SitesBLAST
Comparing BPHYT_RS13365 FitnessBrowser__BFirm:BPHYT_RS13365 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
62% identity, 96% coverage: 19:528/530 of query aligns to 4:515/518 of 4rmnA
- active site: S176 (= S191), T196 (= T211), T324 (= T335), E325 (= E336), K422 (= K433), Y427 (= Y438), K507 (= K520)
- binding thiophene-2-carboxylic acid: A217 (= A232), F221 (= F236), Y223 (= Y238), G269 (= G280), A270 (≠ V281), A297 (= A308), G298 (= G309), G322 (= G333), S323 (= S334), H328 (= H339), I329 (= I340), K422 (= K433), G425 (= G436)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
62% identity, 96% coverage: 19:528/530 of query aligns to 5:516/518 of 4rm3A
- active site: S177 (= S191), T197 (= T211), T325 (= T335), E326 (= E336), K423 (= K433), Y428 (= Y438), K508 (= K520)
- binding 2-furoic acid: A223 (= A237), Y224 (= Y238), A298 (= A308), G323 (= G333), H329 (= H339), I330 (= I340), K423 (= K433)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
62% identity, 96% coverage: 19:528/530 of query aligns to 4:515/516 of 4rm2A
- active site: S176 (= S191), T196 (= T211), T324 (= T335), E325 (= E336), K422 (= K433), Y427 (= Y438), K507 (= K520)
- binding 2-fluorobenzoic acid: A216 (= A231), A222 (= A237), Y223 (= Y238), P246 (= P261), T247 (= T262), V251 (≠ I266), F267 (= F278), G269 (= G280), A270 (≠ V281), G273 (≠ L284), M277 (= M288), A297 (= A308), G298 (= G309), I321 (= I332), G322 (= G333), S323 (= S334), H328 (= H339), K422 (= K433)
4zjzA Crystal structure of a benzoate coenzyme a ligase with benzoyl-amp (see paper)
62% identity, 96% coverage: 19:528/530 of query aligns to 4:515/517 of 4zjzA
- active site: S176 (= S191), T196 (= T211), T324 (= T335), E325 (= E336), K422 (= K433), Y427 (= Y438), K507 (= K520)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: A222 (= A237), Y223 (= Y238), A297 (= A308), G298 (= G309), E299 (= E310), A300 (= A311), G320 (= G331), I321 (= I332), G322 (= G333), S323 (= S334), T324 (= T335), H328 (= H339), I329 (= I340), D401 (= D412), R416 (= R427), K422 (= K433), Y427 (= Y438)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
62% identity, 96% coverage: 19:528/530 of query aligns to 4:515/519 of 4rlfB
- active site: S176 (= S191), T196 (= T211), T324 (= T335), E325 (= E336), K422 (= K433), Y427 (= Y438), K507 (= K520)
- binding 2-methylbenzoic acid: A222 (= A237), Y223 (= Y238), G298 (= G309), I321 (= I332), G322 (= G333), S323 (= S334), H328 (= H339)
- binding 4-methylbenzoic acid: A216 (= A231), P246 (= P261), P248 (≠ A263), G269 (= G280), A270 (≠ V281), G273 (≠ L284)
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)
61% identity, 96% coverage: 19:528/530 of query aligns to 4:515/518 of 6m2uA
- active site: S176 (= S191), T196 (= T211), T324 (= T335), E325 (= E336), K422 (= K433), Y427 (= Y438), K507 (= K520)
- binding adenosine monophosphate: G298 (= G309), E299 (= E310), A300 (= A311), D319 (= D330), G320 (= G331), I321 (= I332), G322 (= G333), T324 (= T335), D401 (= D412), R416 (= R427), K422 (= K433), Y427 (= Y438)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (= Y238), A297 (= A308), G322 (= G333), S323 (= S334), A328 (≠ H339)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
61% identity, 96% coverage: 19:528/530 of query aligns to 4:515/518 of 6m2tA
- active site: S176 (= S191), T196 (= T211), T324 (= T335), E325 (= E336), K422 (= K433), Y427 (= Y438), K507 (= K520)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (= Y238), G322 (= G333), S323 (= S334), A328 (≠ H339)
- binding adenosine monophosphate: G298 (= G309), E299 (= E310), A300 (= A311), G320 (= G331), I321 (= I332), S323 (= S334), T324 (= T335), D401 (= D412), R416 (= R427), K422 (= K433), Y427 (= Y438)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
41% identity, 96% coverage: 20:527/530 of query aligns to 7:509/518 of 4wv3B
- active site: S175 (= S191), T320 (= T335), E321 (= E336), K418 (= K433), W423 (≠ Y438), K502 (= K520)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (= F236), T221 (≠ A237), F222 (≠ Y238), A293 (= A308), S294 (≠ G309), E295 (= E310), A296 (= A311), G316 (= G331), I317 (= I332), G318 (= G333), C319 (≠ S334), T320 (= T335), D397 (= D412), H409 (≠ Y424), R412 (= R427), K502 (= K520)
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, 93% coverage: 36:530/530 of query aligns to 13:490/702 of B2HIL6
Sites not aligning to the query:
- 576 S→A: Catalyzes pHBA-AMP formation, indicating this residue is not essential for adenylation activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
33% identity, 91% coverage: 48:528/530 of query aligns to 28:499/506 of 4gxqA
- active site: T163 (≠ S191), N183 (vs. gap), H207 (≠ F236), T303 (= T335), E304 (= E336), I403 (≠ K433), N408 (≠ Y438), A491 (≠ K520)
- binding adenosine-5'-triphosphate: T163 (≠ S191), S164 (= S192), G165 (= G193), T166 (≠ S194), T167 (= T195), H207 (≠ F236), S277 (≠ G309), A278 (≠ E310), P279 (≠ A311), E298 (≠ D330), M302 (≠ S334), T303 (= T335), D382 (≠ K413), R397 (= R427)
- binding carbonate ion: H207 (≠ F236), S277 (≠ G309), R299 (≠ G331), G301 (= G333)
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
29% identity, 96% coverage: 20:529/530 of query aligns to 9:532/535 of 3dayA
- active site: T189 (≠ S191), T332 (= T335), E333 (= E336), N435 (≠ K433), R440 (≠ Y438), K523 (= K520)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (≠ S191), S190 (= S192), G191 (= G193), T192 (≠ S194), S193 (≠ T195), K197 (= K199), G306 (= G309), E307 (= E310), S308 (≠ A311), Y329 (≠ I332), G330 (= G333), Q331 (≠ S334), T332 (= T335), D414 (= D412), F426 (≠ Y424), R429 (= R427), K523 (= K520)
- binding magnesium ion: M451 (≠ V449), H453 (= H451), V456 (= V454)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
29% identity, 96% coverage: 20:529/530 of query aligns to 9:534/537 of 3b7wA
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
29% identity, 96% coverage: 20:529/530 of query aligns to 8:533/536 of 3c5eA
- active site: T188 (≠ S191), T331 (= T335), E332 (= E336), N434 (≠ K433), R439 (≠ Y438), K524 (= K520)
- binding adenosine-5'-triphosphate: T188 (≠ S191), S189 (= S192), G190 (= G193), T191 (≠ S194), S192 (≠ T195), G305 (= G309), E306 (= E310), S307 (≠ A311), G329 (= G333), Q330 (≠ S334), T331 (= T335), D413 (= D412), F425 (≠ Y424), R428 (= R427), K524 (= K520)
- binding magnesium ion: M450 (≠ V449), H452 (= H451), V455 (= V454)
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, 96% coverage: 20:529/530 of query aligns to 5:530/533 of 3eq6A
- active site: T185 (≠ S191), T328 (= T335), E329 (= E336), N431 (≠ K433), R436 (≠ Y438), K521 (= K520)
- binding adenosine monophosphate: G302 (= G309), E303 (= E310), S304 (≠ A311), E323 (≠ D330), S324 (≠ G331), Y325 (≠ I332), G326 (= G333), Q327 (≠ S334), T328 (= T335), D410 (= D412), F422 (≠ Y424), R425 (= R427), R436 (≠ Y438)
- binding Butyryl Coenzyme A: W229 (≠ F236), F255 (≠ P261), I277 (≠ T283), V301 (≠ A308), S433 (= S435), G434 (= G436), Y435 (≠ Q437), P501 (= P500), Y502 (≠ H501), Y504 (= Y503), R506 (= R505)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
29% identity, 96% coverage: 20:529/530 of query aligns to 5:530/533 of 2wd9A
- active site: T185 (≠ S191), T328 (= T335), E329 (= E336), N431 (≠ K433), R436 (≠ Y438), K521 (= K520)
- binding ibuprofen: I230 (≠ A237), L231 (≠ Y238), G326 (= G333), Q327 (≠ S334), T328 (= T335), R436 (≠ Y438)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
29% identity, 96% coverage: 20:529/530 of query aligns to 5:530/533 of 2vzeA
- active site: T185 (≠ S191), T328 (= T335), E329 (= E336), N431 (≠ K433), R436 (≠ Y438), K521 (= K520)
- binding adenosine monophosphate: W229 (≠ F236), G302 (= G309), E303 (= E310), S304 (≠ A311), E323 (≠ D330), Y325 (≠ I332), G326 (= G333), Q327 (≠ S334), T328 (= T335), D410 (= D412), F422 (≠ Y424), R425 (= R427), R436 (≠ Y438)
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)
28% identity, 96% coverage: 20:529/530 of query aligns to 41:566/577 of Q08AH3
- Q139 (≠ L106) binding
- 221:229 (vs. 191:199, 56% identical) binding
- ESYGQT 359:364 (≠ DGIGST 330:335) binding
- T364 (= T335) binding
- D446 (= D412) binding
- R461 (= R427) binding
- SGY 469:471 (≠ SGQ 435:437) binding
- R472 (≠ Y438) binding
- R501 (≠ H464) binding
- S513 (≠ R478) to L: in dbSNP:rs1133607
- K532 (= K495) binding
- YPR 540:542 (= YPR 503:505) binding
- K557 (= K520) binding
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: 70:429/530 of query aligns to 48:394/394 of 5oe6A
- active site: T162 (≠ S191), G178 (≠ W210), F204 (= F236), T299 (= T335), E300 (= E336)
- binding 6-fluoroanthraniloyl-AMP: T162 (≠ S191), F204 (= F236), Y206 (= Y238), G274 (= G309), S275 (≠ E310), P276 (≠ A311), G295 (= G331), I296 (= I332), G297 (= G333), A298 (≠ S334), T299 (= T335), H303 (= H339), D377 (= D412)
5oe3A Crystal structure of the n-terminal domain of pqsa in complex with anthraniloyl-amp (crystal form 1) (see paper)
34% identity, 68% coverage: 70:429/530 of query aligns to 49:394/394 of 5oe3A
- active site: T163 (= T195), G178 (≠ W210), F204 (= F236), T299 (= T335), E300 (= E336)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F204 (= F236), Y206 (= Y238), G274 (= G309), S275 (≠ E310), P276 (≠ A311), G295 (= G331), I296 (= I332), G297 (= G333), A298 (≠ S334), T299 (= T335), H303 (= H339), D377 (= D412), H389 (≠ Y424)
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
29% identity, 96% coverage: 20:529/530 of query aligns to 6:529/532 of 3gpcA
- active site: T186 (≠ S191), T327 (= T335), E328 (= E336), N430 (≠ K433), R435 (≠ Y438), K520 (= K520)
- binding coenzyme a: G301 (= G309), E302 (= E310), S303 (≠ A311), E322 (≠ D330), Y324 (≠ I332), G325 (= G333), Q326 (≠ S334), T327 (= T335), D409 (= D412), F421 (≠ Y424), R424 (= R427), T516 (= T516), K520 (= K520), Q522 (= Q522)
- binding magnesium ion: H448 (= H451), V451 (= V454)
Query Sequence
>BPHYT_RS13365 FitnessBrowser__BFirm:BPHYT_RS13365
MEALLEKAANQPAATAEAPPALFNFAAYLFRLNETRATKTAYIDDTGSITYGELEERARR
FASALRTLGVHPEERVLLVMLDTIALPVAFLGALYAGVVPVVANTLLTPADYVYMLTHSH
ARAVIASGALVQNVTQALDSSEHDGCQLIVSQPCEGEPLLAPLLEELIDAAAPAAKAAAT
GCDDIAFWLYSSGSTGKPKGTVHTHANLYWTAELYAKPILGIAESDVVFSAAKLFFAYGL
GNGLTFPLSVGATAILMAERPTADAIFMRLVKHRPTVFYGVPTLYANMLVSPNLPARADV
AMRICTSAGEALPREIGERFTAHFGCEILDGIGSTEMLHIFLSNRAGAVEYGTTGRPVPG
YEVELRDDAGHAVADGEVGDLYIKGPSAAVMYWNNREKTRATFLGEWIRSGDKYCRLANG
CYVYAGRSDDMLKVSGQYVSPVEVEMVLVQHGAVLEAAVVGVDHGGLVKTRAFVVLKREF
AASEILAEELKAFVKDRLAPHKYPRDIVFVDDLPKTATGKIQRFKLREQS
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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