52% identity, 93% coverage: 33:522/528 of query aligns to 21:514/518 of 4rmnA
- active site: S176 (= S184), T196 (= T204), T324 (= T329), E325 (= E330), K422 (= K427), Y427 (≠ W432), K507 (= K515)
- binding thiophene-2-carboxylic acid: A217 (= A225), F221 (= F229), Y223 (= Y231), G269 (= G273), A270 (≠ V274), A297 (= A302), G298 (= G303), G322 (= G327), S323 (= S328), H328 (= H333), I329 (= I334), K422 (= K427), G425 (= G430)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
52% identity, 93% coverage: 33:522/528 of query aligns to 21:514/519 of 4rlfB
- active site: S176 (= S184), T196 (= T204), T324 (= T329), E325 (= E330), K422 (= K427), Y427 (≠ W432), K507 (= K515)
- binding 2-methylbenzoic acid: A222 (= A230), Y223 (= Y231), G298 (= G303), I321 (≠ L326), G322 (= G327), S323 (= S328), H328 (= H333)
- binding 4-methylbenzoic acid: A216 (= A224), P246 (= P254), P248 (= P256), G269 (= G273), A270 (≠ V274), G273 (≠ L277)
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)
51% identity, 93% coverage: 33:522/528 of query aligns to 21:514/518 of 6m2uA
- active site: S176 (= S184), T196 (= T204), T324 (= T329), E325 (= E330), K422 (= K427), Y427 (≠ W432), K507 (= K515)
- binding adenosine monophosphate: G298 (= G303), E299 (= E304), A300 (= A305), D319 (= D324), G320 (= G325), I321 (≠ L326), G322 (= G327), T324 (= T329), D401 (= D406), R416 (= R421), K422 (= K427), Y427 (≠ W432)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (= Y231), A297 (= A302), G322 (= G327), S323 (= S328), A328 (≠ H333)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
51% identity, 93% coverage: 33:522/528 of query aligns to 21:514/518 of 6m2tA
- active site: S176 (= S184), T196 (= T204), T324 (= T329), E325 (= E330), K422 (= K427), Y427 (≠ W432), K507 (= K515)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (= Y231), G322 (= G327), S323 (= S328), A328 (≠ H333)
- binding adenosine monophosphate: G298 (= G303), E299 (= E304), A300 (= A305), G320 (= G325), I321 (≠ L326), S323 (= S328), T324 (= T329), D401 (= D406), R416 (= R421), K422 (= K427), Y427 (≠ W432)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
46% identity, 97% coverage: 11:524/528 of query aligns to 3:511/518 of 4wv3B
- active site: S175 (= S184), T320 (= T329), E321 (= E330), K418 (= K427), W423 (= W432), K502 (= K515)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (= F229), T221 (≠ A230), F222 (≠ Y231), A293 (= A302), S294 (≠ G303), E295 (= E304), A296 (= A305), G316 (= G325), I317 (≠ L326), G318 (= G327), C319 (≠ S328), T320 (= T329), D397 (= D406), H409 (≠ Y418), R412 (= R421), K502 (= K515)
B2HIL6 p-hydroxybenzoic acid--AMP ligase FadD22; p-HB--AMP ligase FadD22; p-hydroxybenzoic acid-AMP synthetase; p-HB-AMP synthetase; EC 6.2.1.50 from Mycobacterium marinum (strain ATCC BAA-535 / M) (see paper)
32% identity, 96% coverage: 16:523/528 of query aligns to 2:488/702 of B2HIL6
Sites not aligning to the query:
- 576 S→A: Catalyzes pHBA-AMP formation, indicating this residue is not essential for adenylation activity.
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
29% identity, 97% coverage: 13:522/528 of query aligns to 7:530/535 of 3dayA
- active site: T189 (≠ S184), T332 (= T329), E333 (= E330), N435 (≠ K427), R440 (≠ W432), K523 (= K515)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (≠ S184), S190 (= S185), G191 (= G186), T192 (≠ S187), S193 (≠ T188), K197 (= K192), G306 (= G303), E307 (= E304), S308 (≠ A305), Y329 (≠ L326), G330 (= G327), Q331 (≠ S328), T332 (= T329), D414 (= D406), F426 (≠ Y418), R429 (= R421), K523 (= K515)
- binding magnesium ion: M451 (≠ I443), H453 (= H445), V456 (= V448)
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, 97% coverage: 13:522/528 of query aligns to 3:528/533 of 3eq6A
- active site: T185 (≠ S184), T328 (= T329), E329 (= E330), N431 (≠ K427), R436 (≠ W432), K521 (= K515)
- binding adenosine monophosphate: G302 (= G303), E303 (= E304), S304 (≠ A305), E323 (≠ D324), S324 (≠ G325), Y325 (≠ L326), G326 (= G327), Q327 (≠ S328), T328 (= T329), D410 (= D406), F422 (≠ Y418), R425 (= R421), R436 (≠ W432)
- binding Butyryl Coenzyme A: W229 (≠ F229), F255 (≠ P254), I277 (≠ T276), V301 (≠ A302), S433 (≠ G429), G434 (= G430), Y435 (≠ I431), P501 (= P495), Y502 (= Y496), Y504 (= Y498), R506 (= R500)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
29% identity, 97% coverage: 13:522/528 of query aligns to 3:528/533 of 2wd9A
- active site: T185 (≠ S184), T328 (= T329), E329 (= E330), N431 (≠ K427), R436 (≠ W432), K521 (= K515)
- binding ibuprofen: I230 (≠ A230), L231 (≠ Y231), G326 (= G327), Q327 (≠ S328), T328 (= T329), R436 (≠ W432)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
29% identity, 97% coverage: 13:522/528 of query aligns to 3:528/533 of 2vzeA
- active site: T185 (≠ S184), T328 (= T329), E329 (= E330), N431 (≠ K427), R436 (≠ W432), K521 (= K515)
- binding adenosine monophosphate: W229 (≠ F229), G302 (= G303), E303 (= E304), S304 (≠ A305), E323 (≠ D324), Y325 (≠ L326), G326 (= G327), Q327 (≠ S328), T328 (= T329), D410 (= D406), F422 (≠ Y418), R425 (= R421), R436 (≠ W432)
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
29% identity, 97% coverage: 13:522/528 of query aligns to 6:531/536 of 3c5eA
- active site: T188 (≠ S184), T331 (= T329), E332 (= E330), N434 (≠ K427), R439 (≠ W432), K524 (= K515)
- binding adenosine-5'-triphosphate: T188 (≠ S184), S189 (= S185), G190 (= G186), T191 (≠ S187), S192 (≠ T188), G305 (= G303), E306 (= E304), S307 (≠ A305), G329 (= G327), Q330 (≠ S328), T331 (= T329), D413 (= D406), F425 (≠ Y418), R428 (= R421), K524 (= K515)
- binding magnesium ion: M450 (≠ I443), H452 (= H445), V455 (= V448)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
29% identity, 97% coverage: 13:522/528 of query aligns to 7:532/537 of 3b7wA
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 90% coverage: 47:522/528 of query aligns to 30:498/506 of 4gxqA
- active site: T163 (≠ S184), N183 (vs. gap), H207 (≠ F229), T303 (= T329), E304 (= E330), I403 (≠ K427), N408 (≠ W432), A491 (≠ K515)
- binding adenosine-5'-triphosphate: T163 (≠ S184), S164 (= S185), G165 (= G186), T166 (≠ S187), T167 (= T188), H207 (≠ F229), S277 (≠ G303), A278 (≠ E304), P279 (≠ A305), E298 (≠ D324), M302 (≠ S328), T303 (= T329), D382 (= D406), R397 (= R421)
- binding carbonate ion: H207 (≠ F229), S277 (≠ G303), R299 (≠ G325), G301 (= G327)
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, 97% coverage: 13:522/528 of query aligns to 39:564/577 of Q08AH3
- Q139 (≠ L103) binding
- 221:229 (vs. 184:192, 56% identical) binding
- ESYGQT 359:364 (≠ DGLGST 324:329) binding
- T364 (= T329) binding
- D446 (= D406) binding
- R461 (= R421) binding
- SGY 469:471 (≠ GGI 429:431) binding
- R472 (≠ W432) binding
- R501 (≠ G461) binding
- S513 (≠ P473) to L: in dbSNP:rs1133607
- K532 (= K490) binding
- YPR 540:542 (= YPR 498:500) binding
- K557 (= K515) binding
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
29% identity, 97% coverage: 13:522/528 of query aligns to 4:527/532 of 3gpcA
- active site: T186 (≠ S184), T327 (= T329), E328 (= E330), N430 (≠ K427), R435 (≠ W432), K520 (= K515)
- binding coenzyme a: G301 (= G303), E302 (= E304), S303 (≠ A305), E322 (≠ D324), Y324 (≠ L326), G325 (= G327), Q326 (≠ S328), T327 (= T329), D409 (= D406), F421 (≠ Y418), R424 (= R421), T516 (= T511), K520 (= K515), Q522 (= Q517)
- binding magnesium ion: H448 (= H445), V451 (= V448)
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
31% identity, 97% coverage: 12:521/528 of query aligns to 32:543/562 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 (≠ G234), G321 (= G303), E322 (= E304), P323 (≠ A305), D342 (= D324), F343 (≠ G325), Y344 (≠ L326), Q346 (≠ S328), T347 (= T329), D428 (= D406), F440 (≠ Y418), K449 (= K427), R454 (≠ W432)
- binding coenzyme a: N128 (≠ L103), W247 (≠ F229), K249 (≠ Y231), K273 (≠ R253), L274 (≠ P254), Q300 (≠ T280), D452 (≠ G430), Y453 (≠ I431), R483 (≠ G461), P517 (= P495)
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
31% identity, 97% coverage: 12:521/528 of query aligns to 30:541/561 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 (= G303), E320 (= E304), P321 (≠ A305), D340 (= D324), F341 (≠ G325), Y342 (≠ L326), G343 (= G327), Q344 (≠ S328), T345 (= T329), D426 (= D406), F438 (≠ Y418), K447 (= K427), R452 (≠ W432)
Query Sequence
>WP_011385246.1 NCBI__GCF_000009985.1:WP_011385246.1
MTSLNASSEHALDIPRDYNAATWFIDRHIKDGRSAKVAFIDADGSHTYAQLGEKVNRAGN
ALKSLGLHMENRIAMIMLDTVDFPSVFWGAIKAGIVPIPLNTLLTTGDYGYMLSDSRARV
LVISEELFDKVEPILPDLPLLEHVVISGKNAHGHTLLSDMMAAAEPKLKTAETTRDDVAF
WLYSSGSTGAPKGAVHLQRDLPATAVHYGQQVLGITEDDVTFSAAKLFFAYGLGNGMTFS
LHVGATSVLLKDRPTPEAVMKILKDHQPTIFYGVPTLYGTILADPQYRRETASTRLRACV
SAGEALPEDVGRRWEERFGAAILDGLGSTEMLHIFLSNRHGEVRYGTSGKAVPGYDLKIV
ADDGHELPQGEMGELVVRGPSSATAYWNQREKSLKTFRGEWTHTGDKYFVDDDGYYRYAG
RGDDMLKVGGIWVSPFEVEAALISHEMVLEAAVVGEADSEGLVKPKAFVVLAPGETGSEV
LKEQLQAYVKAKLAPYKYPRWIEFVEALPKTATGKIQRFKLRGSLSQM
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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