SitesBLAST
Comparing AZOBR_RS19780 FitnessBrowser__azobra:AZOBR_RS19780 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)
35% identity, 96% coverage: 19:537/538 of query aligns to 8:534/537 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)
35% identity, 96% coverage: 19:537/538 of query aligns to 4:530/533 of 3eq6A
- active site: T185 (= T193), T328 (= T339), E329 (= E340), N431 (≠ T440), R436 (= R445), K521 (= K528)
- binding adenosine monophosphate: G302 (= G312), E303 (≠ G313), S304 (≠ E314), E323 (= E334), S324 (≠ F335), Y325 (= Y336), G326 (= G337), Q327 (= Q338), T328 (= T339), D410 (= D419), F422 (= F431), R425 (= R434), R436 (= R445)
- binding Butyryl Coenzyme A: W229 (= W239), F255 (= F265), I277 (≠ T287), V301 (≠ S311), S433 (≠ A442), G434 (= G443), Y435 (= Y444), P501 (≠ A508), Y502 (≠ H509), Y504 (= Y511), R506 (= R513)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
35% identity, 96% coverage: 19:537/538 of query aligns to 4:530/533 of 2wd9A
- active site: T185 (= T193), T328 (= T339), E329 (= E340), N431 (≠ T440), R436 (= R445), K521 (= K528)
- binding ibuprofen: I230 (= I240), L231 (≠ G241), G326 (= G337), Q327 (= Q338), T328 (= T339), R436 (= R445)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
35% identity, 96% coverage: 19:537/538 of query aligns to 4:530/533 of 2vzeA
- active site: T185 (= T193), T328 (= T339), E329 (= E340), N431 (≠ T440), R436 (= R445), K521 (= K528)
- binding adenosine monophosphate: W229 (= W239), G302 (= G312), E303 (≠ G313), S304 (≠ E314), E323 (= E334), Y325 (= Y336), G326 (= G337), Q327 (= Q338), T328 (= T339), D410 (= D419), F422 (= F431), R425 (= R434), R436 (= R445)
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
35% identity, 96% coverage: 19:537/538 of query aligns to 7:533/536 of 3c5eA
- active site: T188 (= T193), T331 (= T339), E332 (= E340), N434 (≠ T440), R439 (= R445), K524 (= K528)
- binding adenosine-5'-triphosphate: T188 (= T193), S189 (= S194), G190 (= G195), T191 (= T196), S192 (≠ T197), G305 (= G312), E306 (≠ G313), S307 (≠ E314), G329 (= G337), Q330 (= Q338), T331 (= T339), D413 (= D419), F425 (= F431), R428 (= R434), K524 (= K528)
- binding magnesium ion: M450 (≠ I456), H452 (= H458), V455 (= V461)
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)
35% identity, 96% coverage: 19:537/538 of query aligns to 40:566/577 of Q08AH3
- Q139 (≠ L112) binding
- 221:229 (vs. 193:201, 78% identical) binding
- ESYGQT 359:364 (≠ EFYGQT 334:339) binding
- T364 (= T339) binding
- D446 (= D419) binding
- R461 (= R434) binding
- SGY 469:471 (≠ AGY 442:444) binding
- R472 (= R445) binding
- R501 (= R474) binding
- S513 (≠ D486) to L: in dbSNP:rs1133607
- K532 (= K503) binding
- YPR 540:542 (= YPR 511:513) binding
- K557 (= K528) binding
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
35% identity, 96% coverage: 19:537/538 of query aligns to 5:529/532 of 3gpcA
- active site: T186 (= T193), T327 (= T339), E328 (= E340), N430 (≠ T440), R435 (= R445), K520 (= K528)
- binding coenzyme a: G301 (= G312), E302 (≠ G313), S303 (≠ E314), E322 (= E334), Y324 (= Y336), G325 (= G337), Q326 (= Q338), T327 (= T339), D409 (= D419), F421 (= F431), R424 (= R434), T516 (= T524), K520 (= K528), Q522 (≠ I530)
- binding magnesium ion: H448 (= H458), V451 (= V461)
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
35% identity, 96% coverage: 19:537/538 of query aligns to 8:532/535 of 3dayA
- active site: T189 (= T193), T332 (= T339), E333 (= E340), N435 (≠ T440), R440 (= R445), K523 (= K528)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T193), S190 (= S194), G191 (= G195), T192 (= T196), S193 (≠ T197), K197 (= K201), G306 (= G312), E307 (≠ G313), S308 (≠ E314), Y329 (= Y336), G330 (= G337), Q331 (= Q338), T332 (= T339), D414 (= D419), F426 (= F431), R429 (= R434), K523 (= K528)
- binding magnesium ion: M451 (≠ I456), H453 (= H458), V456 (= V461)
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
35% identity, 95% coverage: 22:534/538 of query aligns to 34:541/561 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 (= G313), E320 (= E314), P321 (≠ T315), D340 (≠ E334), F341 (= F335), Y342 (= Y336), G343 (= G337), Q344 (= Q338), T345 (= T339), D426 (= D419), F438 (= F431), K447 (≠ T440), R452 (= R445)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
35% identity, 95% coverage: 22:534/538 of query aligns to 35:542/562 of 8biqA
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
35% identity, 95% coverage: 22:534/538 of query aligns to 36:543/562 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 (= W239), G321 (= G313), E322 (= E314), P323 (≠ T315), D342 (≠ E334), F343 (= F335), Y344 (= Y336), Q346 (= Q338), T347 (= T339), D428 (= D419), F440 (= F431), K449 (≠ T440), R454 (= R445)
- binding coenzyme a: N128 (≠ L112), W247 (= W232), K249 (≠ D236), K273 (= K264), L274 (≠ F265), Q300 (≠ M291), D452 (≠ G443), Y453 (= Y444), R483 (= R474), P517 (≠ A508)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
32% identity, 96% coverage: 19:535/538 of query aligns to 6:509/518 of 4wv3B
- active site: S175 (≠ T193), T320 (= T339), E321 (= E340), K418 (≠ T440), W423 (≠ R445), K502 (= K528)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ W239), T221 (≠ I240), F222 (≠ G241), A293 (≠ G312), S294 (≠ G313), E295 (= E314), A296 (≠ T315), G316 (≠ F335), I317 (≠ Y336), G318 (= G337), C319 (≠ Q338), T320 (= T339), D397 (= D419), H409 (≠ F431), R412 (= R434), K502 (= K528)
P27550 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Escherichia coli (strain K12) (see paper)
29% identity, 95% coverage: 24:535/538 of query aligns to 76:616/652 of P27550
- K609 (= K528) modified: N6-acetyllysine; by autocatalysis
Q99NB1 Acetyl-coenzyme A synthetase 2-like, mitochondrial; Acetate--CoA ligase 2; Acetyl-CoA synthetase 2; AceCS2; Acyl-CoA synthetase short-chain family member 1; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Mus musculus (Mouse) (see paper)
30% identity, 96% coverage: 17:535/538 of query aligns to 95:642/682 of Q99NB1
- K635 (= K528) modified: N6-acetyllysine
5gxdA Structure of acryloyl-coa lyase prpe from dinoroseobacter shibae dfl 12
29% identity, 96% coverage: 15:531/538 of query aligns to 42:590/627 of 5gxdA
- active site: T238 (= T193), T390 (= T339), E391 (= E340), N498 (≠ T440), R503 (= R445), K587 (= K528)
- binding adenosine monophosphate: G364 (= G313), E365 (= E314), R366 (≠ T315), H386 (≠ F335), W387 (≠ Y336), W388 (≠ G337), Q389 (= Q338), T390 (= T339), D477 (= D419), I489 (≠ F431), R492 (= R434), N498 (≠ T440), R503 (= R445)
- binding coenzyme a: F139 (= F110), G140 (≠ S111), G141 (≠ L112), E167 (vs. gap), R170 (≠ K139), S279 (≠ A235), K307 (≠ E263), P308 (≠ K264), A332 (≠ P285), T334 (= T287), A363 (≠ G312), A500 (= A442), H502 (≠ Y444), K532 (≠ R474), R562 (≠ K503), P567 (≠ A508), V568 (≠ H509)
7kvyA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate and co-enzyme a from coccidioides immitis rs
29% identity, 96% coverage: 17:535/538 of query aligns to 78:619/633 of 7kvyA
- active site: T271 (= T193), T422 (= T339), E423 (= E340), N529 (≠ T440), R534 (= R445), K612 (= K528)
- binding coenzyme a: F172 (= F110), G174 (≠ L112), R200 (vs. gap), G312 (≠ A235), Y362 (≠ F283), V363 (≠ L284), A364 (≠ P285), S531 (≠ A442), G532 (= G443), R592 (≠ K503), F598 (≠ H509)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: G393 (= G313), E394 (= E314), P395 (≠ T315), T418 (≠ F335), Y419 (= Y336), W420 (≠ G337), Q421 (= Q338), T422 (= T339), D508 (= D419), I520 (≠ F431), R523 (= R434), R534 (= R445)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
28% identity, 95% coverage: 24:535/538 of query aligns to 72:612/640 of 5jrhA
- active site: T260 (= T193), T412 (= T339), E413 (= E340), N517 (≠ T440), R522 (= R445), K605 (= K528)
- binding (r,r)-2,3-butanediol: W93 (≠ H45), E140 (= E91), G169 (≠ Y120), K266 (≠ Q199), P267 (= P200)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G313), E384 (= E314), P385 (≠ T315), T408 (≠ F335), W409 (≠ Y336), W410 (≠ G337), Q411 (= Q338), T412 (= T339), D496 (= D419), I508 (≠ F431), N517 (≠ T440), R522 (= R445)
- binding coenzyme a: F159 (= F110), G160 (≠ S111), G161 (≠ L112), R187 (vs. gap), S519 (≠ A442), R580 (≠ K503), P585 (≠ A508)
- binding magnesium ion: V533 (≠ I456), H535 (= H458), I538 (≠ V461)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
28% identity, 95% coverage: 24:535/538 of query aligns to 71:611/637 of 2p2fA
- active site: T259 (= T193), T411 (= T339), E412 (= E340), N516 (≠ T440), R521 (= R445), K604 (= K528)
- binding adenosine monophosphate: G382 (= G313), E383 (= E314), P384 (≠ T315), T407 (≠ F335), W408 (≠ Y336), W409 (≠ G337), Q410 (= Q338), T411 (= T339), D495 (= D419), I507 (≠ F431), R510 (= R434), N516 (≠ T440), R521 (= R445)
- binding coenzyme a: F158 (= F110), R186 (vs. gap), W304 (= W239), T306 (≠ G241), P329 (vs. gap), A352 (≠ P285), A355 (= A288), S518 (≠ A442), R579 (≠ K503), P584 (≠ A508)
Q8ZKF6 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 4 papers)
28% identity, 95% coverage: 24:535/538 of query aligns to 76:616/652 of Q8ZKF6
- R194 (vs. gap) mutation to A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 3-fold reduction for CoA.; mutation to E: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 2-fold reduction for CoA.
- T311 (≠ G241) binding
- N335 (vs. gap) binding
- A357 (≠ P285) mutation to V: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 3-fold reduction for CoA.
- D517 (= D436) mutation to G: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 10-fold reduction for CoA.; mutation to P: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold reduction in the affinity for ATP and 4.5-fold reduction for CoA.
- S523 (≠ A442) binding
- G524 (= G443) mutation to L: No acetyl-coenzyme A synthetase activity.; mutation to S: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. Almost the same affinity as the wild-type for ATP, but 9-fold reduction in the affinity for CoA.
- R526 (= R445) mutation to A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 4-fold reduction for CoA.
- R584 (≠ K503) binding ; mutation to A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 7-fold reduction for CoA.; mutation to E: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 8-fold reduction for CoA.
- K609 (= K528) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
28% identity, 95% coverage: 24:535/538 of query aligns to 72:612/641 of 2p20A
- active site: T260 (= T193), T412 (= T339), E413 (= E340), N517 (≠ T440), R522 (= R445), K605 (= K528)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G313), E384 (= E314), P385 (≠ T315), T408 (≠ F335), W409 (≠ Y336), W410 (≠ G337), Q411 (= Q338), T412 (= T339), D496 (= D419), I508 (≠ F431), R511 (= R434), R522 (= R445)
Query Sequence
>AZOBR_RS19780 FitnessBrowser__azobra:AZOBR_RS19780
MLPEADSYEGLRDRFVWSVPERYNIGVDVCDKWAERDPDRTALIHKRRDGAVETHSFADI
RRLSNRLANALAAHGVARGDRVGILLPQAPETAVSHVAVYKMGGVAVPLFSLFGVEALEY
RLGNCGARAVVTDAVGAAKIAQIRDRLPELKLVLRIDEAGEGELDWHALVDAASEDFTPV
DTAADDPAVIIYTSGTTGQPKGALHAHRVLLGHLPGVEISHDLFPQPGDRIWTPADWAWI
GGLLDVLMPAWHHGVTVVSHRFEKFDAEEAFRLIADFQVRNAFLPPTALKMMRAVKDPQT
RWNYSMRSVASGGETLGAELLDWGRQTFGLTINEFYGQTECNMIVSSCATVMPPKPGVMG
RPAPGHDVAVIDGQGNRLPPGEIGLIAVHRPDPVMFLQYWNNPEATAAKFVGDWLVTGDQ
GELDTDGYIRFVGRDDDVITSAGYRIGPGEIEDCLIGHPAVRMAAVVGVPNPLRTEIVKA
FIVLQDGVRPSDALAAEIQAHVKTRLAAHEYPRAVEFVDSLPMTTTGKIIRRELRGRG
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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