SitesBLAST
Comparing WP_050464817.1 NCBI__GCF_001189915.1:WP_050464817.1 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
45% identity, 100% coverage: 2:634/636 of query aligns to 1:621/627 of 5gxdA
- active site: T238 (= T240), T390 (= T397), E391 (= E398), N498 (= N507), R503 (= R512), K587 (= K600)
- binding adenosine monophosphate: G364 (= G371), E365 (= E372), R366 (≠ P373), H386 (≠ N393), W387 (≠ Y394), W388 (= W395), Q389 (= Q396), T390 (= T397), D477 (= D486), I489 (= I498), R492 (= R501), N498 (= N507), R503 (= R512)
- binding coenzyme a: F139 (= F139), G140 (= G140), G141 (= G141), E167 (≠ R167), R170 (≠ K170), S279 (= S281), K307 (≠ L309), P308 (= P310), A332 (= A341), T334 (= T343), A363 (= A370), A500 (= A509), H502 (= H511), K532 (= K541), R562 (≠ D575), P567 (≠ A580), V568 (= V581)
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)
40% identity, 100% coverage: 2:636/636 of query aligns to 22:644/648 of Q89WV5
- G263 (= G242) mutation to I: Loss of activity.
- G266 (= G245) mutation to I: Great decrease in activity.
- K269 (= K248) mutation to G: Great decrease in activity.
- E414 (= E398) 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)
39% identity, 99% coverage: 3:632/636 of query aligns to 20:636/640 of 5jrhA
- active site: T260 (= T240), T412 (= T397), E413 (= E398), N517 (= N507), R522 (= R512), K605 (= K600)
- binding (r,r)-2,3-butanediol: W93 (≠ A73), E140 (= E120), G169 (≠ S149), K266 (= K246), P267 (= P247)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G371), E384 (= E372), P385 (= P373), T408 (≠ N393), W409 (≠ Y394), W410 (= W395), Q411 (= Q396), T412 (= T397), D496 (= D486), I508 (= I498), N517 (= N507), R522 (= R512)
- binding coenzyme a: F159 (= F139), G160 (= G140), G161 (= G141), R187 (= R167), S519 (≠ A509), R580 (≠ D575), P585 (≠ A580)
- binding magnesium ion: V533 (≠ S523), H535 (= H525), I538 (≠ V528)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
38% identity, 99% coverage: 3:632/636 of query aligns to 20:637/641 of 2p20A
- active site: T260 (= T240), T412 (= T397), E413 (= E398), N517 (= N507), R522 (= R512), K605 (= K600)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G371), E384 (= E372), P385 (= P373), T408 (≠ N393), W409 (≠ Y394), W410 (= W395), Q411 (= Q396), T412 (= T397), D496 (= D486), I508 (= I498), R511 (= R501), R522 (= R512)
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
39% identity, 97% coverage: 2:619/636 of query aligns to 30:630/630 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 (= G371), E392 (= E372), P393 (= P373), T416 (≠ N393), W417 (≠ Y394), W418 (= W395), Q419 (= Q396), T420 (= T397), D502 (= D486), R517 (= R501), K523 (≠ N507), R528 (= R512)
- binding magnesium ion: V539 (≠ S523), H541 (= H525)
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)
38% identity, 99% coverage: 3:632/636 of query aligns to 24:643/652 of Q8ZKF6
- R194 (≠ K170) 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 (≠ V287) binding CoA
- N335 (≠ V311) binding CoA
- A357 (= A341) 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 CoA
- 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 (≠ D575) 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 (= K600) modified: N6-acetyllysine; by Pat; mutation to A: No 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)
38% identity, 99% coverage: 3:632/636 of query aligns to 24:643/652 of P27550
- K609 (= K600) modified: N6-acetyllysine; by autocatalysis
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
38% identity, 99% coverage: 3:632/636 of query aligns to 19:633/637 of 2p2fA
- active site: T259 (= T240), T411 (= T397), E412 (= E398), N516 (= N507), R521 (= R512), K604 (= K600)
- binding adenosine monophosphate: G382 (= G371), E383 (= E372), P384 (= P373), T407 (≠ N393), W408 (≠ Y394), W409 (= W395), Q410 (= Q396), T411 (= T397), D495 (= D486), I507 (= I498), R510 (= R501), N516 (= N507), R521 (= R512)
- binding coenzyme a: F158 (= F139), R186 (= R167), W304 (= W285), T306 (≠ V287), P329 (= P310), A352 (= A341), A355 (= A344), S518 (≠ A509), R579 (≠ D575), P584 (≠ A580)
8rwjD Cryoem structure of acs1 filament determined by filamentid (see paper)
37% identity, 100% coverage: 2:635/636 of query aligns to 38:675/676 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 (= G371), P408 (= P373), T431 (≠ N393), Y432 (= Y394), Q434 (= Q396), T435 (= T397), D522 (= D486), R537 (= R501), K638 (= K600)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
39% identity, 97% coverage: 3:616/636 of query aligns to 20:623/634 of 1pg3A
- active site: T260 (= T240), T412 (= T397), E413 (= E398), N517 (= N507), R522 (= R512), K605 (= K600)
- binding coenzyme a: F159 (= F139), G160 (= G140), R187 (= R167), R190 (≠ K170), A301 (≠ S281), T307 (≠ V287), P330 (= P310), A356 (= A344), S519 (≠ A509), R580 (≠ D575), P585 (≠ A580)
- binding magnesium ion: V533 (≠ S523), H535 (= H525), I538 (≠ V528)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G371), E384 (= E372), P385 (= P373), T408 (≠ N393), W409 (≠ Y394), W410 (= W395), Q411 (= Q396), T412 (= T397), D496 (= D486), R511 (= R501), R522 (= R512)
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)
40% identity, 99% coverage: 6:633/636 of query aligns to 28:650/651 of P9WQD1
- K617 (= K600) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
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: 2:636/636 of query aligns to 39:675/683 of P52910
- K506 (≠ S475) 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
39% identity, 96% coverage: 1:609/636 of query aligns to 31:621/633 of 7kvyA
- active site: T271 (= T240), T422 (= T397), E423 (= E398), N529 (= N507), R534 (= R512), K612 (= K600)
- binding coenzyme a: F172 (= F139), G174 (= G141), R200 (= R167), G312 (≠ S281), Y362 (≠ F339), V363 (≠ S340), A364 (= A341), S531 (≠ A509), G532 (= G510), R592 (≠ D575), F598 (≠ V581)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: G393 (= G371), E394 (= E372), P395 (= P373), T418 (≠ N393), Y419 (= Y394), W420 (= W395), Q421 (= Q396), T422 (= T397), D508 (= D486), I520 (= I498), R523 (= R501), R534 (= R512)
1ry2A Crystal structure of yeast acetyl-coenzyme a synthetase in complex with amp (see paper)
37% identity, 98% coverage: 2:627/636 of query aligns to 2:615/615 of 1ry2A
- active site: T247 (= T240), T399 (= T397), N507 (= N507), K590 (= K600)
- binding adenosine monophosphate: G370 (= G371), E371 (= E372), P372 (= P373), T395 (≠ N393), Y396 (= Y394), W397 (= W395), Q398 (= Q396), T399 (= T397), D486 (= D486), I498 (= I498), R501 (= R501)
8w0dA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with an isopropyl amp ester inhibitor
37% identity, 99% coverage: 3:634/636 of query aligns to 37:660/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G371), E399 (= E372), P400 (= P373), T423 (≠ N393), Y424 (= Y394), W425 (= W395), Q426 (= Q396), T427 (= T397), D513 (= D486), I525 (= I498), R528 (= R501), R539 (= R512)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
37% identity, 99% coverage: 3:634/636 of query aligns to 37:660/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G371), E399 (= E372), P400 (= P373), T423 (≠ N393), Y424 (= Y394), Q426 (= Q396), T427 (= T397), D513 (= D486), I525 (= I498), R528 (= R501), R539 (= R512)
- binding coenzyme a: F175 (= F139), R203 (= R167), R206 (≠ K170), G316 (≠ S281), H538 (= H511), R599 (≠ D575), F605 (≠ V581)
8w0cA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopentyl ester amp inhibitor
37% identity, 99% coverage: 3:634/636 of query aligns to 38:661/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G371), E400 (= E372), P401 (= P373), T424 (≠ N393), Y425 (= Y394), W426 (= W395), Q427 (= Q396), T428 (= T397), D514 (= D486), R529 (= R501), R540 (= R512)
8w0bA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopropyl amp ester inhibitor
37% identity, 99% coverage: 3:634/636 of query aligns to 38:661/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ A370), G399 (= G371), E400 (= E372), P401 (= P373), T424 (≠ N393), Y425 (= Y394), W426 (= W395), Q427 (= Q396), T428 (= T397), D514 (= D486), I526 (= I498), R529 (= R501), R540 (= R512)
7l3qA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-methylphosphate and co-enzyme a from coccidioides immitis rs
39% identity, 96% coverage: 1:609/636 of query aligns to 32:619/631 of 7l3qA
- active site: T272 (= T240), T423 (= T397), E424 (= E398), N530 (= N507), R535 (= R512)
- binding coenzyme a: F173 (= F139), A174 (≠ G140), G175 (= G141), R201 (= R167), G313 (≠ S281), Y363 (≠ F339), A365 (= A341), S532 (≠ A509), G533 (= G510), R593 (≠ D575), P598 (≠ A580), F599 (≠ V581)
- binding 5'-O-[(R)-hydroxy(methoxy)phosphoryl]adenosine: I318 (≠ V286), G394 (= G371), E395 (= E372), P396 (= P373), T419 (≠ N393), Y420 (= Y394), Q422 (= Q396), T423 (= T397), D509 (= D486), R524 (= R501), R535 (= R512)
8w0jA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a propyne amp ester inhibitor
37% identity, 99% coverage: 3:634/636 of query aligns to 38:656/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G371), E400 (= E372), P401 (= P373), T424 (≠ N393), Y425 (= Y394), W426 (= W395), Q427 (= Q396), T428 (= T397), D514 (= D486), I526 (= I498), R529 (= R501), R540 (= R512)
Query Sequence
>WP_050464817.1 NCBI__GCF_001189915.1:WP_050464817.1
MNFDSFYRQSIDDPNTFWANEARRIDWHQPFTNTLDYSRPPFARWFIDGQTNLCHNAIDR
HLPARAEQAALIAISTETGTEKTYSFGALHAEVNRMAAIMLAQGVAQGDRVLIYMPMIAE
AVFAMLACARIGAVHSVVFGGFASNSLASRIDDAQPKLIVSADAGSRGGKVVAYKGLLDE
AIRLAQHKPAHVLLVDRGLAEMPRTAGRDLDYSALRQQYLDAQVPVTWLESNQPSYILYT
SGTTGKPKGVQRDVGGYAVALAASMQHVFCGNPGEAYFCTSDIGWVVGHSYIVYGPLIAG
MATVLYEGLPVLARAAGEAQADAGIWWRIVEKYKVTRMFSAPTAIRVLKKQPPEFMSKYD
LSSLKALYLAGEPLDETTSSWISSALQVPIIDNYWQTESGWPILSIAKGIEDKPTKLGSP
GVPLYGYRMHIIDEATGEACGPNQKGVVTIEGPLPPGCMQTIYGDDERFVKTYWSNFPRM
AYSTFDWGIRDEDGYYFILGRTDDVINVAGHRLGTREIEESISSHPNVSEVAVVGVEDKL
KGQVAIAFVIPKNADSTASKEQKQAFEAEVMRVVDKQIGAVGRPARVLVVSLLPKTRSGK
LLRRSIQAICEGRDPGDLTTIEDPTSLQQIRQALEN
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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