SitesBLAST
Comparing WP_015739815.1 NCBI__GCF_000024605.1:WP_015739815.1 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)
36% identity, 93% coverage: 29:557/567 of query aligns to 75:630/630 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 (= G322), E392 (= E323), P393 (≠ A324), T416 (= T344), W417 (= W345), W418 (≠ F346), Q419 (≠ M347), T420 (= T348), D502 (= D429), R517 (= R444), K523 (= K450), R528 (= R455)
- binding magnesium ion: V539 (≠ L466), H541 (= H468)
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)
34% identity, 90% coverage: 33:545/567 of query aligns to 73:624/651 of P9WQD1
- K617 (= K538) 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)
34% identity, 90% coverage: 33:545/567 of query aligns to 75:616/652 of P27550
- K609 (= K538) modified: N6-acetyllysine; by autocatalysis
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)
34% identity, 90% coverage: 33:545/567 of query aligns to 74:613/648 of Q89WV5
- G263 (= G207) mutation to I: Loss of activity.
- G266 (= G210) mutation to I: Great decrease in activity.
- K269 (= K213) mutation to G: Great decrease in activity.
- E414 (= E349) mutation to Q: Great decrease in activity.
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
33% identity, 92% coverage: 33:556/567 of query aligns to 71:623/634 of 1pg3A
- active site: T260 (= T205), T412 (= T348), E413 (= E349), N517 (≠ K450), R522 (= R455), K605 (= K538)
- binding coenzyme a: F159 (= F120), G160 (≠ E121), R187 (≠ L148), R190 (= R153), A301 (= A245), T307 (= T251), P330 (≠ L274), A356 (≠ I297), S519 (≠ G452), R580 (= R513), P585 (≠ D518)
- binding magnesium ion: V533 (≠ L466), H535 (= H468), I538 (≠ V471)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G322), E384 (= E323), P385 (≠ A324), T408 (= T344), W409 (= W345), W410 (≠ F346), Q411 (≠ M347), T412 (= T348), D496 (= D429), R511 (= R444), R522 (= R455)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
33% identity, 91% coverage: 33:550/567 of query aligns to 71:620/640 of 5jrhA
- active site: T260 (= T205), T412 (= T348), E413 (= E349), N517 (≠ K450), R522 (= R455), K605 (= K538)
- binding (r,r)-2,3-butanediol: W93 (= W57), E140 (= E101), G169 (≠ E130), K266 (= K211), P267 (= P212)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G322), E384 (= E323), P385 (≠ A324), T408 (= T344), W409 (= W345), W410 (≠ F346), Q411 (≠ M347), T412 (= T348), D496 (= D429), I508 (≠ Y441), N517 (≠ K450), R522 (= R455)
- binding coenzyme a: F159 (= F120), G160 (≠ E121), G161 (= G122), R187 (≠ L148), S519 (≠ G452), R580 (= R513), P585 (≠ D518)
- binding magnesium ion: V533 (≠ L466), H535 (= H468), I538 (≠ V471)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
33% identity, 90% coverage: 33:545/567 of query aligns to 70:611/637 of 2p2fA
- active site: T259 (= T205), T411 (= T348), E412 (= E349), N516 (≠ K450), R521 (= R455), K604 (= K538)
- binding adenosine monophosphate: G382 (= G322), E383 (= E323), P384 (≠ A324), T407 (= T344), W408 (= W345), W409 (≠ F346), Q410 (≠ M347), T411 (= T348), D495 (= D429), I507 (≠ Y441), R510 (= R444), N516 (≠ K450), R521 (= R455)
- binding coenzyme a: F158 (= F120), R186 (≠ L148), W304 (= W249), T306 (= T251), P329 (≠ L274), A352 (≠ T294), A355 (≠ I297), S518 (≠ G452), R579 (= R513), P584 (≠ D518)
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)
33% identity, 90% coverage: 33:545/567 of query aligns to 75:616/652 of Q8ZKF6
- R194 (= R153) 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 (= T251) binding CoA
- N335 (≠ E275) binding CoA
- A357 (≠ T294) 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 (= D446) 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 (≠ G452) binding CoA
- G524 (≠ E453) 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 (= R455) 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 (= R513) 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 (= K538) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
32% identity, 92% coverage: 33:555/567 of query aligns to 71:622/641 of 2p20A
- active site: T260 (= T205), T412 (= T348), E413 (= E349), N517 (≠ K450), R522 (= R455), K605 (= K538)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G322), E384 (= E323), P385 (≠ A324), T408 (= T344), W409 (= W345), W410 (≠ F346), Q411 (≠ M347), T412 (= T348), D496 (= D429), I508 (≠ Y441), R511 (= R444), R522 (= R455)
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)
32% identity, 90% coverage: 34:545/567 of query aligns to 102:668/701 of Q9NR19
- T363 (= T251) mutation to A: Loss of catalytic 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. 533:545, 54% identical) Nuclear localization signal
- S659 (≠ N536) 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 541:542) 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
8sf3A Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (amp, acetate and coa bound)
32% identity, 95% coverage: 10:550/567 of query aligns to 57:633/662 of 8sf3A
- binding adenosine monophosphate: G398 (= G322), E399 (= E323), P400 (≠ A324), T423 (= T344), W424 (= W345), Q426 (≠ M347), T427 (= T348), D511 (= D429), R526 (= R444), R537 (= R455)
- binding coenzyme a: F171 (= F120), G172 (≠ E121), G173 (= G122), R199 (≠ P145), K202 (≠ L148), R595 (= R513), P600 (≠ D518)
8u2rA Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (ethyl amp bound)
32% identity, 95% coverage: 10:550/567 of query aligns to 56:635/664 of 8u2rA
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I323 (≠ V250), G400 (= G322), E401 (= E323), P402 (≠ A324), T425 (= T344), W426 (= W345), W427 (≠ F346), Q428 (≠ M347), T429 (= T348), D513 (= D429), I525 (≠ Y441), R528 (= R444), R539 (= R455)
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)
31% identity, 90% coverage: 34:545/567 of query aligns to 102:668/701 of Q9QXG4
- K661 (= K538) modified: N6-acetyllysine
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)
32% identity, 85% coverage: 65:545/567 of query aligns to 118:625/662 of P78773
- T596 (≠ R515) modified: Phosphothreonine
7kvyA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate and co-enzyme a from coccidioides immitis rs
33% identity, 85% coverage: 64:545/567 of query aligns to 116:619/633 of 7kvyA
- active site: T271 (= T205), T422 (= T348), E423 (= E349), N529 (≠ K450), R534 (= R455), K612 (= K538)
- binding coenzyme a: F172 (= F120), G174 (= G122), R200 (vs. gap), G312 (≠ A245), Y362 (= Y292), V363 (≠ T293), A364 (≠ T294), S531 (≠ G452), G532 (≠ E453), R592 (= R513), F598 (≠ Y519)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: G393 (= G322), E394 (= E323), P395 (≠ A324), T418 (= T344), Y419 (≠ W345), W420 (≠ F346), Q421 (≠ M347), T422 (= T348), D508 (= D429), I520 (≠ Y441), R523 (= R444), R534 (= R455)
7l3qA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-methylphosphate and co-enzyme a from coccidioides immitis rs
33% identity, 85% coverage: 64:544/567 of query aligns to 117:620/631 of 7l3qA
- active site: T272 (= T205), T423 (= T348), E424 (= E349), N530 (≠ K450), R535 (= R455)
- binding coenzyme a: F173 (= F120), A174 (≠ E121), G175 (= G122), R201 (vs. gap), G313 (≠ A245), Y363 (= Y292), A365 (≠ T294), S532 (≠ G452), G533 (≠ E453), R593 (= R513), P598 (≠ D518), F599 (≠ Y519)
- binding 5'-O-[(R)-hydroxy(methoxy)phosphoryl]adenosine: I318 (≠ V250), G394 (= G322), E395 (= E323), P396 (≠ A324), T419 (= T344), Y420 (≠ W345), Q422 (≠ M347), T423 (= T348), D509 (= D429), R524 (= R444), R535 (= R455)
7kdnA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-propylphosphate from aspergillus fumigatus
32% identity, 85% coverage: 65:545/567 of query aligns to 117:619/622 of 7kdnA
- active site: T271 (= T205), T422 (= T348), E423 (= E349), N529 (≠ K450), R534 (= R455), K612 (= K538)
- binding adenosine-5'-monophosphate-propyl ester: G393 (= G322), E394 (= E323), P395 (≠ A324), T418 (= T344), Y419 (≠ W345), W420 (≠ F346), Q421 (≠ M347), T422 (= T348), D508 (= D429), I520 (≠ Y441), R523 (= R444), R534 (= R455)
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)
31% identity, 91% coverage: 32:545/567 of query aligns to 100:642/682 of Q99NB1
- K635 (= K538) 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)
31% identity, 91% coverage: 32:545/567 of query aligns to 107:649/689 of Q9NUB1
- V488 (≠ L387) to M: in dbSNP:rs6050249
- K642 (= K538) modified: N6-acetyllysine; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
7mmzA Crystal structure of acetyl-coenzyme a synthetase from legionella pneumophila philadelphia 1 in complex with ethyl-amp (see paper)
32% identity, 87% coverage: 33:526/567 of query aligns to 46:557/559 of 7mmzA
- active site: T231 (= T205), T383 (= T348), E384 (= E349), N486 (≠ K450), R491 (= R455)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I277 (≠ V250), G354 (= G322), E355 (= E323), P356 (≠ A324), T379 (= T344), W380 (= W345), W381 (≠ F346), Q382 (≠ M347), T383 (= T348), D465 (= D429), I477 (≠ Y441), R480 (= R444), R491 (= R455)
Query Sequence
>WP_015739815.1 NCBI__GCF_000024605.1:WP_015739815.1
MLRPNLEDYEEVCRTFTWEQAEEELGVKNSSRINLAALAVDQPCREGKGDRIALRFWDGV
KECSFTFAELKGLSDRFALVLEKLGVEPGDRVALFGPPAPELYASFLGIIKRGAIAVPLF
EGYMPEALAEFLREAEAKVLVTSAPGRLKFDWRSVPELKYILVVGLVEAREAGGVISWYR
AVGEAVGEPKVVPLPKEAPFVLLFTSGSTGKPKGILLPHRAAVQYYQTGKWVLDLKENDV
YWCTAGLSWVTGVAYGVLAPWLNRVTTVIYGGELEPENFYETFRRFGVTVWYTTPMILRT
LMAAEKVLPPVSHRLRHILTVGEALNPALVRWSRTVFGVEVYDTWFMTETGGHMIANFRC
LPVKAGSMGKPVPGVKVAVLDPQGKELGPYEIGQLALLPPWPAMFQGVWRDEARYQEYFR
LAPWYLTGDLVYRDKEGYYWYQGRVDDLIKVGEKRVGPCEIESKLLEHPAVLEAGVIGKP
DFWRGEIVKAFIVLRPGYQWSAKLQAELTRFIRTRLADYLVPQEFEVLPQLPRTPNGKLL
RRVLKAWDMGLPCDDGTGRGEAWKSGR
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