SitesBLAST
Comparing WP_036258835.1 NCBI__GCF_000746085.1:WP_036258835.1 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)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
63% identity, 100% coverage: 1:505/507 of query aligns to 1:506/506 of 4gxqA
- active site: T163 (= T165), N183 (= N185), H207 (= H209), T303 (= T305), E304 (= E306), I403 (= I405), N408 (= N410), A491 (≠ K490)
- binding adenosine-5'-triphosphate: T163 (= T165), S164 (= S166), G165 (= G167), T166 (= T168), T167 (= T169), H207 (= H209), S277 (= S279), A278 (= A280), P279 (= P281), E298 (= E300), M302 (= M304), T303 (= T305), D382 (= D384), R397 (= R399)
- binding carbonate ion: H207 (= H209), S277 (= S279), R299 (= R301), G301 (= G303)
Q4G176 Malonate--CoA ligase ACSF3, mitochondrial; Acyl-CoA synthetase family member 3; EC 6.2.1.76 from Homo sapiens (Human) (see 2 papers)
33% identity, 94% coverage: 18:496/507 of query aligns to 55:569/576 of Q4G176
- R354 (= R301) mutation to A: Impairs malonyl-CoA synthase activity.; mutation to L: Impairs malonyl-CoA synthase activity.
- V372 (≠ E318) to M: in dbSNP:rs3743979
Sites not aligning to the query:
- 2 L → P: in dbSNP:rs7188200
- 17 A → P: in dbSNP:rs11547019
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
35% identity, 93% coverage: 26:497/507 of query aligns to 26:484/486 of 8wevA
Sites not aligning to the query:
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)
34% identity, 98% coverage: 8:503/507 of query aligns to 7:500/503 of P9WQ37
- R9 (= R10) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D17) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K173) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T196) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ A198) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ T210) 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 (= A216) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (= T219) 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 (≠ S246) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G303) 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 (≠ F379) 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 (= D384) 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 (= R399) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ T406) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G408) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K490) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
3nyrA Malonyl-coa ligase ternary product complex with malonyl-coa and amp bound (see paper)
39% identity, 79% coverage: 83:485/507 of query aligns to 71:460/460 of 3nyrA
- active site: T137 (= T165), T157 (≠ N185), H181 (= H209), T281 (= T305), E282 (= E306), K379 (≠ I405), K384 (≠ N410)
- binding adenosine monophosphate: S255 (= S279), A256 (= A280), A257 (≠ P281), R277 (= R301), Y278 (= Y302), G279 (= G303), M280 (= M304), T281 (= T305), D357 (= D384), K379 (≠ I405), K384 (≠ N410)
- binding malonyl-coenzyme a: P178 (= P206), H181 (= H209), T226 (= T253), R230 (= R257), S255 (= S279), R277 (= R301), G279 (= G303), G381 (= G407), G382 (= G408), Y383 (≠ F409)
3nyqA Malonyl-coa ligase ternary product complex with methylmalonyl-coa and amp bound (see paper)
39% identity, 79% coverage: 83:485/507 of query aligns to 71:460/460 of 3nyqA
- active site: T137 (= T165), T157 (≠ N185), H181 (= H209), T281 (= T305), E282 (= E306), K379 (≠ I405), K384 (≠ N410)
- binding adenosine monophosphate: S255 (= S279), A256 (= A280), A257 (≠ P281), R277 (= R301), Y278 (= Y302), G279 (= G303), M280 (= M304), T281 (= T305), D357 (= D384), K379 (≠ I405), K384 (≠ N410)
- binding methylmalonyl-coenzyme a: P178 (= P206), H181 (= H209), H183 (= H211), T226 (= T253), R230 (= R257), S255 (= S279), R277 (= R301), G279 (= G303), M280 (= M304), M285 (= M309), G381 (= G407), G382 (= G408), Y383 (≠ F409)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
33% identity, 98% coverage: 8:503/507 of query aligns to 10:500/502 of 3r44A
Sites not aligning to the query:
5ie2A Crystal structure of a plant enzyme (see paper)
33% identity, 95% coverage: 18:500/507 of query aligns to 19:505/506 of 5ie2A
- active site: T165 (= T165), S185 (≠ N185), H209 (= H209), T310 (= T305), E311 (= E306), N410 (≠ I405), K415 (≠ N410), K495 (= K490)
- binding adenosine-5'-triphosphate: T165 (= T165), S166 (= S166), G167 (= G167), T168 (= T168), T169 (= T169), S284 (= S279), A285 (= A280), S286 (≠ P281), Y307 (= Y302), A308 (≠ G303), M309 (= M304), T310 (= T305), D389 (= D384), L401 (≠ I396), R404 (= R399), K495 (= K490)
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)
33% identity, 95% coverage: 18:500/507 of query aligns to 19:510/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 165:169) binding ATP
- H214 (= H209) binding ATP; mutation to A: Abolished activity.
- S289 (= S279) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ SAP 279:281) binding ATP
- EA 310:311 (≠ ER 300:301) binding ATP
- M314 (= M304) binding oxalate
- T315 (= T305) binding ATP
- H319 (≠ N308) binding oxalate; mutation to A: Abolished activity.
- D394 (= D384) binding ATP
- R409 (= R399) binding ATP; mutation to A: Abolished activity.
- K500 (= K490) binding ATP; binding oxalate; mutation to A: Abolished activity.
5ie3A Crystal structure of a plant enzyme (see paper)
33% identity, 95% coverage: 18:500/507 of query aligns to 19:503/504 of 5ie3A