SitesBLAST
Comparing CA265_RS16340 FitnessBrowser__Pedo557:CA265_RS16340 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)
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)
58% identity, 98% coverage: 7:625/631 of query aligns to 22:642/652 of P27550
- K609 (= K592) modified: N6-acetyllysine; by autocatalysis
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)
57% identity, 98% coverage: 7:625/631 of query aligns to 22:642/652 of Q8ZKF6
- R194 (≠ K178) 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 (= T293) binding
- N335 (≠ T317) binding
- A357 (= A339) 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 (= D500) 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 (= S506) binding
- G524 (= G507) 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 (= R509) 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 (≠ T567) 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 (= K592) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
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)
55% identity, 98% coverage: 8:625/631 of query aligns to 22:639/648 of Q89WV5
- G263 (= G248) mutation to I: Loss of activity.
- G266 (= G251) mutation to I: Great decrease in activity.
- K269 (= K254) mutation to G: Great decrease in activity.
- E414 (= E399) mutation to Q: Great decrease in activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
57% identity, 98% coverage: 7:625/631 of query aligns to 18:636/641 of 2p20A
- active site: T260 (= T246), T412 (= T398), E413 (= E399), N517 (= N504), R522 (= R509), K605 (= K592)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G369), E384 (= E370), P385 (= P371), T408 (= T394), W409 (= W395), W410 (= W396), Q411 (= Q397), T412 (= T398), D496 (= D483), I508 (= I495), R511 (= R498), R522 (= R509)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
56% identity, 98% coverage: 7:625/631 of query aligns to 18:635/640 of 5jrhA
- active site: T260 (= T246), T412 (= T398), E413 (= E399), N517 (= N504), R522 (= R509), K605 (= K592)
- binding (r,r)-2,3-butanediol: W93 (= W80), E140 (= E128), G169 (≠ D157), K266 (= K252), P267 (= P253)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G369), E384 (= E370), P385 (= P371), T408 (= T394), W409 (= W395), W410 (= W396), Q411 (= Q397), T412 (= T398), D496 (= D483), I508 (= I495), N517 (= N504), R522 (= R509)
- binding coenzyme a: F159 (= F147), G160 (= G148), G161 (= G149), R187 (= R175), S519 (= S506), R580 (≠ T567), P585 (≠ A572)
- binding magnesium ion: V533 (≠ N520), H535 (= H522), I538 (≠ V525)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
56% identity, 98% coverage: 7:625/631 of query aligns to 17:632/637 of 2p2fA
- active site: T259 (= T246), T411 (= T398), E412 (= E399), N516 (= N504), R521 (= R509), K604 (= K592)
- binding adenosine monophosphate: G382 (= G369), E383 (= E370), P384 (= P371), T407 (= T394), W408 (= W395), W409 (= W396), Q410 (= Q397), T411 (= T398), D495 (= D483), I507 (= I495), R510 (= R498), N516 (= N504), R521 (= R509)
- binding coenzyme a: F158 (= F147), R186 (= R175), W304 (= W291), T306 (= T293), P329 (= P316), A352 (= A339), A355 (= A342), S518 (= S506), R579 (≠ T567), P584 (≠ A572)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
55% identity, 98% coverage: 7:625/631 of query aligns to 18:629/634 of 1pg3A
- active site: T260 (= T246), T412 (= T398), E413 (= E399), N517 (= N504), R522 (= R509), K605 (= K592)
- binding coenzyme a: F159 (= F147), G160 (= G148), R187 (= R175), R190 (≠ K178), A301 (= A287), T307 (= T293), P330 (= P316), A356 (= A342), S519 (= S506), R580 (≠ T567), P585 (≠ A572)
- binding magnesium ion: V533 (≠ N520), H535 (= H522), I538 (≠ V525)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G369), E384 (= E370), P385 (= P371), T408 (= T394), W409 (= W395), W410 (= W396), Q411 (= Q397), T412 (= T398), D496 (= D483), R511 (= R498), R522 (= R509)
Q9NUB1 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 Homo sapiens (Human) (see 3 papers)
51% identity, 98% coverage: 15:630/631 of query aligns to 64:680/689 of Q9NUB1
- V488 (≠ I438) to M: in dbSNP:rs6050249
- K642 (= K592) modified: N6-acetyllysine; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
8u2rA Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (ethyl amp bound)
53% identity, 98% coverage: 13:631/631 of query aligns to 28:662/664 of 8u2rA
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I323 (= I292), G400 (= G369), E401 (= E370), P402 (= P371), T425 (= T394), W426 (= W395), W427 (= W396), Q428 (= Q397), T429 (= T398), D513 (= D483), I525 (= I495), R528 (= R498), R539 (= R509)
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)
50% identity, 98% coverage: 15:630/631 of query aligns to 57:673/682 of Q99NB1
- K635 (= K592) modified: N6-acetyllysine
8sf3A Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (amp, acetate and coa bound)
53% identity, 98% coverage: 13:631/631 of query aligns to 29:660/662 of 8sf3A
- binding adenosine monophosphate: G398 (= G369), E399 (= E370), P400 (= P371), T423 (= T394), W424 (= W395), Q426 (= Q397), T427 (= T398), D511 (= D483), R526 (= R498), R537 (= R509)
- binding coenzyme a: F171 (= F147), G172 (= G148), G173 (= G149), R199 (= R175), K202 (= K178), R595 (≠ T567), P600 (≠ A572)
Q9NR19 Acetyl-coenzyme A synthetase, cytoplasmic; Acetate--CoA ligase; Acetyl-CoA synthetase; ACS; AceCS; Acetyl-CoA synthetase 1; AceCS1; Acyl-CoA synthetase short-chain family member 2; Acyl-activating enzyme; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Homo sapiens (Human) (see paper)
50% identity, 99% coverage: 2:626/631 of query aligns to 40:694/701 of Q9NR19
- T363 (= T293) mutation to A: Loss of catlytic activity but no effect on its nuclear translocation upon glucose deprivation. Loss of ability to promote gene transcription for lysosomal biogenesis and autophagy.
- 656:668 (vs. 587:599, 92% identical) Nuclear localization signal
- S659 (= S590) modified: Phosphoserine; by AMPK; mutation to A: No effect on catalytic activity. Loss of AMPK-mediated phosphorylation, interaction with KPNA1 and nuclear translocation upon glucose deprivation. Loss of ability to promote gene transcription for lysosomal biogenesis and autophagy.
- RR 664:665 (= RR 595:596) mutation to AA: No effect on catalytic activity. Loss of interaction with KPNA1 and nuclear translocation upon glucose deprivation. Loss of ability to promote gene transcription for lysosomal biogenesis and autophagy.
Sites not aligning to the query:
- 1:107 Interaction with TFEB
Q9QXG4 Acetyl-coenzyme A synthetase, cytoplasmic; Acetate--CoA ligase; Acetyl-CoA synthetase; ACS; AceCS; Acetyl-CoA synthetase 1; AceCS1; Acyl-CoA synthetase short-chain family member 2; Acyl-activating enzyme; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Mus musculus (Mouse) (see paper)
50% identity, 99% coverage: 2:626/631 of query aligns to 40:694/701 of Q9QXG4
- K661 (= K592) modified: N6-acetyllysine
7l4gB Crystal structure of acetyl-coa synthetase in complex with acetyl adenylate from cryptococcus neoformans h99
50% identity, 98% coverage: 5:624/631 of query aligns to 38:663/668 of 7l4gB
- active site: T280 (= T246), T432 (= T398), E433 (= E399), N539 (= N504), R544 (= R509), K631 (= K592)
- 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: W325 (= W291), G403 (= G369), E404 (= E370), P405 (= P371), T428 (= T394), Y429 (≠ W395), W430 (= W396), M431 (≠ Q397), T432 (= T398), D518 (= D483), I530 (= I495), R533 (= R498)
5u29A Crystal structure of cryptococcus neoformans h99 acetyl-coa synthetase in complex with ac-ams
50% identity, 98% coverage: 5:624/631 of query aligns to 38:663/668 of 5u29A
- active site: T280 (= T246), T432 (= T398), E433 (= E399), N539 (= N504), R544 (= R509), K631 (= K592)
- binding 5'-O-(acetylsulfamoyl)adenosine: W325 (= W291), G403 (= G369), E404 (= E370), P405 (= P371), T428 (= T394), Y429 (≠ W395), W430 (= W396), M431 (≠ Q397), T432 (= T398), D518 (= D483), I530 (= I495), R533 (= R498)
8g0vA Crystal structure of acetyl-coa synthetase in complex with a propyne ester amp inhibitor from cryptococcus neoformans h99
50% identity, 98% coverage: 5:624/631 of query aligns to 38:661/666 of 8g0vA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: W323 (= W291), I324 (= I292), V400 (= V368), G401 (= G369), E402 (= E370), P403 (= P371), T426 (= T394), Y427 (≠ W395), W428 (= W396), M429 (≠ Q397), T430 (= T398), D516 (= D483)
8g0uA Crystal structure of acetyl-coa synthetase in complex with an isopropyl ester amp inhibitor from cryptococcus neoformans h99
50% identity, 98% coverage: 5:624/631 of query aligns to 38:661/666 of 8g0uA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: W323 (= W291), I324 (= I292), G401 (= G369), E402 (= E370), P403 (= P371), T426 (= T394), Y427 (≠ W395), W428 (= W396), M429 (≠ Q397), T430 (= T398), D516 (= D483), I528 (= I495), R531 (= R498)
7knoA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate from cryptococcus neoformans var. Grubii serotype a (h99)
50% identity, 98% coverage: 5:624/631 of query aligns to 38:661/666 of 7knoA
- active site: T280 (= T246), T430 (= T398), E431 (= E399), N537 (= N504), R542 (= R509), K629 (= K592)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: W323 (= W291), I324 (= I292), G401 (= G369), E402 (= E370), P403 (= P371), T426 (= T394), Y427 (≠ W395), W428 (= W396), M429 (≠ Q397), T430 (= T398), D516 (= D483), R531 (= R498)
7mmzA Crystal structure of acetyl-coenzyme a synthetase from legionella pneumophila philadelphia 1 in complex with ethyl-amp (see paper)
53% identity, 89% coverage: 22:582/631 of query aligns to 9:559/559 of 7mmzA
- active site: T231 (= T246), T383 (= T398), E384 (= E399), N486 (= N504), R491 (= R509)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I277 (= I292), G354 (= G369), E355 (= E370), P356 (= P371), T379 (= T394), W380 (= W395), W381 (= W396), Q382 (= Q397), T383 (= T398), D465 (= D483), I477 (= I495), R480 (= R498), R491 (= R509)
5k8fA Crystal structure of acetyl-coa synthetase in complex with atp and acetyl-amp from cryptococcus neoformans h99
50% identity, 98% coverage: 5:624/631 of query aligns to 38:651/656 of 5k8fA
- active site: T280 (= T246), T432 (= T398), E433 (= E399), N539 (= N504), R544 (= R509), K631 (= K592)
- 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: W325 (= W291), I326 (= I292), G403 (= G369), E404 (= E370), P405 (= P371), T428 (= T394), Y429 (≠ W395), W430 (= W396), M431 (≠ Q397), T432 (= T398), D518 (= D483), I530 (= I495), R533 (= R498), K631 (= K592)
- binding adenosine-5'-triphosphate: T280 (= T246), S281 (= S247), G282 (= G248), S283 (= S249), T284 (= T250), K288 (= K254), G403 (= G369), E404 (= E370), P405 (= P371), T428 (= T394), Y429 (≠ W395), M431 (≠ Q397), T432 (= T398), D518 (= D483), I530 (= I495), R533 (= R498), K631 (= K592)
Query Sequence
>CA265_RS16340 FitnessBrowser__Pedo557:CA265_RS16340
MQITSFKQYEEDYKKSVENPEQFWGEVAQNFQWRKPWFKVLSWNFNEPNIKWFEGAKLNI
TENCLDRHLATNGDKPAIVWEPNNPEEESVTYTYKMLHERVCRFANVLKRNGAKKGDRIC
IYMPMVPELAIAVLACARIGAVHSVIFGGFSAKSIADRINDSKCKVVITADGSYRGNKQI
PLKDVIDDALIGCPTVEKCIVLTHIRTPVSMLKGRDVWWEDEVKHVNDICEAEEMDAEDM
LFILYTSGSTGKPKGVVHTCGGYMVYAGYTFSNVFNYQPGEVYFCTADIGWITGHSYIVY
GPLSQGATSVLFEGIPTYPTPSRFWDIVEKHKVNTLYTAPTAIRSLMSYGDDPLNGKDLS
SIRVLGSVGEPINEEAWHWFDEKIGHGKAPIVDTWWQTETGGIMISPIATVTPTKPSFAT
LPLPGIQPILVDENGNEIEGNGVMGNLCIKFPWPGMLRTTYGDHERCKQTYFSTYDNLYF
TGDGCLRDEDGYYRITGRVDDVLNVSGHRIGTAEVENAINMHAGVVESAVVGYPHDVKGQ
GIYAFVIYPEMHGEAELSKKDILQTVTRVIGAIAKPDKILFVSGLPKTRSGKIMRRILRK
IAEGDTSNLGDTSTLLDPGVVEEIIAAAKKL
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