SitesBLAST
Comparing 3608151 FitnessBrowser__Dino:3608151 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)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
26% identity, 88% coverage: 55:509/519 of query aligns to 44:532/537 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)
26% identity, 88% coverage: 55:509/519 of query aligns to 40:528/533 of 3eq6A
- active site: T185 (= T179), T328 (≠ S320), E329 (= E321), N431 (= N419), R436 (= R424), K521 (= K502)
- binding adenosine monophosphate: G302 (= G294), E303 (= E295), S304 (≠ A296), E323 (= E315), S324 (≠ A316), Y325 (≠ L317), G326 (= G318), Q327 (≠ M319), T328 (≠ S320), D410 (= D398), F422 (≠ Y410), R425 (= R413), R436 (= R424)
- binding Butyryl Coenzyme A: W229 (= W223), F255 (≠ A246), I277 (≠ G270), V301 (≠ A293), S433 (≠ G421), G434 (= G422), Y435 (≠ F423), P501 (≠ R482), Y502 (= Y483), Y504 (≠ Q485), R506 (= R487)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
26% identity, 88% coverage: 55:509/519 of query aligns to 40:528/533 of 2wd9A
- active site: T185 (= T179), T328 (≠ S320), E329 (= E321), N431 (= N419), R436 (= R424), K521 (= K502)
- binding ibuprofen: I230 (≠ T224), L231 (≠ Y225), G326 (= G318), Q327 (≠ M319), T328 (≠ S320), R436 (= R424)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
26% identity, 88% coverage: 55:509/519 of query aligns to 40:528/533 of 2vzeA
- active site: T185 (= T179), T328 (≠ S320), E329 (= E321), N431 (= N419), R436 (= R424), K521 (= K502)
- binding adenosine monophosphate: W229 (= W223), G302 (= G294), E303 (= E295), S304 (≠ A296), E323 (= E315), Y325 (≠ L317), G326 (= G318), Q327 (≠ M319), T328 (≠ S320), D410 (= D398), F422 (≠ Y410), R425 (= R413), R436 (= R424)
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
26% identity, 88% coverage: 55:509/519 of query aligns to 43:531/536 of 3c5eA
- active site: T188 (= T179), T331 (≠ S320), E332 (= E321), N434 (= N419), R439 (= R424), K524 (= K502)
- binding adenosine-5'-triphosphate: T188 (= T179), S189 (= S180), G190 (= G181), T191 (≠ S182), S192 (= S183), G305 (= G294), E306 (= E295), S307 (≠ A296), G329 (= G318), Q330 (≠ M319), T331 (≠ S320), D413 (= D398), F425 (≠ Y410), R428 (= R413), K524 (= K502)
- binding magnesium ion: M450 (≠ H435), H452 (≠ R437), V455 (≠ I440)
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
25% identity, 88% coverage: 55:509/519 of query aligns to 44:530/535 of 3dayA
- active site: T189 (= T179), T332 (≠ S320), E333 (= E321), N435 (= N419), R440 (= R424), K523 (= K502)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T179), S190 (= S180), G191 (= G181), T192 (≠ S182), S193 (= S183), K197 (≠ R187), G306 (= G294), E307 (= E295), S308 (≠ A296), Y329 (≠ L317), G330 (= G318), Q331 (≠ M319), T332 (≠ S320), D414 (= D398), F426 (≠ Y410), R429 (= R413), K523 (= K502)
- binding magnesium ion: M451 (≠ H435), H453 (≠ R437), V456 (≠ I440)
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)
26% identity, 92% coverage: 30:509/519 of query aligns to 41:564/577 of Q08AH3
- Q139 (≠ A117) binding
- 221:229 (vs. 179:187, 67% identical) binding
- ESYGQT 359:364 (≠ EALGMS 315:320) binding
- T364 (≠ S320) binding
- D446 (= D398) binding
- R461 (= R413) binding
- SGY 469:471 (≠ GGF 421:423) binding
- R472 (= R424) binding
- R501 (≠ D453) binding
- S513 (≠ A465) to L: in dbSNP:rs1133607
- K532 (vs. gap) binding
- YPR 540:542 (≠ QPR 485:487) binding
- K557 (= K502) binding
4zjzA Crystal structure of a benzoate coenzyme a ligase with benzoyl-amp (see paper)
29% identity, 93% coverage: 27:509/519 of query aligns to 2:514/517 of 4zjzA
- active site: S176 (≠ T179), T196 (≠ A198), T324 (≠ S320), E325 (= E321), K422 (≠ N419), Y427 (≠ R424), K507 (= K502)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: A222 (≠ T224), Y223 (= Y225), A297 (= A293), G298 (= G294), E299 (= E295), A300 (= A296), G320 (≠ A316), I321 (≠ L317), G322 (= G318), S323 (≠ M319), T324 (≠ S320), H328 (≠ S323), I329 (≠ T324), D401 (= D398), R416 (= R413), K422 (≠ N419), Y427 (≠ R424)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
29% identity, 93% coverage: 27:509/519 of query aligns to 3:515/518 of 4rm3A
- active site: S177 (≠ T179), T197 (≠ A198), T325 (≠ S320), E326 (= E321), K423 (≠ N419), Y428 (≠ R424), K508 (= K502)
- binding 2-furoic acid: A223 (≠ T224), Y224 (= Y225), A298 (= A293), G323 (= G318), H329 (≠ S323), I330 (≠ T324), K423 (≠ N419)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
29% identity, 93% coverage: 27:509/519 of query aligns to 2:514/516 of 4rm2A
- active site: S176 (≠ T179), T196 (≠ A198), T324 (≠ S320), E325 (= E321), K422 (≠ N419), Y427 (≠ R424), K507 (= K502)
- binding 2-fluorobenzoic acid: A216 (= A218), A222 (≠ T224), Y223 (= Y225), P246 (≠ G247), T247 (= T248), V251 (≠ A252), F267 (= F265), G269 (≠ A267), A270 (≠ V268), G273 (≠ V271), M277 (≠ I275), A297 (= A293), G298 (= G294), I321 (≠ L317), G322 (= G318), S323 (≠ M319), H328 (≠ S323), K422 (≠ N419)
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)
29% identity, 93% coverage: 27:509/519 of query aligns to 2:514/518 of 6m2uA
- active site: S176 (≠ T179), T196 (≠ A198), T324 (≠ S320), E325 (= E321), K422 (≠ N419), Y427 (≠ R424), K507 (= K502)
- binding adenosine monophosphate: G298 (= G294), E299 (= E295), A300 (= A296), D319 (≠ E315), G320 (≠ A316), I321 (≠ L317), G322 (= G318), T324 (≠ S320), D401 (= D398), R416 (= R413), K422 (≠ N419), Y427 (≠ R424)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (= Y225), A297 (= A293), G322 (= G318), S323 (≠ M319), A328 (≠ S323)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
29% identity, 93% coverage: 27:509/519 of query aligns to 2:514/518 of 6m2tA
- active site: S176 (≠ T179), T196 (≠ A198), T324 (≠ S320), E325 (= E321), K422 (≠ N419), Y427 (≠ R424), K507 (= K502)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (= Y225), G322 (= G318), S323 (≠ M319), A328 (≠ S323)
- binding adenosine monophosphate: G298 (= G294), E299 (= E295), A300 (= A296), G320 (≠ A316), I321 (≠ L317), S323 (≠ M319), T324 (≠ S320), D401 (= D398), R416 (= R413), K422 (≠ N419), Y427 (≠ R424)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
29% identity, 93% coverage: 27:509/519 of query aligns to 2:514/518 of 4rmnA
- active site: S176 (≠ T179), T196 (≠ A198), T324 (≠ S320), E325 (= E321), K422 (≠ N419), Y427 (≠ R424), K507 (= K502)
- binding thiophene-2-carboxylic acid: A217 (≠ G219), F221 (≠ W223), Y223 (= Y225), G269 (≠ A267), A270 (≠ V268), A297 (= A293), G298 (= G294), G322 (= G318), S323 (≠ M319), H328 (≠ S323), I329 (≠ T324), K422 (≠ N419), G425 (= G422)
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
29% identity, 93% coverage: 27:509/519 of query aligns to 2:514/519 of 4rlfB
- active site: S176 (≠ T179), T196 (≠ A198), T324 (≠ S320), E325 (= E321), K422 (≠ N419), Y427 (≠ R424), K507 (= K502)
- binding 2-methylbenzoic acid: A222 (≠ T224), Y223 (= Y225), G298 (= G294), I321 (≠ L317), G322 (= G318), S323 (≠ M319), H328 (≠ S323)
- binding 4-methylbenzoic acid: A216 (= A218), P246 (≠ G247), P248 (≠ D249), G269 (≠ A267), A270 (≠ V268), G273 (≠ V271)
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
25% identity, 88% coverage: 55:509/519 of query aligns to 41:527/532 of 3gpcA
- active site: T186 (= T179), T327 (≠ S320), E328 (= E321), N430 (= N419), R435 (= R424), K520 (= K502)
- binding coenzyme a: G301 (= G294), E302 (= E295), S303 (≠ A296), E322 (= E315), Y324 (≠ L317), G325 (= G318), Q326 (≠ M319), T327 (≠ S320), D409 (= D398), F421 (≠ Y410), R424 (= R413), T516 (≠ G498), K520 (= K502), Q522 (≠ D504)
- binding magnesium ion: H448 (≠ R437), V451 (≠ I440)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
28% identity, 91% coverage: 44:513/519 of query aligns to 15:502/506 of 4gxqA
- active site: T163 (= T179), N183 (≠ R199), H207 (≠ W223), T303 (≠ S320), E304 (= E321), I403 (≠ N419), N408 (≠ R424), A491 (≠ K502)
- binding adenosine-5'-triphosphate: T163 (= T179), S164 (= S180), G165 (= G181), T166 (≠ S182), T167 (≠ S183), H207 (≠ W223), S277 (≠ E295), A278 (= A296), P279 (vs. gap), E298 (= E315), M302 (= M319), T303 (≠ S320), D382 (= D398), R397 (= R413)
- binding carbonate ion: H207 (≠ W223), S277 (≠ E295), R299 (≠ A316), G301 (= G318)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
27% identity, 87% coverage: 61:511/519 of query aligns to 37:511/518 of 4wv3B
- active site: S175 (≠ T179), T320 (≠ S320), E321 (= E321), K418 (≠ N419), W423 (≠ R424), K502 (= K502)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ W223), T221 (= T224), F222 (≠ Y225), A293 (= A293), S294 (≠ G294), E295 (= E295), A296 (= A296), G316 (≠ A316), I317 (≠ L317), G318 (= G318), C319 (≠ M319), T320 (≠ S320), D397 (= D398), H409 (≠ Y410), R412 (= R413), K502 (= K502)
O30409 Tyrocidine synthase 3; Tyrocidine synthase III from Brevibacillus parabrevis (see paper)
28% identity, 86% coverage: 61:508/519 of query aligns to 5683:6147/6486 of O30409
Sites not aligning to the query:
- 3075 modified: O-(pantetheine 4'-phosphoryl)serine
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
25% identity, 85% coverage: 56:497/519 of query aligns to 27:494/504 of 6qjzA
- active site: T169 (= T179), S189 (≠ R199), H213 (≠ W223), T314 (≠ S320), E315 (= E321), N414 (= N419), K419 (≠ R424)
- binding adenosine monophosphate: H213 (≠ W223), S288 (≠ G294), A289 (≠ E295), S290 (≠ A296), A312 (≠ G318), M313 (= M319), T314 (≠ S320), D393 (= D398), L405 (≠ Y410), K410 (≠ D415), K419 (≠ R424)
P9WQ37 Long-chain-fatty-acid--CoA ligase FadD13; Fatty acyl-CoA ligase; FACL; FACL13; Fatty acyl-CoA synthetase; ACS; FACS; Very-long-chain fatty-acyl-CoA synthetase; ACSVL; EC 6.2.1.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
27% identity, 88% coverage: 58:514/519 of query aligns to 28:499/503 of P9WQ37
- K172 (≠ R187) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ G210) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ E212) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ T224) mutation to D: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced. Slight increase of susceptibility to proteolysis.
- A211 (≠ T226) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V229) mutation to W: Shows a marked decrease in the activity with lauric and palmitic acid (C12 and C16 fatty acid) with a simultaneous increase in the activity with caprylic acid (C8 fatty acid).
- R244 (≠ G261) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G318) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.; mutation to W: Does not show activity with small, medium or long acyl chains.
- W377 (= W393) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding. No significant change in the total expression level, however the cytoplasmic expression is low. Slight increase of susceptibility to proteolysis.
- D382 (= D398) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced.
- R397 (= R413) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ A420) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G422) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K502) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
Sites not aligning to the query:
- 9 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- 17 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
Query Sequence
>3608151 FitnessBrowser__Dino:3608151
MSGDLQPRRAGPSTGVMPLPDDFDPAAPCPAPFNLAGYVLAAGDEDKIALEVLGGGAVRW
TFGDLRRAVAGYAAALRTEGLAPGDKLLMRLGNTVEFPLLFLAAVAAGVVPVPTSAALTV
EEVDWIAADLAPALTVQAPGVAGPSRGRVVALEALVPDRDAPLAPVPGDPDRMAYVVYTS
GSSGRPRAVAHAHRAIWARRMMWRDWYGMGPEDRILHAGAFNWTYTLGVGLLDPWAMGAT
ALIPEAGTDSAALPEALAASGASIFAAVPGVYRQILKQEALPRLPRLRHGLTAGEALPDS
LRAAWRDRVGTELYEALGMSECSTFISAHPGRQAPPGHAGFAQAGRRIAALDADGVEVAR
GTSGVLGVHRGDPGLMLGYLEGGRPRLPLTGDWFVTGDMVEIASDGAVRYLGRGDDMMNA
GGFRVSPLEVEKAFHGRPEIGEAAAVEVKIKADVTVIALFYVAAAPVTEAALAAEAAQHL
ARYKQPRLYIPVETLPKGRTGKLDRRALRAAYEARHDQA
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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