SitesBLAST
Comparing Pf6N2E2_5149 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_5149 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)
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, 98% coverage: 15:645/645 of query aligns to 14:645/648 of Q89WV5
- G263 (= G263) mutation to I: Loss of activity.
- G266 (= G266) mutation to I: Great decrease in activity.
- K269 (= K269) mutation to G: Great decrease in activity.
- E414 (= E414) mutation to Q: Great decrease in activity.
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)
62% identity, 97% coverage: 19:642/645 of query aligns to 19:645/652 of P27550
- K609 (= K606) 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)
62% identity, 97% coverage: 19:642/645 of query aligns to 19:645/652 of Q8ZKF6
- R194 (= R193) 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 (= T308) binding
- N335 (≠ S332) binding
- A357 (= A354) 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 (= D514) 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 (= S520) binding
- G524 (= G521) 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 (= R523) 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 (≠ S581) 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 (= K606) 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)
62% identity, 97% coverage: 19:642/645 of query aligns to 15:638/640 of 5jrhA
- active site: T260 (= T261), T412 (= T413), E413 (= E414), N517 (= N518), R522 (= R523), K605 (= K606)
- binding (r,r)-2,3-butanediol: W93 (= W96), E140 (= E143), G169 (≠ D172), K266 (= K267), P267 (= P268)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G384), E384 (= E385), P385 (= P386), T408 (= T409), W409 (= W410), W410 (= W411), Q411 (= Q412), T412 (= T413), D496 (= D497), I508 (= I509), N517 (= N518), R522 (= R523)
- binding coenzyme a: F159 (= F162), G160 (= G163), G161 (= G164), R187 (= R190), S519 (= S520), R580 (≠ S581), P585 (≠ S586)
- binding magnesium ion: V533 (= V534), H535 (= H536), I538 (= I539)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
62% identity, 97% coverage: 19:642/645 of query aligns to 15:639/641 of 2p20A
- active site: T260 (= T261), T412 (= T413), E413 (= E414), N517 (= N518), R522 (= R523), K605 (= K606)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G384), E384 (= E385), P385 (= P386), T408 (= T409), W409 (= W410), W410 (= W411), Q411 (= Q412), T412 (= T413), D496 (= D497), I508 (= I509), R511 (= R512), R522 (= R523)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
62% identity, 97% coverage: 19:642/645 of query aligns to 14:635/637 of 2p2fA
- active site: T259 (= T261), T411 (= T413), E412 (= E414), N516 (= N518), R521 (= R523), K604 (= K606)
- binding adenosine monophosphate: G382 (= G384), E383 (= E385), P384 (= P386), T407 (= T409), W408 (= W410), W409 (= W411), Q410 (= Q412), T411 (= T413), D495 (= D497), I507 (= I509), R510 (= R512), N516 (= N518), R521 (= R523)
- binding coenzyme a: F158 (= F162), R186 (= R190), W304 (= W306), T306 (= T308), P329 (= P331), A352 (= A354), A355 (= A357), S518 (= S520), R579 (≠ S581), P584 (≠ S586)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
61% identity, 97% coverage: 19:642/645 of query aligns to 15:632/634 of 1pg3A
- active site: T260 (= T261), T412 (= T413), E413 (= E414), N517 (= N518), R522 (= R523), K605 (= K606)
- binding coenzyme a: F159 (= F162), G160 (= G163), R187 (= R190), R190 (= R193), A301 (= A302), T307 (= T308), P330 (= P331), A356 (= A357), S519 (= S520), R580 (≠ S581), P585 (≠ S586)
- binding magnesium ion: V533 (= V534), H535 (= H536), I538 (= I539)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G384), E384 (= E385), P385 (= P386), T408 (= T409), W409 (= W410), W410 (= W411), Q411 (= Q412), T412 (= T413), D496 (= D497), R511 (= R512), R522 (= R523)
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)
53% identity, 98% coverage: 13:642/645 of query aligns to 35:696/701 of Q9QXG4
- K661 (= K606) modified: N6-acetyllysine
7mmzA Crystal structure of acetyl-coenzyme a synthetase from legionella pneumophila philadelphia 1 in complex with ethyl-amp (see paper)
59% identity, 87% coverage: 33:596/645 of query aligns to 5:559/559 of 7mmzA
- active site: T231 (= T261), T383 (= T413), E384 (= E414), N486 (= N518), R491 (= R523)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I277 (≠ V307), G354 (= G384), E355 (= E385), P356 (= P386), T379 (= T409), W380 (= W410), W381 (= W411), Q382 (= Q412), T383 (= T413), D465 (= D497), I477 (= I509), R480 (= R512), R491 (= R523)
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)
53% identity, 96% coverage: 24:639/645 of query aligns to 51:668/682 of Q99NB1
- K635 (= K606) modified: N6-acetyllysine
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: 24:639/645 of query aligns to 58:675/689 of Q9NUB1
- V488 (≠ I453) to M: in dbSNP:rs6050249
- K642 (= K606) modified: N6-acetyllysine; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
7kdnA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-propylphosphate from aspergillus fumigatus
55% identity, 92% coverage: 22:615/645 of query aligns to 32:621/622 of 7kdnA
- active site: T271 (= T261), T422 (= T413), E423 (= E414), N529 (= N518), R534 (= R523), K612 (= K606)
- binding adenosine-5'-monophosphate-propyl ester: G393 (= G384), E394 (= E385), P395 (= P386), T418 (= T409), Y419 (≠ W410), W420 (= W411), Q421 (= Q412), T422 (= T413), D508 (= D497), I520 (= I509), R523 (= R512), R534 (= R523)
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)
52% identity, 96% coverage: 20:639/645 of query aligns to 31:651/662 of P78773
- T596 (≠ E583) 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)
50% identity, 97% coverage: 23:645/645 of query aligns to 39:676/683 of P52910
- K506 (= K487) 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
55% identity, 94% coverage: 38:641/645 of query aligns to 57:666/668 of 7l4gB
- active site: T280 (= T261), T432 (= T413), E433 (= E414), N539 (= N518), R544 (= R523), K631 (= K606)
- 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 (= W306), G403 (= G384), E404 (= E385), P405 (= P386), T428 (= T409), Y429 (≠ W410), W430 (= W411), M431 (≠ Q412), T432 (= T413), D518 (= D497), I530 (= I509), R533 (= R512)
5u29A Crystal structure of cryptococcus neoformans h99 acetyl-coa synthetase in complex with ac-ams
55% identity, 94% coverage: 38:641/645 of query aligns to 57:666/668 of 5u29A
- active site: T280 (= T261), T432 (= T413), E433 (= E414), N539 (= N518), R544 (= R523), K631 (= K606)
- binding 5'-O-(acetylsulfamoyl)adenosine: W325 (= W306), G403 (= G384), E404 (= E385), P405 (= P386), T428 (= T409), Y429 (≠ W410), W430 (= W411), M431 (≠ Q412), T432 (= T413), D518 (= D497), I530 (= I509), R533 (= R512)
8u2rA Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (ethyl amp bound)
52% identity, 95% coverage: 26:639/645 of query aligns to 26:656/664 of 8u2rA
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I323 (≠ V307), G400 (= G384), E401 (= E385), P402 (= P386), T425 (= T409), W426 (= W410), W427 (= W411), Q428 (= Q412), T429 (= T413), D513 (= D497), I525 (= I509), R528 (= R512), R539 (= R523)
8sf3A Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (amp, acetate and coa bound)
52% identity, 95% coverage: 26:639/645 of query aligns to 27:654/662 of 8sf3A
- binding adenosine monophosphate: G398 (= G384), E399 (= E385), P400 (= P386), T423 (= T409), W424 (= W410), Q426 (= Q412), T427 (= T413), D511 (= D497), R526 (= R512), R537 (= R523)
- binding coenzyme a: F171 (= F162), G172 (= G163), G173 (= G164), R199 (= R190), K202 (≠ R193), R595 (≠ S581), P600 (≠ S586)
8w0dA Acetyl-coenzyme A synthetase 2
51% identity, 96% coverage: 22:639/645 of query aligns to 35:657/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G384), E399 (= E385), P400 (= P386), T423 (= T409), Y424 (≠ W410), W425 (= W411), Q426 (= Q412), T427 (= T413), D513 (= D497), I525 (= I509), R528 (= R512), R539 (= R523)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
51% identity, 96% coverage: 22:639/645 of query aligns to 35:657/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G384), E399 (= E385), P400 (= P386), T423 (= T409), Y424 (≠ W410), Q426 (= Q412), T427 (= T413), D513 (= D497), I525 (= I509), R528 (= R512), R539 (= R523)
- binding coenzyme a: F175 (= F162), R203 (= R190), R206 (= R193), G316 (≠ A302), H538 (= H522), R599 (≠ S581), F605 (= F587)
Query Sequence
>Pf6N2E2_5149 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_5149
MFDISQYPQADAVRRAAQLSQDEYKRLYKESIEHPSAFWAEQATRFLDWMTPWQTVQRYD
LKNGDATWFAGGKLNVSANCLDRHLQTRGDQTAIIWEGDDPAESAEITYKKLHNHVCRLA
NVLKSRGVKKGDRVCIYMPMIPEAAYAMLACTRIGAVHSVVFGGFSPDSLRDRILDADCR
TVITADEGVRGGRFVPLKRNVDKALESCPNVSTVLVVERTQGEVNWVEGRDLWYHQAMHE
MSDDCPPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLLQAAMTFKYVLDYRDNEVFWC
TADVGWVTGHSYIVYGPLANGATTLIFEGVPSYPSSSRFWQVIDKHQVNIFYTAPTALRA
LMREGAGPLQETSRKSLRLLGSVGEPINPEAWEWYFNTVGEQRCPIVDTWWQTETGGIML
SPLVSAPRLKPGCATRPMFGVQPVLLDEVGKEISGAGSGVLAIKSSWPGQIRSVYGDHQR
MVDTYFKPYPGYYFTGDGARRDEDGDYWITGRIDDVINVSGHRIGTAEVESALVLHDNIA
EAAVVGYPHDLKGQGIYAFVTPMNGVEANDELKKELLAHVSKEIGSFAKPELIQWAPALP
KTRSGKIMRRILRKIACNELDSLGDTSTLADPSVVEGLIDKRLNR
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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