SitesBLAST
Comparing Ac3H11_951 FitnessBrowser__acidovorax_3H11:Ac3H11_951 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)
51% identity, 94% coverage: 36:660/664 of query aligns to 24:641/652 of P27550
- K609 (= K629) modified: N6-acetyllysine; by autocatalysis
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)
52% identity, 95% coverage: 33:662/664 of query aligns to 20:640/648 of Q89WV5
- G263 (= G276) mutation to I: Loss of activity.
- G266 (= G279) mutation to I: Great decrease in activity.
- K269 (= K282) mutation to G: Great decrease in activity.
- E414 (= E431) mutation to Q: Great decrease in activity.
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
51% identity, 94% coverage: 36:660/664 of query aligns to 20:635/641 of 2p20A
- active site: T260 (= T274), T412 (= T430), E413 (= E431), N517 (= N537), R522 (= R542), K605 (= K629)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G401), E384 (= E402), P385 (= P403), T408 (= T426), W409 (≠ F427), W410 (= W428), Q411 (= Q429), T412 (= T430), D496 (= D515), I508 (= I528), R511 (= R531), R522 (= R542)
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)
51% identity, 94% coverage: 36:660/664 of query aligns to 24:641/652 of Q8ZKF6
- R194 (≠ K204) 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 (= T321) binding
- N335 (≠ T345) binding
- A357 (= A367) 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 (= D533) 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 (= S539) binding
- G524 (= G540) 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 (= R542) 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 (≠ A604) 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 (= K629) 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)
51% identity, 94% coverage: 36:660/664 of query aligns to 20:634/640 of 5jrhA
- active site: T260 (= T274), T412 (= T430), E413 (= E431), N517 (= N537), R522 (= R542), K605 (= K629)
- binding (r,r)-2,3-butanediol: W93 (≠ F108), E140 (= E154), G169 (≠ E183), K266 (= K280), P267 (= P281)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G401), E384 (= E402), P385 (= P403), T408 (= T426), W409 (≠ F427), W410 (= W428), Q411 (= Q429), T412 (= T430), D496 (= D515), I508 (= I528), N517 (= N537), R522 (= R542)
- binding coenzyme a: F159 (= F173), G160 (= G174), G161 (= G175), R187 (= R201), S519 (= S539), R580 (≠ A604), P585 (= P609)
- binding magnesium ion: V533 (= V553), H535 (≠ K555), I538 (≠ V559)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
51% identity, 94% coverage: 36:660/664 of query aligns to 19:631/637 of 2p2fA
- active site: T259 (= T274), T411 (= T430), E412 (= E431), N516 (= N537), R521 (= R542), K604 (= K629)
- binding adenosine monophosphate: G382 (= G401), E383 (= E402), P384 (= P403), T407 (= T426), W408 (≠ F427), W409 (= W428), Q410 (= Q429), T411 (= T430), D495 (= D515), I507 (= I528), R510 (= R531), N516 (= N537), R521 (= R542)
- binding coenzyme a: F158 (= F173), R186 (= R201), W304 (= W319), T306 (= T321), P329 (= P344), A352 (= A367), A355 (= A370), S518 (= S539), R579 (≠ A604), P584 (= P609)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
50% identity, 94% coverage: 36:660/664 of query aligns to 20:628/634 of 1pg3A
- active site: T260 (= T274), T412 (= T430), E413 (= E431), N517 (= N537), R522 (= R542), K605 (= K629)
- binding coenzyme a: F159 (= F173), G160 (= G174), R187 (= R201), R190 (≠ K204), A301 (= A315), T307 (= T321), P330 (= P344), A356 (= A370), S519 (= S539), R580 (≠ A604), P585 (= P609)
- binding magnesium ion: V533 (= V553), H535 (≠ K555), I538 (≠ V559)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G401), E384 (= E402), P385 (= P403), T408 (= T426), W409 (≠ F427), W410 (= W428), Q411 (= Q429), T412 (= T430), D496 (= D515), R511 (= R531), R522 (= R542)
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, 94% coverage: 39:664/664 of query aligns to 28:651/651 of P9WQD1
- K617 (= K629) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
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)
48% identity, 95% coverage: 30:663/664 of query aligns to 34:672/683 of P52910
- K506 (≠ E505) 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, 99% coverage: 9:663/664 of query aligns to 8:653/662 of P78773
- T596 (≠ E606) modified: Phosphothreonine
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)
48% identity, 94% coverage: 36:660/664 of query aligns to 58:674/689 of Q9NUB1
- V488 (= V470) to M: in dbSNP:rs6050249
- K642 (= K629) modified: N6-acetyllysine; mutation to Q: Loss of activity.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
8w0cA Acetyl-coenzyme A synthetase 2
47% identity, 95% coverage: 36:663/664 of query aligns to 38:660/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G401), E400 (= E402), P401 (= P403), T424 (= T426), Y425 (≠ F427), W426 (= W428), Q427 (= Q429), T428 (= T430), D514 (= D515), R529 (= R531), R540 (= R542)
8w0bA Acetyl-coenzyme A synthetase 2
47% identity, 95% coverage: 36:663/664 of query aligns to 38:660/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (= V400), G399 (= G401), E400 (= E402), P401 (= P403), T424 (= T426), Y425 (≠ F427), W426 (= W428), Q427 (= Q429), T428 (= T430), D514 (= D515), I526 (= I528), R529 (= R531), R540 (= R542)
8w0dA Acetyl-coenzyme A synthetase 2
47% identity, 95% coverage: 36:663/664 of query aligns to 37:659/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G401), E399 (= E402), P400 (= P403), T423 (= T426), Y424 (≠ F427), W425 (= W428), Q426 (= Q429), T427 (= T430), D513 (= D515), I525 (= I528), R528 (= R531), R539 (= R542)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
47% identity, 95% coverage: 36:663/664 of query aligns to 37:659/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G401), E399 (= E402), P400 (= P403), T423 (= T426), Y424 (≠ F427), Q426 (= Q429), T427 (= T430), D513 (= D515), I525 (= I528), R528 (= R531), R539 (= R542)
- binding coenzyme a: F175 (= F173), R203 (= R201), R206 (≠ K204), G316 (≠ A315), H538 (= H541), R599 (≠ A604), F605 (≠ I610)
8w0jA Acetyl-coenzyme A synthetase 2
47% identity, 95% coverage: 36:663/664 of query aligns to 38:655/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G401), E400 (= E402), P401 (= P403), T424 (= T426), Y425 (≠ F427), W426 (= W428), Q427 (= Q429), T428 (= T430), D514 (= D515), I526 (= I528), R529 (= R531), R540 (= R542)
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
47% identity, 95% coverage: 36:663/664 of query aligns to 37:654/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (= P150), A176 (≠ G174), G177 (= G175), R203 (= R201), T208 (≠ L206), D317 (= D316), E342 (= E341), G343 (= G342), P345 (= P344), G398 (= G401), E399 (= E402), P400 (= P403), T423 (= T426), W425 (= W428), Q426 (= Q429), T427 (= T430), D513 (= D515), I525 (= I528), R528 (= R531), R539 (= R542)
8v4oA Crystal structure of acetyl-coa synthetase 2 in complex with amp from candida albicans
47% identity, 95% coverage: 36:663/664 of query aligns to 37:654/660 of 8v4oA
- binding adenosine monophosphate: G398 (= G401), E399 (= E402), P400 (= P403), T423 (= T426), Y424 (≠ F427), W425 (= W428), Q426 (= Q429), T427 (= T430), D513 (= D515), I525 (= I528), R528 (= R531), R539 (= R542)
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, 95% coverage: 36:663/664 of query aligns to 51:670/682 of Q99NB1
- K635 (= K629) modified: N6-acetyllysine
7kdsA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-propylphosphate from candida albicans
47% identity, 95% coverage: 36:663/664 of query aligns to 37:649/654 of 7kdsA
- active site: T275 (= T274), T427 (= T430), E428 (= E431), N534 (= N537), R539 (= R542), K620 (= K629)
- binding adenosine-5'-monophosphate-propyl ester: I321 (= I320), G398 (= G401), E399 (= E402), P400 (= P403), D422 (= D425), T423 (= T426), Y424 (≠ F427), W425 (= W428), Q426 (= Q429), T427 (= T430), D513 (= D515), R528 (= R531), N534 (= N537), R539 (= R542)
Query Sequence
>Ac3H11_951 FitnessBrowser__acidovorax_3H11:Ac3H11_951
MSAPTSAIESVLVENRVFPPSDAVVKAARVSGMAGYDALCAEADKDFEGFWARLARENVN
WTKPFNRTLDTSNAPFFKWFDDGELNASANCLDRHIGTPTENKTAIVFEADDGTVTRITY
KELLARVSQFANALKAHGVTKGDRVLIYMPMTIEGVIAMQACARIGATHSVVFGGFSAKA
VQERIIDAGAVAVITANYQMRGGKELPLKAIIDEALAMGGCDTIRNVFVYQRTATACNMV
AGRDKTFGEMLAGQSTECAPVPVGAEHPLFILYTSGSTGKPKGVQHATGGYLLWAKLTMD
WTFDLRADDVFWCTADIGWITGHTYVAYGPLAAGATQIIFEGVPTFPNAGRFWQMIEKHK
CTIFYTAPTAIRSLIKAAEGDAAVHPARSDLSSLRILGSVGEPINPEAWMWYHKNVGGER
CPIVDTFWQTETGGHVITPLPGATPLVPGSCTLPLPGISAAIVDEMGNDVANGAGGILVI
KKPWPSMIRTIWNDPERFKKAYFPEELKGYYLAGDGAVRSADRGYFRITGRIDDVLNVSG
HRMGTMEIESALVSKTDLVAEAAVVGRPDDVTGEAICAFVVLKRSRPTGEEAKQIANELR
NWVAKEIGPIAKPKDIRFGDNLPKTRSGKIMRRLLRSIAKGEAITQDTSTLENPAILDQL
AKAN
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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