SitesBLAST
Comparing YP_001328853.1 NCBI__GCF_000017145.1:YP_001328853.1 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)
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)
71% identity, 100% coverage: 1:648/649 of query aligns to 1:645/648 of Q89WV5
- G263 (= G266) mutation to I: Loss of activity.
- G266 (= G269) mutation to I: Great decrease in activity.
- K269 (= K272) mutation to G: Great decrease in activity.
- E414 (= E417) 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)
67% identity, 98% coverage: 14:646/649 of query aligns to 15:646/652 of P27550
- K609 (= K609) 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)
67% identity, 98% coverage: 14:646/649 of query aligns to 15:646/652 of Q8ZKF6
- R194 (≠ K192) 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 (= T311) binding CoA
- N335 (= N335) binding CoA
- A357 (= A357) 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 (= D517) 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 (= S523) binding CoA
- G524 (= G524) 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 (= R526) 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 (= R584) 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 (= K609) 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)
67% identity, 98% coverage: 14:646/649 of query aligns to 11:639/640 of 5jrhA
- active site: T260 (= T264), T412 (= T416), E413 (= E417), N517 (= N521), R522 (= R526), K605 (= K609)
- binding (r,r)-2,3-butanediol: W93 (= W95), E140 (= E142), G169 (= G171), K266 (= K270), P267 (= P271)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G387), E384 (= E388), P385 (= P389), T408 (= T412), W409 (= W413), W410 (= W414), Q411 (= Q415), T412 (= T416), D496 (= D500), I508 (= I512), N517 (= N521), R522 (= R526)
- binding coenzyme a: F159 (= F161), G160 (= G162), G161 (= G163), R187 (= R189), S519 (= S523), R580 (= R584), P585 (= P589)
- binding magnesium ion: V533 (= V537), H535 (= H539), I538 (≠ V542)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
66% identity, 98% coverage: 14:646/649 of query aligns to 11:640/641 of 2p20A
- active site: T260 (= T264), T412 (= T416), E413 (= E417), N517 (= N521), R522 (= R526), K605 (= K609)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G387), E384 (= E388), P385 (= P389), T408 (= T412), W409 (= W413), W410 (= W414), Q411 (= Q415), T412 (= T416), D496 (= D500), I508 (= I512), R511 (= R515), R522 (= R526)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
66% identity, 98% coverage: 14:646/649 of query aligns to 10:636/637 of 2p2fA
- active site: T259 (= T264), T411 (= T416), E412 (= E417), N516 (= N521), R521 (= R526), K604 (= K609)
- binding adenosine monophosphate: G382 (= G387), E383 (= E388), P384 (= P389), T407 (= T412), W408 (= W413), W409 (= W414), Q410 (= Q415), T411 (= T416), D495 (= D500), I507 (= I512), R510 (= R515), N516 (= N521), R521 (= R526)
- binding coenzyme a: F158 (= F161), R186 (= R189), W304 (= W309), T306 (= T311), P329 (= P334), A352 (= A357), A355 (= A360), S518 (= S523), R579 (= R584), P584 (= P589)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
66% identity, 98% coverage: 14:646/649 of query aligns to 11:633/634 of 1pg3A
- active site: T260 (= T264), T412 (= T416), E413 (= E417), N517 (= N521), R522 (= R526), K605 (= K609)
- binding coenzyme a: F159 (= F161), G160 (= G162), R187 (= R189), R190 (≠ K192), A301 (= A305), T307 (= T311), P330 (= P334), A356 (= A360), S519 (= S523), R580 (= R584), P585 (= P589)
- binding magnesium ion: V533 (= V537), H535 (= H539), I538 (≠ V542)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G387), E384 (= E388), P385 (= P389), T408 (= T412), W409 (= W413), W410 (= W414), Q411 (= Q415), T412 (= T416), D496 (= D500), R511 (= R515), R522 (= R526)
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)
53% identity, 98% coverage: 7:645/649 of query aligns to 31:696/701 of Q9NR19
- T363 (= T311) 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. 604:616, 92% identical) Nuclear localization signal
- S659 (= S607) 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 612:613) 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)
53% identity, 98% coverage: 7:645/649 of query aligns to 31:696/701 of Q9QXG4
- K661 (= K609) modified: N6-acetyllysine
8u2rA Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (ethyl amp bound)
54% identity, 96% coverage: 24:647/649 of query aligns to 25:661/664 of 8u2rA
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I323 (≠ V310), G400 (= G387), E401 (= E388), P402 (= P389), T425 (= T412), W426 (= W413), W427 (= W414), Q428 (= Q415), T429 (= T416), D513 (= D500), I525 (= I512), R528 (= R515), R539 (= R526)
8sf3A Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (amp, acetate and coa bound)
54% identity, 96% coverage: 24:647/649 of query aligns to 26:659/662 of 8sf3A
- binding adenosine monophosphate: G398 (= G387), E399 (= E388), P400 (= P389), T423 (= T412), W424 (= W413), Q426 (= Q415), T427 (= T416), D511 (= D500), R526 (= R515), R537 (= R526)
- binding coenzyme a: F171 (= F161), G172 (= G162), G173 (= G163), R199 (= R189), K202 (= K192), R595 (= R584), P600 (= P589)
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)
52% identity, 96% coverage: 22:647/649 of query aligns to 57:680/689 of Q9NUB1
- V488 (= V456) to M: in dbSNP:rs6050249
- K642 (= K609) modified: N6-acetyllysine; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
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)
53% identity, 96% coverage: 22:647/649 of query aligns to 50:673/682 of Q99NB1
- K635 (= K609) modified: N6-acetyllysine
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)
49% identity, 97% coverage: 19:648/649 of query aligns to 36:676/683 of P52910
- K506 (≠ S490) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
7mmzA Crystal structure of acetyl-coenzyme a synthetase from legionella pneumophila philadelphia 1 in complex with ethyl-amp (see paper)
56% identity, 87% coverage: 37:599/649 of query aligns to 10:559/559 of 7mmzA
- active site: T231 (= T264), T383 (= T416), E384 (= E417), N486 (= N521), R491 (= R526)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I277 (≠ V310), G354 (= G387), E355 (= E388), P356 (= P389), T379 (= T412), W380 (= W413), W381 (= W414), Q382 (= Q415), T383 (= T416), D465 (= D500), I477 (= I512), R480 (= R515), R491 (= R526)
7l4gB Crystal structure of acetyl-coa synthetase in complex with acetyl adenylate from cryptococcus neoformans h99
52% identity, 96% coverage: 21:641/649 of query aligns to 40:663/668 of 7l4gB
- active site: T280 (= T264), T432 (= T416), E433 (= E417), N539 (= N521), R544 (= R526), K631 (= K609)
- 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 (= W309), G403 (= G387), E404 (= E388), P405 (= P389), T428 (= T412), Y429 (≠ W413), W430 (= W414), M431 (≠ Q415), T432 (= T416), D518 (= D500), I530 (= I512), R533 (= R515)
5u29A Crystal structure of cryptococcus neoformans h99 acetyl-coa synthetase in complex with ac-ams
52% identity, 96% coverage: 21:641/649 of query aligns to 40:663/668 of 5u29A
- active site: T280 (= T264), T432 (= T416), E433 (= E417), N539 (= N521), R544 (= R526), K631 (= K609)
- binding 5'-O-(acetylsulfamoyl)adenosine: W325 (= W309), G403 (= G387), E404 (= E388), P405 (= P389), T428 (= T412), Y429 (≠ W413), W430 (= W414), M431 (≠ Q415), T432 (= T416), D518 (= D500), I530 (= I512), R533 (= R515)
8g0vA Crystal structure of acetyl-coa synthetase in complex with a propyne ester amp inhibitor from cryptococcus neoformans h99
51% identity, 96% coverage: 21:641/649 of query aligns to 40:661/666 of 8g0vA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: W323 (= W309), I324 (≠ V310), V400 (= V386), G401 (= G387), E402 (= E388), P403 (= P389), T426 (= T412), Y427 (≠ W413), W428 (= W414), M429 (≠ Q415), T430 (= T416), D516 (= D500)
8g0uA Crystal structure of acetyl-coa synthetase in complex with an isopropyl ester amp inhibitor from cryptococcus neoformans h99
51% identity, 96% coverage: 21:641/649 of query aligns to 40:661/666 of 8g0uA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: W323 (= W309), I324 (≠ V310), G401 (= G387), E402 (= E388), P403 (= P389), T426 (= T412), Y427 (≠ W413), W428 (= W414), M429 (≠ Q415), T430 (= T416), D516 (= D500), I528 (= I512), R531 (= R515)
7knoA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate from cryptococcus neoformans var. Grubii serotype a (h99)
51% identity, 96% coverage: 21:641/649 of query aligns to 40:661/666 of 7knoA
- active site: T280 (= T264), T430 (= T416), E431 (= E417), N537 (= N521), R542 (= R526), K629 (= K609)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: W323 (= W309), I324 (≠ V310), G401 (= G387), E402 (= E388), P403 (= P389), T426 (= T412), Y427 (≠ W413), W428 (= W414), M429 (≠ Q415), T430 (= T416), D516 (= D500), R531 (= R515)
Query Sequence
>YP_001328853.1 NCBI__GCF_000017145.1:YP_001328853.1
MDVKTYPVLEAAKNRTLLDNETYLKWYQESVADPETFWGEHGKRIDWFEPYTKVKNTTFE
GDVSIKWFEDGLTNVSYNCIDRHLKAHGDKTAIIWEGDNPYLDKKITYNELYDTVCRLAN
VLKKHGVKKGDRVTIYMPMIPEAAYAMLACTRIGAVHSVVFGGFSPEALAGRIVDCESTF
VITCDEGVRGGKPVALKENTDTAVGIAAKQNVTVGKVLVVRRTGGKVGWAPERDLWYHQE
TAAVEPHCPPERMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYASMTHQYVFDYQDGDI
YWCTADVGWVTGHSYIVYGPLANAATTLMFEGVPNFPDAGRFWEVVDKHKVNIFYTAPTA
IRSLMGAGDDFVKRSSRSSLRLLGTVGEPINPEAWEWYYHVVGDERCPVVDTWWQTETGG
ILITPLPGATDLKPGSATRPFFGVQPQIVDGEGNVVEGAADGNLCIIDSWPGQMRTVYGD
HERFIQTYFSTYKGKYFTGDGCRRDEDGYYWITGRVDDVLNVSGHRLGTAEVESALVSHQ
LVSEAAVVGYPHSIKGQGIYCYVSLMAGEVGNDELRQALVKHVRSEIGPIATPDKIQFAP
GLPKTRSGKIMRRILRKIAEDDFGSLGDTSTLADPSVVDDLIANRQNRA
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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