SitesBLAST
Comparing GFF4246 FitnessBrowser__WCS417:GFF4246 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)
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)
69% identity, 100% coverage: 1:648/651 of query aligns to 1:648/652 of P27550
- K609 (= K609) 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)
68% identity, 100% coverage: 1:648/651 of query aligns to 1:648/652 of Q8ZKF6
- R194 (≠ K194) 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 (= T311) binding
- N335 (= N335) binding
- A357 (= A357) 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 (= D517) 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 (= S523) binding
- G524 (= G524) 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 (= R526) 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 (= R584) 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 (= K609) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
70% identity, 97% coverage: 13:643/651 of query aligns to 9:636/640 of 5jrhA
- active site: T260 (= T264), T412 (= T416), E413 (= E417), N517 (= N521), R522 (= R526), K605 (= K609)
- binding (r,r)-2,3-butanediol: W93 (= W97), E140 (= E144), G169 (= G173), K266 (= K270), P267 (= P271)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G387), E384 (= E388), P385 (= P389), T408 (= T412), W409 (= W413), W410 (= W414), Q411 (= Q415), T412 (= T416), D496 (= D500), I508 (= I512), N517 (= N521), R522 (= R526)
- binding coenzyme a: F159 (= F163), G160 (= G164), G161 (= G165), R187 (= R191), S519 (= S523), R580 (= R584), P585 (= P589)
- binding magnesium ion: V533 (= V537), H535 (= H539), I538 (≠ V542)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
69% identity, 97% coverage: 13:643/651 of query aligns to 9:637/641 of 2p20A
- active site: T260 (= T264), T412 (= T416), E413 (= E417), N517 (= N521), R522 (= R526), K605 (= K609)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G387), E384 (= E388), P385 (= P389), T408 (= T412), W409 (= W413), W410 (= W414), Q411 (= Q415), T412 (= T416), D496 (= D500), I508 (= I512), R511 (= R515), R522 (= R526)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
69% identity, 97% coverage: 13:646/651 of query aligns to 8:636/637 of 2p2fA
- active site: T259 (= T264), T411 (= T416), E412 (= E417), N516 (= N521), R521 (= R526), K604 (= K609)
- binding adenosine monophosphate: G382 (= G387), E383 (= E388), P384 (= P389), T407 (= T412), W408 (= W413), W409 (= W414), Q410 (= Q415), T411 (= T416), D495 (= D500), I507 (= I512), R510 (= R515), N516 (= N521), R521 (= R526)
- binding coenzyme a: F158 (= F163), R186 (= R191), W304 (= W309), T306 (= T311), P329 (= P334), A352 (= A357), A355 (= A360), S518 (= S523), R579 (= R584), P584 (= P589)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
69% identity, 97% coverage: 13:643/651 of query aligns to 9:630/634 of 1pg3A
- active site: T260 (= T264), T412 (= T416), E413 (= E417), N517 (= N521), R522 (= R526), K605 (= K609)
- binding coenzyme a: F159 (= F163), G160 (= G164), R187 (= R191), R190 (≠ K194), A301 (= A305), T307 (= T311), P330 (= P334), A356 (= A360), S519 (= S523), R580 (= R584), P585 (= P589)
- binding magnesium ion: V533 (= V537), H535 (= H539), I538 (≠ V542)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G387), E384 (= E388), P385 (= P389), T408 (= T412), W409 (= W413), W410 (= W414), Q411 (= Q415), T412 (= T416), D496 (= D500), R511 (= R515), R522 (= R526)
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)
65% identity, 100% coverage: 3:651/651 of query aligns to 2:648/648 of Q89WV5
- G263 (= G266) mutation to I: Loss of activity.
- G266 (= G269) mutation to I: Great decrease in activity.
- K269 (= K272) mutation to G: Great decrease in activity.
- E414 (= E417) mutation to Q: Great decrease in activity.
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)
52% identity, 96% coverage: 23:646/651 of query aligns to 57:679/689 of Q9NUB1
- V488 (≠ I456) to M: in dbSNP:rs6050249
- K642 (= K609) modified: N6-acetyllysine; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
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)
52% identity, 96% coverage: 23:646/651 of query aligns to 50:672/682 of Q99NB1
- K635 (= K609) modified: N6-acetyllysine
7mmzA Crystal structure of acetyl-coenzyme a synthetase from legionella pneumophila philadelphia 1 in complex with ethyl-amp (see paper)
56% identity, 86% coverage: 38:599/651 of query aligns to 10:559/559 of 7mmzA
- active site: T231 (= T264), T383 (= T416), E384 (= E417), N486 (= N521), R491 (= R526)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I277 (≠ V310), G354 (= G387), E355 (= E388), P356 (= P389), T379 (= T412), W380 (= W413), W381 (= W414), Q382 (= Q415), T383 (= T416), D465 (= D500), I477 (= I512), R480 (= R515), R491 (= R526)
8u2rA Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (ethyl amp bound)
51% identity, 96% coverage: 27:648/651 of query aligns to 27:662/664 of 8u2rA
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I323 (≠ V310), G400 (= G387), E401 (= E388), P402 (= P389), T425 (= T412), W426 (= W413), W427 (= W414), Q428 (= Q415), T429 (= T416), D513 (= D500), I525 (= I512), R528 (= R515), R539 (= R526)
8sf3A Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (amp, acetate and coa bound)
51% identity, 96% coverage: 27:648/651 of query aligns to 28:660/662 of 8sf3A
- binding adenosine monophosphate: G398 (= G387), E399 (= E388), P400 (= P389), T423 (= T412), W424 (= W413), Q426 (= Q415), T427 (= T416), D511 (= D500), R526 (= R515), R537 (= R526)
- binding coenzyme a: F171 (= F163), G172 (= G164), G173 (= G165), R199 (= R191), K202 (= K194), R595 (= R584), P600 (= P589)
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)
51% identity, 98% coverage: 8:643/651 of query aligns to 15:652/662 of P78773
- T596 (≠ E586) modified: Phosphothreonine
P52910 Acetyl-coenzyme A synthetase 2; Acetate--CoA ligase 2; Acyl-activating enzyme 2; EC 6.2.1.1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
49% identity, 96% coverage: 18:642/651 of query aligns to 34:670/683 of P52910
- K506 (= K490) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
7l4gB Crystal structure of acetyl-coa synthetase in complex with acetyl adenylate from cryptococcus neoformans h99
52% identity, 93% coverage: 34:641/651 of query aligns to 53:663/668 of 7l4gB
- active site: T280 (= T264), T432 (= T416), E433 (= E417), N539 (= N521), R544 (= R526), K631 (= K609)
- 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 (= W309), G403 (= G387), E404 (= E388), P405 (= P389), T428 (= T412), Y429 (≠ W413), W430 (= W414), M431 (≠ Q415), T432 (= T416), D518 (= D500), I530 (= I512), R533 (= R515)
5u29A Crystal structure of cryptococcus neoformans h99 acetyl-coa synthetase in complex with ac-ams
52% identity, 93% coverage: 34:641/651 of query aligns to 53:663/668 of 5u29A
- active site: T280 (= T264), T432 (= T416), E433 (= E417), N539 (= N521), R544 (= R526), K631 (= K609)
- binding 5'-O-(acetylsulfamoyl)adenosine: W325 (= W309), G403 (= G387), E404 (= E388), P405 (= P389), T428 (= T412), Y429 (≠ W413), W430 (= W414), M431 (≠ Q415), T432 (= T416), D518 (= D500), I530 (= I512), R533 (= R515)
8g0vA Crystal structure of acetyl-coa synthetase in complex with a propyne ester amp inhibitor from cryptococcus neoformans h99
52% identity, 93% coverage: 34:641/651 of query aligns to 53:661/666 of 8g0vA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: W323 (= W309), I324 (≠ V310), V400 (= V386), G401 (= G387), E402 (= E388), P403 (= P389), T426 (= T412), Y427 (≠ W413), W428 (= W414), M429 (≠ Q415), T430 (= T416), D516 (= D500)
8g0uA Crystal structure of acetyl-coa synthetase in complex with an isopropyl ester amp inhibitor from cryptococcus neoformans h99
52% identity, 93% coverage: 34:641/651 of query aligns to 53:661/666 of 8g0uA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: W323 (= W309), I324 (≠ V310), G401 (= G387), E402 (= E388), P403 (= P389), T426 (= T412), Y427 (≠ W413), W428 (= W414), M429 (≠ Q415), T430 (= T416), D516 (= D500), I528 (= I512), R531 (= R515)
7knoA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate from cryptococcus neoformans var. Grubii serotype a (h99)
52% identity, 93% coverage: 34:641/651 of query aligns to 53:661/666 of 7knoA
- active site: T280 (= T264), T430 (= T416), E431 (= E417), N537 (= N521), R542 (= R526), K629 (= K609)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: W323 (= W309), I324 (≠ V310), G401 (= G387), E402 (= E388), P403 (= P389), T426 (= T412), Y427 (≠ W413), W428 (= W414), M429 (≠ Q415), T430 (= T416), D516 (= D500), R531 (= R515)
8w0cA Acetyl-coenzyme A synthetase 2
50% identity, 96% coverage: 18:642/651 of query aligns to 32:658/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G387), E400 (= E388), P401 (= P389), T424 (= T412), Y425 (≠ W413), W426 (= W414), Q427 (= Q415), T428 (= T416), D514 (= D500), R529 (= R515), R540 (= R526)
Query Sequence
>GFF4246 FitnessBrowser__WCS417:GFF4246
MSAASLYPVRPEVAANTLTDEATYKAMYQQSVVNPDGFWREQAKRLDWIKPFTTVKQTSF
DDHHVDIKWFADGTLNVSYNCLDRHLAERGDQAAIIWEGDDPSESRTITYRELHEEVCKF
ANALRGQDVHRGDVVTIYMPMIPEAVVAMLACTRIGAIHSVVFGGFSPEALAGRIIDCKS
KVVITADEGIRAGKKIPLKANVDDALTNPETSSIQKVIVCKRTNGNIKWNQHRDIWYEDL
MKVAGTVCAPKEMGAEEALFILYTSGSTGKPKGVQHTTGGYLLYAALTHERVFDYRPGEI
YWCTADVGWVTGHTYIVYGPLANGATTLLFEGVPNYPDITRVAKIVDKHKVNILYTAPTA
IRAMMASGTAACEGADGSSLRLLGSVGEPINPEAWDWYYKNVGQSRCPIVDTWWQTETGG
NMMSPLPGAHALKPGSAARPFFGVVPALVDNLGNLIEGAAEGNLVILDSWPGQARTLFGD
HDRFVDTYFKTFRGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRMGTAEIESAMVAHP
KVAEAAVVGVPHDIKGQGIYVYVTLKNGEEPNEALRLELKNWVRKEIGPIASPDVIQWAP
GLPKTRSGKIMRRILRKIATGEYDGLGDISTLADPGVVAHLIETHKTMNVA
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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