SitesBLAST
Comparing Ac3H11_4867 FitnessBrowser__acidovorax_3H11:Ac3H11_4867 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)
4wd1A Acetoacetyl-coa synthetase from streptomyces lividans (see paper)
47% identity, 96% coverage: 25:704/710 of query aligns to 1:646/646 of 4wd1A
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)
29% identity, 86% coverage: 54:663/710 of query aligns to 28:617/651 of P9WQD1
- K617 (= K663) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
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)
26% identity, 89% coverage: 50:679/710 of query aligns to 57:658/689 of Q9NUB1
- V488 (= V492) to M: in dbSNP:rs6050249
- K642 (= K663) 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)
26% identity, 88% coverage: 50:673/710 of query aligns to 50:645/682 of Q99NB1
- K635 (= K663) modified: N6-acetyllysine
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)
26% identity, 91% coverage: 51:694/710 of query aligns to 24:639/652 of P27550
- K609 (= K663) 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)
25% identity, 91% coverage: 49:694/710 of query aligns to 22:639/652 of Q8ZKF6
- R194 (= R220) 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 (≠ M343) binding
- N335 (≠ D369) binding
- A357 (≠ G391) 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 (= D571) 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 (≠ H577) binding
- G524 (= G578) 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 (= R580) 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 (= R638) 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 (= K663) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
8sf3A Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (amp, acetate and coa bound)
26% identity, 91% coverage: 52:698/710 of query aligns to 37:655/662 of 8sf3A
- binding adenosine monophosphate: G398 (= G421), E399 (≠ S422), P400 (= P423), T423 (≠ I444), W424 (= W445), Q426 (≠ N447), T427 (≠ N448), D511 (= D554), R526 (= R569), R537 (= R580)
- binding coenzyme a: F171 (≠ A189), G172 (≠ P190), G173 (≠ D191), R199 (≠ Y217), K202 (≠ R220), R595 (= R638), P600 (= P643)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
25% identity, 91% coverage: 49:694/710 of query aligns to 18:632/640 of 5jrhA
- active site: T260 (≠ S289), T412 (≠ N448), E413 (≠ I449), N517 (= N575), R522 (= R580), K605 (= K663)
- binding (r,r)-2,3-butanediol: W93 (≠ I123), E140 (= E170), G169 (≠ D199), K266 (≠ L295), P267 (= P296)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G421), E384 (≠ S422), P385 (= P423), T408 (≠ I444), W409 (= W445), W410 (= W446), Q411 (≠ N447), T412 (≠ N448), D496 (= D554), I508 (= I566), N517 (= N575), R522 (= R580)
- binding coenzyme a: F159 (≠ A189), G160 (≠ P190), G161 (≠ D191), R187 (≠ Y217), S519 (≠ H577), R580 (= R638), P585 (= P643)
- binding magnesium ion: V533 (≠ E591), H535 (≠ L593), I538 (≠ V596)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
25% identity, 91% coverage: 49:694/710 of query aligns to 17:629/637 of 2p2fA
- active site: T259 (≠ S289), T411 (≠ N448), E412 (≠ I449), N516 (= N575), R521 (= R580), K604 (= K663)
- binding adenosine monophosphate: G382 (= G421), E383 (≠ S422), P384 (= P423), T407 (≠ I444), W408 (= W445), W409 (= W446), Q410 (≠ N447), T411 (≠ N448), D495 (= D554), I507 (= I566), R510 (= R569), N516 (= N575), R521 (= R580)
- binding coenzyme a: F158 (≠ A189), R186 (≠ Y217), W304 (= W341), T306 (≠ M343), P329 (= P364), A352 (≠ G391), A355 (≠ F394), S518 (≠ H577), R579 (= R638), P584 (= P643)
8u2rA Crystal structure of acetyl-coenzyme a synthetase from leishmania infantum (ethyl amp bound)
26% identity, 91% coverage: 52:698/710 of query aligns to 36:657/664 of 8u2rA
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I323 (≠ V342), G400 (= G421), E401 (≠ S422), P402 (= P423), T425 (≠ I444), W426 (= W445), W427 (= W446), Q428 (≠ N447), T429 (≠ N448), D513 (= D554), I525 (= I566), R528 (= R569), R539 (= R580)
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)
26% identity, 90% coverage: 51:690/710 of query aligns to 40:663/683 of P52910
- K506 (≠ D527) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
25% identity, 91% coverage: 49:694/710 of query aligns to 18:633/641 of 2p20A
- active site: T260 (≠ S289), T412 (≠ N448), E413 (≠ I449), N517 (= N575), R522 (= R580), K605 (= K663)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G421), E384 (≠ S422), P385 (= P423), T408 (≠ I444), W409 (= W445), W410 (= W446), Q411 (≠ N447), T412 (≠ N448), D496 (= D554), I508 (= I566), R511 (= R569), R522 (= R580)
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)
25% identity, 91% coverage: 50:694/710 of query aligns to 22:636/648 of Q89WV5
- G263 (= G291) mutation to I: Loss of activity.
- G266 (= G294) mutation to I: Great decrease in activity.
- K269 (= K297) mutation to G: Great decrease in activity.
- E414 (≠ I449) mutation to Q: Great decrease in activity.
7kvyA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate and co-enzyme a from coccidioides immitis rs
25% identity, 88% coverage: 35:660/710 of query aligns to 18:614/633 of 7kvyA
- active site: T271 (≠ S289), T422 (≠ N448), E423 (≠ I449), N529 (= N575), R534 (= R580), K612 (≠ R658)
- binding coenzyme a: F172 (≠ A189), G174 (≠ D191), R200 (≠ Y217), G312 (≠ S337), Y362 (≠ G389), V363 (≠ A390), A364 (≠ G391), S531 (≠ H577), G532 (= G578), R592 (= R638), F598 (≠ R644)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: G393 (= G421), E394 (≠ S422), P395 (= P423), T418 (≠ I444), Y419 (≠ W445), W420 (= W446), Q421 (≠ N447), T422 (≠ N448), D508 (≠ G539), I520 (= I566), R523 (= R569), R534 (= R580)
1ry2A Crystal structure of yeast acetyl-coenzyme a synthetase in complex with amp (see paper)
27% identity, 86% coverage: 66:673/710 of query aligns to 28:600/615 of 1ry2A
- active site: T247 (≠ S289), T399 (≠ N448), N507 (= N575), K590 (= K663)
- binding adenosine monophosphate: G370 (= G421), E371 (≠ S422), P372 (= P423), T395 (≠ I444), Y396 (≠ W445), W397 (= W446), Q398 (≠ N447), T399 (≠ N448), D486 (≠ G539), I498 (= I566), R501 (= R569)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
25% identity, 91% coverage: 49:694/710 of query aligns to 18:626/634 of 1pg3A
- active site: T260 (≠ S289), T412 (≠ N448), E413 (≠ I449), N517 (= N575), R522 (= R580), K605 (= K663)
- binding coenzyme a: F159 (≠ A189), G160 (≠ P190), R187 (≠ Y217), R190 (= R220), A301 (≠ S337), T307 (≠ M343), P330 (= P364), A356 (≠ F394), S519 (≠ H577), R580 (= R638), P585 (= P643)
- binding magnesium ion: V533 (≠ E591), H535 (≠ L593), I538 (≠ V596)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G421), E384 (≠ S422), P385 (= P423), T408 (≠ I444), W409 (= W445), W410 (= W446), Q411 (≠ N447), T412 (≠ N448), D496 (= D554), R511 (= R569), R522 (= R580)
8w0cA Acetyl-coenzyme A synthetase 2
27% identity, 88% coverage: 81:702/710 of query aligns to 68:664/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G421), E400 (≠ S422), P401 (= P423), T424 (≠ I444), Y425 (≠ W445), W426 (= W446), Q427 (≠ N447), T428 (≠ N448), D514 (= D541), R529 (= R569), R540 (= R580)
8w0bA Acetyl-coenzyme A synthetase 2
27% identity, 88% coverage: 81:702/710 of query aligns to 68:664/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ T420), G399 (= G421), E400 (≠ S422), P401 (= P423), T424 (≠ I444), Y425 (≠ W445), W426 (= W446), Q427 (≠ N447), T428 (≠ N448), D514 (= D541), I526 (= I566), R529 (= R569), R540 (= R580)
8w0dA Acetyl-coenzyme A synthetase 2
27% identity, 88% coverage: 81:702/710 of query aligns to 67:663/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G421), E399 (≠ S422), P400 (= P423), T423 (≠ I444), Y424 (≠ W445), W425 (= W446), Q426 (≠ N447), T427 (≠ N448), D513 (= D541), I525 (= I566), R528 (= R569), R539 (= R580)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
27% identity, 88% coverage: 81:702/710 of query aligns to 67:663/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G421), E399 (≠ S422), P400 (= P423), T423 (≠ I444), Y424 (≠ W445), Q426 (≠ N447), T427 (≠ N448), D513 (= D541), I525 (= I566), R528 (= R569), R539 (= R580)
- binding coenzyme a: F175 (≠ A189), R203 (≠ Y217), R206 (= R220), G316 (≠ S337), H538 (≠ L579), R599 (= R638), F605 (≠ R644)
Query Sequence
>Ac3H11_4867 FitnessBrowser__acidovorax_3H11:Ac3H11_4867
VSAATLPGMETNPPPHRPGPPATGPQPPYIPQIRLYQNWLRDERGLQWDSYDALWRWSTT
ELDAFWQSVWDYFQIESPTPHTAVLGKNTMPGAQWFPGAQVNYARQALRHVDAAHAAGLP
AIISRNEKGQHRELSWPELRRQVASLALHLKAQGVMPGDRVAAYLPNVPEAMIAFLATVS
IGGVWSICAPDMGTHAVLDRFRQIAPKVLIGVDGVSYGGRDHDRRPVLAELREALPSVQH
AVLLGNLDASVSIAGWASWTGATARSDAETTAFEPLWLPFDHPLWIVYSSGTTGLPKPIV
HGHGGTVLVALQLKVLHNDIGCSYEPNSFGERYHWYSSTGWVMWNAQLSGLLSGTTCVIY
DGNPGGSKDNPDWGVLWRFAAETGVTFFGAGAAFFANCMKAGITLADYGDLTRIRALGTT
GSPLSPEVQEWGTAQFEALGTSDIWWNNISGGTDFCGAFIGGHREMPQVPGEMQCRMLGA
AVESWDAEGRPVQDAVGELVCAQPIPSMPLYLWGDKDGSRYLSSYFDMYPAGHGRQPGGG
DGPAAMGAVWRHGDWLKIGANGGCVIYGRSDATINRHGLRMGTSEIYSAVESLPEVLDSL
VVDLEYLGRESYMPLFVVLRPGYALDDALRARINGAVRTALSPRFVPDDIFAVAEVPRTL
SGKKQELPIKKLLLGQPIEKVVNKDAMANPGCLDWYVAFAAERAGMLRNA
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