SitesBLAST
Comparing WP_013537306.1 NCBI__GCF_000185805.1:WP_013537306.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
55% identity, 98% coverage: 10:627/631 of query aligns to 1:630/630 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 (= G388), E392 (= E389), P393 (= P390), T416 (= T413), W417 (= W414), W418 (= W415), Q419 (= Q416), T420 (= T417), D502 (= D499), R517 (= R514), K523 (≠ N520), R528 (= R525)
- binding magnesium ion: V539 (= V536), H541 (= H538)
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)
50% identity, 97% coverage: 17:631/631 of query aligns to 13:640/651 of P9WQD1
- K617 (= K608) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase 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)
50% identity, 96% coverage: 27:631/631 of query aligns to 20:634/652 of P27550
- K609 (= K608) modified: N6-acetyllysine; by autocatalysis
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
51% identity, 96% coverage: 27:631/631 of query aligns to 16:627/640 of 5jrhA
- active site: T260 (= T265), T412 (= T417), E413 (= E418), N517 (= N520), R522 (= R525), K605 (= K608)
- binding (r,r)-2,3-butanediol: W93 (= W101), E140 (= E147), G169 (≠ H176), K266 (= K271), P267 (= P272)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G388), E384 (= E389), P385 (= P390), T408 (= T413), W409 (= W414), W410 (= W415), Q411 (= Q416), T412 (= T417), D496 (= D499), I508 (= I511), N517 (= N520), R522 (= R525)
- binding coenzyme a: F159 (≠ Y166), G160 (≠ A167), G161 (= G168), R187 (= R194), S519 (= S522), R580 (≠ K583), P585 (≠ A588)
- binding magnesium ion: V533 (= V536), H535 (= H538), I538 (≠ V541)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
50% identity, 96% coverage: 27:631/631 of query aligns to 16:628/641 of 2p20A
- active site: T260 (= T265), T412 (= T417), E413 (= E418), N517 (= N520), R522 (= R525), K605 (= K608)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G388), E384 (= E389), P385 (= P390), T408 (= T413), W409 (= W414), W410 (= W415), Q411 (= Q416), T412 (= T417), D496 (= D499), I508 (= I511), R511 (= R514), R522 (= R525)
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)
49% identity, 97% coverage: 19:631/631 of query aligns to 9:631/648 of Q89WV5
- G263 (= G267) mutation to I: Loss of activity.
- G266 (= G270) mutation to I: Great decrease in activity.
- K269 (= K273) mutation to G: Great decrease in activity.
- E414 (= E418) mutation to Q: Great decrease in activity.
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)
50% identity, 96% coverage: 27:631/631 of query aligns to 20:634/652 of Q8ZKF6
- R194 (= R197) 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 (= T312) binding CoA
- N335 (= N336) binding CoA
- A357 (= A358) 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 (= D516) 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 (= S522) binding CoA
- G524 (= G523) 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 (= R525) 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 (≠ K583) 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 (= K608) 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)
50% identity, 96% coverage: 27:631/631 of query aligns to 15:624/637 of 2p2fA
- active site: T259 (= T265), T411 (= T417), E412 (= E418), N516 (= N520), R521 (= R525), K604 (= K608)
- binding adenosine monophosphate: G382 (= G388), E383 (= E389), P384 (= P390), T407 (= T413), W408 (= W414), W409 (= W415), Q410 (= Q416), T411 (= T417), D495 (= D499), I507 (= I511), R510 (= R514), N516 (= N520), R521 (= R525)
- binding coenzyme a: F158 (≠ Y166), R186 (= R194), W304 (= W310), T306 (= T312), P329 (= P335), A352 (= A358), A355 (= A361), S518 (= S522), R579 (≠ K583), P584 (≠ A588)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
50% identity, 96% coverage: 27:629/631 of query aligns to 16:628/634 of 1pg3A
- active site: T260 (= T265), T412 (= T417), E413 (= E418), N517 (= N520), R522 (= R525), K605 (= K608)
- binding coenzyme a: F159 (≠ Y166), G160 (≠ A167), R187 (= R194), R190 (= R197), A301 (= A306), T307 (= T312), P330 (= P335), A356 (= A361), S519 (= S522), R580 (≠ K583), P585 (≠ A588)
- binding magnesium ion: V533 (= V536), H535 (= H538), I538 (≠ V541)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G388), E384 (= E389), P385 (= P390), T408 (= T413), W409 (= W414), W410 (= W415), Q411 (= Q416), T412 (= T417), D496 (= D499), R511 (= R514), R522 (= R525)
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)
47% identity, 96% coverage: 26:631/631 of query aligns to 46:660/682 of Q99NB1
- K635 (= K608) 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)
47% identity, 95% coverage: 30:631/631 of query aligns to 57:667/689 of Q9NUB1
- V488 (= V456) to M: in dbSNP:rs6050249
- K642 (= K608) modified: N6-acetyllysine; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
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)
45% identity, 100% coverage: 1:631/631 of query aligns to 1:643/662 of P78773
- T596 (≠ E585) modified: Phosphothreonine
7mmzA Crystal structure of acetyl-coenzyme a synthetase from legionella pneumophila philadelphia 1 in complex with ethyl-amp (see paper)
50% identity, 88% coverage: 43:597/631 of query aligns to 8:558/559 of 7mmzA
- active site: T231 (= T265), T383 (= T417), E384 (= E418), N486 (= N520), R491 (= R525)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I277 (= I311), G354 (= G388), E355 (= E389), P356 (= P390), T379 (= T413), W380 (= W414), W381 (= W415), Q382 (= Q416), T383 (= T417), D465 (= D499), I477 (= I511), R480 (= R514), R491 (= R525)
8w0dA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with an isopropyl amp ester inhibitor
44% identity, 97% coverage: 18:631/631 of query aligns to 18:649/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G388), E399 (= E389), P400 (= P390), T423 (= T413), Y424 (≠ W414), W425 (= W415), Q426 (= Q416), T427 (= T417), D513 (= D499), I525 (= I511), R528 (= R514), R539 (= R525)
8w0cA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopentyl ester amp inhibitor
44% identity, 97% coverage: 18:631/631 of query aligns to 19:650/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G388), E400 (= E389), P401 (= P390), T424 (= T413), Y425 (≠ W414), W426 (= W415), Q427 (= Q416), T428 (= T417), D514 (= D499), R529 (= R514), R540 (= R525)
8w0bA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopropyl amp ester inhibitor
44% identity, 97% coverage: 18:631/631 of query aligns to 19:650/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (= V387), G399 (= G388), E400 (= E389), P401 (= P390), T424 (= T413), Y425 (≠ W414), W426 (= W415), Q427 (= Q416), T428 (= T417), D514 (= D499), I526 (= I511), R529 (= R514), R540 (= R525)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
44% identity, 97% coverage: 18:631/631 of query aligns to 18:649/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G388), E399 (= E389), P400 (= P390), T423 (= T413), Y424 (≠ W414), Q426 (= Q416), T427 (= T417), D513 (= D499), I525 (= I511), R528 (= R514), R539 (= R525)
- binding coenzyme a: F175 (≠ Y166), R203 (= R194), R206 (= R197), G316 (≠ A306), H538 (= H524), R599 (≠ K583), F605 (≠ L589)
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
44% identity, 97% coverage: 18:631/631 of query aligns to 18:644/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (= P143), A176 (= A167), G177 (= G168), R203 (= R194), T208 (≠ I199), D317 (= D307), E342 (= E332), G343 (= G333), P345 (= P335), G398 (= G388), E399 (= E389), P400 (= P390), T423 (= T413), W425 (= W415), Q426 (= Q416), T427 (= T417), D513 (= D499), I525 (= I511), R528 (= R514), R539 (= R525)
8v4oA Crystal structure of acetyl-coa synthetase 2 in complex with amp from candida albicans
44% identity, 97% coverage: 18:631/631 of query aligns to 18:644/660 of 8v4oA
- binding adenosine monophosphate: G398 (= G388), E399 (= E389), P400 (= P390), T423 (= T413), Y424 (≠ W414), W425 (= W415), Q426 (= Q416), T427 (= T417), D513 (= D499), I525 (= I511), R528 (= R514), R539 (= R525)
8w0jA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a propyne amp ester inhibitor
44% identity, 97% coverage: 18:631/631 of query aligns to 19:645/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G388), E400 (= E389), P401 (= P390), T424 (= T413), Y425 (≠ W414), W426 (= W415), Q427 (= Q416), T428 (= T417), D514 (= D499), I526 (= I511), R529 (= R514), R540 (= R525)
Query Sequence
>WP_013537306.1 NCBI__GCF_000185805.1:WP_013537306.1
MSKEQLDHLLKKELVIPPPEEFVKNANVKDYEAEYKRFLENPEKFWEEVAQQLIWFKKWE
KVLEWNYPYAKWFVGGKTNITVNALDRHVKGDKRNKVAFFWEDELGNEKVVTYGELYRLV
NKLANALKRAGIKKGDRVVIYMPLVIEQVAAMLACARIGAIHSVVYAGFSASALRHRIED
AEAKMVITADVTIRRGRAIPLKQIVDQAILDLPTVEKVVVLRRLRPLVDLIGEKEVDFYS
FIENEPDYCEPEEMDAEDPLFILYTSGSTGKPKGVLHTTGGYMVGTYYSVKTVFDLKEDD
VYWCTADPGWITGHSYIVYGPLVAGATQVIAEGAPNYPDFGRWWRIVEKYGVNIFYTAPT
AIRMFMRAGEEWPNKYDLSSLRLLGSVGEPINPEAWLWYYRVIGKERCPIVDTWWQTETG
AVMITTIDGLPMKPGKAGKPVPGVIADVVDKEGNPVEPEKGGFLVIKFPWPSMMRTIWKN
PQRYEQYWNTIPNCYTAGDVAVKDKDGYIMILGRADDVINVSGHRIGTMEVESALVSHPA
VAEAAVIGKPDPVKGEAIKAFVILKAGVEPSDKLVEDLKYHVKMELGALAVPSEIEFVEK
LPKTRSGKIMRRVLKARELGIDPGDLSTLED
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