SitesBLAST
Comparing Pf6N2E2_1143 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1143 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)
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)
34% identity, 91% coverage: 48:553/557 of query aligns to 68:577/577 of Q08AH3
- Q139 (≠ A118) binding
- 221:229 (vs. 200:208, 67% identical) binding
- ESYGQT 359:364 (≠ DHYGQT 339:344) binding
- T364 (= T344) binding
- D446 (= D424) binding
- R461 (= R439) binding
- SGY 469:471 (= SGY 447:449) binding
- R472 (= R450) binding
- R501 (= R479) binding
- S513 (≠ T491) to L: in dbSNP:rs1133607
- K532 (≠ R508) binding
- YPR 540:542 (= YPR 516:518) binding
- K557 (= K533) binding
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
33% identity, 94% coverage: 18:543/557 of query aligns to 5:534/536 of 3c5eA
- active site: T188 (= T200), T331 (= T344), E332 (= E345), N434 (≠ T445), R439 (= R450), K524 (= K533)
- binding adenosine-5'-triphosphate: T188 (= T200), S189 (= S201), G190 (= G202), T191 (= T203), S192 (≠ T204), G305 (= G318), E306 (= E319), S307 (≠ P320), G329 (= G342), Q330 (= Q343), T331 (= T344), D413 (= D424), F425 (= F436), R428 (= R439), K524 (= K533)
- binding magnesium ion: M450 (≠ I461), H452 (= H463), V455 (= V466)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
33% identity, 94% coverage: 18:543/557 of query aligns to 6:535/537 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)
33% identity, 94% coverage: 18:543/557 of query aligns to 2:531/533 of 3eq6A
- active site: T185 (= T200), T328 (= T344), E329 (= E345), N431 (≠ T445), R436 (= R450), K521 (= K533)
- binding adenosine monophosphate: G302 (= G318), E303 (= E319), S304 (≠ P320), E323 (≠ D339), S324 (≠ H340), Y325 (= Y341), G326 (= G342), Q327 (= Q343), T328 (= T344), D410 (= D424), F422 (= F436), R425 (= R439), R436 (= R450)
- binding Butyryl Coenzyme A: W229 (= W244), F255 (≠ Y265), I277 (≠ T291), V301 (≠ A317), S433 (= S447), G434 (= G448), Y435 (= Y449), P501 (≠ A513), Y502 (≠ H514), Y504 (= Y516), R506 (= R518)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
33% identity, 94% coverage: 18:543/557 of query aligns to 2:531/533 of 2wd9A
- active site: T185 (= T200), T328 (= T344), E329 (= E345), N431 (≠ T445), R436 (= R450), K521 (= K533)
- binding ibuprofen: I230 (≠ A245), L231 (≠ Y246), G326 (= G342), Q327 (= Q343), T328 (= T344), R436 (= R450)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
33% identity, 94% coverage: 18:543/557 of query aligns to 2:531/533 of 2vzeA
- active site: T185 (= T200), T328 (= T344), E329 (= E345), N431 (≠ T445), R436 (= R450), K521 (= K533)
- binding adenosine monophosphate: W229 (= W244), G302 (= G318), E303 (= E319), S304 (≠ P320), E323 (≠ D339), Y325 (= Y341), G326 (= G342), Q327 (= Q343), T328 (= T344), D410 (= D424), F422 (= F436), R425 (= R439), R436 (= R450)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
35% identity, 88% coverage: 46:536/557 of query aligns to 54:539/562 of 8biqA
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
35% identity, 88% coverage: 46:536/557 of query aligns to 55:540/562 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 (≠ Y249), G321 (= G318), E322 (= E319), P323 (= P320), D342 (= D339), F343 (≠ H340), Y344 (= Y341), Q346 (= Q343), T347 (= T344), D428 (= D424), F440 (= F436), K449 (≠ T445), R454 (= R450)
- binding coenzyme a: N128 (≠ A118), W247 (= W244), K249 (≠ Y246), K273 (≠ P268), L274 (≠ F269), Q300 (≠ L295), D452 (≠ G448), Y453 (= Y449), R483 (= R479), P517 (≠ A513)
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
35% identity, 88% coverage: 46:536/557 of query aligns to 53:538/561 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 (= G318), E320 (= E319), P321 (= P320), D340 (= D339), F341 (≠ H340), Y342 (= Y341), G343 (= G342), Q344 (= Q343), T345 (= T344), D426 (= D424), F438 (= F436), K447 (≠ T445), R452 (= R450)
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
33% identity, 94% coverage: 18:543/557 of query aligns to 3:530/532 of 3gpcA
- active site: T186 (= T200), T327 (= T344), E328 (= E345), N430 (≠ T445), R435 (= R450), K520 (= K533)
- binding coenzyme a: G301 (= G318), E302 (= E319), S303 (≠ P320), E322 (≠ D339), Y324 (= Y341), G325 (= G342), Q326 (= Q343), T327 (= T344), D409 (= D424), F421 (= F436), R424 (= R439), T516 (= T529), K520 (= K533), Q522 (= Q535)
- binding magnesium ion: H448 (= H463), V451 (= V466)
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
33% identity, 94% coverage: 18:543/557 of query aligns to 6:533/535 of 3dayA
- active site: T189 (= T200), T332 (= T344), E333 (= E345), N435 (≠ T445), R440 (= R450), K523 (= K533)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T200), S190 (= S201), G191 (= G202), T192 (= T203), S193 (≠ T204), K197 (= K208), G306 (= G318), E307 (= E319), S308 (≠ P320), Y329 (= Y341), G330 (= G342), Q331 (= Q343), T332 (= T344), D414 (= D424), F426 (= F436), R429 (= R439), K523 (= K533)
- binding magnesium ion: M451 (≠ I461), H453 (= H463), V456 (= V466)
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)
31% identity, 92% coverage: 31:541/557 of query aligns to 75:617/652 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 (≠ Y246) binding
- N335 (vs. gap) binding
- A357 (≠ S289) 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 (= D441) 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 (= S447) binding
- G524 (= G448) 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 (= R450) 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 (= R508) 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 (= K533) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
31% identity, 92% coverage: 31:541/557 of query aligns to 70:612/637 of 2p2fA
- active site: T259 (= T200), T411 (= T344), E412 (= E345), N516 (≠ T445), R521 (= R450), K604 (= K533)
- binding adenosine monophosphate: G382 (= G318), E383 (= E319), P384 (= P320), T407 (≠ H340), W408 (≠ Y341), W409 (≠ G342), Q410 (= Q343), T411 (= T344), D495 (= D424), I507 (≠ F436), R510 (= R439), N516 (≠ T445), R521 (= R450)
- binding coenzyme a: F158 (= F116), R186 (vs. gap), W304 (= W244), T306 (≠ Y246), P329 (vs. gap), A352 (≠ S289), A355 (= A292), S518 (= S447), R579 (= R508), P584 (≠ A513)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
31% identity, 92% coverage: 31:541/557 of query aligns to 71:613/640 of 5jrhA
- active site: T260 (= T200), T412 (= T344), E413 (= E345), N517 (≠ T445), R522 (= R450), K605 (= K533)
- binding (r,r)-2,3-butanediol: W93 (= W51), E140 (= E97), G169 (≠ H126), K266 (≠ P206), P267 (≠ A207)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G318), E384 (= E319), P385 (= P320), T408 (≠ H340), W409 (≠ Y341), W410 (≠ G342), Q411 (= Q343), T412 (= T344), D496 (= D424), I508 (≠ F436), N517 (≠ T445), R522 (= R450)
- binding coenzyme a: F159 (= F116), G160 (≠ T117), G161 (≠ A118), R187 (vs. gap), S519 (= S447), R580 (= R508), P585 (≠ A513)
- binding magnesium ion: V533 (≠ I461), H535 (= H463), I538 (≠ V466)
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)
31% identity, 92% coverage: 31:541/557 of query aligns to 75:617/652 of P27550
- K609 (= K533) modified: N6-acetyllysine; by autocatalysis
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
31% identity, 92% coverage: 31:541/557 of query aligns to 71:613/641 of 2p20A
- active site: T260 (= T200), T412 (= T344), E413 (= E345), N517 (≠ T445), R522 (= R450), K605 (= K533)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G318), E384 (= E319), P385 (= P320), T408 (≠ H340), W409 (≠ Y341), W410 (≠ G342), Q411 (= Q343), T412 (= T344), D496 (= D424), I508 (≠ F436), R511 (= R439), R522 (= R450)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
31% identity, 92% coverage: 31:541/557 of query aligns to 71:613/634 of 1pg3A
- active site: T260 (= T200), T412 (= T344), E413 (= E345), N517 (≠ T445), R522 (= R450), K605 (= K533)
- binding coenzyme a: F159 (= F116), G160 (≠ T117), R187 (vs. gap), R190 (vs. gap), A301 (= A240), T307 (≠ Y246), P330 (vs. gap), A356 (= A292), S519 (= S447), R580 (= R508), P585 (≠ A513)
- binding magnesium ion: V533 (≠ I461), H535 (= H463), I538 (≠ V466)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G318), E384 (= E319), P385 (= P320), T408 (≠ H340), W409 (≠ Y341), W410 (≠ G342), Q411 (= Q343), T412 (= T344), D496 (= D424), R511 (= R439), R522 (= R450)
P78773 Probable acetyl-coenzyme A synthetase; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
31% identity, 92% coverage: 30:541/557 of query aligns to 84:626/662 of P78773
- T596 (≠ R510) modified: Phosphothreonine
Q89WV5 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110) (see paper)
31% identity, 92% coverage: 31:541/557 of query aligns to 74:614/648 of Q89WV5
- G263 (= G202) mutation to I: Loss of activity.
- G266 (= G205) mutation to I: Great decrease in activity.
- K269 (= K208) mutation to G: Great decrease in activity.
- E414 (= E345) mutation to Q: Great decrease in activity.
P9WQD1 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
32% identity, 92% coverage: 31:541/557 of query aligns to 73:625/651 of P9WQD1
- K617 (= K533) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
Query Sequence
>Pf6N2E2_1143 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1143
MLVMRDYSSATSQFDYLQTVNAALHGSLEALNACVECCDRHALPGRIALFWEGRDGSDAT
WTYRDLQDNAARFANFLRAQGVGKGDKVAGLLPRTAELLIVVLATWRIGAVYQPLFTAFG
PKAIEHRVGSSGARIVVTDAVNRPKLNEIAGCPTIVTVGGEKGQGIVRGDYSFWAEVANH
SSQCEPLMLTGEDPFLLMFTSGTTGPAKALSVPLKAIVAFQSYTRDAVDLRPEDAFWNVA
DPGWAYGIYFGVTGPLAMGHPITFYDGPFTLESTCRVINKYGITNLTGSPTAYRLLIAGG
EQFARSIKGKLRIVSSAGEPLNPEVIRWFADNLNVVIHDHYGQTELGMVLCNHHGLEHPV
HLGAAGFASPGHRIVVLDENQRELGVGQPGILAVDRSQSPMCWFAGYEGAPTKAFVGDYY
LSGDTVELNLDGSISFVGRSDDVITTSGYRVGPFDVESALIEHPAVVEAAVIGKPDPERT
ELVKAFVVLSTQYRASPELAEELRLHVRKRLAAHAYPREIEFVSDLPKTPSGKLQRFILR
NQEIAKAQEAAAQNVSA
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