SitesBLAST
Comparing H281DRAFT_05523 H281DRAFT_05523 propionyl-CoA synthetase (EC 6.2.1.17) 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
51% identity, 97% coverage: 10:637/648 of query aligns to 9:625/627 of 5gxdA
- active site: T238 (= T237), T390 (= T398), E391 (= E399), N498 (= N507), R503 (= R512), K587 (= K596)
- binding adenosine monophosphate: G364 (= G372), E365 (= E373), R366 (= R374), H386 (= H394), W387 (= W395), W388 (= W396), Q389 (= Q397), T390 (= T398), D477 (= D486), I489 (≠ V498), R492 (= R501), N498 (= N507), R503 (= R512)
- binding coenzyme a: F139 (= F140), G140 (= G141), G141 (= G142), E167 (= E168), R170 (= R171), S279 (= S278), K307 (= K306), P308 (= P307), A332 (= A331), T334 (= T333), A363 (= A371), A500 (= A509), H502 (= H511), K532 (= K541), R562 (= R571), P567 (≠ A576), V568 (= V577)
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)
37% identity, 96% coverage: 12:636/648 of query aligns to 32:645/648 of Q89WV5
- G263 (= G239) mutation to I: Loss of activity.
- G266 (= G242) mutation to I: Great decrease in activity.
- K269 (= K245) mutation to G: Great decrease in activity.
- E414 (= E399) mutation to Q: Great decrease in activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
37% identity, 96% coverage: 12:633/648 of query aligns to 29:639/641 of 2p20A
- active site: T260 (= T237), T412 (= T398), E413 (= E399), N517 (= N507), R522 (= R512), K605 (= K596)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G372), E384 (= E373), P385 (≠ R374), T408 (≠ H394), W409 (= W395), W410 (= W396), Q411 (= Q397), T412 (= T398), D496 (= D486), I508 (≠ V498), R511 (= R501), R522 (= R512)
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)
37% identity, 96% coverage: 12:633/648 of query aligns to 33:645/652 of Q8ZKF6
- R194 (= R171) 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 (≠ V284) binding
- N335 (≠ G309) binding
- A357 (= A331) 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 (= D503) 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 (≠ A509) binding
- G524 (= G510) 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 (= R512) 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 (= R571) 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 (= K596) 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)
37% identity, 96% coverage: 12:633/648 of query aligns to 28:635/637 of 2p2fA
- active site: T259 (= T237), T411 (= T398), E412 (= E399), N516 (= N507), R521 (= R512), K604 (= K596)
- binding adenosine monophosphate: G382 (= G372), E383 (= E373), P384 (≠ R374), T407 (≠ H394), W408 (= W395), W409 (= W396), Q410 (= Q397), T411 (= T398), D495 (= D486), I507 (≠ V498), R510 (= R501), N516 (= N507), R521 (= R512)
- binding coenzyme a: F158 (= F140), R186 (≠ E168), W304 (= W282), T306 (≠ V284), P329 (= P307), A352 (= A331), A355 (= A334), S518 (≠ A509), R579 (= R571), P584 (≠ A576)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
37% identity, 96% coverage: 12:633/648 of query aligns to 29:638/640 of 5jrhA
- active site: T260 (= T237), T412 (= T398), E413 (= E399), N517 (= N507), R522 (= R512), K605 (= K596)
- binding (r,r)-2,3-butanediol: W93 (≠ F74), E140 (≠ Q121), G169 (≠ K150), K266 (≠ S243), P267 (= P244)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G372), E384 (= E373), P385 (≠ R374), T408 (≠ H394), W409 (= W395), W410 (= W396), Q411 (= Q397), T412 (= T398), D496 (= D486), I508 (≠ V498), N517 (= N507), R522 (= R512)
- binding coenzyme a: F159 (= F140), G160 (= G141), G161 (= G142), R187 (≠ E168), S519 (≠ A509), R580 (= R571), P585 (≠ A576)
- binding magnesium ion: V533 (≠ S523), H535 (≠ L525), I538 (≠ V528)
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)
37% identity, 96% coverage: 5:623/648 of query aligns to 27:644/651 of P9WQD1
- K617 (= K596) 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)
37% identity, 92% coverage: 13:606/648 of query aligns to 13:600/615 of 1ry2A
- active site: T247 (= T237), T399 (= T398), N507 (= N507), K590 (= K596)
- binding adenosine monophosphate: G370 (= G372), E371 (= E373), P372 (≠ R374), T395 (≠ H394), Y396 (≠ W395), W397 (= W396), Q398 (= Q397), T399 (= T398), D486 (= D486), I498 (≠ V498), R501 (= R501)
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)
36% identity, 96% coverage: 14:633/648 of query aligns to 35:645/652 of P27550
- K609 (= K596) modified: N6-acetyllysine; by autocatalysis
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
37% identity, 96% coverage: 12:633/648 of query aligns to 29:632/634 of 1pg3A
- active site: T260 (= T237), T412 (= T398), E413 (= E399), N517 (= N507), R522 (= R512), K605 (= K596)
- binding coenzyme a: F159 (= F140), G160 (= G141), R187 (≠ E168), R190 (= R171), A301 (≠ S278), T307 (≠ V284), P330 (= P307), A356 (= A334), S519 (≠ A509), R580 (= R571), P585 (≠ A576)
- binding magnesium ion: V533 (≠ S523), H535 (≠ L525), I538 (≠ V528)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G372), E384 (= E373), P385 (≠ R374), T408 (≠ H394), W409 (= W395), W410 (= W396), Q411 (= Q397), T412 (= T398), D496 (= D486), R511 (= R501), R522 (= R512)
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)
36% identity, 95% coverage: 13:626/648 of query aligns to 68:674/689 of Q9NUB1
- V488 (= V441) to M: in dbSNP:rs6050249
- K642 (= K596) 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)
36% identity, 95% coverage: 13:626/648 of query aligns to 61:667/682 of Q99NB1
- K635 (= K596) modified: N6-acetyllysine
8w0dA Acetyl-coenzyme A synthetase 2
35% identity, 96% coverage: 13:634/648 of query aligns to 47:661/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G372), E399 (= E373), P400 (≠ R374), T423 (≠ H394), Y424 (≠ W395), W425 (= W396), Q426 (= Q397), T427 (= T398), D513 (= D486), I525 (≠ V498), R528 (= R501), R539 (= R512)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
35% identity, 96% coverage: 13:634/648 of query aligns to 47:661/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G372), E399 (= E373), P400 (≠ R374), T423 (≠ H394), Y424 (≠ W395), Q426 (= Q397), T427 (= T398), D513 (= D486), I525 (≠ V498), R528 (= R501), R539 (= R512)
- binding coenzyme a: F175 (= F140), R203 (≠ E168), R206 (= R171), G316 (≠ S278), H538 (= H511), R599 (= R571), F605 (≠ V577)
8w0cA Acetyl-coenzyme A synthetase 2
35% identity, 96% coverage: 13:634/648 of query aligns to 48:662/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G372), E400 (= E373), P401 (≠ R374), T424 (≠ H394), Y425 (≠ W395), W426 (= W396), Q427 (= Q397), T428 (= T398), D514 (= D486), R529 (= R501), R540 (= R512)
8w0bA Acetyl-coenzyme A synthetase 2
35% identity, 96% coverage: 13:634/648 of query aligns to 48:662/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ A371), G399 (= G372), E400 (= E373), P401 (≠ R374), T424 (≠ H394), Y425 (≠ W395), W426 (= W396), Q427 (= Q397), T428 (= T398), D514 (= D486), I526 (≠ V498), R529 (= R501), R540 (= R512)
7kdsA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-propylphosphate from candida albicans
35% identity, 96% coverage: 13:634/648 of query aligns to 47:651/654 of 7kdsA
- active site: T275 (= T237), T427 (= T398), E428 (= E399), N534 (= N507), R539 (= R512), K620 (= K596)
- binding adenosine-5'-monophosphate-propyl ester: I321 (≠ V283), G398 (= G372), E399 (= E373), P400 (≠ R374), D422 (= D393), T423 (≠ H394), Y424 (≠ W395), W425 (= W396), Q426 (= Q397), T427 (= T398), D513 (= D486), R528 (= R501), N534 (= N507), R539 (= R512)
8w0jA Acetyl-coenzyme A synthetase 2
35% identity, 96% coverage: 13:634/648 of query aligns to 48:657/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G372), E400 (= E373), P401 (≠ R374), T424 (≠ H394), Y425 (≠ W395), W426 (= W396), Q427 (= Q397), T428 (= T398), D514 (= D486), I526 (≠ V498), R529 (= R501), R540 (= R512)
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
35% identity, 97% coverage: 5:634/648 of query aligns to 39:656/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (= P117), A176 (≠ G141), G177 (= G142), R203 (≠ E168), T208 (≠ I173), D317 (= D279), E342 (= E304), G343 (= G305), P345 (= P307), G398 (= G372), E399 (= E373), P400 (≠ R374), T423 (≠ H394), W425 (= W396), Q426 (= Q397), T427 (= T398), D513 (= D486), I525 (≠ V498), R528 (= R501), R539 (= R512)
8v4oA Crystal structure of acetyl-coa synthetase 2 in complex with amp from candida albicans
35% identity, 97% coverage: 5:634/648 of query aligns to 39:656/660 of 8v4oA
- binding adenosine monophosphate: G398 (= G372), E399 (= E373), P400 (≠ R374), T423 (≠ H394), Y424 (≠ W395), W425 (= W396), Q426 (= Q397), T427 (= T398), D513 (= D486), I525 (≠ V498), R528 (= R501), R539 (= R512)
Query Sequence
>H281DRAFT_05523 H281DRAFT_05523 propionyl-CoA synthetase (EC 6.2.1.17)
MNEGEFREDWRTDPMAFWARAASSVAWSRPWDEVLTHQPGQRFSWFDGAYTNASYNCLDR
HVEAGRGEQVAIAFESPVTGTAQTLTYASLRDQVAGFAGVLQLQGVRMGDVVVIYMPVIP
QAIIAMLACARIGATHCVVFGGFAASELAKRLRDTLPRVIVTASCGFEVKRRIPYKETVD
EAVLQSAWQGPVIVYQRELGRVELAERDVDWERAMCGTYGVSPIPVPAGHPLYILHTSGT
TGSPKGIQRDTGGYMTALLWSMNNIYRSLPGDVFWAASDIGWVVGHSYMTYGPLLNGCTT
VLFEGKPVGTPDAAAFWRVIAKHRVNVLFTAPTALRAIKKEDPGGYQLREPVMGELHWRY
DLGSLRSVFLAGERCDTTTIEWAEDLLHVPVLDHWWQTEAGWPMAASTAKGALGGERRRG
AAGRALPGWDVRCVDDQGAEVDAGASGNVVCGLPLPPGAMTTIWNAHERYERSYFGRFPG
WYDTGDAGYVDADGFVFVMGRTDDVINVAGHRLSTGAIEEIVSRLDAVAECAVVGMAHPL
KGQVPLVFLVLKDGSKDGADAAETAAVKVVREQLGAVASMQAAFVVERLPKTRSGKILRR
SLLQIVDGKAVAIPATIEDPGVLVDVERIVKARGIKGESLFGSSHDPE
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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