SitesBLAST
Comparing AO353_21765 FitnessBrowser__pseudo3_N2E3:AO353_21765 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)
41% identity, 98% coverage: 5:643/651 of query aligns to 4:632/646 of 4wd1A
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)
27% identity, 94% coverage: 32:643/651 of query aligns to 31:650/662 of P78773
- T596 (≠ N590) modified: Phosphothreonine
8w0dA Acetyl-coenzyme A synthetase 2
26% identity, 98% coverage: 4:641/651 of query aligns to 5:654/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G393), E399 (≠ S394), P400 (≠ A395), T423 (vs. gap), Y424 (vs. gap), W425 (vs. gap), Q426 (vs. gap), T427 (≠ M417), 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
26% identity, 98% coverage: 4:641/651 of query aligns to 5:654/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G393), E399 (≠ S394), P400 (≠ A395), T423 (vs. gap), Y424 (vs. gap), Q426 (vs. gap), T427 (≠ M417), D513 (= D505), I525 (= I517), R528 (= R520), R539 (= R531)
- binding coenzyme a: F175 (≠ S170), R203 (≠ Y198), R206 (≠ K201), G316 (≠ T313), H538 (≠ V530), R599 (= R588), F605 (≠ R594)
8w0cA Acetyl-coenzyme A synthetase 2
26% identity, 98% coverage: 4:641/651 of query aligns to 6:655/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G393), E400 (≠ S394), P401 (≠ A395), T424 (vs. gap), Y425 (vs. gap), W426 (vs. gap), Q427 (vs. gap), T428 (≠ M417), D514 (= D505), R529 (= R520), R540 (= R531)
8w0bA Acetyl-coenzyme A synthetase 2
26% identity, 98% coverage: 4:641/651 of query aligns to 6:655/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ T392), G399 (= G393), E400 (≠ S394), P401 (≠ A395), T424 (vs. gap), Y425 (vs. gap), W426 (vs. gap), Q427 (vs. gap), T428 (≠ M417), D514 (= D505), I526 (= I517), R529 (= R520), R540 (= R531)
8v4pA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-allylphosphate from candida albicans
25% identity, 98% coverage: 4:641/651 of query aligns to 5:649/660 of 8v4pA
- binding 5'-O-{(S)-hydroxy[(prop-2-en-1-yl)oxy]phosphoryl}adenosine: P152 (= P147), A176 (≠ P171), G177 (≠ D172), R203 (≠ Y198), T208 (≠ I203), D317 (≠ T314), E342 (≠ D337), G343 (= G338), P345 (= P340), G398 (= G393), E399 (≠ S394), P400 (≠ A395), T423 (vs. gap), W425 (vs. gap), Q426 (vs. gap), T427 (≠ M417), D513 (= D505), I525 (= I517), R528 (= R520), R539 (= R531)
8v4oA Crystal structure of acetyl-coa synthetase 2 in complex with amp from candida albicans
25% identity, 98% coverage: 4:641/651 of query aligns to 5:649/660 of 8v4oA
- binding adenosine monophosphate: G398 (= G393), E399 (≠ S394), P400 (≠ A395), T423 (vs. gap), Y424 (vs. gap), W425 (vs. gap), Q426 (vs. gap), T427 (≠ M417), D513 (= D505), I525 (= I517), R528 (= R520), R539 (= R531)
8w0jA Acetyl-coenzyme A synthetase 2
25% identity, 98% coverage: 4:641/651 of query aligns to 6:650/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G393), E400 (≠ S394), P401 (≠ A395), T424 (vs. gap), Y425 (vs. gap), W426 (vs. gap), Q427 (vs. gap), T428 (≠ M417), D514 (= D505), I526 (= I517), R529 (= R520), R540 (= R531)
7kdsA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-propylphosphate from candida albicans
26% identity, 98% coverage: 4:641/651 of query aligns to 5:644/654 of 7kdsA
- active site: T275 (≠ S272), T427 (≠ M417), E428 (≠ S418), N534 (= N526), R539 (= R531), K620 (= K613)
- binding adenosine-5'-monophosphate-propyl ester: I321 (≠ M318), G398 (= G393), E399 (≠ S394), P400 (≠ A395), D422 (vs. gap), T423 (vs. gap), Y424 (vs. gap), W425 (vs. gap), Q426 (vs. gap), T427 (≠ M417), D513 (= D505), R528 (= R520), N534 (= N526), R539 (= R531)
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)
26% identity, 94% coverage: 34:643/651 of query aligns to 21:638/648 of Q89WV5
- G263 (= G274) mutation to I: Loss of activity.
- G266 (= G277) mutation to I: Great decrease in activity.
- K269 (= K280) mutation to G: Great decrease in activity.
- E414 (≠ M417) mutation to Q: Great decrease in activity.
7l4gB Crystal structure of acetyl-coa synthetase in complex with acetyl adenylate from cryptococcus neoformans h99
27% identity, 93% coverage: 43:646/651 of query aligns to 49:666/668 of 7l4gB
- active site: T280 (≠ S272), T432 (= T421), E433 (≠ D422), N539 (= N526), R544 (= R531), K631 (= K613)
- 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: W325 (= W317), G403 (= G393), E404 (≠ S394), P405 (≠ A395), T428 (≠ M417), Y429 (≠ S418), W430 (≠ G419), M431 (≠ G420), T432 (= T421), D518 (= D505), I530 (= I517), R533 (= R520)
5u29A Crystal structure of cryptococcus neoformans h99 acetyl-coa synthetase in complex with ac-ams
27% identity, 93% coverage: 43:646/651 of query aligns to 49:666/668 of 5u29A
- active site: T280 (≠ S272), T432 (= T421), E433 (≠ D422), N539 (= N526), R544 (= R531), K631 (= K613)
- binding 5'-O-(acetylsulfamoyl)adenosine: W325 (= W317), G403 (= G393), E404 (≠ S394), P405 (≠ A395), T428 (≠ M417), Y429 (≠ S418), W430 (≠ G419), M431 (≠ G420), T432 (= T421), D518 (= D505), I530 (= I517), R533 (= R520)
5k8fA Crystal structure of acetyl-coa synthetase in complex with atp and acetyl-amp from cryptococcus neoformans h99
28% identity, 90% coverage: 43:627/651 of query aligns to 49:645/656 of 5k8fA
- active site: T280 (≠ S272), T432 (= T421), E433 (≠ D422), N539 (= N526), R544 (= R531), K631 (= K613)
- 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: W325 (= W317), I326 (≠ M318), G403 (= G393), E404 (≠ S394), P405 (≠ A395), T428 (≠ M417), Y429 (≠ S418), W430 (≠ G419), M431 (≠ G420), T432 (= T421), D518 (= D505), I530 (= I517), R533 (= R520), K631 (= K613)
- binding adenosine-5'-triphosphate: T280 (≠ S272), S281 (= S273), G282 (= G274), S283 (≠ T275), T284 (= T276), K288 (= K280), G403 (= G393), E404 (≠ S394), P405 (≠ A395), T428 (≠ M417), Y429 (≠ S418), M431 (≠ G420), T432 (= T421), D518 (= D505), I530 (= I517), R533 (= R520), K631 (= K613)
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)
25% identity, 94% coverage: 32:643/651 of query aligns to 43:692/701 of Q9QXG4
- K661 (= K613) modified: N6-acetyllysine
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
26% identity, 93% coverage: 36:643/651 of query aligns to 20:635/641 of 2p20A
- active site: T260 (≠ S272), T412 (≠ S416), E413 (≠ M417), N517 (= N526), R522 (= R531), K605 (= K613)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G393), E384 (≠ S394), P385 (≠ A395), T408 (vs. gap), W409 (vs. gap), W410 (≠ L414), Q411 (≠ S415), T412 (≠ S416), D496 (= D505), I508 (= I517), R511 (= R520), R522 (= R531)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
26% identity, 93% coverage: 36:643/651 of query aligns to 20:634/640 of 5jrhA
- active site: T260 (≠ S272), T412 (≠ S416), E413 (≠ M417), N517 (= N526), R522 (= R531), K605 (= K613)
- binding (r,r)-2,3-butanediol: W93 (≠ I104), E140 (≠ Q151), G169 (≠ D180), K266 (≠ V278), P267 (= P279)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G393), E384 (≠ S394), P385 (≠ A395), T408 (vs. gap), W409 (vs. gap), W410 (≠ L414), Q411 (≠ S415), T412 (≠ S416), D496 (= D505), I508 (= I517), N517 (= N526), R522 (= R531)
- binding coenzyme a: F159 (≠ S170), G160 (≠ P171), G161 (≠ D172), R187 (≠ Y198), S519 (≠ G528), R580 (= R588), P585 (= P593)
- binding magnesium ion: V533 (≠ E542), H535 (≠ I544), I538 (≠ V547)
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, 93% coverage: 36:643/651 of query aligns to 24:641/652 of P27550
- K609 (= K613) 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)
26% identity, 93% coverage: 36:643/651 of query aligns to 24:641/652 of Q8ZKF6
- R194 (≠ K201) 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 (≠ M319) binding
- N335 (≠ F341) binding
- A357 (≠ S363) 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 (≠ G528) binding
- 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 (= R588) 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 (= K613) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
8g0vA Crystal structure of acetyl-coa synthetase in complex with a propyne ester amp inhibitor from cryptococcus neoformans h99
27% identity, 93% coverage: 43:646/651 of query aligns to 49:664/666 of 8g0vA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: W323 (= W317), I324 (≠ M318), V400 (≠ T392), G401 (= G393), E402 (≠ S394), P403 (≠ A395), T426 (≠ M417), Y427 (≠ S418), W428 (≠ G419), M429 (≠ G420), T430 (= T421), D516 (= D505)
Query Sequence
>AO353_21765 FitnessBrowser__pseudo3_N2E3:AO353_21765
MSEVLWQPSAERIGKTRMDAFRRFSNQRYNLTLADYPALHQWSIDQREDFWQAIVDFFEI
KFHQPASTVLREGPQMPNAEWFPGATLNFAEHLLRRRDNAIAVIAIAENGQRESLSYREL
AEHVAGLQKSLRAAGVGQGDRVAACMPNTWQTLVGMLATTSLGAIWSCSSPDFGTHGVVD
RFGQIEPKVLITCAGYRYAGKKIDQTTKVNEILERLPSLQQLIIVPYARPQARVDDYKTQ
ANVALWDSFYRPGGEPGFVAVPFAHPLYILYSSGTTGVPKCIIHSVGGVLLQHVKEHGLH
VDLGPDDRLFYYTTCGWMMWNWLVSALAVGSSVVLYDGSPFHPGPQRLIDLIDSEAISVF
GTSPKYLATLESNEIQPRLSHDLGSLKALLSTGSALSPQSYDYVYREIKSDLCLSSMSGG
TDIISCFLAGNPVLPVRRGEMQCKGLGMAVEVWNEAGQPVIGEKGELVCTRHFPAMPIGL
WNDPQQEKLRASYFSQFPGVWAQGDYAEQRPNGSWLIHGRSDAVLNPGGVRIGTAEIYRQ
VEKIHQVLDSVAIGQQWQDDVRVVLFVRLRDGVTLDEKLEQEIRQVIRANTTPRHVPAKI
VAVTDIPRTISGKVVELAVRNVVHGQPVKNTDALANPEALEQFRDRPELAN
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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