SitesBLAST
Comparing WP_081429907.1 NCBI__GCF_000020465.1:WP_081429907.1 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
62% identity, 93% coverage: 35:660/671 of query aligns to 1:626/627 of 5gxdA
- active site: T238 (= T272), T390 (= T424), E391 (= E425), N498 (= N532), R503 (= R537), K587 (= K621)
- binding adenosine monophosphate: G364 (= G398), E365 (= E399), R366 (= R400), H386 (= H420), W387 (= W421), W388 (= W422), Q389 (= Q423), T390 (= T424), D477 (= D511), I489 (= I523), R492 (= R526), N498 (= N532), R503 (= R537)
- binding coenzyme a: F139 (= F173), G140 (= G174), G141 (= G175), E167 (= E201), R170 (= R204), S279 (= S313), K307 (= K341), P308 (= P342), A332 (= A366), T334 (= T368), A363 (= A397), A500 (= A534), H502 (= H536), K532 (= K566), R562 (= R596), P567 (= P601), V568 (= V602)
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)
39% identity, 94% coverage: 31:658/671 of query aligns to 19:648/652 of P27550
- K609 (= K621) 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)
39% identity, 94% coverage: 31:658/671 of query aligns to 19:648/652 of Q8ZKF6
- R194 (= R204) 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 (≠ V319) binding CoA
- N335 (≠ G344) binding CoA
- A357 (= A366) 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 (= D528) 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 (≠ A534) binding CoA
- G524 (= G535) 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 (= R537) 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 (= R596) binding CoA; 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 (= K621) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
39% identity, 93% coverage: 31:656/671 of query aligns to 15:640/641 of 2p20A
- active site: T260 (= T272), T412 (= T424), E413 (= E425), N517 (= N532), R522 (= R537), K605 (= K621)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G398), E384 (= E399), P385 (≠ R400), T408 (≠ H420), W409 (= W421), W410 (= W422), Q411 (= Q423), T412 (= T424), D496 (= D511), I508 (= I523), R511 (= R526), R522 (= R537)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
39% identity, 93% coverage: 31:656/671 of query aligns to 14:636/637 of 2p2fA
- active site: T259 (= T272), T411 (= T424), E412 (= E425), N516 (= N532), R521 (= R537), K604 (= K621)
- binding adenosine monophosphate: G382 (= G398), E383 (= E399), P384 (≠ R400), T407 (≠ H420), W408 (= W421), W409 (= W422), Q410 (= Q423), T411 (= T424), D495 (= D511), I507 (= I523), R510 (= R526), N516 (= N532), R521 (= R537)
- binding coenzyme a: F158 (= F173), R186 (≠ E201), W304 (= W317), T306 (≠ V319), P329 (= P342), A352 (= A366), A355 (= A369), S518 (≠ A534), R579 (= R596), P584 (= P601)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
39% identity, 93% coverage: 31:656/671 of query aligns to 15:639/640 of 5jrhA
- active site: T260 (= T272), T412 (= T424), E413 (= E425), N517 (= N532), R522 (= R537), K605 (= K621)
- binding (r,r)-2,3-butanediol: W93 (≠ Y107), E140 (= E154), G169 (≠ I183), K266 (≠ Q278), P267 (= P279)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G398), E384 (= E399), P385 (≠ R400), T408 (≠ H420), W409 (= W421), W410 (= W422), Q411 (= Q423), T412 (= T424), D496 (= D511), I508 (= I523), N517 (= N532), R522 (= R537)
- binding coenzyme a: F159 (= F173), G160 (= G174), G161 (= G175), R187 (≠ E201), S519 (≠ A534), R580 (= R596), P585 (= P601)
- binding magnesium ion: V533 (≠ C548), H535 (= H550), I538 (≠ V553)
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)
39% identity, 93% coverage: 36:657/671 of query aligns to 23:644/648 of Q89WV5
- G263 (= G274) mutation to I: Loss of activity.
- G266 (= G277) mutation to I: Great decrease in activity.
- K269 (= K280) mutation to G: Great decrease in activity.
- E414 (= E425) mutation to Q: Great decrease in activity.
8rwjD Cryoem structure of acs1 filament determined by filamentid (see paper)
38% identity, 93% coverage: 34:656/671 of query aligns to 37:675/676 of 8rwjD
- 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: G406 (= G398), P408 (≠ R400), T431 (≠ H420), Y432 (≠ W421), Q434 (= Q423), T435 (= T424), D522 (= D511), R537 (= R526), K638 (= K621)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
39% identity, 93% coverage: 31:656/671 of query aligns to 15:633/634 of 1pg3A
- active site: T260 (= T272), T412 (= T424), E413 (= E425), N517 (= N532), R522 (= R537), K605 (= K621)
- binding coenzyme a: F159 (= F173), G160 (= G174), R187 (≠ E201), R190 (= R204), A301 (≠ S313), T307 (≠ V319), P330 (= P342), A356 (= A369), S519 (≠ A534), R580 (= R596), P585 (= P601)
- binding magnesium ion: V533 (≠ C548), H535 (= H550), I538 (≠ V553)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G398), E384 (= E399), P385 (≠ R400), T408 (≠ H420), W409 (= W421), W410 (= W422), Q411 (= Q423), T412 (= T424), D496 (= D511), R511 (= R526), R522 (= R537)
1ry2A Crystal structure of yeast acetyl-coenzyme a synthetase in complex with amp (see paper)
39% identity, 89% coverage: 34:630/671 of query aligns to 1:599/615 of 1ry2A
- active site: T247 (= T272), T399 (= T424), N507 (= N532), K590 (= K621)
- binding adenosine monophosphate: G370 (= G398), E371 (= E399), P372 (≠ R400), T395 (≠ H420), Y396 (≠ W421), W397 (= W422), Q398 (= Q423), T399 (= T424), D486 (= D511), I498 (= I523), R501 (= R526)
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)
38% identity, 92% coverage: 39:654/671 of query aligns to 28:650/651 of P9WQD1
- K617 (= K621) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
38% identity, 89% coverage: 34:628/671 of query aligns to 29:618/630 of 8rplB
- 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: G391 (= G398), E392 (= E399), P393 (≠ R400), T416 (≠ H420), W417 (= W421), W418 (= W422), Q419 (= Q423), T420 (= T424), D502 (= D511), R517 (= R526), K523 (≠ N532), R528 (= R537)
- binding magnesium ion: V539 (≠ C548), H541 (= H550)
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)
37% identity, 94% coverage: 36:666/671 of query aligns to 35:662/662 of P78773
- T596 (≠ N598) modified: Phosphothreonine
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)
37% identity, 92% coverage: 34:651/671 of query aligns to 45:692/701 of Q9QXG4
- K661 (= K621) modified: N6-acetyllysine
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)
37% identity, 93% coverage: 30:656/671 of query aligns to 45:672/682 of Q99NB1
- K635 (= K621) modified: N6-acetyllysine
8w0dA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with an isopropyl amp ester inhibitor
37% identity, 93% coverage: 34:655/671 of query aligns to 35:660/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G398), E399 (= E399), P400 (≠ R400), T423 (≠ H420), Y424 (≠ W421), W425 (= W422), Q426 (= Q423), T427 (= T424), D513 (= D511), I525 (= I523), R528 (= R526), R539 (= R537)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
37% identity, 93% coverage: 34:655/671 of query aligns to 35:660/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G398), E399 (= E399), P400 (≠ R400), T423 (≠ H420), Y424 (≠ W421), Q426 (= Q423), T427 (= T424), D513 (= D511), I525 (= I523), R528 (= R526), R539 (= R537)
- binding coenzyme a: F175 (= F173), R203 (≠ E201), R206 (= R204), G316 (≠ S313), H538 (= H536), R599 (= R596), F605 (≠ V602)
8w0cA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopentyl ester amp inhibitor
37% identity, 93% coverage: 34:655/671 of query aligns to 36:661/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G398), E400 (= E399), P401 (≠ R400), T424 (≠ H420), Y425 (≠ W421), W426 (= W422), Q427 (= Q423), T428 (= T424), D514 (= D511), R529 (= R526), R540 (= R537)
8w0bA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopropyl amp ester inhibitor
37% identity, 93% coverage: 34:655/671 of query aligns to 36:661/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ A397), G399 (= G398), E400 (= E399), P401 (≠ R400), T424 (≠ H420), Y425 (≠ W421), W426 (= W422), Q427 (= Q423), T428 (= T424), D514 (= D511), I526 (= I523), R529 (= R526), R540 (= R537)
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)
36% identity, 97% coverage: 17:665/671 of query aligns to 21:683/683 of P52910
- K506 (≠ T501) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Query Sequence
>WP_081429907.1 NCBI__GCF_000020465.1:WP_081429907.1
MSRQAGTLVYPCCSSLPVFLNNLRFQRGLSVMPQSYNTVFQQSIEQPDEFWGAAASELHW
YKKWDSVLDSSNPPFYRWFSGGMTNTCYNALDRHVDEGRGNQLAVIYDSPVTGAKERYTY
REFRDIVALFAGALQSRGVRKGDRVIIYMPMIPEAVVAMLACARIGAIHSVVFGGFASHE
LAIRIDDCKPKVIISASCGIEHGRVVDYKRLLDFAIELAHFKPEICIIKQREQLKAELNE
DRDLTWKQSLLGAEPAQCVPVESSDPLYILYTSGTTGQPKGIVRDNGGHMVAMKWSMENV
YNVKPGEVYWAASDVGWVVGHSYIVYAPLLHGCTTLIFEGKPVGTPDPGTFWRIVNEYSV
AVLFTAPTAFRAIKKEDPKGMYMKKYDLSSLRTLFLAGERADPDTVKWAEEKLQVPVVDH
WWQTETGWAIAANCQGIEPGPVKYGSASRAVPGYNVQVINQEMERLPAGQMGDIVIKLPL
PPGTMLSLWKADIRFIESYMTSFPGYYQTSDAGFIDEDGYIHIMSRTDDIINVAGHRLST
GSIEAALCEHPDVAESAVIGVHDDLKGQVPLGFLVLKANVDTPETQIVKHVIEYVRENIG
PVASFKHAVIVNRLPKTRSGKILRGTMRKIANSEEYAMPATIDDPAILDEIREALQTIGY
AVKSRPVTKEA
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