SitesBLAST
Comparing WP_047006433.1 NCBI__GCF_001010925.1:WP_047006433.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
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)
36% identity, 96% coverage: 14:558/570 of query aligns to 21:560/561 of P69451
- Y213 (= Y209) mutation to A: Loss of activity.
- T214 (= T210) mutation to A: 10% of wild-type activity.
- G216 (= G212) mutation to A: Decreases activity.
- T217 (= T213) mutation to A: Decreases activity.
- G219 (= G215) mutation to A: Decreases activity.
- K222 (= K218) mutation to A: Decreases activity.
- E361 (= E355) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
32% identity, 96% coverage: 12:556/570 of query aligns to 4:506/506 of 4gxqA
- active site: T163 (= T210), N183 (= N230), H207 (= H256), T303 (= T354), E304 (= E355), I403 (≠ L456), N408 (= N461), A491 (≠ K541)
- binding adenosine-5'-triphosphate: T163 (= T210), S164 (≠ G211), G165 (= G212), T166 (= T213), T167 (= T214), H207 (= H256), S277 (≠ G328), A278 (= A329), P279 (= P330), E298 (= E349), M302 (≠ L353), T303 (= T354), D382 (= D435), R397 (= R450)
- binding carbonate ion: H207 (= H256), S277 (≠ G328), R299 (≠ G350), G301 (= G352)
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)
30% identity, 90% coverage: 39:549/570 of query aligns to 61:548/556 of Q9S725
- K211 (= K218) mutation to S: Drastically reduces the activity.
- M293 (≠ F298) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ C325) mutation K->L,A: Affects the substrate specificity.
- E401 (= E403) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C405) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R450) mutation to Q: Drastically reduces the activity.
- K457 (≠ S458) mutation to S: Drastically reduces the activity.
- K540 (= K541) mutation to N: Abolishes the activity.
Q67W82 4-coumarate--CoA ligase 4; 4CL 4; Os4CL4; (E)-ferulate--CoA ligase; 4-coumaroyl-CoA synthase 4; Protein RESISTANCE TO ALUMINUM 1; EC 6.2.1.12; EC 6.2.1.34 from Oryza sativa subsp. japonica (Rice) (see paper)
32% identity, 90% coverage: 39:553/570 of query aligns to 57:547/559 of Q67W82
- G395 (= G402) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
5ie3A Crystal structure of a plant enzyme (see paper)
31% identity, 94% coverage: 18:551/570 of query aligns to 6:502/504 of 5ie3A
- active site: T163 (= T210), S183 (≠ N230), H207 (= H256), T308 (= T354), E309 (= E355), N408 (≠ L456), K413 (≠ N461), K493 (= K541)
- binding adenosine monophosphate: S164 (≠ G211), S282 (≠ C325), A283 (≠ S326), S284 (≠ G327), Y305 (= Y351), A306 (≠ G352), M307 (≠ L353), T308 (= T354), D387 (= D435), L399 (≠ I447), R402 (= R450), K493 (= K541)
- binding oxalic acid: V208 (= V257), S282 (≠ C325), A306 (≠ G352), M307 (≠ L353), H312 (≠ P358), K493 (= K541)
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)
32% identity, 97% coverage: 10:560/570 of query aligns to 27:582/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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: 18:551/570 of query aligns to 6:509/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 210:214) binding ATP
- H214 (= H256) binding ATP; mutation to A: Abolished activity.
- S289 (≠ C325) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ CSG 325:327) binding ATP
- EA 310:311 (≠ EG 349:350) binding ATP
- M314 (≠ L353) binding oxalate
- T315 (= T354) binding ATP
- H319 (≠ P358) binding oxalate; mutation to A: Abolished activity.
- D394 (= D435) binding ATP
- R409 (= R450) binding ATP; mutation to A: Abolished activity.
- K500 (= K541) binding ATP; binding oxalate; mutation to A: Abolished activity.
5ie2A Crystal structure of a plant enzyme (see paper)
31% identity, 94% coverage: 18:551/570 of query aligns to 6:504/506 of 5ie2A
- active site: T165 (= T210), S185 (≠ N230), H209 (= H256), T310 (= T354), E311 (= E355), N410 (≠ L456), K415 (≠ N461), K495 (= K541)
- binding adenosine-5'-triphosphate: T165 (= T210), S166 (≠ G211), G167 (= G212), T168 (= T213), T169 (= T214), S284 (≠ C325), A285 (≠ S326), S286 (≠ G327), Y307 (= Y351), A308 (≠ G352), M309 (≠ L353), T310 (= T354), D389 (= D435), L401 (≠ I447), R404 (= R450), K495 (= K541)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
30% identity, 92% coverage: 26:547/570 of query aligns to 28:525/528 of 3ni2A