SitesBLAST
Comparing WP_013835422.1 NCBI__GCF_000214825.1:WP_013835422.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
54% identity, 96% coverage: 23:648/651 of query aligns to 14:638/648 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 (= E421) 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)
53% identity, 96% coverage: 21:648/651 of query aligns to 13:641/652 of P27550
- K609 (= K617) modified: N6-acetyllysine; by autocatalysis
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
52% identity, 97% coverage: 21:650/651 of query aligns to 9:637/641 of 2p20A
- active site: T260 (= T268), T412 (= T420), E413 (= E421), N517 (= N526), R522 (= R531), K605 (= K617)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G391), E384 (= E392), P385 (= P393), T408 (= T416), W409 (= W417), W410 (= W418), Q411 (= Q419), T412 (= T420), D496 (= D505), I508 (= I517), R511 (= R520), R522 (= R531)
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, 97% coverage: 21:650/651 of query aligns to 13:643/652 of Q8ZKF6
- R194 (≠ K199) 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 CoA
- N335 (≠ T339) binding CoA
- 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 (= D522) 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 (= S528) binding CoA
- G524 (= G529) 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 (= R531) 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 (≠ A592) 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 (= 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)
52% identity, 97% coverage: 21:650/651 of query aligns to 9:636/640 of 5jrhA
- active site: T260 (= T268), T412 (= T420), E413 (= E421), N517 (= N526), R522 (= R531), K605 (= K617)
- binding (r,r)-2,3-butanediol: W93 (≠ F103), E140 (≠ Q149), G169 (≠ D178), K266 (≠ T274), P267 (= P275)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G391), E384 (= E392), P385 (= P393), T408 (= T416), W409 (= W417), W410 (= W418), Q411 (= Q419), T412 (= T420), D496 (= D505), I508 (= I517), N517 (= N526), R522 (= R531)
- binding coenzyme a: F159 (= F168), G160 (= G169), G161 (= G170), R187 (= R196), S519 (= S528), R580 (≠ A592), P585 (= P597)
- binding magnesium ion: V533 (= V542), H535 (= H544), I538 (≠ V547)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
52% identity, 97% coverage: 21:650/651 of query aligns to 8:633/637 of 2p2fA
- active site: T259 (= T268), T411 (= T420), E412 (= E421), N516 (= N526), R521 (= R531), K604 (= K617)
- binding adenosine monophosphate: G382 (= G391), E383 (= E392), P384 (= P393), T407 (= T416), W408 (= W417), W409 (= W418), Q410 (= Q419), T411 (= T420), D495 (= D505), I507 (= I517), R510 (= R520), N516 (= N526), R521 (= R531)
- binding coenzyme a: F158 (= F168), R186 (= R196), W304 (= W313), T306 (= T315), P329 (= P338), A352 (= A361), A355 (= A364), S518 (= S528), R579 (≠ A592), P584 (= P597)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
51% identity, 97% coverage: 21:650/651 of query aligns to 9:630/634 of 1pg3A
- active site: T260 (= T268), T412 (= T420), E413 (= E421), N517 (= N526), R522 (= R531), K605 (= K617)
- binding coenzyme a: F159 (= F168), G160 (= G169), R187 (= R196), R190 (≠ K199), A301 (= A309), T307 (= T315), P330 (= P338), A356 (= A364), S519 (= S528), R580 (≠ A592), P585 (= P597)
- binding magnesium ion: V533 (= V542), H535 (= H544), I538 (≠ V547)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G391), E384 (= E392), P385 (= P393), T408 (= T416), W409 (= W417), W410 (= W418), Q411 (= Q419), T412 (= T420), D496 (= D505), R511 (= R520), R522 (= R531)
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)
52% identity, 99% coverage: 6:651/651 of query aligns to 3:650/651 of P9WQD1
- K617 (= K617) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
49% identity, 96% coverage: 9:632/651 of query aligns to 1:626/630 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 (= G391), E392 (= E392), P393 (= P393), T416 (= T416), W417 (= W417), W418 (= W418), Q419 (= Q419), T420 (= T420), D502 (= D505), R517 (= R520), K523 (≠ N526), R528 (= R531)
- binding magnesium ion: V539 (= V542), H541 (= H544)
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, 98% coverage: 13:648/651 of query aligns to 27:692/701 of Q9NR19
- T363 (= T315) 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. 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)
47% identity, 98% coverage: 13:648/651 of query aligns to 27:692/701 of Q9QXG4
- K661 (= K617) 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, 95% coverage: 35:651/651 of query aligns to 43:672/683 of P52910
- K506 (≠ A494) 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)
48% identity, 96% coverage: 30:651/651 of query aligns to 33:653/662 of P78773
- T596 (≠ E594) modified: Phosphothreonine
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)
48% identity, 96% coverage: 25:651/651 of query aligns to 44:670/682 of Q99NB1
- K635 (= K617) modified: N6-acetyllysine
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
48% identity, 96% coverage: 30:651/651 of query aligns to 35:654/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (= P145), A176 (≠ G169), G177 (= G170), R203 (= R196), T208 (≠ I201), D317 (= D310), E342 (= E335), G343 (= G336), P345 (= P338), G398 (= G391), E399 (= E392), P400 (= P393), T423 (= T416), W425 (= W418), Q426 (= Q419), T427 (= T420), D513 (= D505), I525 (= I517), R528 (= R520), R539 (= R531)
8v4oA Crystal structure of acetyl-coa synthetase 2 in complex with amp from candida albicans
48% identity, 96% coverage: 30:651/651 of query aligns to 35:654/660 of 8v4oA
- binding adenosine monophosphate: G398 (= G391), E399 (= E392), P400 (= P393), T423 (= T416), Y424 (≠ W417), W425 (= W418), Q426 (= Q419), T427 (= T420), D513 (= D505), I525 (= I517), R528 (= R520), R539 (= R531)
8w0dA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with an isopropyl amp ester inhibitor
48% identity, 96% coverage: 30:651/651 of query aligns to 35:659/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G391), E399 (= E392), P400 (= P393), T423 (= T416), Y424 (≠ W417), W425 (= W418), Q426 (= Q419), T427 (= T420), D513 (= D505), I525 (= I517), R528 (= R520), R539 (= R531)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
48% identity, 96% coverage: 30:651/651 of query aligns to 35:659/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G391), E399 (= E392), P400 (= P393), T423 (= T416), Y424 (≠ W417), Q426 (= Q419), T427 (= T420), D513 (= D505), I525 (= I517), R528 (= R520), R539 (= R531)
- binding coenzyme a: F175 (= F168), R203 (= R196), R206 (≠ K199), G316 (≠ A309), H538 (= H530), R599 (= R588), F605 (≠ I598)
8w0jA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a propyne amp ester inhibitor
48% identity, 96% coverage: 30:651/651 of query aligns to 36:655/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G391), E400 (= E392), P401 (= P393), T424 (= T416), Y425 (≠ W417), W426 (= W418), Q427 (= Q419), T428 (= T420), D514 (= D505), I526 (= I517), R529 (= R520), R540 (= R531)
8w0cA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopentyl ester amp inhibitor
48% identity, 96% coverage: 30:651/651 of query aligns to 36:660/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G391), E400 (= E392), P401 (= P393), T424 (= T416), Y425 (≠ W417), W426 (= W418), Q427 (= Q419), T428 (= T420), D514 (= D505), R529 (= R520), R540 (= R531)
Query Sequence
>WP_013835422.1 NCBI__GCF_000214825.1:WP_013835422.1
MSNNIESILTETRVFEPSDAIKQQAAIKADKLDAMYAKAEQDHVGFWADLAKEKLSWHKP
FTKALDDSKAPLYRWFTDGELNVSYNCIDRHLDTKSDKLAIIFEGDKGDVHHYTYQELHD
EVCRFANTLKTQGIKQGDRVIIYMPMIPQAVIAMQACARVGAIHSVVFGGFSAEALKDRV
ENAAAKLIITTDGGLRGGKAIPLKGAVDQALAKGCDSVKKVIVYQRTKQEVVMQDGRDIW
WHEAEAGMSNYHDPVMLPADHPLFLLYTSGSTGTPKGVQHGSGGYLLNAMLTNEWMFDLN
DKDVFWCTADVGWITGHSYVAYGPLAMGATIVMFEGVPTYPDAGRFWQVCQDHGVTVFYT
APTAIRALMKFGKDIPAQYDLSKLRILGTVGEPINPEAWMWYHEVIGRGECPIIDTWWQT
ETGAHMIAPFPGVTPLKPGSCTRPLPGIDAIVVDEEGHEIGNNSGGYLVVRKPWPSMLQT
VWGDDQRYIDTYFAKFNNQYYVVGDSAHKDADGYIWILGRIDDVLNVSGHRLGTMEIESA
LVAHPKVAEAAVVGKPHDVKGESVFAFVVLNTDLPAGAERDAMVNELRNWVAQEIGPIAK
PDDIRFGTNLPKTRSGKIMRRLLRTIAKGEEITQDTSTLEDPSILKQLQQA
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