SitesBLAST
Comparing PP_3071 FitnessBrowser__Putida:PP_3071 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)
43% identity, 98% coverage: 5:642/650 of query aligns to 4:632/646 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)
30% identity, 92% coverage: 45:643/650 of query aligns to 34:648/651 of P9WQD1
- K617 (= K612) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
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)
27% identity, 95% coverage: 36:650/650 of query aligns to 23:647/648 of Q89WV5
- G263 (= G273) mutation to I: Loss of activity.
- G266 (= G276) mutation to I: Great decrease in activity.
- K269 (= K279) mutation to G: Great decrease in activity.
- E414 (≠ M416) mutation to Q: Great decrease in activity.
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)
28% identity, 94% coverage: 32:642/650 of query aligns to 31:650/662 of P78773
- T596 (≠ V585) modified: Phosphothreonine
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)
27% identity, 94% coverage: 29:639/650 of query aligns to 33:666/683 of P52910
- K506 (≠ S494) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
1ry2A Crystal structure of yeast acetyl-coenzyme a synthetase in complex with amp (see paper)
27% identity, 94% coverage: 35:648/650 of query aligns to 2:615/615 of 1ry2A
- active site: T247 (≠ S271), T399 (= T420), N507 (= N525), K590 (= K612)
- binding adenosine monophosphate: G370 (= G392), E371 (≠ S393), P372 (= P394), T395 (≠ M416), Y396 (≠ S417), W397 (≠ G418), Q398 (≠ G419), T399 (= T420), D486 (= D504), I498 (= I516), R501 (= R519)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
27% identity, 94% coverage: 36:647/650 of query aligns to 20:640/641 of 2p20A
- active site: T260 (≠ S271), T412 (≠ S415), E413 (≠ M416), N517 (= N525), R522 (= R530), K605 (= K612)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G392), E384 (≠ S393), P385 (= P394), T408 (≠ L411), W409 (= W412), W410 (≠ L413), Q411 (≠ V414), T412 (≠ S415), D496 (= D504), I508 (= I516), R511 (= R519), R522 (= R530)
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)
27% identity, 94% coverage: 36:647/650 of query aligns to 24:646/652 of P27550
- K609 (= K612) modified: N6-acetyllysine; by autocatalysis
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
27% identity, 94% coverage: 36:647/650 of query aligns to 20:639/640 of 5jrhA
- active site: T260 (≠ S271), T412 (≠ S415), E413 (≠ M416), N517 (= N525), R522 (= R530), K605 (= K612)
- binding (r,r)-2,3-butanediol: W93 (≠ A105), E140 (≠ Q151), G169 (≠ D180), K266 (≠ V277), P267 (= P278)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G392), E384 (≠ S393), P385 (= P394), T408 (≠ L411), W409 (= W412), W410 (≠ L413), Q411 (≠ V414), T412 (≠ S415), D496 (= D504), I508 (= I516), N517 (= N525), R522 (= R530)
- binding coenzyme a: F159 (≠ S170), G160 (≠ P171), G161 (≠ E172), R187 (≠ Y198), S519 (≠ G527), R580 (= R587), P585 (= P592)
- binding magnesium ion: V533 (≠ E541), H535 (≠ V543), I538 (≠ V546)
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)
27% identity, 94% coverage: 36:647/650 of query aligns to 24:646/652 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 (≠ M318) binding
- N335 (≠ F340) binding
- A357 (≠ S362) 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 (= D521) 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 (≠ G527) binding
- G524 (= G528) 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 (= R530) 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 ; 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.
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
27% identity, 94% coverage: 36:647/650 of query aligns to 19:636/637 of 2p2fA
- active site: T259 (≠ S271), T411 (≠ S415), E412 (≠ M416), N516 (= N525), R521 (= R530), K604 (= K612)
- binding adenosine monophosphate: G382 (= G392), E383 (≠ S393), P384 (= P394), T407 (≠ L411), W408 (= W412), W409 (≠ L413), Q410 (≠ V414), T411 (≠ S415), D495 (= D504), I507 (= I516), R510 (= R519), N516 (= N525), R521 (= R530)
- binding coenzyme a: F158 (≠ S170), R186 (≠ Y198), W304 (= W316), T306 (≠ M318), P329 (= P339), A352 (≠ S362), A355 (≠ Y365), S518 (≠ G527), R579 (= R587), P584 (= P592)
7l4gB Crystal structure of acetyl-coa synthetase in complex with acetyl adenylate from cryptococcus neoformans h99
28% identity, 90% coverage: 60:645/650 of query aligns to 66:666/668 of 7l4gB
- active site: T280 (≠ S271), T432 (= T420), E433 (≠ D421), N539 (= N525), R544 (= R530), K631 (= K612)
- 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 (= W316), G403 (= G392), E404 (≠ S393), P405 (= P394), T428 (≠ M416), Y429 (≠ S417), W430 (≠ G418), M431 (≠ G419), T432 (= T420), D518 (= D504), I530 (= I516), R533 (= R519)
5u29A Crystal structure of cryptococcus neoformans h99 acetyl-coa synthetase in complex with ac-ams
28% identity, 90% coverage: 60:645/650 of query aligns to 66:666/668 of 5u29A
- active site: T280 (≠ S271), T432 (= T420), E433 (≠ D421), N539 (= N525), R544 (= R530), K631 (= K612)
- binding 5'-O-(acetylsulfamoyl)adenosine: W325 (= W316), G403 (= G392), E404 (≠ S393), P405 (= P394), T428 (≠ M416), Y429 (≠ S417), W430 (≠ G418), M431 (≠ G419), T432 (= T420), D518 (= D504), I530 (= I516), R533 (= R519)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
27% identity, 94% coverage: 36:647/650 of query aligns to 20:633/634 of 1pg3A
- active site: T260 (≠ S271), T412 (≠ S415), E413 (≠ M416), N517 (= N525), R522 (= R530), K605 (= K612)
- binding coenzyme a: F159 (vs. gap), G160 (vs. gap), R187 (≠ Y198), R190 (≠ K201), A301 (≠ T312), T307 (≠ M318), P330 (= P339), A356 (≠ Y365), S519 (≠ G527), R580 (= R587), P585 (= P592)
- binding magnesium ion: V533 (≠ E541), H535 (≠ V543), I538 (≠ V546)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G392), E384 (≠ S393), P385 (= P394), T408 (≠ L411), W409 (= W412), W410 (≠ L413), Q411 (≠ V414), T412 (≠ S415), D496 (= D504), R511 (= R519), R522 (= R530)
5k8fA Crystal structure of acetyl-coa synthetase in complex with atp and acetyl-amp from cryptococcus neoformans h99
28% identity, 87% coverage: 60:626/650 of query aligns to 66:645/656 of 5k8fA
- active site: T280 (≠ S271), T432 (= T420), E433 (≠ D421), N539 (= N525), R544 (= R530), K631 (= K612)
- 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 (= W316), I326 (≠ M317), G403 (= G392), E404 (≠ S393), P405 (= P394), T428 (≠ M416), Y429 (≠ S417), W430 (≠ G418), M431 (≠ G419), T432 (= T420), D518 (= D504), I530 (= I516), R533 (= R519), K631 (= K612)
- binding adenosine-5'-triphosphate: T280 (≠ S271), S281 (= S272), G282 (= G273), S283 (≠ T274), T284 (= T275), K288 (= K279), G403 (= G392), E404 (≠ S393), P405 (= P394), T428 (≠ M416), Y429 (≠ S417), M431 (≠ G419), T432 (= T420), D518 (= D504), I530 (= I516), R533 (= R519), K631 (= K612)
8g0vA Crystal structure of acetyl-coa synthetase in complex with a propyne ester amp inhibitor from cryptococcus neoformans h99
27% identity, 90% coverage: 60:645/650 of query aligns to 66:664/666 of 8g0vA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: W323 (= W316), I324 (≠ M317), V400 (≠ T391), G401 (= G392), E402 (≠ S393), P403 (= P394), T426 (≠ M416), Y427 (≠ S417), W428 (≠ G418), M429 (≠ G419), T430 (= T420), D516 (= D504)
8g0uA Crystal structure of acetyl-coa synthetase in complex with an isopropyl ester amp inhibitor from cryptococcus neoformans h99
27% identity, 90% coverage: 60:645/650 of query aligns to 66:664/666 of 8g0uA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: W323 (= W316), I324 (≠ M317), G401 (= G392), E402 (≠ S393), P403 (= P394), T426 (≠ M416), Y427 (≠ S417), W428 (≠ G418), M429 (≠ G419), T430 (= T420), D516 (= D504), I528 (= I516), R531 (= R519)
7knoA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate from cryptococcus neoformans var. Grubii serotype a (h99)
27% identity, 90% coverage: 60:645/650 of query aligns to 66:664/666 of 7knoA
- active site: T280 (≠ S271), T430 (= T420), E431 (≠ D421), N537 (= N525), R542 (= R530), K629 (= K612)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: W323 (= W316), I324 (≠ M317), G401 (= G392), E402 (≠ S393), P403 (= P394), T426 (≠ M416), Y427 (≠ S417), W428 (≠ G418), M429 (≠ G419), T430 (= T420), D516 (= D504), R531 (= R519)
8v5gA Crystal structure of acetyl-coa synthetase from cryptococcus neoformans h99 in complex with an ethylsulfamide amp inhibitor
28% identity, 90% coverage: 60:645/650 of query aligns to 65:654/655 of 8v5gA
- binding 5'-deoxy-5'-(ethylsulfamamido)adenosine: V401 (≠ T391), G402 (= G392), E403 (≠ S393), P404 (= P394), T427 (≠ M416), Y428 (≠ S417), W429 (≠ G418), M430 (≠ G419), D517 (= D504), I529 (= I516), K628 (= K612)
8g0tA Crystal structure of acetyl-coa synthetase in complex with a cyclopropyl ester amp inhibitor from cryptococcus neoformans h99
27% identity, 90% coverage: 60:645/650 of query aligns to 65:654/656 of 8g0tA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: W321 (= W316), I322 (≠ M317), G399 (= G392), E400 (≠ S393), P401 (= P394), D423 (≠ S415), T424 (≠ M416), Y425 (≠ S417), W426 (≠ G418), M427 (≠ G419), T428 (= T420), D514 (= D504), R529 (= R519), K627 (= K612)
Query Sequence
>PP_3071 FitnessBrowser__Putida:PP_3071
MNDVLWRPSTTQIEASRMDAFRRRVNLRYNLQLNDYQALHGWSIEQRPAFWQTLAEYFQV
HWHTPPSQVLSEGPQMPDAQWFANATLNFAEHLLRRRDDRPAVVAVREDGQREVFTHAEL
AAQVAGLQTAFKAVGIVPGDRVAAIMPNTWQTLVAMLACTSLGAVWSTSSPEFGVHGIID
RFGQIEPKLLIVCAGYQYAGKAIDQVTKVNQVCAQLPGLEHLIVVPHTRKGTRADEFQAA
NVSLWNDFFQPGGEPRFTPLPFDHPLYILYSSGTTGVPKCIVHRAGGVLLQHLKEHGLHN
DLKADDVLFYYTTCGWMMWNWLASGLAVGATLVLYDGSPFHPGPERLLDLIEAEGIHAFG
TSAKYLAALEQAGLEPANSHCLTSLRLLLSTGSPLSPHSYDYVYDKIKADLWLVSMSGGT
DIVSCFVLGNPTLPVRRGEIQCKGLGMAVEVWNEQGQPVVDEKGELVCTRNFPSMPLGFW
NDPDGRRYHDAYFSQFPGVWAQGDYAEQRASGGMVIHGRSDAVLNPGGVRIGTAEIYRQV
EKVEQVVESVAIGQDWNGDVRVVLFVRLQDGLQLDEALRQHIRQVIRQYTTPRHVPAVIA
QVSDIPRTISGKLVELAIRDVVHGRPVKNTDALANPEALEQFRDRAELKS
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