SitesBLAST
Comparing WP_013259512.1 NCBI__GCF_000143965.1:WP_013259512.1 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)
5gxdA Structure of acryloyl-coa lyase prpe from dinoroseobacter shibae dfl 12
62% identity, 99% coverage: 4:628/634 of query aligns to 2:626/627 of 5gxdA
- active site: T238 (= T240), T390 (= T392), E391 (= E393), N498 (= N500), R503 (= R505), K587 (= K589)
- binding adenosine monophosphate: G364 (= G366), E365 (= E367), R366 (= R368), H386 (= H388), W387 (= W389), W388 (= W390), Q389 (= Q391), T390 (= T392), D477 (= D479), I489 (= I491), R492 (= R494), N498 (= N500), R503 (= R505)
- binding coenzyme a: F139 (= F141), G140 (= G142), G141 (= G143), E167 (= E169), R170 (= R172), S279 (= S281), K307 (= K309), P308 (= P310), A332 (= A334), T334 (= T336), A363 (= A365), A500 (= A502), H502 (= H504), K532 (= K534), R562 (= R564), P567 (= P569), V568 (= V570)
2p20A Acetyl-coa synthetase, r584a mutation (see paper)
38% identity, 97% coverage: 4:619/634 of query aligns to 20:635/641 of 2p20A
- active site: T260 (= T240), T412 (= T392), E413 (= E393), N517 (= N500), R522 (= R505), K605 (= K589)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G366), E384 (= E367), P385 (≠ R368), T408 (≠ H388), W409 (= W389), W410 (= W390), Q411 (= Q391), T412 (= T392), D496 (= D479), I508 (= I491), R511 (= R494), R522 (= R505)
2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
39% identity, 97% coverage: 4:619/634 of query aligns to 19:631/637 of 2p2fA
- active site: T259 (= T240), T411 (= T392), E412 (= E393), N516 (= N500), R521 (= R505), K604 (= K589)
- binding adenosine monophosphate: G382 (= G366), E383 (= E367), P384 (≠ R368), T407 (≠ H388), W408 (= W389), W409 (= W390), Q410 (= Q391), T411 (= T392), D495 (= D479), I507 (= I491), R510 (= R494), N516 (= N500), R521 (= R505)
- binding coenzyme a: F158 (= F141), R186 (≠ E169), W304 (= W285), T306 (≠ V287), P329 (= P310), A352 (= A334), A355 (= A337), S518 (≠ A502), R579 (= R564), P584 (= P569)
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)
38% identity, 97% coverage: 4:619/634 of query aligns to 24:641/652 of Q8ZKF6
- R194 (= R172) 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 (≠ V287) binding CoA
- N335 (≠ G312) binding CoA
- A357 (= A334) 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 (= D496) 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 (≠ A502) binding CoA
- G524 (= G503) 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 (= R505) 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 (= R564) 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 (= K589) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.
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)
39% identity, 98% coverage: 2:622/634 of query aligns to 23:650/651 of P9WQD1
- K617 (= K589) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.
5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
39% identity, 97% coverage: 4:619/634 of query aligns to 20:634/640 of 5jrhA
- active site: T260 (= T240), T412 (= T392), E413 (= E393), N517 (= N500), R522 (= R505), K605 (= K589)
- binding (r,r)-2,3-butanediol: W93 (≠ Y75), E140 (≠ Q122), G169 (≠ V151), K266 (≠ S246), P267 (= P247)
- binding adenosine-3',5'-cyclic-monophosphate: G383 (= G366), E384 (= E367), P385 (≠ R368), T408 (≠ H388), W409 (= W389), W410 (= W390), Q411 (= Q391), T412 (= T392), D496 (= D479), I508 (= I491), N517 (= N500), R522 (= R505)
- binding coenzyme a: F159 (= F141), G160 (= G142), G161 (= G143), R187 (≠ E169), S519 (≠ A502), R580 (= R564), P585 (= P569)
- binding magnesium ion: V533 (≠ A516), H535 (= H518), I538 (≠ V521)
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)
38% identity, 100% coverage: 1:632/634 of query aligns to 37:682/683 of P52910
- K506 (≠ T469) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
8rwjD Cryoem structure of acs1 filament determined by filamentid (see paper)
38% identity, 95% coverage: 4:603/634 of query aligns to 39:652/676 of 8rwjD
- 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: G406 (= G366), P408 (≠ R368), T431 (≠ H388), Y432 (≠ W389), Q434 (= Q391), T435 (= T392), D522 (= D479), R537 (= R494), K638 (= K589)
1ry2A Crystal structure of yeast acetyl-coenzyme a synthetase in complex with amp (see paper)
38% identity, 94% coverage: 4:598/634 of query aligns to 3:599/615 of 1ry2A
- active site: T247 (= T240), T399 (= T392), N507 (= N500), K590 (= K589)
- binding adenosine monophosphate: G370 (= G366), E371 (= E367), P372 (≠ R368), T395 (≠ H388), Y396 (≠ W389), W397 (= W390), Q398 (= Q391), T399 (= T392), D486 (= D479), I498 (= I491), R501 (= R494)
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)
38% identity, 97% coverage: 4:619/634 of query aligns to 24:641/652 of P27550
- K609 (= K589) modified: N6-acetyllysine; by autocatalysis
1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
39% identity, 95% coverage: 4:606/634 of query aligns to 20:622/634 of 1pg3A
- active site: T260 (= T240), T412 (= T392), E413 (= E393), N517 (= N500), R522 (= R505), K605 (= K589)
- binding coenzyme a: F159 (= F141), G160 (= G142), R187 (≠ E169), R190 (= R172), A301 (≠ S281), T307 (≠ V287), P330 (= P310), A356 (= A337), S519 (≠ A502), R580 (= R564), P585 (= P569)
- binding magnesium ion: V533 (≠ A516), H535 (= H518), I538 (≠ V521)
- binding adenosine-5'-monophosphate-propyl ester: G383 (= G366), E384 (= E367), P385 (≠ R368), T408 (≠ H388), W409 (= W389), W410 (= W390), Q411 (= Q391), T412 (= T392), D496 (= D479), R511 (= R494), R522 (= R505)
8rplB Amp-forming acetyl-coa synthetase from chloroflexota bacterium with bound acetyl amp (see paper)
37% identity, 94% coverage: 4:596/634 of query aligns to 31:618/630 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 (= G366), E392 (= E367), P393 (≠ R368), T416 (≠ H388), W417 (= W389), W418 (= W390), Q419 (= Q391), T420 (= T392), D502 (= D479), R517 (= R494), K523 (≠ N500), R528 (= R505)
- binding magnesium ion: V539 (≠ A516), H541 (= H518)
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)
38% identity, 97% coverage: 4:619/634 of query aligns to 23:638/648 of Q89WV5
- G263 (= G242) mutation to I: Loss of activity.
- G266 (= G245) mutation to I: Great decrease in activity.
- K269 (= K248) mutation to G: Great decrease in activity.
- E414 (= E393) mutation to Q: Great decrease in activity.
8w0dA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with an isopropyl amp ester inhibitor
37% identity, 98% coverage: 1:623/634 of query aligns to 34:660/666 of 8w0dA
- binding 5'-O-{(R)-hydroxy[(propan-2-yl)oxy]phosphoryl}adenosine: G398 (= G366), E399 (= E367), P400 (≠ R368), T423 (≠ H388), Y424 (≠ W389), W425 (= W390), Q426 (= Q391), T427 (= T392), D513 (= D479), I525 (= I491), R528 (= R494), R539 (= R505)
8v4rA Crystal structure of acetyl-coa synthetase 2 in complex with amp and coa from candida albicans
37% identity, 98% coverage: 1:623/634 of query aligns to 34:660/666 of 8v4rA
- binding adenosine monophosphate: G398 (= G366), E399 (= E367), P400 (≠ R368), T423 (≠ H388), Y424 (≠ W389), Q426 (= Q391), T427 (= T392), D513 (= D479), I525 (= I491), R528 (= R494), R539 (= R505)
- binding coenzyme a: F175 (= F141), R203 (≠ E169), R206 (= R172), G316 (≠ S281), H538 (= H504), R599 (= R564), F605 (≠ V570)
8w0cA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopentyl ester amp inhibitor
37% identity, 98% coverage: 1:623/634 of query aligns to 35:661/667 of 8w0cA
- binding 5'-O-[(S)-(cyclopentyloxy)(hydroxy)phosphoryl]adenosine: G399 (= G366), E400 (= E367), P401 (≠ R368), T424 (≠ H388), Y425 (≠ W389), W426 (= W390), Q427 (= Q391), T428 (= T392), D514 (= D479), R529 (= R494), R540 (= R505)
8w0bA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a cyclopropyl amp ester inhibitor
37% identity, 98% coverage: 1:623/634 of query aligns to 35:661/667 of 8w0bA
- binding 5'-O-[(R)-(cyclopropyloxy)(hydroxy)phosphoryl]adenosine: V398 (≠ A365), G399 (= G366), E400 (= E367), P401 (≠ R368), T424 (≠ H388), Y425 (≠ W389), W426 (= W390), Q427 (= Q391), T428 (= T392), D514 (= D479), I526 (= I491), R529 (= R494), R540 (= R505)
7kdsA Crystal structure of acetyl-coa synthetase 2 in complex with adenosine-5'-propylphosphate from candida albicans
37% identity, 98% coverage: 1:623/634 of query aligns to 34:650/654 of 7kdsA
- active site: T275 (= T240), T427 (= T392), E428 (= E393), N534 (= N500), R539 (= R505), K620 (= K589)
- binding adenosine-5'-monophosphate-propyl ester: I321 (≠ V286), G398 (= G366), E399 (= E367), P400 (≠ R368), D422 (= D387), T423 (≠ H388), Y424 (≠ W389), W425 (= W390), Q426 (= Q391), T427 (= T392), D513 (= D479), R528 (= R494), N534 (= N500), R539 (= R505)
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)
37% identity, 98% coverage: 1:619/634 of query aligns to 32:650/662 of P78773
- T596 (≠ Q566) modified: Phosphothreonine
8w0jA Crystal structure of acetyl-coa synthetase 2 from candida albicans in complex with a propyne amp ester inhibitor
37% identity, 98% coverage: 1:623/634 of query aligns to 35:656/662 of 8w0jA
- binding 5'-O-{(S)-hydroxy[(prop-2-yn-1-yl)oxy]phosphoryl}adenosine: G399 (= G366), E400 (= E367), P401 (≠ R368), T424 (≠ H388), Y425 (≠ W389), W426 (= W390), Q427 (= Q391), T428 (= T392), D514 (= D479), I526 (= I491), R529 (= R494), R540 (= R505)
Query Sequence
>WP_013259512.1 NCBI__GCF_000143965.1:WP_013259512.1
MGAYEKAFRQSIEDPEVFWGQAAQAIDWDRRWDKVLDDSNAPFYRWFSGGMLNTCHNALD
RHVAGGRAKQAALIYDSPVTGVKQVFSYEQLLELTAKCAGALVRLGLAKGDTAIIYMPMA
PQAVVAMLACARIGAAHSVVFGGFAAKELAVRIDDAKPKVVISASCGIEINRVIEYKPLL
DKAIDMAVHKPESCLILQRPQATAALTAGRDHDWDQALATADPAPCVSVAATDPLYILYT
SGTTGSPKGIVRDNGGHAVALAWTMKNIYGLEPGEVFWAASDVGWVVGHSYIVYAPLIHG
CTSVLYEGKPVGTPDAGAFWRVIAEHGVKALFTAPTAFRAIKREDPEGRLFKAHDLGRFQ
TLFLAGERTDPDTLHWAGQLLQRPVVDHWWQTETGWAIAANCVGLEMLPIKPGSPTKAAP
GWDVRILREDGSEAAPLEAGVVVVRLPLPPGSLPTLWNAPERFRETYLTAFPGYYFTGDE
GYVDDDGYLFIMGRVDDVINVAGHRLSTGAMEEVVAQHPDVAECAVIGAADSFKGQLPVA
MVVLKAGAKTAPEQIKDDLVRMVREQIGPVASFKEAVVVARLPKTRSGKILRGVMRKIAD
GRAATPPSTIEDPAALDEIGAALRSIGYGQAQGA
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