SitesBLAST
Comparing WP_083924434.1 NCBI__GCF_000341125.1:WP_083924434.1 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)
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)
64% identity, 97% coverage: 1:427/438 of query aligns to 213:647/651 of P9WQD1
- K617 (= K397) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
52% identity, 98% coverage: 1:430/438 of query aligns to 210:638/641 of 2p20A
- active site: T260 (= T50), T412 (= T203), E413 (= E204), N517 (≠ L308), R522 (≠ N313), K605 (= K397)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G174), E384 (= E175), P385 (= P176), T408 (= T199), W409 (= W200), W410 (= W201), Q411 (= Q202), T412 (= T203), D496 (= D287), I508 (≠ L299), R511 (= R302), R522 (≠ N313)
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)
52% identity, 99% coverage: 1:435/438 of query aligns to 214:649/652 of Q8ZKF6
- T311 (= T98) binding CoA
- N335 (≠ D122) binding CoA
- A357 (= A144) 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 (= D304) 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 (= S310) binding CoA
- G524 (= G311) 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 (≠ N313) 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 (≠ G372) 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 (= K397) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
Sites not aligning to the query:
- 194 R→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.; R→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.
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)
52% identity, 99% coverage: 1:435/438 of query aligns to 214:649/652 of P27550
- K609 (= K397) modified: N6-acetyllysine; by autocatalysis
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
53% identity, 98% coverage: 1:430/438 of query aligns to 210:637/640 of 5jrhA
- active site: T260 (= T50), T412 (= T203), E413 (= E204), N517 (≠ L308), R522 (≠ N313), K605 (= K397)
- binding (r,r)-2,3-butanediol: K266 (= K56), P267 (= P57)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G174), E384 (= E175), P385 (= P176), T408 (= T199), W409 (= W200), W410 (= W201), Q411 (= Q202), T412 (= T203), D496 (= D287), I508 (≠ L299), N517 (≠ L308), R522 (≠ N313)
- binding coenzyme a: S519 (= S310), R580 (≠ G372), P585 (= P377)
- binding magnesium ion: V533 (= V324), H535 (= H326), I538 (≠ V329)
Sites not aligning to the query:
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)
51% identity, 97% coverage: 4:430/438 of query aligns to 214:641/648 of Q89WV5
- G263 (= G52) mutation to I: Loss of activity.
- G266 (≠ A55) mutation to I: Great decrease in activity.
- K269 (= K58) mutation to G: Great decrease in activity.
- E414 (= E204) mutation to Q: Great decrease in activity.
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
53% identity, 98% coverage: 1:430/438 of query aligns to 209:634/637 of 2p2fA
- active site: T259 (= T50), T411 (= T203), E412 (= E204), N516 (≠ L308), R521 (≠ N313), K604 (= K397)
- binding adenosine monophosphate: G382 (= G174), E383 (= E175), P384 (= P176), T407 (= T199), W408 (= W200), W409 (= W201), Q410 (= Q202), T411 (= T203), D495 (= D287), I507 (≠ L299), R510 (= R302), N516 (≠ L308), R521 (≠ N313)
- binding coenzyme a: W304 (= W96), T306 (= T98), P329 (= P121), A352 (= A144), A355 (= A147), S518 (= S310), R579 (≠ G372), P584 (= P377)
Sites not aligning to the query:
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
54% identity, 93% coverage: 1:407/438 of query aligns to 210:615/634 of 1pg3A
- active site: T260 (= T50), T412 (= T203), E413 (= E204), N517 (≠ L308), R522 (≠ N313), K605 (= K397)
- binding coenzyme a: A301 (= A92), T307 (= T98), P330 (= P121), A356 (= A147), S519 (= S310), R580 (≠ G372), P585 (= P377)
- binding magnesium ion: V533 (= V324), H535 (= H326), I538 (≠ V329)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G174), E384 (= E175), P385 (= P176), T408 (= T199), W409 (= W200), W410 (= W201), Q411 (= Q202), T412 (= T203), D496 (= D287), R511 (= R302), R522 (≠ N313)
Sites not aligning to the query:
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)
51% identity, 96% coverage: 7:425/438 of query aligns to 270:690/701 of Q9QXG4
- K661 (= K397) 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)
51% identity, 96% coverage: 7:425/438 of query aligns to 270:690/701 of Q9NR19
- T363 (= T98) 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. 392:404, 92% identical) Nuclear localization signal
- S659 (= S395) 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 400:401) 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
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
53% identity, 95% coverage: 1:416/438 of query aligns to 216:630/630 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 (= G174), E392 (= E175), P393 (= P176), T416 (= T199), W417 (= W200), W418 (= W201), Q419 (= Q202), T420 (= T203), D502 (= D287), R517 (= R302), K523 (≠ L308), R528 (≠ N313)
- binding magnesium ion: V539 (= V324), H541 (= H326)
7l4gB Crystal structure of acetyl-coa synthetase in complex with acetyl adenylate from cryptococcus neoformans h99
48% identity, 98% coverage: 1:431/438 of query aligns to 230:667/668 of 7l4gB
- active site: T280 (= T50), T432 (= T203), E433 (= E204), N539 (≠ L308), R544 (≠ N313), K631 (= K397)
- 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: W325 (= W96), G403 (= G174), E404 (= E175), P405 (= P176), T428 (= T199), Y429 (≠ W200), W430 (= W201), M431 (≠ Q202), T432 (= T203), D518 (= D287), I530 (≠ L299), R533 (= R302)
5u29A Crystal structure of cryptococcus neoformans h99 acetyl-coa synthetase in complex with ac-ams
48% identity, 98% coverage: 1:431/438 of query aligns to 230:667/668 of 5u29A
- active site: T280 (= T50), T432 (= T203), E433 (= E204), N539 (≠ L308), R544 (≠ N313), K631 (= K397)
- binding 5'-O-(acetylsulfamoyl)adenosine: W325 (= W96), G403 (= G174), E404 (= E175), P405 (= P176), T428 (= T199), Y429 (≠ W200), W430 (= W201), M431 (≠ Q202), T432 (= T203), D518 (= D287), I530 (≠ L299), R533 (= R302)
8g0vA Crystal structure of acetyl-coa synthetase in complex with a propyne ester amp inhibitor from cryptococcus neoformans h99
48% identity, 98% coverage: 1:431/438 of query aligns to 230:665/666 of 8g0vA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: W323 (= W96), I324 (≠ V97), V400 (= V173), G401 (= G174), E402 (= E175), P403 (= P176), T426 (= T199), Y427 (≠ W200), W428 (= W201), M429 (≠ Q202), T430 (= T203), D516 (= D287)
8g0uA Crystal structure of acetyl-coa synthetase in complex with an isopropyl ester amp inhibitor from cryptococcus neoformans h99
48% identity, 98% coverage: 1:431/438 of query aligns to 230:665/666 of 8g0uA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: W323 (= W96), I324 (≠ V97), G401 (= G174), E402 (= E175), P403 (= P176), T426 (= T199), Y427 (≠ W200), W428 (= W201), M429 (≠ Q202), T430 (= T203), D516 (= D287), I528 (≠ L299), R531 (= R302)
7knoA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate from cryptococcus neoformans var. Grubii serotype a (h99)
48% identity, 98% coverage: 1:431/438 of query aligns to 230:665/666 of 7knoA
- active site: T280 (= T50), T430 (= T203), E431 (= E204), N537 (≠ L308), R542 (≠ N313), K629 (= K397)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: W323 (= W96), I324 (≠ V97), G401 (= G174), E402 (= E175), P403 (= P176), T426 (= T199), Y427 (≠ W200), W428 (= W201), M429 (≠ Q202), T430 (= T203), D516 (= D287), R531 (= R302)
5k8fA Crystal structure of acetyl-coa synthetase in complex with atp and acetyl-amp from cryptococcus neoformans h99
50% identity, 93% coverage: 1:406/438 of query aligns to 230:640/656 of 5k8fA
- active site: T280 (= T50), T432 (= T203), E433 (= E204), N539 (≠ L308), R544 (≠ N313), K631 (= K397)
- 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: W325 (= W96), I326 (≠ V97), G403 (= G174), E404 (= E175), P405 (= P176), T428 (= T199), Y429 (≠ W200), W430 (= W201), M431 (≠ Q202), T432 (= T203), D518 (= D287), I530 (≠ L299), R533 (= R302), K631 (= K397)
- binding adenosine-5'-triphosphate: T280 (= T50), S281 (= S51), G282 (= G52), S283 (≠ T53), T284 (= T54), K288 (= K58), G403 (= G174), E404 (= E175), P405 (= P176), T428 (= T199), Y429 (≠ W200), M431 (≠ Q202), T432 (= T203), D518 (= D287), I530 (≠ L299), R533 (= R302), K631 (= K397)
8g0tA Crystal structure of acetyl-coa synthetase in complex with a cyclopropyl ester amp inhibitor from cryptococcus neoformans h99
49% identity, 95% coverage: 1:414/438 of query aligns to 229:644/656 of 8g0tA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: W321 (= W96), I322 (≠ V97), G399 (= G174), E400 (= E175), P401 (= P176), D423 (= D198), T424 (= T199), Y425 (≠ W200), W426 (= W201), M427 (≠ Q202), T428 (= T203), D514 (= D287), R529 (= R302), K627 (= K397)
7knpA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-butylphosphate from cryptococcus neoformans var. Grubii serotype a (h99)
50% identity, 93% coverage: 1:406/438 of query aligns to 230:638/653 of 7knpA
- active site: T280 (= T50), T430 (= T203), E431 (= E204), N537 (≠ L308), R542 (≠ N313), K629 (= K397)
- binding 5'-O-[(S)-butoxy(hydroxy)phosphoryl]adenosine: T325 (= T98), V400 (= V173), G401 (= G174), E402 (= E175), P403 (= P176), T426 (= T199), Y427 (≠ W200), W428 (= W201), M429 (≠ Q202), T430 (= T203), D516 (= D287), I528 (≠ L299), R531 (= R302)
7mmzA Crystal structure of acetyl-coenzyme a synthetase from legionella pneumophila philadelphia 1 in complex with ethyl-amp (see paper)
52% identity, 83% coverage: 18:381/438 of query aligns to 199:553/559 of 7mmzA
- active site: T231 (= T50), T383 (= T203), E384 (= E204), N486 (≠ L308), R491 (≠ N313)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I277 (≠ V97), G354 (= G174), E355 (= E175), P356 (= P176), T379 (= T199), W380 (= W200), W381 (= W201), Q382 (= Q202), T383 (= T203), D465 (= D287), I477 (≠ L299), R480 (= R302), R491 (≠ N313)
Query Sequence
>WP_083924434.1 NCBI__GCF_000341125.1:WP_083924434.1
MENVLVVRRTGQDVEWTDRDVWWHEAVEAASTEHTPEAHDAEDPLYIMYTSGTTAKPKGI
LHTTGGYLTQVSYTHWAVFDLKADTDVFWCAADIGWVTGHSYIVYGPLSNAATTVMYEGT
PDTPHRGRFWEIVEKYKVTIAYMAPTAIRTFMKWGDDIPAKFDLSSLRVIGSVGEPINPE
AYVWYREHIGGGRTPVVDTWWQTETGAIMVSPLPGVTAGKPGAAMRGLPGVVADVVDEAG
DSVPDGEGGFIVIREPWPSMLRGIWGDPERYKDTYWSRFEGLYFPGDGAKKDEDGDLWLL
GRVDDVMLVSGHNISTTEVESALVSHPKVAEAAVVGATDKVTGQAIVGFVILRGGAEEVP
EELVKELRDHVGASLGPIAKPARLLAVPELPKTRSGKIMRRLLRDIAENRAVGDTSTLTD
SSIMDVIARQLPSAAKGE
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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