SitesBLAST
Comparing 3610172 Dshi_3553 acetate--CoA ligase (RefSeq) 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)
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)
68% identity, 98% coverage: 11:657/658 of query aligns to 3:646/648 of Q89WV5
- G263 (= G272) mutation to I: Loss of activity.
- G266 (= G275) mutation to I: Great decrease in activity.
- K269 (= K278) mutation to G: Great decrease in activity.
- E414 (= E423) mutation to Q: Great decrease in 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)
63% identity, 97% coverage: 16:653/658 of query aligns to 9:645/652 of P27550
- K609 (= K617) modified: N6-acetyllysine; by autocatalysis
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)
63% identity, 97% coverage: 15:653/658 of query aligns to 8:645/652 of Q8ZKF6
- R194 (= R202) 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 (= T317) binding
- N335 (≠ T341) binding
- A357 (= A363) 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 (= D525) 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 (= S531) binding
- G524 (= G532) 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 (= R534) 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 (= R592) 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 (= K617) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
63% identity, 97% coverage: 15:653/658 of query aligns to 4:638/640 of 5jrhA
- active site: T260 (= T270), T412 (= T422), E413 (= E423), N517 (= N529), R522 (= R534), K605 (= K617)
- binding (r,r)-2,3-butanediol: W93 (≠ F104), E140 (= E152), G169 (≠ A181), K266 (≠ Q276), P267 (= P277)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G393), E384 (= E394), P385 (= P395), T408 (= T418), W409 (= W419), W410 (= W420), Q411 (= Q421), T412 (= T422), D496 (= D508), I508 (= I520), N517 (= N529), R522 (= R534)
- binding coenzyme a: F159 (= F171), G160 (≠ A172), G161 (= G173), R187 (= R199), S519 (= S531), R580 (= R592), P585 (= P597)
- binding magnesium ion: V533 (= V545), H535 (= H547), I538 (≠ V550)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
62% identity, 97% coverage: 15:653/658 of query aligns to 4:639/641 of 2p20A
- active site: T260 (= T270), T412 (= T422), E413 (= E423), N517 (= N529), R522 (= R534), K605 (= K617)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G393), E384 (= E394), P385 (= P395), T408 (= T418), W409 (= W419), W410 (= W420), Q411 (= Q421), T412 (= T422), D496 (= D508), I508 (= I520), R511 (= R523), R522 (= R534)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
62% identity, 97% coverage: 15:653/658 of query aligns to 3:635/637 of 2p2fA
- active site: T259 (= T270), T411 (= T422), E412 (= E423), N516 (= N529), R521 (= R534), K604 (= K617)
- binding adenosine monophosphate: G382 (= G393), E383 (= E394), P384 (= P395), T407 (= T418), W408 (= W419), W409 (= W420), Q410 (= Q421), T411 (= T422), D495 (= D508), I507 (= I520), R510 (= R523), N516 (= N529), R521 (= R534)
- binding coenzyme a: F158 (= F171), R186 (= R199), W304 (= W315), T306 (= T317), P329 (= P340), A352 (= A363), A355 (= A366), S518 (= S531), R579 (= R592), P584 (= P597)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
62% identity, 97% coverage: 15:653/658 of query aligns to 4:632/634 of 1pg3A
- active site: T260 (= T270), T412 (= T422), E413 (= E423), N517 (= N529), R522 (= R534), K605 (= K617)
- binding coenzyme a: F159 (= F171), G160 (≠ A172), R187 (= R199), R190 (= R202), A301 (= A311), T307 (= T317), P330 (= P340), A356 (= A366), S519 (= S531), R580 (= R592), P585 (= P597)
- binding magnesium ion: V533 (= V545), H535 (= H547), I538 (≠ V550)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G393), E384 (= E394), P385 (= P395), T408 (= T418), W409 (= W419), W410 (= W420), Q411 (= Q421), T412 (= T422), D496 (= D508), R511 (= R523), R522 (= R534)
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)
55% identity, 97% coverage: 19:653/658 of query aligns to 34:696/701 of Q9NR19
- T363 (= T317) 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. 612:624, 92% identical) Nuclear localization signal
- S659 (= S615) 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 620:621) 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
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)
54% identity, 97% coverage: 19:653/658 of query aligns to 34:696/701 of Q9QXG4
- K661 (= K617) modified: N6-acetyllysine
8u2rA Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (ethyl amp bound)
52% identity, 94% coverage: 33:650/658 of query aligns to 26:656/664 of 8u2rA
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I323 (≠ V316), G400 (= G393), E401 (= E394), P402 (= P395), T425 (= T418), W426 (= W419), W427 (= W420), Q428 (= Q421), T429 (= T422), D513 (= D508), I525 (= I520), R528 (= R523), R539 (= R534)
8sf3A Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (amp, acetate and coa bound)
51% identity, 96% coverage: 17:650/658 of query aligns to 9:654/662 of 8sf3A
- binding adenosine monophosphate: G398 (= G393), E399 (= E394), P400 (= P395), T423 (= T418), W424 (= W419), Q426 (= Q421), T427 (= T422), D511 (= D508), R526 (= R523), R537 (= R534)
- binding coenzyme a: F171 (= F171), G172 (≠ A172), G173 (= G173), R199 (= R199), K202 (≠ R202), R595 (= R592), P600 (= P597)
8w0cA Acetyl-coenzyme A synthetase 2
50% identity, 98% coverage: 8:650/658 of query aligns to 10:658/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G393), E400 (= E394), P401 (= P395), T424 (= T418), Y425 (≠ W419), W426 (= W420), Q427 (= Q421), T428 (= T422), D514 (= D508), R529 (= R523), R540 (= R534)
8w0bA Acetyl-coenzyme A synthetase 2
50% identity, 98% coverage: 8:650/658 of query aligns to 10:658/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (= V392), G399 (= G393), E400 (= E394), P401 (= P395), T424 (= T418), Y425 (≠ W419), W426 (= W420), Q427 (= Q421), T428 (= T422), D514 (= D508), I526 (= I520), R529 (= R523), R540 (= R534)
8w0dA Acetyl-coenzyme A synthetase 2
50% identity, 98% coverage: 8:650/658 of query aligns to 9:657/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G393), E399 (= E394), P400 (= P395), T423 (= T418), Y424 (≠ W419), W425 (= W420), Q426 (= Q421), T427 (= T422), D513 (= D508), I525 (= I520), R528 (= R523), R539 (= R534)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
50% identity, 98% coverage: 8:650/658 of query aligns to 9:657/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G393), E399 (= E394), P400 (= P395), T423 (= T418), Y424 (≠ W419), Q426 (= Q421), T427 (= T422), D513 (= D508), I525 (= I520), R528 (= R523), R539 (= R534)
- binding coenzyme a: F175 (= F171), R203 (= R199), R206 (= R202), G316 (≠ A311), H538 (= H533), R599 (= R592), F605 (≠ I598)
8w0jA Acetyl-coenzyme A synthetase 2
50% identity, 98% coverage: 8:650/658 of query aligns to 10:653/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G393), E400 (= E394), P401 (= P395), T424 (= T418), Y425 (≠ W419), W426 (= W420), Q427 (= Q421), T428 (= T422), D514 (= D508), I526 (= I520), R529 (= R523), R540 (= R534)
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
50% identity, 98% coverage: 8:650/658 of query aligns to 9:652/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (= P148), A176 (= A172), G177 (= G173), R203 (= R199), T208 (= T204), D317 (= D312), E342 (= E337), G343 (= G338), P345 (= P340), G398 (= G393), E399 (= E394), P400 (= P395), T423 (= T418), W425 (= W420), Q426 (= Q421), T427 (= T422), D513 (= D508), I525 (= I520), R528 (= R523), R539 (= R534)
8v4oA Crystal structure of acetyl-coa synthetase 2 in complex with amp from candida albicans
50% identity, 98% coverage: 8:650/658 of query aligns to 9:652/660 of 8v4oA
- binding adenosine monophosphate: G398 (= G393), E399 (= E394), P400 (= P395), T423 (= T418), Y424 (≠ W419), W425 (= W420), Q426 (= Q421), T427 (= T422), D513 (= D508), I525 (= I520), R528 (= R523), R539 (= R534)
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)
50% identity, 94% coverage: 30:650/658 of query aligns to 34:651/662 of P78773
- T596 (≠ E594) modified: Phosphothreonine
7kdsA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-propylphosphate from candida albicans
49% identity, 98% coverage: 8:650/658 of query aligns to 9:647/654 of 7kdsA
- active site: T275 (= T270), T427 (= T422), E428 (= E423), N534 (= N529), R539 (= R534), K620 (= K617)
- binding adenosine-5'-monophosphate-propyl ester: I321 (≠ V316), G398 (= G393), E399 (= E394), P400 (= P395), D422 (= D417), T423 (= T418), Y424 (≠ W419), W425 (= W420), Q426 (= Q421), T427 (= T422), D513 (= D508), R528 (= R523), N534 (= N529), R539 (= R534)
Query Sequence
>3610172 Dshi_3553 acetate--CoA ligase (RefSeq)
MTEQKPIASGEIIKAVSEEFAANAHIDSSKYSEMYAASVSDPEGFWGEHGRSLDWIKPYT
KVKDTSFAHDDVHVRWFEDGTLNVAANCIDRHLATRGDQTAIIFEPDDPAEPAQHITYRE
LHRQVCKLSNVLEDLGVRKGDRVILYMPMIPEAAYAMLACARIGAIHSIVFAGFSPDALS
ARINGADARLLITADYAPRGGRQTPLKSNADAALLHTRDDVKMLVVKRTGGQTTWVDGRD
FDYHELMLEADEVQHPVEVEAEHPLFILYTSGSTGQPKGVVHSSGGYLLYAAMTQKYVFD
VHEGDVYWCTADVGWVTGHSYIVYGPLANGGTTVMFEGVPTYPDASRFWQVCDKHKVTQF
YTAPTAIRALMAKGPEFVETCDLSSLRVLGTVGEPINPEAWNWYNDLVGKGRCPIVDTWW
QTETGGHLLTPLPGAIATKPGSATLPFFGVQPVVLDPHSGAEITETECEGVLCLKDSWPG
QMRTVYGDHERFVKTYFSDYKGYYFSGDGCRRDADGYYWITGRVDDVINVSGHRMGTAEV
ESALVAHAKVAEAAVVGYPHDIKGQGIYCYVTLMNGEEPSEELRKELRTWVRTEIGPIAA
PDLIQWAPGLPKTRSGKIMRRILRKIAEDDFGALGDTSTLADPSVVEDLIENRMNKKG
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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