SitesBLAST
Comparing 5210124 FitnessBrowser__PV4:5210124 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)
5gxdA Structure of acryloyl-coa lyase prpe from dinoroseobacter shibae dfl 12
62% identity, 94% coverage: 33:657/662 of query aligns to 2:626/627 of 5gxdA
- active site: T238 (= T269), T390 (= T421), E391 (= E422), N498 (= N529), R503 (= R534), K587 (= K618)
- binding adenosine monophosphate: G364 (= G395), E365 (= E396), R366 (= R397), H386 (= H417), W387 (= W418), W388 (= W419), Q389 (= Q420), T390 (= T421), D477 (= D508), I489 (= I520), R492 (= R523), N498 (= N529), R503 (= R534)
- binding coenzyme a: F139 (= F170), G140 (= G171), G141 (= G172), E167 (= E198), R170 (≠ G201), S279 (= S310), K307 (= K338), P308 (= P339), A332 (= A363), T334 (= T365), A363 (= A394), A500 (= A531), H502 (= H533), K532 (= K563), R562 (= R593), P567 (= P598), V568 (= V599)
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, 93% coverage: 33:650/662 of query aligns to 23:641/648 of Q89WV5
- G263 (= G271) mutation to I: Loss of activity.
- G266 (= G274) mutation to I: Great decrease in activity.
- K269 (= K277) mutation to G: Great decrease in activity.
- E414 (= E422) mutation to Q: Great decrease in activity.
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)
40% identity, 92% coverage: 37:646/662 of query aligns to 28:639/652 of Q8ZKF6
- R194 (≠ G201) 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 (≠ V316) binding
- N335 (≠ G341) 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 (≠ A531) 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 (= R593) 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 (= K618) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
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)
40% identity, 93% coverage: 35:651/662 of query aligns to 27:650/651 of P9WQD1
- K617 (= K618) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
40% identity, 92% coverage: 37:646/662 of query aligns to 24:633/641 of 2p20A
- active site: T260 (= T269), T412 (= T421), E413 (= E422), N517 (= N529), R522 (= R534), K605 (= K618)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G395), E384 (= E396), P385 (≠ R397), T408 (≠ H417), W409 (= W418), W410 (= W419), Q411 (= Q420), T412 (= T421), D496 (= D508), I508 (= I520), R511 (= R523), R522 (= R534)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
40% identity, 92% coverage: 37:646/662 of query aligns to 23:629/637 of 2p2fA
- active site: T259 (= T269), T411 (= T421), E412 (= E422), N516 (= N529), R521 (= R534), K604 (= K618)
- binding adenosine monophosphate: G382 (= G395), E383 (= E396), P384 (≠ R397), T407 (≠ H417), W408 (= W418), W409 (= W419), Q410 (= Q420), T411 (= T421), D495 (= D508), I507 (= I520), R510 (= R523), N516 (= N529), R521 (= R534)
- binding coenzyme a: F158 (= F170), R186 (≠ E198), W304 (= W314), T306 (≠ V316), P329 (= P339), A352 (= A363), A355 (= A366), S518 (≠ A531), R579 (= R593), P584 (= P598)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
40% identity, 92% coverage: 37:646/662 of query aligns to 24:632/640 of 5jrhA
- active site: T260 (= T269), T412 (= T421), E413 (= E422), N517 (= N529), R522 (= R534), K605 (= K618)
- binding (r,r)-2,3-butanediol: W93 (≠ Y104), E140 (= E151), G169 (≠ T180), K266 (≠ Q275), P267 (= P276)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G395), E384 (= E396), P385 (≠ R397), T408 (≠ H417), W409 (= W418), W410 (= W419), Q411 (= Q420), T412 (= T421), D496 (= D508), I508 (= I520), N517 (= N529), R522 (= R534)
- binding coenzyme a: F159 (= F170), G160 (= G171), G161 (= G172), R187 (≠ E198), S519 (≠ A531), R580 (= R593), P585 (= P598)
- binding magnesium ion: V533 (≠ C545), H535 (= H547), I538 (≠ V550)
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)
40% identity, 93% coverage: 33:646/662 of query aligns to 24:639/652 of P27550
- K609 (= K618) modified: N6-acetyllysine; by autocatalysis
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
41% identity, 89% coverage: 37:628/662 of query aligns to 24:615/634 of 1pg3A
- active site: T260 (= T269), T412 (= T421), E413 (= E422), N517 (= N529), R522 (= R534), K605 (= K618)
- binding coenzyme a: F159 (= F170), G160 (= G171), R187 (≠ E198), R190 (≠ G201), A301 (≠ S310), T307 (≠ V316), P330 (= P339), A356 (= A366), S519 (≠ A531), R580 (= R593), P585 (= P598)
- binding magnesium ion: V533 (≠ C545), H535 (= H547), I538 (≠ V550)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G395), E384 (= E396), P385 (≠ R397), T408 (≠ H417), W409 (= W418), W410 (= W419), Q411 (= Q420), T412 (= T421), D496 (= D508), R511 (= R523), R522 (= R534)
7kvyA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate and co-enzyme a from coccidioides immitis rs
41% identity, 91% coverage: 24:627/662 of query aligns to 18:621/633 of 7kvyA
- active site: T271 (= T269), T422 (= T421), E423 (= E422), N529 (= N529), R534 (= R534), K612 (= K618)
- binding coenzyme a: F172 (= F170), G174 (= G172), R200 (≠ E198), G312 (≠ S310), Y362 (≠ F361), V363 (≠ T362), A364 (= A363), S531 (≠ A531), G532 (= G532), R592 (= R593), F598 (≠ V599)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: G393 (= G395), E394 (= E396), P395 (≠ R397), T418 (≠ H417), Y419 (≠ W418), W420 (= W419), Q421 (= Q420), T422 (= T421), D508 (= D508), I520 (= I520), R523 (= R523), R534 (= R534)
7l3qA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-methylphosphate and co-enzyme a from coccidioides immitis rs
41% identity, 91% coverage: 24:627/662 of query aligns to 19:619/631 of 7l3qA
- active site: T272 (= T269), T423 (= T421), E424 (= E422), N530 (= N529), R535 (= R534)
- binding coenzyme a: F173 (= F170), A174 (≠ G171), G175 (= G172), R201 (≠ E198), G313 (≠ S310), Y363 (≠ F361), A365 (= A363), S532 (≠ A531), G533 (= G532), R593 (= R593), P598 (= P598), F599 (≠ V599)
- binding 5'-O-[(R)-hydroxy(methoxy)phosphoryl]adenosine: I318 (≠ V315), G394 (= G395), E395 (= E396), P396 (≠ R397), T419 (≠ H417), Y420 (≠ W418), Q422 (= Q420), T423 (= T421), D509 (= D508), R524 (= R523), R535 (= R534)
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, 92% coverage: 33:642/662 of query aligns to 47:686/701 of Q9QXG4
- K661 (= K618) 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)
40% identity, 94% coverage: 31:652/662 of query aligns to 33:654/662 of P78773
- T596 (≠ Q595) modified: Phosphothreonine
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)
38% identity, 92% coverage: 33:642/662 of query aligns to 47:686/701 of Q9NR19
- T363 (≠ V316) 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. 613:625, 69% identical) Nuclear localization signal
- S659 (= S616) 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 (≠ RG 621:622) 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
8w0dA Acetyl-coenzyme A synthetase 2
39% identity, 95% coverage: 25:652/662 of query aligns to 29:660/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G395), E399 (= E396), P400 (≠ R397), T423 (≠ H417), Y424 (≠ W418), W425 (= W419), Q426 (= Q420), T427 (= T421), 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
39% identity, 95% coverage: 25:652/662 of query aligns to 29:660/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G395), E399 (= E396), P400 (≠ R397), T423 (≠ H417), Y424 (≠ W418), Q426 (= Q420), T427 (= T421), D513 (= D508), I525 (= I520), R528 (= R523), R539 (= R534)
- binding coenzyme a: F175 (= F170), R203 (≠ E198), R206 (≠ G201), G316 (≠ S310), H538 (= H533), R599 (= R593), F605 (≠ V599)
8w0cA Acetyl-coenzyme A synthetase 2
39% identity, 95% coverage: 25:652/662 of query aligns to 30:661/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G395), E400 (= E396), P401 (≠ R397), T424 (≠ H417), Y425 (≠ W418), W426 (= W419), Q427 (= Q420), T428 (= T421), D514 (= D508), R529 (= R523), R540 (= R534)
8w0bA Acetyl-coenzyme A synthetase 2
39% identity, 95% coverage: 25:652/662 of query aligns to 30:661/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ A394), G399 (= G395), E400 (= E396), P401 (≠ R397), T424 (≠ H417), Y425 (≠ W418), W426 (= W419), Q427 (= Q420), T428 (= T421), D514 (= D508), I526 (= I520), R529 (= R523), R540 (= R534)
8w0jA Acetyl-coenzyme A synthetase 2
38% identity, 95% coverage: 25:652/662 of query aligns to 30:656/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G395), E400 (= E396), P401 (≠ R397), T424 (≠ H417), Y425 (≠ W418), W426 (= W419), Q427 (= Q420), T428 (= T421), 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
38% identity, 95% coverage: 25:652/662 of query aligns to 29:655/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (= P147), A176 (≠ G171), G177 (= G172), R203 (≠ E198), T208 (≠ V203), D317 (= D311), E342 (= E336), G343 (= G337), P345 (= P339), G398 (= G395), E399 (= E396), P400 (≠ R397), T423 (≠ H417), W425 (= W419), Q426 (= Q420), T427 (= T421), D513 (= D508), I525 (= I520), R528 (= R523), R539 (= R534)
Query Sequence
>5210124 FitnessBrowser__PV4:5210124
MAHKPNRMEGEADMSTVSGGRMSFGEDHMKDLHNQLHQESIDNPNAFWGEAAGALAWDKT
FERVLDDSQAPMYRWFSGGQLNTCYNAVDRHVEAGRGEQVAIQYVSPITGTEYGITYNEL
QAQVSRLAGYMASQGVVKGDRVIIYMPMVPETAYAMLACARLGAIHSVVFGGFAANELAT
RIDDATPKMILSASCGVEPSGVVAYKPLLDDALEQASHKVEQCVILNRPQLQADLVDGRD
VDWQGAMADAPNIECQTVEATDPLYILYTSGTTGQPKGVVRDNGGHAVALAWSMKHIYDI
DPGDVFWAASDVGWVVGHSYIVYGPLLVGATTVLFEGKPVGTPDPGIFWRTIAKYNVKSF
FTAPTAIRAIKRDDPEGDYLKDVDLSCLGTLFLAGERCDPDTLHWAEQQLDKPVIDHWWQ
TETGWPVAANLMGTAPVPVKAGSPAKAVPGYDVQVLDEMGDVVAPDQSGNVVIKLPLPPG
TLATLWQNEGRYKESYLSMYPGYYLTGDAGYMDEDGYLYIMSRIDDIINVAGHRLSTGRF
EEVLCQHEAVAEAAVIGVDDKLKGQVPLGLVVLKKGCDLSDEQLYKELIALVREQIGPVA
AFKLVSAVPKLPKTRSGKILRGTMRKIADNQEFKMPATIEDPYTLELVRNALTRMGYADA
HV
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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