SitesBLAST
Comparing WP_058930181.1 NCBI__GCF_001484605.1:WP_058930181.1 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)
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)
54% identity, 88% coverage: 80:725/738 of query aligns to 9:648/651 of P9WQD1
- K617 (= K694) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase 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)
44% identity, 86% coverage: 102:734/738 of query aligns to 38:648/652 of P27550
- K609 (= K694) modified: N6-acetyllysine; by autocatalysis
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
43% identity, 87% coverage: 87:731/738 of query aligns to 19:639/641 of 2p20A
- active site: T260 (= T343), T412 (≠ S501), E413 (= E502), N517 (= N608), R522 (≠ L613), K605 (= K694)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G472), E384 (= E473), P385 (≠ A474), T408 (= T497), W409 (= W498), W410 (= W499), Q411 (= Q500), T412 (≠ S501), D496 (= D587), I508 (= I599), R511 (= R602), R522 (≠ L613)
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)
43% identity, 88% coverage: 87:734/738 of query aligns to 23:648/652 of Q8ZKF6
- R194 (≠ V270) 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 (= T395) binding CoA
- N335 (= N419) binding CoA
- A357 (= A441) 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 (= D604) 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 (= S610) binding CoA
- G524 (= G611) 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 (≠ L613) 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 (≠ A669) 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 (= K694) 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)
43% identity, 87% coverage: 87:731/738 of query aligns to 18:635/637 of 2p2fA
- active site: T259 (= T343), T411 (≠ S501), E412 (= E502), N516 (= N608), R521 (≠ L613), K604 (= K694)
- binding adenosine monophosphate: G382 (= G472), E383 (= E473), P384 (≠ A474), T407 (= T497), W408 (= W498), W409 (= W499), Q410 (= Q500), T411 (≠ S501), D495 (= D587), I507 (= I599), R510 (= R602), N516 (= N608), R521 (≠ L613)
- binding coenzyme a: F158 (= F239), R186 (= R267), W304 (= W393), T306 (= T395), P329 (= P418), A352 (= A441), A355 (≠ L444), S518 (= S610), R579 (≠ A669), P584 (= P674)
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
43% identity, 87% coverage: 87:731/738 of query aligns to 19:638/640 of 5jrhA
- active site: T260 (= T343), T412 (≠ S501), E413 (= E502), N517 (= N608), R522 (≠ L613), K605 (= K694)
- binding (r,r)-2,3-butanediol: W93 (≠ F174), E140 (= E220), G169 (≠ F249), K266 (= K349), P267 (= P350)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G472), E384 (= E473), P385 (≠ A474), T408 (= T497), W409 (= W498), W410 (= W499), Q411 (= Q500), T412 (≠ S501), D496 (= D587), I508 (= I599), N517 (= N608), R522 (≠ L613)
- binding coenzyme a: F159 (= F239), G160 (= G240), G161 (= G241), R187 (= R267), S519 (= S610), R580 (≠ A669), P585 (= P674)
- binding magnesium ion: V533 (= V624), H535 (= H626), I538 (≠ V629)
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
43% identity, 84% coverage: 87:706/738 of query aligns to 19:617/634 of 1pg3A
- active site: T260 (= T343), T412 (≠ S501), E413 (= E502), N517 (= N608), R522 (≠ L613), K605 (= K694)
- binding coenzyme a: F159 (= F239), G160 (= G240), R187 (= R267), R190 (≠ V270), A301 (= A389), T307 (= T395), P330 (= P418), A356 (≠ L444), S519 (= S610), R580 (≠ A669), P585 (= P674)
- binding magnesium ion: V533 (= V624), H535 (= H626), I538 (≠ V629)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G472), E384 (= E473), P385 (≠ A474), T408 (= T497), W409 (= W498), W410 (= W499), Q411 (= Q500), T412 (≠ S501), D496 (= D587), R511 (= R602), R522 (≠ L613)
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)
43% identity, 88% coverage: 86:731/738 of query aligns to 21:642/648 of Q89WV5
- G263 (= G345) mutation to I: Loss of activity.
- G266 (= G348) mutation to I: Great decrease in activity.
- K269 (= K351) mutation to G: Great decrease in activity.
- E414 (= E502) mutation to Q: Great decrease in activity.
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
43% identity, 85% coverage: 88:713/738 of query aligns to 31:630/630 of 8rplB
- 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: G391 (= G472), E392 (= E473), P393 (≠ A474), T416 (= T497), W417 (= W498), W418 (= W499), Q419 (= Q500), T420 (≠ S501), D502 (= D587), R517 (= R602), K523 (≠ N608), R528 (≠ L613)
- binding magnesium ion: V539 (= V624), H541 (= H626)
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)
43% identity, 80% coverage: 145:736/738 of query aligns to 95:701/701 of Q9QXG4
- K661 (= K694) modified: N6-acetyllysine
7l4gB Crystal structure of acetyl-coa synthetase in complex with acetyl adenylate from cryptococcus neoformans h99
44% identity, 79% coverage: 142:725/738 of query aligns to 84:664/668 of 7l4gB
- active site: T280 (= T343), T432 (≠ S501), E433 (= E502), N539 (= N608), R544 (≠ L613), K631 (= K694)
- 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 (= W393), G403 (= G472), E404 (= E473), P405 (≠ A474), T428 (= T497), Y429 (≠ W498), W430 (= W499), M431 (≠ Q500), T432 (≠ S501), D518 (= D587), I530 (= I599), R533 (= R602)
5u29A Crystal structure of cryptococcus neoformans h99 acetyl-coa synthetase in complex with ac-ams
44% identity, 79% coverage: 142:725/738 of query aligns to 84:664/668 of 5u29A
- active site: T280 (= T343), T432 (≠ S501), E433 (= E502), N539 (= N608), R544 (≠ L613), K631 (= K694)
- binding 5'-O-(acetylsulfamoyl)adenosine: W325 (= W393), G403 (= G472), E404 (= E473), P405 (≠ A474), T428 (= T497), Y429 (≠ W498), W430 (= W499), M431 (≠ Q500), T432 (≠ S501), D518 (= D587), I530 (= I599), R533 (= R602)
7mmzA Crystal structure of acetyl-coenzyme a synthetase from legionella pneumophila philadelphia 1 in complex with ethyl-amp (see paper)
45% identity, 79% coverage: 102:682/738 of query aligns to 10:556/559 of 7mmzA
- active site: T231 (= T343), T383 (≠ S501), E384 (= E502), N486 (= N608), R491 (≠ L613)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: I277 (≠ V394), G354 (= G472), E355 (= E473), P356 (≠ A474), T379 (= T497), W380 (= W498), W381 (= W499), Q382 (= Q500), T383 (≠ S501), D465 (= D587), I477 (= I599), R480 (= R602), R491 (≠ L613)
5k8fA Crystal structure of acetyl-coa synthetase in complex with atp and acetyl-amp from cryptococcus neoformans h99
44% identity, 77% coverage: 142:706/738 of query aligns to 84:643/656 of 5k8fA
- active site: T280 (= T343), T432 (≠ S501), E433 (= E502), N539 (= N608), R544 (≠ L613), K631 (= K694)
- 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 (= W393), I326 (≠ V394), G403 (= G472), E404 (= E473), P405 (≠ A474), T428 (= T497), Y429 (≠ W498), W430 (= W499), M431 (≠ Q500), T432 (≠ S501), D518 (= D587), I530 (= I599), R533 (= R602), K631 (= K694)
- binding adenosine-5'-triphosphate: T280 (= T343), S281 (= S344), G282 (= G345), S283 (≠ T346), T284 (= T347), K288 (= K351), G403 (= G472), E404 (= E473), P405 (≠ A474), T428 (= T497), Y429 (≠ W498), M431 (≠ Q500), T432 (≠ S501), D518 (= D587), I530 (= I599), R533 (= R602), K631 (= K694)
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)
42% identity, 79% coverage: 142:724/738 of query aligns to 81:669/683 of P52910
- K506 (≠ S575) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
8g0vA Crystal structure of acetyl-coa synthetase in complex with a propyne ester amp inhibitor from cryptococcus neoformans h99
43% identity, 79% coverage: 142:725/738 of query aligns to 84:662/666 of 8g0vA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: W323 (= W393), I324 (≠ V394), V400 (= V471), G401 (= G472), E402 (= E473), P403 (≠ A474), T426 (= T497), Y427 (≠ W498), W428 (= W499), M429 (≠ Q500), T430 (≠ S501), D516 (= D587)
8g0uA Crystal structure of acetyl-coa synthetase in complex with an isopropyl ester amp inhibitor from cryptococcus neoformans h99
43% identity, 79% coverage: 142:725/738 of query aligns to 84:662/666 of 8g0uA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: W323 (= W393), I324 (≠ V394), G401 (= G472), E402 (= E473), P403 (≠ A474), T426 (= T497), Y427 (≠ W498), W428 (= W499), M429 (≠ Q500), T430 (≠ S501), D516 (= D587), I528 (= I599), R531 (= R602)
7knoA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-ethylphosphate from cryptococcus neoformans var. Grubii serotype a (h99)
43% identity, 79% coverage: 142:725/738 of query aligns to 84:662/666 of 7knoA
- active site: T280 (= T343), T430 (≠ S501), E431 (= E502), N537 (= N608), R542 (≠ L613), K629 (= K694)
- binding 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine: W323 (= W393), I324 (≠ V394), G401 (= G472), E402 (= E473), P403 (≠ A474), T426 (= T497), Y427 (≠ W498), W428 (= W499), M429 (≠ Q500), T430 (≠ S501), D516 (= D587), R531 (= R602)
7kdnA Crystal structure of acetyl-coa synthetase in complex with adenosine- 5'-propylphosphate from aspergillus fumigatus
41% identity, 87% coverage: 61:704/738 of query aligns to 7:622/622 of 7kdnA
- active site: T271 (= T343), T422 (≠ S501), E423 (= E502), N529 (= N608), R534 (≠ L613), K612 (= K694)
- binding adenosine-5'-monophosphate-propyl ester: G393 (= G472), E394 (= E473), P395 (≠ A474), T418 (= T497), Y419 (≠ W498), W420 (= W499), Q421 (= Q500), T422 (≠ S501), D508 (= D587), I520 (= I599), R523 (= R602), R534 (≠ L613)
8g0tA Crystal structure of acetyl-coa synthetase in complex with a cyclopropyl ester amp inhibitor from cryptococcus neoformans h99
44% identity, 77% coverage: 142:711/738 of query aligns to 83:644/656 of 8g0tA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: W321 (= W393), I322 (≠ V394), G399 (= G472), E400 (= E473), P401 (≠ A474), D423 (= D496), T424 (= T497), Y425 (≠ W498), W426 (= W499), M427 (≠ Q500), T428 (≠ S501), D514 (= D587), R529 (= R602), K627 (= K694)
Query Sequence
>WP_058930181.1 NCBI__GCF_001484605.1:WP_058930181.1
MTSDLSSATPLSTLSPVSAAAAAATTDSLQSTSNATAIEAGLRDAAGPTNSPSGWSSTGL
QDVAVHGAPSGGPARHGSTTSSTTAAQHTAEHEAAQPDNVAFWEQQALRLDWAQPAGISG
GKPWHTAHRRVPADAAAGKGPEITWFEGGKLNVAYNCVDRHVANGRGDNVAFHFEGEPGD
RRTVTYAELQREVSKAANALLALGITKGDRVVIYLPVIPETVIITLAVARIGAIHSLVFG
GFSADALKFRVEDTGAKLLVTTDGQFRRGVAVPVKDNADAAVAGDNAIEHVLVVNRTTAP
EDLAAVPMTEGRDVWWHDAVGSAADVHEPEAFDAETPLFIMYTSGTTGKPKGLVHTSGGY
LTQASWSFEHLFSNPDPALRDQDVHWCTADLAWVTAHTYEIYGPLSNGATQVIFEGTPNT
PHPGRHFEIIERYGVTQYYTAPTLVRSLMGWFPDGVPDSYDLSSIRLLGTVGEAVNPEAW
RWLRQNVGAGTAPVVDTWWQSETGATILSPAPTDTEFKPGCAARPLPGVSTRIVDDAGNT
VPPGVQGFIVVDTPGPAIARTVWGNPRRYYDAYWSKYVEQGWFLAGDGAKYDADGDIWIL
GRVDDTLNVSGHLLSTIEIESALVSHADVVEAGVCPVADPTTGHAIVAFVVLKRGVSREV
ATELRNHVAKAIGPIAKPRDVVVVPDVPKTRSGKIMRRLLTQLFEGTALGDTTSLQNEPA
IAGIQDVLRERALVKENS
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