SitesBLAST
Comparing WP_008200408.1 NCBI__GCF_000166275.1:WP_008200408.1 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)
Q4G176 Malonate--CoA ligase ACSF3, mitochondrial; Acyl-CoA synthetase family member 3; EC 6.2.1.76 from Homo sapiens (Human) (see 2 papers)
42% identity, 97% coverage: 14:492/492 of query aligns to 56:573/576 of Q4G176
- R354 (= R296) mutation to A: Impairs malonyl-CoA synthase activity.; mutation to L: Impairs malonyl-CoA synthase activity.
- V372 (≠ E313) to M: in dbSNP:rs3743979
Sites not aligning to the query:
- 2 L → P: in dbSNP:rs7188200
- 17 A → P: in dbSNP:rs11547019
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
34% identity, 98% coverage: 10:492/492 of query aligns to 14:501/506 of 4gxqA
- active site: T163 (= T150), N183 (≠ Q170), H207 (= H194), T303 (= T300), E304 (= E301), I403 (≠ K399), N408 (≠ K404), A491 (≠ K482)
- binding adenosine-5'-triphosphate: T163 (= T150), S164 (= S151), G165 (= G152), T166 (= T153), T167 (= T154), H207 (= H194), S277 (= S274), A278 (= A275), P279 (≠ A276), E298 (= E295), M302 (= M299), T303 (= T300), D382 (= D378), R397 (= R392)
- binding carbonate ion: H207 (= H194), S277 (= S274), R299 (= R296), G301 (= G298)
3nyrA Malonyl-coa ligase ternary product complex with malonyl-coa and amp bound (see paper)
37% identity, 79% coverage: 88:477/492 of query aligns to 81:460/460 of 3nyrA
- active site: T137 (= T150), T157 (≠ Q170), H181 (= H194), T281 (= T300), E282 (= E301), K379 (= K399), K384 (= K404)
- binding adenosine monophosphate: S255 (= S274), A256 (= A275), A257 (= A276), R277 (= R296), Y278 (= Y297), G279 (= G298), M280 (= M299), T281 (= T300), D357 (= D378), K379 (= K399), K384 (= K404)
- binding malonyl-coenzyme a: P178 (= P191), H181 (= H194), T226 (= T240), R230 (≠ K244), S255 (= S274), R277 (= R296), G279 (= G298), G381 (= G401), G382 (= G402), Y383 (= Y403)
3nyqA Malonyl-coa ligase ternary product complex with methylmalonyl-coa and amp bound (see paper)
37% identity, 79% coverage: 88:477/492 of query aligns to 81:460/460 of 3nyqA
- active site: T137 (= T150), T157 (≠ Q170), H181 (= H194), T281 (= T300), E282 (= E301), K379 (= K399), K384 (= K404)
- binding adenosine monophosphate: S255 (= S274), A256 (= A275), A257 (= A276), R277 (= R296), Y278 (= Y297), G279 (= G298), M280 (= M299), T281 (= T300), D357 (= D378), K379 (= K399), K384 (= K404)
- binding methylmalonyl-coenzyme a: P178 (= P191), H181 (= H194), H183 (= H196), T226 (= T240), R230 (≠ K244), S255 (= S274), R277 (= R296), G279 (= G298), M280 (= M299), M285 (= M304), G381 (= G401), G382 (= G402), Y383 (= Y403)
P69451 Long-chain-fatty-acid--CoA ligase; Long-chain acyl-CoA synthetase; Acyl-CoA synthetase; EC 6.2.1.3 from Escherichia coli (strain K12) (see paper)
28% identity, 99% coverage: 3:489/492 of query aligns to 31:550/561 of P69451
- Y213 (= Y149) mutation to A: Loss of activity.
- T214 (= T150) mutation to A: 10% of wild-type activity.
- G216 (= G152) mutation to A: Decreases activity.
- T217 (= T153) mutation to A: Decreases activity.
- G219 (≠ S155) mutation to A: Decreases activity.
- K222 (= K158) mutation to A: Decreases activity.
- E361 (= E301) mutation to A: Loss of activity.
P9WQ37 Long-chain-fatty-acid--CoA ligase FadD13; Fatty acyl-CoA ligase; FACL; FACL13; Fatty acyl-CoA synthetase; ACS; FACS; Very-long-chain fatty-acyl-CoA synthetase; ACSVL; EC 6.2.1.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
27% identity, 95% coverage: 25:492/492 of query aligns to 31:497/503 of P9WQ37
- K172 (= K158) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ S181) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ D183) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V195) mutation to D: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced. Slight increase of susceptibility to proteolysis.
- A211 (≠ G197) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ N200) mutation to W: Shows a marked decrease in the activity with lauric and palmitic acid (C12 and C16 fatty acid) with a simultaneous increase in the activity with caprylic acid (C8 fatty acid).
- R244 (≠ K231) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ Y292) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.; mutation to W: Does not show activity with small, medium or long acyl chains.
- W377 (= W373) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding. No significant change in the total expression level, however the cytoplasmic expression is low. Slight increase of susceptibility to proteolysis.
- D382 (= D378) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced.
- R397 (≠ D393) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S400) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G402) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K482) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
Sites not aligning to the query:
- 9 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- 17 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
29% identity, 97% coverage: 8:482/492 of query aligns to 14:499/504 of 6qjzA
- active site: T169 (= T150), S189 (≠ Q170), H213 (= H194), T314 (= T300), E315 (= E301), N414 (≠ K399), K419 (= K404)
- binding adenosine monophosphate: H213 (= H194), S288 (= S274), A289 (= A275), S290 (≠ A276), A312 (≠ G298), M313 (= M299), T314 (= T300), D393 (= D378), L405 (≠ I389), K410 (≠ S394), K419 (= K404)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
27% identity, 95% coverage: 25:492/492 of query aligns to 34:497/502 of 3r44A
Sites not aligning to the query:
Q9SMT7 Oxalate--CoA ligase; 4-coumarate--CoA ligase isoform 8; At4CL8; 4-coumarate--CoA ligase-like 10; Acyl-activating enzyme 3; Adenosine monophosphate binding protein 3; AtMPBP3; Oxalyl-CoA synthetase; EC 6.2.1.8 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
28% identity, 99% coverage: 8:492/492 of query aligns to 14:510/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 150:154) binding ATP
- H214 (= H194) binding ATP; mutation to A: Abolished activity.
- S289 (= S274) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ SAA 274:276) binding ATP
- EA 310:311 (≠ ER 295:296) binding ATP
- M314 (= M299) binding oxalate
- T315 (= T300) binding ATP
- H319 (≠ M304) binding oxalate; mutation to A: Abolished activity.
- D394 (= D378) binding ATP
- R409 (= R392) binding ATP; mutation to A: Abolished activity.
- K500 (= K482) binding ATP; binding oxalate; mutation to A: Abolished activity.
O74976 Oxalate--CoA ligase; Oxalyl-CoA synthetase; Peroxisomal-coenzyme A synthetase; EC 6.2.1.8 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 90% coverage: 51:492/492 of query aligns to 54:504/512 of O74976