SitesBLAST
Comparing H281DRAFT_04125 FitnessBrowser__Burk376:H281DRAFT_04125 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)
34% identity, 93% coverage: 35:518/520 of query aligns to 15:499/506 of 4gxqA
- active site: T163 (= T182), N183 (≠ I202), H207 (= H226), T303 (= T326), E304 (= E327), I403 (= I426), N408 (= N431), A491 (≠ K510)
- binding adenosine-5'-triphosphate: T163 (= T182), S164 (≠ T183), G165 (= G184), T166 (= T185), T167 (= T186), H207 (= H226), S277 (≠ G300), A278 (≠ S301), P279 (= P302), E298 (≠ N321), M302 (= M325), T303 (= T326), D382 (= D405), R397 (= R420)
- binding carbonate ion: H207 (= H226), S277 (≠ G300), R299 (≠ G322), G301 (= G324)
Q9S725 4-coumarate--CoA ligase 2; 4CL 2; 4-coumarate--CoA ligase isoform 2; At4CL2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; EC 6.2.1.12; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
29% identity, 88% coverage: 61:517/520 of query aligns to 77:547/556 of Q9S725
- K211 (= K190) mutation to S: Drastically reduces the activity.
- M293 (≠ Q268) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ Y297) mutation K->L,A: Affects the substrate specificity.
- E401 (= E372) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ W374) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R420) mutation to Q: Drastically reduces the activity.
- K457 (≠ S428) mutation to S: Drastically reduces the activity.
- K540 (= K510) mutation to N: Abolishes the 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)
34% identity, 91% coverage: 47:518/520 of query aligns to 29:495/503 of P9WQ37
- K172 (= K190) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R213) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ D215) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V227) 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 (≠ G229) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ S232) 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 (= R263) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G324) 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 (= W400) 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 (= D405) 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 (= R420) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R427) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G429) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K510) 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.
Q4WR83 Acyl-CoA ligase sidI; Siderophore biosynthesis protein I; EC 6.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
30% identity, 97% coverage: 14:519/520 of query aligns to 32:572/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
35% identity, 66% coverage: 177:518/520 of query aligns to 209:551/561 of P69451
- Y213 (= Y181) mutation to A: Loss of activity.
- T214 (= T182) mutation to A: 10% of wild-type activity.
- G216 (= G184) mutation to A: Decreases activity.
- T217 (= T185) mutation to A: Decreases activity.
- G219 (= G187) mutation to A: Decreases activity.
- K222 (= K190) mutation to A: Decreases activity.
- E361 (= E327) mutation to A: Loss of activity.
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)
29% identity, 91% coverage: 45:516/520 of query aligns to 55:536/546 of Q84P21
- K530 (= K510) mutation to N: Lossed enzymatic activity.
Q4G176 Malonate--CoA ligase ACSF3, mitochondrial; Acyl-CoA synthetase family member 3; EC 6.2.1.76 from Homo sapiens (Human) (see 2 papers)
31% identity, 94% coverage: 29:519/520 of query aligns to 50:573/576 of Q4G176
- R354 (≠ G322) mutation to A: Impairs malonyl-CoA synthase activity.; mutation to L: Impairs malonyl-CoA synthase activity.
- V372 (≠ P340) to M: in dbSNP:rs3743979
Sites not aligning to the query:
- 2 L → P: in dbSNP:rs7188200
- 17 A → P: in dbSNP:rs11547019
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
31% identity, 93% coverage: 36:518/520 of query aligns to 15:475/475 of 5burA
- active site: T150 (= T182), S170 (≠ I202), H194 (= H226), T287 (= T326), E288 (= E327)
- binding adenosine-5'-triphosphate: T150 (= T182), S151 (≠ T183), T153 (= T185), T154 (= T186), K158 (= K190), G263 (≠ S301), S283 (≠ G322), T287 (= T326), D365 (= D405), V377 (≠ I417), R380 (= R420)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
31% identity, 93% coverage: 36:518/520 of query aligns to 15:475/481 of 5busA
- active site: T150 (= T182), S170 (≠ I202), H194 (= H226), T287 (= T326), E288 (= E327)
- binding adenosine monophosphate: H194 (= H226), G262 (= G300), G263 (≠ S301), S283 (≠ G322), M286 (= M325), T287 (= T326), D365 (= D405), V377 (≠ I417), R380 (= R420), K467 (= K510)
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)
31% identity, 93% coverage: 36:518/520 of query aligns to 16:478/485 of 5x8fB