SitesBLAST
Comparing BPHYT_RS27780 BPHYT_RS27780 acetyl-CoA synthetase 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)
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)
50% identity, 95% coverage: 30:654/658 of query aligns to 24:641/652 of P27550
- K609 (= K623) modified: N6-acetyllysine; by autocatalysis
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
49% identity, 97% coverage: 16:654/658 of query aligns to 5:635/641 of 2p20A
- active site: T260 (= T268), T412 (= T424), E413 (= E425), N517 (= N532), R522 (= R537), K605 (= K623)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G395), E384 (= E396), P385 (= P397), T408 (= T420), W409 (≠ F421), W410 (= W422), Q411 (= Q423), T412 (= T424), D496 (= D510), I508 (= I523), R511 (= R526), R522 (= R537)
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, 95% coverage: 30:654/658 of query aligns to 23:638/648 of Q89WV5
- G263 (= G270) mutation to I: Loss of activity.
- G266 (= G273) mutation to I: Great decrease in activity.
- K269 (= K276) mutation to G: Great decrease in activity.
- E414 (= E425) 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)
49% identity, 98% coverage: 10:654/658 of query aligns to 3:641/652 of Q8ZKF6
- R194 (≠ K198) 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 (= T315) binding
- N335 (≠ T339) binding
- A357 (= A361) 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 (= D528) 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 (= S534) binding
- G524 (= G535) 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 (= R537) 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 (≠ G598) 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 (= K623) 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)
49% identity, 97% coverage: 16:654/658 of query aligns to 5:634/640 of 5jrhA
- active site: T260 (= T268), T412 (= T424), E413 (= E425), N517 (= N532), R522 (= R537), K605 (= K623)
- binding (r,r)-2,3-butanediol: W93 (≠ F102), E140 (= E148), G169 (≠ E177), K266 (≠ A274), P267 (= P275)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G395), E384 (= E396), P385 (= P397), T408 (= T420), W409 (≠ F421), W410 (= W422), Q411 (= Q423), T412 (= T424), D496 (= D510), I508 (= I523), N517 (= N532), R522 (= R537)
- binding coenzyme a: F159 (= F167), G160 (= G168), G161 (= G169), R187 (= R195), S519 (= S534), R580 (≠ G598), P585 (= P603)
- binding magnesium ion: V533 (≠ S548), H535 (= H550), I538 (≠ V553)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
49% identity, 97% coverage: 16:654/658 of query aligns to 4:631/637 of 2p2fA
- active site: T259 (= T268), T411 (= T424), E412 (= E425), N516 (= N532), R521 (= R537), K604 (= K623)
- binding adenosine monophosphate: G382 (= G395), E383 (= E396), P384 (= P397), T407 (= T420), W408 (≠ F421), W409 (= W422), Q410 (= Q423), T411 (= T424), D495 (= D510), I507 (= I523), R510 (= R526), N516 (= N532), R521 (= R537)
- binding coenzyme a: F158 (= F167), R186 (= R195), W304 (= W313), T306 (= T315), P329 (= P338), A352 (= A361), A355 (= A364), S518 (= S534), R579 (≠ G598), P584 (= P603)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
50% identity, 94% coverage: 16:636/658 of query aligns to 5:618/634 of 1pg3A
- active site: T260 (= T268), T412 (= T424), E413 (= E425), N517 (= N532), R522 (= R537), K605 (= K623)
- binding coenzyme a: F159 (= F167), G160 (= G168), R187 (= R195), R190 (≠ K198), A301 (= A309), T307 (= T315), P330 (= P338), A356 (= A364), S519 (= S534), R580 (≠ G598), P585 (= P603)
- binding magnesium ion: V533 (≠ S548), H535 (= H550), I538 (≠ V553)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G395), E384 (= E396), P385 (= P397), T408 (= T420), W409 (≠ F421), W410 (= W422), Q411 (= Q423), T412 (= T424), D496 (= D510), R511 (= R526), R522 (= R537)
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)
51% identity, 99% coverage: 2:651/658 of query aligns to 4:644/651 of P9WQD1
- K617 (= K623) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
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)
47% identity, 97% coverage: 17:656/658 of query aligns to 33:695/701 of Q9QXG4
- K661 (= K623) 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)
47% identity, 97% coverage: 17:656/658 of query aligns to 33:695/701 of Q9NR19
- T363 (= T315) 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. 618:630, 77% identical) Nuclear localization signal
- S659 (= S621) 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 626:627) 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
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)
47% identity, 95% coverage: 24:651/658 of query aligns to 34:666/683 of P52910
- K506 (vs. gap) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
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)
46% identity, 98% coverage: 17:658/658 of query aligns to 22:654/662 of P78773
- T596 (≠ E600) modified: Phosphothreonine
7kdnA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-propylphosphate from aspergillus fumigatus
48% identity, 93% coverage: 22:632/658 of query aligns to 26:621/622 of 7kdnA
- active site: T271 (= T268), T422 (= T424), E423 (= E425), N529 (= N532), R534 (= R537), K612 (= K623)
- binding adenosine-5'-monophosphate-propyl ester: G393 (= G395), E394 (= E396), P395 (= P397), T418 (= T420), Y419 (≠ F421), W420 (= W422), Q421 (= Q423), T422 (= T424), D508 (= D510), I520 (= I523), R523 (= R526), R534 (= R537)
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)
47% identity, 95% coverage: 29:654/658 of query aligns to 50:667/682 of Q99NB1
- K635 (= K623) modified: N6-acetyllysine
8w0dA Acetyl-coenzyme A synthetase 2
47% identity, 96% coverage: 24:654/658 of query aligns to 31:660/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G395), E399 (= E396), P400 (= P397), T423 (= T420), Y424 (≠ F421), W425 (= W422), Q426 (= Q423), T427 (= T424), D513 (= D510), I525 (= I523), R528 (= R526), R539 (= R537)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
47% identity, 96% coverage: 24:654/658 of query aligns to 31:660/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G395), E399 (= E396), P400 (= P397), T423 (= T420), Y424 (≠ F421), Q426 (= Q423), T427 (= T424), D513 (= D510), I525 (= I523), R528 (= R526), R539 (= R537)
- binding coenzyme a: F175 (= F167), R203 (= R195), R206 (≠ K198), G316 (≠ A309), H538 (= H536), R599 (≠ G598), F605 (≠ I604)
8w0cA Acetyl-coenzyme A synthetase 2
47% identity, 96% coverage: 24:654/658 of query aligns to 32:661/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G395), E400 (= E396), P401 (= P397), T424 (= T420), Y425 (≠ F421), W426 (= W422), Q427 (= Q423), T428 (= T424), D514 (= D510), R529 (= R526), R540 (= R537)
8w0bA Acetyl-coenzyme A synthetase 2
47% identity, 96% coverage: 24:654/658 of query aligns to 32:661/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (= V394), G399 (= G395), E400 (= E396), P401 (= P397), T424 (= T420), Y425 (≠ F421), W426 (= W422), Q427 (= Q423), T428 (= T424), D514 (= D510), I526 (= I523), R529 (= R526), R540 (= R537)
7kvyA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate and co-enzyme a from coccidioides immitis rs
48% identity, 93% coverage: 24:632/658 of query aligns to 28:621/633 of 7kvyA
- active site: T271 (= T268), T422 (= T424), E423 (= E425), N529 (= N532), R534 (= R537), K612 (= K623)
- binding coenzyme a: F172 (= F167), G174 (= G169), R200 (= R195), G312 (≠ A309), Y362 (= Y359), V363 (≠ T360), A364 (= A361), S531 (= S534), G532 (= G535), R592 (≠ G598), F598 (≠ I604)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: G393 (= G395), E394 (= E396), P395 (= P397), T418 (= T420), Y419 (≠ F421), W420 (= W422), Q421 (= Q423), T422 (= T424), D508 (= D510), I520 (= I523), R523 (= R526), R534 (= R537)
8u2rA Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (ethyl amp bound)
46% identity, 95% coverage: 31:654/658 of query aligns to 24:655/664 of 8u2rA
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I323 (= I314), G400 (= G395), E401 (= E396), P402 (= P397), T425 (= T420), W426 (≠ F421), W427 (= W422), Q428 (= Q423), T429 (= T424), D513 (= D510), I525 (= I523), R528 (= R526), R539 (= R537)
Query Sequence
>BPHYT_RS27780 BPHYT_RS27780 acetyl-CoA synthetase
MSTIDSASLQPAPRQIPAIEHTAISGMDAYRALVAEAETDHQAFWARLAREHLQWRRPFT
KILDDSNAPFYKWFEDGELNASYNCLDRNLAKGLADKTAIVFEADDGTVTRITYQALYHR
VCRLANALRARGVTRGDRVVIYMPMSIEGIAAMLACARIGAPHSVVFGGFSAKSLHERLV
NVGAVAVMTADEQVRGGKTLPLKAIVDEALAMGGTVAVKTVVVYRRTGGRIPWITQRDAW
LHELEHAQSDTCEPEWVGAEHPLFVLYTSGSTGAPKGVQHSTGGYLLWAAVTMKWTFDIK
PDDVFWCTADIGWITGHTYICYGPTAVGATQVIFEGVPTYPDAGRFWQMIERHKVSIFYT
APTAIRSLIKAADANEAVHPRSFDLSSLRILGTVGEPINPSAWTWYAQHVGGGRCPVLDT
FWQTETGGHMISPLPGVTPLVPGSCTLPMPGIDAAIVDETGHEVPNGHGGVLVIRKPWPS
MIRTIWGNPERFRHGYYPDDLGGKLYLAGDGAIRDRDTGYFTITGRIDDVLNVSGHRLGT
MEIESALSAHPSVAEAAVVGRPDETCGEAIVAFVVLKTARPSGPDAKRVADELRAWVGKE
IGPIAKPKDIRFGDAMPKTRSGKVVRRLLRSVAKGEAITQDTSSVENPTVISQFAHGL
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