SitesBLAST
Comparing WP_012755263.1 NCBI__GCF_000023185.1:WP_012755263.1 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)
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
40% identity, 93% coverage: 25:516/528 of query aligns to 13:485/486 of 8wevA
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)
35% identity, 93% coverage: 25:516/528 of query aligns to 11:495/503 of P9WQ37
- R17 (≠ D31) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K187) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ G210) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ G212) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ T224) 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 (≠ G226) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ A229) 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 (≠ Q260) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G320) 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 (= W397) 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 (= D402) 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 (= R417) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S424) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G426) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K508) 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.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
34% identity, 93% coverage: 25:516/528 of query aligns to 14:495/502 of 3r44A
Sites not aligning to the query:
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
32% identity, 92% coverage: 36:520/528 of query aligns to 21:503/506 of 4gxqA
- active site: T163 (= T179), N183 (≠ A199), H207 (= H223), T303 (≠ S322), E304 (= E323), I403 (= I423), N408 (= N428), A491 (≠ K508)
- binding adenosine-5'-triphosphate: T163 (= T179), S164 (= S180), G165 (= G181), T166 (= T182), T167 (= T183), H207 (= H223), S277 (≠ G297), A278 (= A298), P279 (= P299), E298 (≠ N317), M302 (= M321), T303 (≠ S322), D382 (= D402), R397 (= R417)
- binding carbonate ion: H207 (= H223), S277 (≠ G297), R299 (≠ G318), G301 (= G320)
5x8fB Ternary complex structure of a double mutant i454ra456k of o- succinylbenzoate coa synthetase (mene) from bacillus subtilis bound with amp and its product analogue osb-ncoa at 1.76 angstrom (see paper)
32% identity, 95% coverage: 17:515/528 of query aligns to 1:477/485 of 5x8fB
- active site: T151 (= T179), S171 (≠ A199), H195 (= H223), T288 (≠ S322), E289 (= E323), I387 (= I423), N392 (= N428), K470 (= K508)
- binding magnesium ion: Y23 (≠ A39), E24 (≠ T40), H70 (≠ F88), N178 (≠ V206), L202 (≠ V230), L214 (≠ V243), T296 (≠ P331), L297 (≠ I332), S298 (≠ D333)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R103), L191 (= L219), P192 (= P220), H195 (= H223), I196 (≠ T224), S197 (≠ I225), A237 (= A268), V238 (= V269), L260 (≠ F294), G262 (= G296), G286 (= G320), M287 (= M321), S292 (≠ T326), Q293 (≠ V327), S388 (= S424), G389 (= G425), G390 (= G426), E391 (= E427), K420 (≠ R456), W421 (= W457), K450 (≠ A488), Y451 (≠ F489)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
32% identity, 95% coverage: 17:515/528 of query aligns to 1:477/484 of 5gtdA
- active site: T151 (= T179), S171 (≠ A199), H195 (= H223), T288 (≠ S322), E289 (= E323)
- binding adenosine-5'-monophosphate: G263 (= G297), G264 (≠ A298), Y285 (= Y319), G286 (= G320), M287 (= M321), T288 (≠ S322), D366 (= D402), V378 (≠ I414)
- binding magnesium ion: F314 (≠ P349), S315 (≠ L350)
- binding 2-succinylbenzoate: H195 (= H223), S197 (≠ I225), A237 (= A268), L260 (≠ F294), G262 (= G296), G263 (= G297), G286 (= G320), M287 (= M321), S292 (≠ T326), Q293 (≠ V327)
Q84P21 Peroxisomal OPC-8:0-CoA ligase 1; 4-coumarate--CoA ligase isoform 9; At4CL9; 4-coumarate--CoA ligase-like 5; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 91% coverage: 32:509/528 of query aligns to 46:531/546 of Q84P21
- K530 (= K508) mutation to N: Lossed enzymatic activity.
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
32% identity, 94% coverage: 18:515/528 of query aligns to 1:474/475 of 5burA
- active site: T150 (= T179), S170 (≠ A199), H194 (= H223), T287 (≠ S322), E288 (= E323)
- binding adenosine-5'-triphosphate: T150 (= T179), S151 (= S180), T153 (= T182), T154 (= T183), K158 (= K187), G263 (≠ A298), S283 (≠ G318), T287 (≠ S322), D365 (= D402), V377 (≠ I414), R380 (= R417)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
31% identity, 94% coverage: 18:515/528 of query aligns to 1:474/481 of 5busA
- active site: T150 (= T179), S170 (≠ A199), H194 (= H223), T287 (≠ S322), E288 (= E323)
- binding adenosine monophosphate: H194 (= H223), G262 (= G297), G263 (≠ A298), S283 (≠ G318), M286 (= M321), T287 (≠ S322), D365 (= D402), V377 (≠ I414), R380 (= R417), K467 (= K508)
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)
31% identity, 94% coverage: 26:521/528 of query aligns to 14:512/514 of Q9SMT7