SitesBLAST
Comparing RR42_RS35150 FitnessBrowser__Cup4G11:RR42_RS35150 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)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
70% identity, 98% coverage: 7:517/523 of query aligns to 1:515/519 of 4rlfB
- active site: S176 (= S182), T196 (= T202), T324 (= T326), E325 (= E327), K422 (= K424), Y427 (= Y429), K507 (= K509)
- binding 2-methylbenzoic acid: A222 (= A228), Y223 (= Y229), G298 (= G300), I321 (= I323), G322 (= G324), S323 (= S325), H328 (= H330)
- binding 4-methylbenzoic acid: A216 (= A222), P246 (= P252), P248 (= P254), G269 (= G271), A270 (= A272), G273 (= G275)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
70% identity, 98% coverage: 7:517/523 of query aligns to 1:515/516 of 4rm2A
- active site: S176 (= S182), T196 (= T202), T324 (= T326), E325 (= E327), K422 (= K424), Y427 (= Y429), K507 (= K509)
- binding 2-fluorobenzoic acid: A216 (= A222), A222 (= A228), Y223 (= Y229), P246 (= P252), T247 (= T253), V251 (≠ T257), F267 (= F269), G269 (= G271), A270 (= A272), G273 (= G275), M277 (= M279), A297 (= A299), G298 (= G300), I321 (= I323), G322 (= G324), S323 (= S325), H328 (= H330), K422 (= K424)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
70% identity, 98% coverage: 7:517/523 of query aligns to 1:515/518 of 4rmnA
- active site: S176 (= S182), T196 (= T202), T324 (= T326), E325 (= E327), K422 (= K424), Y427 (= Y429), K507 (= K509)
- binding thiophene-2-carboxylic acid: A217 (= A223), F221 (= F227), Y223 (= Y229), G269 (= G271), A270 (= A272), A297 (= A299), G298 (= G300), G322 (= G324), S323 (= S325), H328 (= H330), I329 (= I331), K422 (= K424), G425 (= G427)
4zjzA Crystal structure of a benzoate coenzyme a ligase with benzoyl-amp (see paper)
70% identity, 98% coverage: 7:517/523 of query aligns to 1:515/517 of 4zjzA
- active site: S176 (= S182), T196 (= T202), T324 (= T326), E325 (= E327), K422 (= K424), Y427 (= Y429), K507 (= K509)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: A222 (= A228), Y223 (= Y229), A297 (= A299), G298 (= G300), E299 (= E301), A300 (= A302), G320 (= G322), I321 (= I323), G322 (= G324), S323 (= S325), T324 (= T326), H328 (= H330), I329 (= I331), D401 (= D403), R416 (= R418), K422 (= K424), Y427 (= Y429)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
70% identity, 98% coverage: 7:517/523 of query aligns to 2:516/518 of 4rm3A
- active site: S177 (= S182), T197 (= T202), T325 (= T326), E326 (= E327), K423 (= K424), Y428 (= Y429), K508 (= K509)
- binding 2-furoic acid: A223 (= A228), Y224 (= Y229), A298 (= A299), G323 (= G324), H329 (= H330), I330 (= I331), K423 (= K424)
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)
69% identity, 98% coverage: 7:517/523 of query aligns to 1:515/518 of 6m2uA
- active site: S176 (= S182), T196 (= T202), T324 (= T326), E325 (= E327), K422 (= K424), Y427 (= Y429), K507 (= K509)
- binding adenosine monophosphate: G298 (= G300), E299 (= E301), A300 (= A302), D319 (= D321), G320 (= G322), I321 (= I323), G322 (= G324), T324 (= T326), D401 (= D403), R416 (= R418), K422 (= K424), Y427 (= Y429)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (= Y229), A297 (= A299), G322 (= G324), S323 (= S325), A328 (≠ H330)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
69% identity, 98% coverage: 7:517/523 of query aligns to 1:515/518 of 6m2tA
- active site: S176 (= S182), T196 (= T202), T324 (= T326), E325 (= E327), K422 (= K424), Y427 (= Y429), K507 (= K509)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (= Y229), G322 (= G324), S323 (= S325), A328 (≠ H330)
- binding adenosine monophosphate: G298 (= G300), E299 (= E301), A300 (= A302), G320 (= G322), I321 (= I323), S323 (= S325), T324 (= T326), D401 (= D403), R416 (= R418), K422 (= K424), Y427 (= Y429)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
44% identity, 94% coverage: 27:516/523 of query aligns to 23:509/518 of 4wv3B
- active site: S175 (= S182), T320 (= T326), E321 (= E327), K418 (= K424), W423 (≠ Y429), K502 (= K509)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (= F227), T221 (≠ A228), F222 (≠ Y229), A293 (= A299), S294 (≠ G300), E295 (= E301), A296 (= A302), G316 (= G322), I317 (= I323), G318 (= G324), C319 (≠ S325), T320 (= T326), D397 (= D403), H409 (≠ Y415), R412 (= R418), K502 (= K509)
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)
31% identity, 91% coverage: 40:516/523 of query aligns to 31:487/702 of B2HIL6
Sites not aligning to the query:
- 576 S→A: Catalyzes pHBA-AMP formation, indicating this residue is not essential for adenylation activity.
P69451 Long-chain-fatty-acid--CoA ligase; Long-chain acyl-CoA synthetase; Acyl-CoA synthetase; EC 6.2.1.3 from Escherichia coli (strain K12) (see paper)
29% identity, 94% coverage: 25:517/523 of query aligns to 34:551/561 of P69451
- Y213 (= Y181) mutation to A: Loss of activity.
- T214 (≠ S182) mutation to A: 10% of wild-type activity.
- G216 (= G184) mutation to A: Decreases activity.
- T217 (≠ S185) mutation to A: Decreases activity.
- G219 (= G187) mutation to A: Decreases activity.
- K222 (= K190) mutation to A: Decreases activity.
- E361 (= E327) mutation to A: Loss of activity.
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
28% identity, 97% coverage: 14:519/523 of query aligns to 11:534/536 of 3c5eA
- active site: T188 (≠ S182), T331 (= T326), E332 (= E327), N434 (≠ K424), R439 (≠ Y429), K524 (= K509)
- binding adenosine-5'-triphosphate: T188 (≠ S182), S189 (= S183), G190 (= G184), T191 (≠ S185), S192 (≠ T186), G305 (= G300), E306 (= E301), S307 (≠ A302), G329 (= G324), Q330 (≠ S325), T331 (= T326), D413 (= D403), F425 (≠ Y415), R428 (= R418), K524 (= K509)
- binding magnesium ion: M450 (≠ A440), H452 (= H442), V455 (= V445)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
28% identity, 97% coverage: 14:519/523 of query aligns to 12:535/537 of 3b7wA
3eq6A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a ternary complex with products (see paper)
28% identity, 97% coverage: 14:519/523 of query aligns to 8:531/533 of 3eq6A
- active site: T185 (≠ S182), T328 (= T326), E329 (= E327), N431 (≠ K424), R436 (≠ Y429), K521 (= K509)
- binding adenosine monophosphate: G302 (= G300), E303 (= E301), S304 (≠ A302), E323 (≠ D321), S324 (≠ G322), Y325 (≠ I323), G326 (= G324), Q327 (≠ S325), T328 (= T326), D410 (= D403), F422 (≠ Y415), R425 (= R418), R436 (≠ Y429)
- binding Butyryl Coenzyme A: W229 (≠ F227), F255 (≠ P252), I277 (≠ T274), V301 (≠ A299), S433 (= S426), G434 (= G427), Y435 (≠ I428), P501 (= P489), Y502 (= Y490), Y504 (= Y492), R506 (= R494)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
28% identity, 97% coverage: 14:519/523 of query aligns to 8:531/533 of 2wd9A
- active site: T185 (≠ S182), T328 (= T326), E329 (= E327), N431 (≠ K424), R436 (≠ Y429), K521 (= K509)
- binding ibuprofen: I230 (≠ A228), L231 (≠ Y229), G326 (= G324), Q327 (≠ S325), T328 (= T326), R436 (≠ Y429)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
28% identity, 97% coverage: 14:519/523 of query aligns to 8:531/533 of 2vzeA
- active site: T185 (≠ S182), T328 (= T326), E329 (= E327), N431 (≠ K424), R436 (≠ Y429), K521 (= K509)
- binding adenosine monophosphate: W229 (≠ F227), G302 (= G300), E303 (= E301), S304 (≠ A302), E323 (≠ D321), Y325 (≠ I323), G326 (= G324), Q327 (≠ S325), T328 (= T326), D410 (= D403), F422 (≠ Y415), R425 (= R418), R436 (≠ Y429)
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, 92% coverage: 41:519/523 of query aligns to 82:567/577 of Q08AH3
- Q139 (≠ L97) binding
- 221:229 (vs. 182:190, 56% identical) binding
- ESYGQT 359:364 (≠ DGIGST 321:326) binding
- T364 (= T326) binding
- D446 (= D403) binding
- R461 (= R418) binding
- SGY 469:471 (≠ SGI 426:428) binding
- R472 (≠ Y429) binding
- R501 (≠ G458) binding
- S513 (≠ P470) to L: in dbSNP:rs1133607
- K532 (= K484) binding
- YPR 540:542 (= YPR 492:494) binding
- K557 (= K509) binding
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
28% identity, 97% coverage: 14:519/523 of query aligns to 12:533/535 of 3dayA
- active site: T189 (≠ S182), T332 (= T326), E333 (= E327), N435 (≠ K424), R440 (≠ Y429), K523 (= K509)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (≠ S182), S190 (= S183), G191 (= G184), T192 (≠ S185), S193 (≠ T186), K197 (= K190), G306 (= G300), E307 (= E301), S308 (≠ A302), Y329 (≠ I323), G330 (= G324), Q331 (≠ S325), T332 (= T326), D414 (= D403), F426 (≠ Y415), R429 (= R418), K523 (= K509)
- binding magnesium ion: M451 (≠ A440), H453 (= H442), V456 (= V445)
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
28% identity, 97% coverage: 14:519/523 of query aligns to 9:530/532 of 3gpcA
- active site: T186 (≠ S182), T327 (= T326), E328 (= E327), N430 (≠ K424), R435 (≠ Y429), K520 (= K509)
- binding coenzyme a: G301 (= G300), E302 (= E301), S303 (≠ A302), E322 (≠ D321), Y324 (≠ I323), G325 (= G324), Q326 (≠ S325), T327 (= T326), D409 (= D403), F421 (≠ Y415), R424 (= R418), T516 (= T505), K520 (= K509), Q522 (= Q511)
- binding magnesium ion: H448 (= H442), V451 (= V445)
5oe6A Crystal structure of the n-terminal domain of pqsa in complex with 6- fluoroanthraniloyl-amp (crystal form 1) (see paper)
34% identity, 68% coverage: 65:420/523 of query aligns to 52:394/394 of 5oe6A
- active site: T162 (≠ S185), G178 (≠ W201), F204 (= F227), T299 (= T326), E300 (= E327)
- binding 6-fluoroanthraniloyl-AMP: T162 (≠ S185), F204 (= F227), Y206 (= Y229), G274 (= G300), S275 (≠ E301), P276 (≠ A302), G295 (= G322), I296 (= I323), G297 (= G324), A298 (≠ S325), T299 (= T326), H303 (= H330), D377 (= D403)
5oe3A Crystal structure of the n-terminal domain of pqsa in complex with anthraniloyl-amp (crystal form 1) (see paper)
35% identity, 68% coverage: 65:420/523 of query aligns to 53:394/394 of 5oe3A
- active site: T163 (= T186), G178 (≠ W201), F204 (= F227), T299 (= T326), E300 (= E327)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F204 (= F227), Y206 (= Y229), G274 (= G300), S275 (≠ E301), P276 (≠ A302), G295 (= G322), I296 (= I323), G297 (= G324), A298 (≠ S325), T299 (= T326), H303 (= H330), D377 (= D403), H389 (≠ Y415)
Query Sequence
>RR42_RS35150 FitnessBrowser__Cup4G11:RR42_RS35150
MTAEPQVQPPGTPFNFAQHLIACNARRPGKTAYIDDHGAMSYGELAERIRRVAAALQASG
IHREERVLLLMHDGNDWPVCFLGAMYAGIVPVAVNTLLTADDYAYMLQHSRAQAVLVSGA
LLPVLQQAMAQGGHEAGTVIVSQPAGPLPDGMIALDGWIDRTAPLAAPASTSPDDPGFWL
YSSGSTGRPKGVLHSQGNPYWTAELYAKPVLSLGEADICFSAAKLYFAYGLGNALTFPLS
VGATVVLMAERPTPEATFRRWLDYQPTVFFGAPTGYAGMLAAPGLPTREQVSLRLCSSAG
EALPADLGERFTAHFGCEIIDGIGSTEMLHIFLSNRPGQVRYGTTGWPVPGYAVELRDED
GHAVPDGDVGDLYIQGPSAALMYWGNREKSRETFRGGWTKSGDKYARNADGSYSYAGRSD
DMLKVSGIYVSPFEVEATLAQHPAVLEAAVIGVPDPAGLTKTKAFVVLKPGAQVSETELK
AFVKERLAPYKYPRVIEFMGALPKTATGKIQRFRLREMEGAPA
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