SitesBLAST
Comparing WP_057507018.1 NCBI__GCF_001431535.1:WP_057507018.1 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)
5gxdA Structure of acryloyl-coa lyase prpe from dinoroseobacter shibae dfl 12
45% identity, 100% coverage: 3:626/626 of query aligns to 2:623/627 of 5gxdA
- active site: T238 (= T241), T390 (= T390), E391 (= E391), N498 (= N500), R503 (= R505), K587 (= K590)
- binding adenosine monophosphate: G364 (= G364), E365 (= E365), R366 (≠ P366), H386 (≠ N386), W387 (≠ Y387), W388 (= W388), Q389 (= Q389), T390 (= T390), D477 (= D479), I489 (= I491), R492 (= R494), N498 (= N500), R503 (= R505)
- binding coenzyme a: F139 (= F139), G140 (= G140), G141 (= G141), E167 (≠ R167), R170 (≠ K170), S279 (= S282), K307 (≠ L310), P308 (= P311), A332 (≠ S334), T334 (= T336), A363 (= A363), A500 (= A502), H502 (= H504), K532 (= K534), R562 (≠ T565), P567 (≠ A570), V568 (= V571)
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)
41% identity, 99% coverage: 3:620/626 of query aligns to 23:638/648 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)
42% identity, 99% coverage: 3:620/626 of query aligns to 20:634/640 of 5jrhA
- active site: T260 (= T241), T412 (= T390), E413 (= E391), N517 (= N500), R522 (= R505), K605 (= K590)
- binding (r,r)-2,3-butanediol: W93 (≠ A73), E140 (= E120), G169 (≠ L149), 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 (= D479), I508 (= I491), N517 (= N500), R522 (= R505)
- binding coenzyme a: F159 (= F139), G160 (= G140), G161 (= G141), R187 (= R167), S519 (≠ A502), R580 (≠ T565), P585 (≠ A570)
- binding magnesium ion: V533 (≠ S516), H535 (= H518), I538 (≠ V521)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
41% identity, 99% coverage: 3:620/626 of query aligns to 20:635/641 of 2p20A
- active site: T260 (= T241), T412 (= T390), E413 (= E391), N517 (= N500), R522 (= R505), K605 (= K590)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G364), E384 (= E365), P385 (= P366), T408 (≠ N386), W409 (≠ Y387), W410 (= W388), Q411 (= Q389), T412 (= T390), D496 (= D479), I508 (= I491), R511 (= R494), R522 (= R505)
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: 3:620/626 of query aligns to 24:641/652 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 (≠ V288) binding
- N335 (≠ T312) binding
- A357 (≠ S334) 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 (= D496) 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 (≠ A502) binding
- G524 (= G503) 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 (= R505) 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 (≠ T565) 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 (= K590) 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)
41% identity, 99% coverage: 3:620/626 of query aligns to 24:641/652 of P27550
- K609 (= K590) modified: N6-acetyllysine; by autocatalysis
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
41% identity, 99% coverage: 3:620/626 of query aligns to 19:631/637 of 2p2fA
- active site: T259 (= T241), T411 (= T390), E412 (= E391), N516 (= N500), R521 (= R505), K604 (= K590)
- binding adenosine monophosphate: G382 (= G364), E383 (= E365), P384 (= P366), T407 (≠ N386), W408 (≠ Y387), W409 (= W388), Q410 (= Q389), T411 (= T390), D495 (= D479), I507 (= I491), R510 (= R494), N516 (= N500), R521 (= R505)
- binding coenzyme a: F158 (= F139), R186 (= R167), W304 (= W286), T306 (≠ V288), P329 (= P311), A352 (≠ S334), A355 (= A337), S518 (≠ A502), R579 (≠ T565), P584 (≠ A570)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
41% identity, 97% coverage: 3:611/626 of query aligns to 20:628/634 of 1pg3A
- active site: T260 (= T241), T412 (= T390), E413 (= E391), N517 (= N500), R522 (= R505), K605 (= K590)
- binding coenzyme a: F159 (= F139), G160 (= G140), R187 (= R167), R190 (≠ K170), A301 (≠ S282), T307 (≠ V288), P330 (= P311), A356 (= A337), S519 (≠ A502), R580 (≠ T565), P585 (≠ A570)
- binding magnesium ion: V533 (≠ S516), H535 (= H518), I538 (≠ V521)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G364), E384 (= E365), P385 (= P366), T408 (≠ N386), W409 (≠ Y387), W410 (= W388), Q411 (= Q389), T412 (= T390), D496 (= D479), R511 (= R494), R522 (= R505)
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: 5:623/626 of query aligns to 27:650/651 of P9WQD1
- K617 (= K590) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
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)
39% identity, 99% coverage: 3:620/626 of query aligns to 47:692/701 of Q9QXG4
- K661 (= K590) modified: N6-acetyllysine
Q9NR19 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 Homo sapiens (Human) (see paper)
39% identity, 99% coverage: 3:620/626 of query aligns to 47:692/701 of Q9NR19
- T363 (≠ V288) mutation to A: Loss of catlytic activity but no effect on its nuclear translocation upon glucose deprivation. Loss of ability to promote gene transcription for lysosomal biogenesis and autophagy.
- 656:668 (vs. 585:597, 69% identical) Nuclear localization signal
- S659 (= S588) modified: Phosphoserine; by AMPK; mutation to A: No effect on catalytic activity. Loss of AMPK-mediated phosphorylation, interaction with KPNA1 and nuclear translocation upon glucose deprivation. Loss of ability to promote gene transcription for lysosomal biogenesis and autophagy.
- RR 664:665 (= RR 593:594) mutation to AA: No effect on catalytic activity. Loss of interaction with KPNA1 and nuclear translocation upon glucose deprivation. Loss of ability to promote gene transcription for lysosomal biogenesis and autophagy.
Sites not aligning to the query:
- 1:107 Interaction with TFEB
1ry2A Crystal structure of yeast acetyl-coenzyme a synthetase in complex with amp (see paper)
39% identity, 98% coverage: 2:617/626 of query aligns to 2:615/615 of 1ry2A
- active site: T247 (= T241), T399 (= T390), N507 (= N500), K590 (= K590)
- binding adenosine monophosphate: G370 (= G364), E371 (= E365), P372 (= P366), T395 (≠ N386), Y396 (= Y387), W397 (= W388), Q398 (= Q389), T399 (= T390), D486 (= D479), I498 (= I491), R501 (= R494)
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)
39% identity, 100% coverage: 2:624/626 of query aligns to 34:654/662 of P78773
- T596 (≠ S567) modified: Phosphothreonine
8u2rA Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (ethyl amp bound)
39% identity, 98% coverage: 7:620/626 of query aligns to 28:655/664 of 8u2rA
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I323 (≠ A287), G400 (= G364), E401 (= E365), P402 (= P366), T425 (≠ N386), W426 (≠ Y387), W427 (= W388), Q428 (= Q389), T429 (= T390), D513 (= D479), I525 (= I491), R528 (= R494), R539 (= R505)
8sf3A Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (amp, acetate and coa bound)
39% identity, 98% coverage: 7:620/626 of query aligns to 29:653/662 of 8sf3A
- binding adenosine monophosphate: G398 (= G364), E399 (= E365), P400 (= P366), T423 (≠ N386), W424 (≠ Y387), Q426 (= Q389), T427 (= T390), D511 (= D479), R526 (= R494), R537 (= R505)
- binding coenzyme a: F171 (= F139), G172 (= G140), G173 (= G141), R199 (= R167), K202 (= K170), R595 (vs. gap), P600 (≠ A570)
8w0dA Acetyl-coenzyme A synthetase 2
37% identity, 100% coverage: 3:625/626 of query aligns to 37:661/666 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 (= D479), I525 (= I491), R528 (= R494), R539 (= R505)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
37% identity, 100% coverage: 3:625/626 of query aligns to 37:661/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G364), E399 (= E365), P400 (= P366), T423 (≠ N386), Y424 (= Y387), Q426 (= Q389), T427 (= T390), D513 (= D479), I525 (= I491), R528 (= R494), R539 (= R505)
- binding coenzyme a: F175 (= F139), R203 (= R167), R206 (≠ K170), G316 (≠ S282), H538 (= H504), R599 (≠ T565), F605 (≠ V571)
8w0cA Acetyl-coenzyme A synthetase 2
37% identity, 100% coverage: 3:625/626 of query aligns to 38:662/667 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 (= D479), R529 (= R494), R540 (= R505)
8w0bA Acetyl-coenzyme A synthetase 2
37% identity, 100% coverage: 3:625/626 of query aligns to 38:662/667 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 (= D479), I526 (= I491), R529 (= R494), R540 (= R505)
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, 99% coverage: 3:624/626 of query aligns to 40:673/683 of P52910
- K506 (≠ S468) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Query Sequence
>WP_057507018.1 NCBI__GCF_001431535.1:WP_057507018.1
MDYEETYRRSIDEPEAFWGEEANRIYWHKPPRQVLDYSNPPFRRWYVGGETNLCYNAVDR
HLAERPDQLALVAVSTETGTTREITYRQLYREVNDFAAVLKRLDVGHGDRVVIYMPNMAE
AVFAMLACARIGAVHSVVFGGFAAHNLALRIDDARPKLLIAADAGMRGGKLIPYKGMVDA
ACAEAQNPPPHVLIVSRGLDPAEPRQAGRDVDYATLRAEVGEVDVPVQWLESSEPSYLLY
TSGTTGKPKGVQRDVGGYAVAMAQSMQTVFDCQPGQVMFSTSDVGWAVGHSYNVYGPLIG
GCTSLLYEGLPTNPDPGIWWALCEQYNVRTLFSSPTAIRVLKKHDVDFIRRHDLKALKYI
FLAGEPLDEPTAHWANEALGKPIIDNYWQTETGWPALTLLPGLDMKPVRFGSPGFPNLGY
RMKVIDENTGVEVAPGQKGVLVMTPPLPPGCMSTVWNDDARFLQSYFSHFKELLYSSLDW
AIRDEDGYTFILGRTDDVINVAGHRLGTREIEEAISGHPRVAEAAVIGVKDELKGQVPLV
FVTLKQGLNGEDPAPVVAEMMAAVTASLGAVARPAHIHVVNALPKTRSGKLLRRSLQALA
EQRDPGDLSTLDDPAALDEIRRALGR
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