SitesBLAST
Comparing GFF3565 FitnessBrowser__WCS417:GFF3565 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)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
31% identity, 94% coverage: 24:535/546 of query aligns to 67:613/640 of 5jrhA
- active site: T260 (= T194), T412 (= T338), E413 (= E339), N517 (≠ T439), R522 (= R444), K605 (= K527)
- binding (r,r)-2,3-butanediol: W93 (≠ C48), E140 (= E94), G169 (≠ Q123), K266 (≠ P200), P267 (≠ A201)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G312), E384 (= E313), P385 (= P314), T408 (≠ H334), W409 (≠ Y335), W410 (≠ G336), Q411 (= Q337), T412 (= T338), D496 (= D418), I508 (≠ F430), N517 (≠ T439), R522 (= R444)
- binding coenzyme a: F159 (= F113), G160 (≠ T114), G161 (≠ A115), R187 (vs. gap), S519 (= S441), R580 (= R502), P585 (≠ A507)
- binding magnesium ion: V533 (≠ I455), H535 (= H457), I538 (≠ V460)
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, 94% coverage: 24:535/546 of query aligns to 71:617/652 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 (≠ Y240) binding
- N335 (≠ A264) binding
- A357 (≠ S283) 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 (= D435) 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 (= S441) binding
- G524 (= G442) 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 (= R444) 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 (= R502) 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 (= K527) 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, 94% coverage: 24:535/546 of query aligns to 66:612/637 of 2p2fA
- active site: T259 (= T194), T411 (= T338), E412 (= E339), N516 (≠ T439), R521 (= R444), K604 (= K527)
- binding adenosine monophosphate: G382 (= G312), E383 (= E313), P384 (= P314), T407 (≠ H334), W408 (≠ Y335), W409 (≠ G336), Q410 (= Q337), T411 (= T338), D495 (= D418), I507 (≠ F430), R510 (= R433), N516 (≠ T439), R521 (= R444)
- binding coenzyme a: F158 (= F113), R186 (vs. gap), W304 (= W238), T306 (≠ Y240), P329 (≠ F263), A352 (≠ S283), A355 (= A286), S518 (= S441), R579 (= R502), P584 (≠ A507)
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, 94% coverage: 24:535/546 of query aligns to 71:617/652 of P27550
- K609 (= K527) modified: N6-acetyllysine; by autocatalysis
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
30% identity, 94% coverage: 24:535/546 of query aligns to 67:613/641 of 2p20A
- active site: T260 (= T194), T412 (= T338), E413 (= E339), N517 (≠ T439), R522 (= R444), K605 (= K527)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G312), E384 (= E313), P385 (= P314), T408 (≠ H334), W409 (≠ Y335), W410 (≠ G336), Q411 (= Q337), T412 (= T338), D496 (= D418), I508 (≠ F430), R511 (= R433), R522 (= R444)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
30% identity, 94% coverage: 24:535/546 of query aligns to 67:613/634 of 1pg3A
- active site: T260 (= T194), T412 (= T338), E413 (= E339), N517 (≠ T439), R522 (= R444), K605 (= K527)
- binding coenzyme a: F159 (= F113), G160 (≠ T114), R187 (vs. gap), R190 (vs. gap), A301 (= A234), T307 (≠ Y240), P330 (≠ F263), A356 (= A286), S519 (= S441), R580 (= R502), P585 (≠ A507)
- binding magnesium ion: V533 (≠ I455), H535 (= H457), I538 (≠ V460)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G312), E384 (= E313), P385 (= P314), T408 (≠ H334), W409 (≠ Y335), W410 (≠ G336), Q411 (= Q337), T412 (= T338), D496 (= D418), R511 (= R433), R522 (= R444)
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, 90% coverage: 45:537/546 of query aligns to 32:531/533 of 3eq6A
- active site: T185 (= T194), T328 (= T338), E329 (= E339), N431 (≠ T439), R436 (= R444), K521 (= K527)
- binding adenosine monophosphate: G302 (= G312), E303 (= E313), S304 (≠ P314), E323 (≠ D333), S324 (≠ H334), Y325 (= Y335), G326 (= G336), Q327 (= Q337), T328 (= T338), D410 (= D418), F422 (= F430), R425 (= R433), R436 (= R444)
- binding Butyryl Coenzyme A: W229 (= W238), F255 (= F263), I277 (≠ T285), V301 (≠ A311), S433 (= S441), G434 (= G442), Y435 (= Y443), P501 (≠ A507), Y502 (≠ H508), Y504 (= Y510), R506 (= R512)
2wd9A Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with ibuprofen (see paper)
33% identity, 90% coverage: 45:537/546 of query aligns to 32:531/533 of 2wd9A
- active site: T185 (= T194), T328 (= T338), E329 (= E339), N431 (≠ T439), R436 (= R444), K521 (= K527)
- binding ibuprofen: I230 (≠ A239), L231 (≠ Y240), G326 (= G336), Q327 (= Q337), T328 (= T338), R436 (= R444)
2vzeA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp (see paper)
33% identity, 90% coverage: 45:537/546 of query aligns to 32:531/533 of 2vzeA
- active site: T185 (= T194), T328 (= T338), E329 (= E339), N431 (≠ T439), R436 (= R444), K521 (= K527)
- binding adenosine monophosphate: W229 (= W238), G302 (= G312), E303 (= E313), S304 (≠ P314), E323 (≠ D333), Y325 (= Y335), G326 (= G336), Q327 (= Q337), T328 (= T338), D410 (= D418), F422 (= F430), R425 (= R433), R436 (= R444)
3b7wA Crystal structure of human acyl-coa synthetase medium-chain family member 2a, with l64p mutation (see paper)
33% identity, 90% coverage: 45:537/546 of query aligns to 36:535/537 of 3b7wA
3c5eA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with atp (see paper)
33% identity, 90% coverage: 45:537/546 of query aligns to 35:534/536 of 3c5eA
- active site: T188 (= T194), T331 (= T338), E332 (= E339), N434 (≠ T439), R439 (= R444), K524 (= K527)
- binding adenosine-5'-triphosphate: T188 (= T194), S189 (= S195), G190 (= G196), T191 (= T197), S192 (≠ T198), G305 (= G312), E306 (= E313), S307 (≠ P314), G329 (= G336), Q330 (= Q337), T331 (= T338), D413 (= D418), F425 (= F430), R428 (= R433), K524 (= K527)
- binding magnesium ion: M450 (≠ I455), H452 (= H457), V455 (= V460)
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)
33% identity, 90% coverage: 45:537/546 of query aligns to 68:567/577 of Q08AH3
- Q139 (≠ A115) binding
- 221:229 (vs. 194:202, 67% identical) binding
- ESYGQT 359:364 (≠ DHYGQT 333:338) binding
- T364 (= T338) binding
- D446 (= D418) binding
- R461 (= R433) binding
- SGY 469:471 (= SGY 441:443) binding
- R472 (= R444) binding
- R501 (= R473) binding
- S513 (= S485) to L: in dbSNP:rs1133607
- K532 (≠ R502) binding
- YPR 540:542 (= YPR 510:512) binding
- K557 (= K527) binding
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)
33% identity, 93% coverage: 28:535/546 of query aligns to 73:625/651 of P9WQD1
- K617 (= K527) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
3dayA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in complex with amp-cpp (see paper)
33% identity, 90% coverage: 45:537/546 of query aligns to 36:533/535 of 3dayA
- active site: T189 (= T194), T332 (= T338), E333 (= E339), N435 (≠ T439), R440 (= R444), K523 (= K527)
- binding diphosphomethylphosphonic acid adenosyl ester: T189 (= T194), S190 (= S195), G191 (= G196), T192 (= T197), S193 (≠ T198), K197 (= K202), G306 (= G312), E307 (= E313), S308 (≠ P314), Y329 (= Y335), G330 (= G336), Q331 (= Q337), T332 (= T338), D414 (= D418), F426 (= F430), R429 (= R433), K523 (= K527)
- binding magnesium ion: M451 (≠ I455), H453 (= H457), V456 (= V460)
3gpcA Crystal structure of human acyl-coa synthetase medium-chain family member 2a (l64p mutation) in a complex with coa (see paper)
33% identity, 90% coverage: 45:537/546 of query aligns to 33:530/532 of 3gpcA
- active site: T186 (= T194), T327 (= T338), E328 (= E339), N430 (≠ T439), R435 (= R444), K520 (= K527)
- binding coenzyme a: G301 (= G312), E302 (= E313), S303 (≠ P314), E322 (≠ D333), Y324 (= Y335), G325 (= G336), Q326 (= Q337), T327 (= T338), D409 (= D418), F421 (= F430), R424 (= R433), T516 (= T523), K520 (= K527), Q522 (= Q529)
- binding magnesium ion: H448 (= H457), V451 (= V460)
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, 93% coverage: 26:535/546 of query aligns to 83:626/662 of P78773
- T596 (≠ R504) modified: Phosphothreonine
8biqB Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
32% identity, 95% coverage: 11:530/546 of query aligns to 35:538/561 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 (= G312), E320 (= E313), P321 (= P314), D340 (= D333), F341 (≠ H334), Y342 (= Y335), G343 (= G336), Q344 (= Q337), T345 (= T338), D426 (= D418), F438 (= F430), K447 (≠ T439), R452 (= R444)
8biqA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with acetyl-amp
32% identity, 95% coverage: 11:530/546 of query aligns to 36:539/562 of 8biqA
8bitA Crystal structure of acyl-coa synthetase from metallosphaera sedula in complex with coenzyme a and acetyl-amp
32% identity, 95% coverage: 11:530/546 of query aligns to 37:540/562 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 (≠ Y243), G321 (= G312), E322 (= E313), P323 (= P314), D342 (= D333), F343 (≠ H334), Y344 (= Y335), Q346 (= Q337), T347 (= T338), D428 (= D418), F440 (= F430), K449 (≠ T439), R454 (= R444)
- binding coenzyme a: N128 (≠ A115), W247 (= W238), K249 (≠ Y240), K273 (≠ P262), L274 (≠ F263), Q300 (≠ L289), D452 (≠ G442), Y453 (= Y443), R483 (= R473), P517 (≠ A507)
1ry2A Crystal structure of yeast acetyl-coenzyme a synthetase in complex with amp (see paper)
32% identity, 94% coverage: 21:535/546 of query aligns to 54:598/615 of 1ry2A
- active site: T247 (= T194), T399 (= T338), N507 (≠ T439), K590 (= K527)
- binding adenosine monophosphate: G370 (= G312), E371 (= E313), P372 (= P314), T395 (≠ H334), Y396 (= Y335), W397 (≠ G336), Q398 (= Q337), T399 (= T338), D486 (= D418), I498 (≠ F430), R501 (= R433)
Query Sequence
>GFF3565 FitnessBrowser__WCS417:GFF3565
MRDYDSAVTSFNYRQLATQDLHGELAAMNACIECCDRHALGDAVALYCETPDGRATHHTF
SELQAHAARFGNFLREQGVKPGERVAGLMPRTVELLIAILGTWRIGAVYQPLFTAFGPKA
IEQRLGCSEARWIVTDAHNRPKLDDVIDCPRIIVTGAGPRNPDDYDFWTVLDRQQADCVP
ELLDASAPFLLMCTSGTTGPAKPLEVPLSAILAFKGYMRDSIDLREDDHFWNLADPGWAY
GLYYAVTGPLACGRATLFYDGPFAVDSTCRIIAKYAITNLAGSPTAYRLLIAAGAAFADT
VRGRLRVISSAGEPLNPQVIRWFADELGVVIHDHYGQTEIGMVLCNHHGLRHPVREGSAG
YAVPGYRIVVLDDAHRELPPGRPGVLAVDRERSPLCWFEGYFGMPTQAFVDRYYLSGDIV
ELNDDGSISFVGRNDDVITTSGYRVGPFDVESALIEHPAVVEAAVIGKPDPQRTELIKAF
VVLNSQSLPSTELAEVLRLHVRQRLAAHAYPREIEFVEHLPKTPSGKLQRFILRNQEIAK
QQAFDT
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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