SitesBLAST
Comparing RR42_RS13560 RR42_RS13560 propionyl-CoA synthetase 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)
5gxdA Structure of acryloyl-coa lyase prpe from dinoroseobacter shibae dfl 12
47% identity, 98% coverage: 13:628/630 of query aligns to 11:621/627 of 5gxdA
- active site: T238 (= T241), T390 (= T390), E391 (= E391), N498 (= N501), R503 (= R506), K587 (= K594)
- binding adenosine monophosphate: G364 (= G364), E365 (= E365), R366 (≠ P366), H386 (≠ N386), W387 (≠ Y387), W388 (= W388), Q389 (= Q389), T390 (= T390), D477 (= D480), I489 (= I492), R492 (= R495), N498 (= N501), R503 (= R506)
- binding coenzyme a: F139 (= F140), G140 (= G141), G141 (= G142), E167 (≠ R168), R170 (≠ K171), S279 (= S282), K307 (≠ T310), P308 (= P311), A332 (= A334), T334 (= T336), A363 (= A363), A500 (= A503), H502 (= H505), K532 (= K535), R562 (≠ D569), P567 (≠ A574), V568 (= V575)
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)
42% identity, 99% coverage: 5:630/630 of query aligns to 24:644/648 of Q89WV5
- G263 (= G243) mutation to I: Loss of activity.
- G266 (= G246) mutation to I: Great decrease in activity.
- K269 (= K249) mutation to G: Great decrease in activity.
- E414 (= E391) mutation to Q: Great decrease in activity.
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
41% identity, 99% coverage: 8:629/630 of query aligns to 24:639/640 of 5jrhA
- active site: T260 (= T241), T412 (= T390), E413 (= E391), N517 (= N501), R522 (= R506), K605 (= K594)
- binding (r,r)-2,3-butanediol: W93 (≠ Y74), E140 (= E121), G169 (≠ A150), K266 (= K247), P267 (= P248)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G364), E384 (= E365), P385 (= P366), T408 (≠ N386), W409 (≠ Y387), W410 (= W388), Q411 (= Q389), T412 (= T390), D496 (= D480), I508 (= I492), N517 (= N501), R522 (= R506)
- binding coenzyme a: F159 (= F140), G160 (= G141), G161 (= G142), R187 (= R168), S519 (≠ A503), R580 (≠ D569), P585 (≠ A574)
- binding magnesium ion: V533 (≠ S517), H535 (= H519), I538 (≠ V522)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
41% identity, 99% coverage: 8:629/630 of query aligns to 24:640/641 of 2p20A
- active site: T260 (= T241), T412 (= T390), E413 (= E391), N517 (= N501), R522 (= R506), K605 (= K594)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G364), E384 (= E365), P385 (= P366), T408 (≠ N386), W409 (≠ Y387), W410 (= W388), Q411 (= Q389), T412 (= T390), D496 (= D480), I508 (= I492), R511 (= R495), R522 (= R506)
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)
41% identity, 99% coverage: 8:629/630 of query aligns to 28:646/652 of Q8ZKF6
- R194 (≠ K171) 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 (≠ V288) binding
- N335 (≠ I312) binding
- A357 (= A334) 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 (= D497) 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 (≠ A503) binding
- G524 (= G504) 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 (= R506) 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 (≠ D569) 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 (= K594) 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)
41% identity, 99% coverage: 8:629/630 of query aligns to 23:636/637 of 2p2fA
- active site: T259 (= T241), T411 (= T390), E412 (= E391), N516 (= N501), R521 (= R506), K604 (= K594)
- binding adenosine monophosphate: G382 (= G364), E383 (= E365), P384 (= P366), T407 (≠ N386), W408 (≠ Y387), W409 (= W388), Q410 (= Q389), T411 (= T390), D495 (= D480), I507 (= I492), R510 (= R495), N516 (= N501), R521 (= R506)
- binding coenzyme a: F158 (= F140), R186 (= R168), W304 (= W286), T306 (≠ V288), P329 (= P311), A352 (= A334), A355 (= A337), S518 (≠ A503), R579 (≠ D569), P584 (≠ A574)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
41% identity, 96% coverage: 8:610/630 of query aligns to 24:623/634 of 1pg3A
- active site: T260 (= T241), T412 (= T390), E413 (= E391), N517 (= N501), R522 (= R506), K605 (= K594)
- binding coenzyme a: F159 (= F140), G160 (= G141), R187 (= R168), R190 (≠ K171), A301 (≠ S282), T307 (≠ V288), P330 (= P311), A356 (= A337), S519 (≠ A503), R580 (≠ D569), P585 (≠ A574)
- binding magnesium ion: V533 (≠ S517), H535 (= H519), I538 (≠ V522)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G364), E384 (= E365), P385 (= P366), T408 (≠ N386), W409 (≠ Y387), W410 (= W388), Q411 (= Q389), T412 (= T390), D496 (= D480), R511 (= R495), R522 (= R506)
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)
40% identity, 99% coverage: 5:629/630 of query aligns to 25:646/652 of P27550
- K609 (= K594) modified: N6-acetyllysine; by autocatalysis
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)
42% identity, 99% coverage: 7:627/630 of query aligns to 28:650/651 of P9WQD1
- K617 (= K594) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
1ry2A Crystal structure of yeast acetyl-coenzyme a synthetase in complex with amp (see paper)
39% identity, 98% coverage: 7:621/630 of query aligns to 6:615/615 of 1ry2A
- active site: T247 (= T241), T399 (= T390), N507 (= N501), K590 (= K594)
- binding adenosine monophosphate: G370 (= G364), E371 (= E365), P372 (= P366), T395 (≠ N386), Y396 (= Y387), W397 (= W388), Q398 (= Q389), T399 (= T390), D486 (= D480), I498 (= I492), R501 (= R495)
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)
41% identity, 99% coverage: 5:629/630 of query aligns to 36:655/662 of P78773
- T596 (≠ Q571) 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)
38% identity, 100% coverage: 1:630/630 of query aligns to 37:675/683 of P52910
- K506 (≠ S468) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
7kvyA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate and co-enzyme a from coccidioides immitis rs
41% identity, 96% coverage: 1:603/630 of query aligns to 31:621/633 of 7kvyA
- active site: T271 (= T241), T422 (= T390), E423 (= E391), N529 (= N501), R534 (= R506), K612 (= K594)
- binding coenzyme a: F172 (= F140), G174 (= G142), R200 (= R168), G312 (≠ S282), Y362 (≠ F332), V363 (≠ S333), A364 (= A334), S531 (≠ A503), G532 (= G504), R592 (≠ D569), F598 (≠ V575)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: G393 (= G364), E394 (= E365), P395 (= P366), T418 (≠ N386), Y419 (= Y387), W420 (= W388), Q421 (= Q389), T422 (= T390), D508 (= D480), I520 (= I492), R523 (= R495), R534 (= R506)
8w0dA Acetyl-coenzyme A synthetase 2
38% identity, 99% coverage: 5:628/630 of query aligns to 38:660/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G364), E399 (= E365), P400 (= P366), T423 (≠ N386), Y424 (= Y387), W425 (= W388), Q426 (= Q389), T427 (= T390), D513 (= D480), I525 (= I492), R528 (= R495), R539 (= R506)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
38% identity, 99% coverage: 5:628/630 of query aligns to 38:660/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G364), E399 (= E365), P400 (= P366), T423 (≠ N386), Y424 (= Y387), Q426 (= Q389), T427 (= T390), D513 (= D480), I525 (= I492), R528 (= R495), R539 (= R506)
- binding coenzyme a: F175 (= F140), R203 (= R168), R206 (≠ K171), G316 (≠ S282), H538 (= H505), R599 (≠ D569), F605 (≠ V575)
8w0cA Acetyl-coenzyme A synthetase 2
38% identity, 99% coverage: 5:628/630 of query aligns to 39:661/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G364), E400 (= E365), P401 (= P366), T424 (≠ N386), Y425 (= Y387), W426 (= W388), Q427 (= Q389), T428 (= T390), D514 (= D480), R529 (= R495), R540 (= R506)
8w0bA Acetyl-coenzyme A synthetase 2
38% identity, 99% coverage: 5:628/630 of query aligns to 39:661/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ A363), G399 (= G364), E400 (= E365), P401 (= P366), T424 (≠ N386), Y425 (= Y387), W426 (= W388), Q427 (= Q389), T428 (= T390), D514 (= D480), I526 (= I492), R529 (= R495), R540 (= R506)
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)
39% identity, 99% coverage: 6:629/630 of query aligns to 53:672/682 of Q99NB1
- K635 (= K594) modified: N6-acetyllysine
8w0jA Acetyl-coenzyme A synthetase 2
38% identity, 99% coverage: 5:628/630 of query aligns to 39:656/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G364), E400 (= E365), P401 (= P366), T424 (≠ N386), Y425 (= Y387), W426 (= W388), Q427 (= Q389), T428 (= T390), D514 (= D480), I526 (= I492), R529 (= R495), R540 (= R506)
7l3qA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-methylphosphate and co-enzyme a from coccidioides immitis rs
41% identity, 95% coverage: 1:600/630 of query aligns to 32:620/631 of 7l3qA
- active site: T272 (= T241), T423 (= T390), E424 (= E391), N530 (= N501), R535 (= R506)
- binding coenzyme a: F173 (= F140), A174 (≠ G141), G175 (= G142), R201 (= R168), G313 (≠ S282), Y363 (≠ F332), A365 (= A334), S532 (≠ A503), G533 (= G504), R593 (≠ D569), P598 (≠ A574), F599 (≠ V575)
- binding 5'-O-[(R)-hydroxy(methoxy)phosphoryl]adenosine: I318 (≠ V287), G394 (= G364), E395 (= E365), P396 (= P366), T419 (≠ N386), Y420 (= Y387), Q422 (= Q389), T423 (= T390), D509 (= D480), R524 (= R495), R535 (= R506)
Query Sequence
>RR42_RS13560 RR42_RS13560 propionyl-CoA synthetase
MTATRALHARSLSDPEGFWAEQARRIDWETPFDTVLDDSRPPFTRWFVGGRTNLCHNAVD
RHLAERADQAALIYVSTETGQHRTYSYAELHDEVNRMAAILQQLGVVKGDRVLIYMPMIP
EAAFAMLACARIGAIHSVVFGGFASVSLAARIDDAQPRVIVSADAGSRAGKVVPYKPLLD
EAVKLATHKPERVLLVDRQLSPMTLTPGRDEDYGAWRERVGAARVPCAWLESSEPSYVLY
TSGTTGKPKGVQRDTGGYAVALAASMEYIFCGKAGDTMFSSSDIGWVVGHSYIIYGPLLA
GMATIMYEGTPIRPDGGILWQLVEQYHVNIMFSAPTAIRVLKKQDPAWLTRYDLSSLRLL
FLAGEPLDEPTASWIQQGIGKPVVDNYWQTETGWPIIAIQRGLDPLPAKLGSPGVPVYGY
DLKIIDEATGAECPPGQKGVVAIDGPLPPGCMTTVWGDDERFVKTYWSGVPGRRCYSTFD
WGVQDEDGYIFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVHDALKGQAAM
AFVIVRDAGRTATQADRLVLEGDVMKTVDQQLGAVARPARVFFVNALPKTRSGKLLRRAM
QAVAEGRDPGDLTTIEDPTALAQLQAAMQG
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