SitesBLAST
Comparing WP_028321206.1 NCBI__GCF_000422285.1:WP_028321206.1 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)
58% identity, 99% coverage: 6:648/652 of query aligns to 4:642/648 of Q89WV5
- G263 (= G268) mutation to I: Loss of activity.
- G266 (= G271) mutation to I: Great decrease in activity.
- K269 (= K274) mutation to G: Great decrease in activity.
- E414 (= E419) 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)
56% identity, 96% coverage: 25:651/652 of query aligns to 22:648/652 of P27550
- K609 (= K612) 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)
56% identity, 96% coverage: 25:651/652 of query aligns to 22:648/652 of Q8ZKF6
- R194 (≠ K196) 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 (= T313) binding CoA
- N335 (= N337) binding CoA
- A357 (= A359) 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 (= D520) 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 (= S526) binding CoA
- G524 (= G527) 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 (= R529) 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 (= R587) 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 (= K612) 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)
57% identity, 96% coverage: 25:648/652 of query aligns to 18:638/640 of 5jrhA
- active site: T260 (= T266), T412 (= T418), E413 (= E419), N517 (= N524), R522 (= R529), K605 (= K612)
- binding (r,r)-2,3-butanediol: W93 (= W99), E140 (= E146), G169 (≠ N175), K266 (= K272), P267 (= P273)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G389), E384 (= E390), P385 (= P391), T408 (= T414), W409 (= W415), W410 (= W416), Q411 (= Q417), T412 (= T418), D496 (= D503), I508 (= I515), N517 (= N524), R522 (= R529)
- binding coenzyme a: F159 (= F165), G160 (= G166), G161 (= G167), R187 (= R193), S519 (= S526), R580 (= R587), P585 (= P592)
- binding magnesium ion: V533 (= V540), H535 (= H542), I538 (≠ V545)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
56% identity, 96% coverage: 25:648/652 of query aligns to 18:639/641 of 2p20A
- active site: T260 (= T266), T412 (= T418), E413 (= E419), N517 (= N524), R522 (= R529), K605 (= K612)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G389), E384 (= E390), P385 (= P391), T408 (= T414), W409 (= W415), W410 (= W416), Q411 (= Q417), T412 (= T418), D496 (= D503), I508 (= I515), R511 (= R518), R522 (= R529)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
56% identity, 96% coverage: 25:648/652 of query aligns to 17:635/637 of 2p2fA
- active site: T259 (= T266), T411 (= T418), E412 (= E419), N516 (= N524), R521 (= R529), K604 (= K612)
- binding adenosine monophosphate: G382 (= G389), E383 (= E390), P384 (= P391), T407 (= T414), W408 (= W415), W409 (= W416), Q410 (= Q417), T411 (= T418), D495 (= D503), I507 (= I515), R510 (= R518), N516 (= N524), R521 (= R529)
- binding coenzyme a: F158 (= F165), R186 (= R193), W304 (= W311), T306 (= T313), P329 (= P336), A352 (= A359), A355 (≠ V362), S518 (= S526), R579 (= R587), P584 (= P592)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
56% identity, 96% coverage: 25:648/652 of query aligns to 18:632/634 of 1pg3A
- active site: T260 (= T266), T412 (= T418), E413 (= E419), N517 (= N524), R522 (= R529), K605 (= K612)
- binding coenzyme a: F159 (= F165), G160 (= G166), R187 (= R193), R190 (≠ K196), A301 (= A307), T307 (= T313), P330 (= P336), A356 (≠ V362), S519 (= S526), R580 (= R587), P585 (= P592)
- binding magnesium ion: V533 (= V540), H535 (= H542), I538 (≠ V545)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G389), E384 (= E390), P385 (= P391), T408 (= T414), W409 (= W415), W410 (= W416), Q411 (= Q417), T412 (= T418), D496 (= D503), R511 (= R518), R522 (= R529)
8sf3A Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (amp, acetate and coa bound)
53% identity, 96% coverage: 24:648/652 of query aligns to 22:657/662 of 8sf3A
- binding adenosine monophosphate: G398 (= G389), E399 (= E390), P400 (= P391), T423 (= T414), W424 (= W415), Q426 (= Q417), T427 (= T418), D511 (= D503), R526 (= R518), R537 (= R529)
- binding coenzyme a: F171 (= F165), G172 (= G166), G173 (= G167), R199 (= R193), K202 (= K196), R595 (= R587), P600 (= P592)
8u2rA Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (ethyl amp bound)
53% identity, 96% coverage: 24:648/652 of query aligns to 21:659/664 of 8u2rA
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I323 (≠ V312), G400 (= G389), E401 (= E390), P402 (= P391), T425 (= T414), W426 (= W415), W427 (= W416), Q428 (= Q417), T429 (= T418), D513 (= D503), I525 (= I515), R528 (= R518), R539 (= R529)
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)
51% identity, 96% coverage: 21:645/652 of query aligns to 29:651/662 of P78773
- T596 (≠ E589) modified: Phosphothreonine
7kdnA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-propylphosphate from aspergillus fumigatus
51% identity, 94% coverage: 10:621/652 of query aligns to 17:621/622 of 7kdnA
- active site: T271 (= T266), T422 (= T418), E423 (= E419), N529 (= N524), R534 (= R529), K612 (= K612)
- binding adenosine-5'-monophosphate-propyl ester: G393 (= G389), E394 (= E390), P395 (= P391), T418 (= T414), Y419 (≠ W415), W420 (= W416), Q421 (= Q417), T422 (= T418), D508 (= D503), I520 (= I515), R523 (= R518), R534 (= R529)
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, 96% coverage: 19:645/652 of query aligns to 32:670/683 of P52910
- K506 (≠ S493) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
7kvyA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate and co-enzyme a from coccidioides immitis rs
51% identity, 93% coverage: 13:621/652 of query aligns to 20:621/633 of 7kvyA
- active site: T271 (= T266), T422 (= T418), E423 (= E419), N529 (= N524), R534 (= R529), K612 (= K612)
- binding coenzyme a: F172 (= F165), G174 (= G167), R200 (= R193), G312 (≠ A307), Y362 (= Y357), V363 (≠ T358), A364 (= A359), S531 (= S526), G532 (= G527), R592 (= R587), F598 (≠ I593)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: G393 (= G389), E394 (= E390), P395 (= P391), T418 (= T414), Y419 (≠ W415), W420 (= W416), Q421 (= Q417), T422 (= T418), D508 (= D503), I520 (= I515), R523 (= R518), R534 (= R529)
8w0cA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopentyl ester amp inhibitor
48% identity, 96% coverage: 21:645/652 of query aligns to 32:658/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G389), E400 (= E390), P401 (= P391), T424 (= T414), Y425 (≠ W415), W426 (= W416), Q427 (= Q417), T428 (= T418), D514 (= D503), R529 (= R518), R540 (= R529)
8w0bA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopropyl amp ester inhibitor
48% identity, 96% coverage: 21:645/652 of query aligns to 32:658/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (= V388), G399 (= G389), E400 (= E390), P401 (= P391), T424 (= T414), Y425 (≠ W415), W426 (= W416), Q427 (= Q417), T428 (= T418), D514 (= D503), I526 (= I515), R529 (= R518), R540 (= R529)
8w0dA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with an isopropyl amp ester inhibitor
48% identity, 96% coverage: 21:645/652 of query aligns to 31:657/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G389), E399 (= E390), P400 (= P391), T423 (= T414), Y424 (≠ W415), W425 (= W416), Q426 (= Q417), T427 (= T418), D513 (= D503), I525 (= I515), R528 (= R518), R539 (= R529)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
48% identity, 96% coverage: 21:645/652 of query aligns to 31:657/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G389), E399 (= E390), P400 (= P391), T423 (= T414), Y424 (≠ W415), Q426 (= Q417), T427 (= T418), D513 (= D503), I525 (= I515), R528 (= R518), R539 (= R529)
- binding coenzyme a: F175 (= F165), R203 (= R193), R206 (≠ K196), G316 (≠ A307), H538 (= H528), R599 (= R587), F605 (≠ I593)
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
48% identity, 96% coverage: 21:645/652 of query aligns to 31:652/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (= P142), A176 (≠ G166), G177 (= G167), R203 (= R193), T208 (≠ V198), D317 (= D308), E342 (= E333), G343 (≠ S334), P345 (= P336), G398 (= G389), E399 (= E390), P400 (= P391), T423 (= T414), W425 (= W416), Q426 (= Q417), T427 (= T418), D513 (= D503), I525 (= I515), R528 (= R518), R539 (= R529)
8v4oA Crystal structure of acetyl-coa synthetase 2 in complex with amp from candida albicans
48% identity, 96% coverage: 21:645/652 of query aligns to 31:652/660 of 8v4oA
- binding adenosine monophosphate: G398 (= G389), E399 (= E390), P400 (= P391), T423 (= T414), Y424 (≠ W415), W425 (= W416), Q426 (= Q417), T427 (= T418), D513 (= D503), I525 (= I515), R528 (= R518), R539 (= R529)
8w0jA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a propyne amp ester inhibitor
48% identity, 96% coverage: 21:645/652 of query aligns to 32:653/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G389), E400 (= E390), P401 (= P391), T424 (= T414), Y425 (≠ W415), W426 (= W416), Q427 (= Q417), T428 (= T418), D514 (= D503), I526 (= I515), R529 (= R518), R540 (= R529)
Query Sequence
>WP_028321206.1 NCBI__GCF_000422285.1:WP_028321206.1
MTDAPKWYDAHLEDYRKVAFINSLEQYQELYRRSIEDPDGFWAEQAGRYLSWDKPWDFVL
RYDFNQADIAWFGGGVLNASANCLDRHMKTLKDKVAYYWEGDNPEETLTVTYGDLYARVN
KMAALLRQKGVKKGDRIIIYMPMIVELPVTMLACARIGAVHSVVFGGFSAEALANRIRDC
GARLVVTVDGGFRAGKPVPLKTNVDNALKTCPGVDTVLVFERAGLKPELDSKREVWVHEA
LEDPSLPDFVEPEPMDAEDPLFILYTSGSTGKPKGVVHTTGGYLLYAAMTTRLVFDLKDD
EVFWCTADIGWVTGHSYSVYGPLTEGLTSVLFESVPNYPGFDRYWAIVEKYRVAKFYTAP
TVIRSLAKEGPEPVQKHDISSLKLLGSVGEPINPEAWRWYYHYVGRDWCPIMDTWWQTET
GGHMLTPLPGVAPIKPGSCSFPFFGVDPVILDETGQEARFPDQEGVLCIRKPWPGMARTV
YGDHERFRQTYFSQVPGMYFTGDGAKKDQDGYFWIIGRIDDVINVSGHRLGTAEVESALV
LHDLVAEAAVVGMPHPVKGQGIYAFVTLNTGVPKSEELKKELIQMVRKEIGPIATIDALQ
WADALPKTRSGKIMRRILQKIAAGRVDELGDTSTIADPSVIETLIKERVGLP
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