SitesBLAST
Comparing Echvi_2567 FitnessBrowser__Cola:Echvi_2567 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)
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)
55% identity, 98% coverage: 6:553/559 of query aligns to 5:552/561 of P69451
- Y213 (= Y214) mutation to A: Loss of activity.
- T214 (= T215) mutation to A: 10% of wild-type activity.
- G216 (= G217) mutation to A: Decreases activity.
- T217 (= T218) mutation to A: Decreases activity.
- G219 (= G220) mutation to A: Decreases activity.
- K222 (= K223) mutation to A: Decreases activity.
- E361 (= E362) mutation to A: Loss of activity.
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)
29% identity, 94% coverage: 36:559/559 of query aligns to 49:585/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
30% identity, 96% coverage: 14:551/559 of query aligns to 28:542/559 of Q67W82
- G395 (= G406) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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, 97% coverage: 9:548/559 of query aligns to 17:534/546 of Q84P21
- K530 (= K544) mutation to N: Lossed enzymatic activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
29% identity, 91% coverage: 45:554/559 of query aligns to 24:501/506 of 4gxqA
- active site: T163 (= T215), N183 (= N235), H207 (= H262), T303 (= T361), E304 (= E362), I403 (≠ L460), N408 (= N465), A491 (≠ K544)
- binding adenosine-5'-triphosphate: T163 (= T215), S164 (≠ G216), G165 (= G217), T166 (= T218), T167 (= T219), H207 (= H262), S277 (≠ G335), A278 (≠ M336), P279 (≠ A337), E298 (= E356), M302 (≠ L360), T303 (= T361), D382 (= D439), R397 (= R454)
- binding carbonate ion: H207 (= H262), S277 (≠ G335), R299 (≠ G357), G301 (= G359)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
31% identity, 91% coverage: 47:552/559 of query aligns to 43:527/528 of 3ni2A
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H262), T329 (= T361), E330 (= E362), K434 (≠ L460), Q439 (≠ N465), K519 (= K544)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F264), S236 (≠ V268), G302 (= G335), A303 (≠ M336), P304 (≠ A337), G325 (= G357), G327 (= G359), T329 (= T361), P333 (= P365), V334 (= V366), D413 (= D439), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
31% identity, 91% coverage: 47:552/559 of query aligns to 43:527/528 of 3a9vA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H262), T329 (= T361), E330 (= E362), K434 (≠ L460), Q439 (≠ N465), K519 (= K544)
- binding adenosine monophosphate: H230 (= H262), G302 (= G335), A303 (≠ M336), P304 (≠ A337), Y326 (= Y358), G327 (= G359), M328 (≠ L360), T329 (= T361), D413 (= D439), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
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)
28% identity, 92% coverage: 35:551/559 of query aligns to 44:547/556 of Q9S725
- K211 (= K223) mutation to S: Drastically reduces the activity.
- M293 (≠ T305) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V332) mutation K->L,A: Affects the substrate specificity.
- E401 (= E407) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C409) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R454) mutation to Q: Drastically reduces the activity.
- K457 (≠ S462) mutation to S: Drastically reduces the activity.
- K540 (= K544) mutation to N: Abolishes the activity.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 90% coverage: 51:551/559 of query aligns to 46:525/528 of 5bsrA
- active site: S181 (≠ T215), S201 (≠ N235), H229 (= H262), T328 (= T361), E329 (= E362), K433 (≠ L460), Q438 (≠ N465), K518 (= K544)
- binding adenosine monophosphate: A301 (≠ G335), G326 (= G359), T328 (= T361), D412 (= D439), K429 (= K456), K433 (≠ L460), Q438 (≠ N465)
- binding coenzyme a: L102 (= L108), P226 (= P259), H229 (= H262), Y231 (≠ F264), F253 (≠ R287), K435 (≠ S462), G436 (= G463), F437 (= F464), F498 (≠ N524)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 90% coverage: 51:551/559 of query aligns to 47:526/529 of 5bsvA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H262), T329 (= T361), E330 (= E362), K434 (≠ L460), Q439 (≠ N465), K519 (= K544)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H262), Y232 (≠ F264), S236 (≠ V268), A302 (≠ G335), A303 (≠ M336), P304 (≠ A337), G325 (= G357), G327 (= G359), M328 (≠ L360), T329 (= T361), P333 (= P365), V334 (= V366), D413 (= D439), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 90% coverage: 51:551/559 of query aligns to 47:526/529 of 5bsuA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H262), T329 (= T361), E330 (= E362), K434 (≠ L460), Q439 (≠ N465), K519 (= K544)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H262), Y232 (≠ F264), S236 (≠ V268), M299 (≠ V332), A302 (≠ G335), A303 (≠ M336), P304 (≠ A337), G325 (= G357), G327 (= G359), M328 (≠ L360), T329 (= T361), P333 (= P365), D413 (= D439), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
30% identity, 90% coverage: 51:551/559 of query aligns to 47:526/529 of 5bstA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H262), T329 (= T361), E330 (= E362), K434 (≠ L460), Q439 (≠ N465), K519 (= K544)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H262), Y232 (≠ F264), S236 (≠ V268), A302 (≠ G335), A303 (≠ M336), P304 (≠ A337), G325 (= G357), Y326 (= Y358), G327 (= G359), M328 (≠ L360), T329 (= T361), P333 (= P365), V334 (= V366), D413 (= D439), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
30% identity, 90% coverage: 51:551/559 of query aligns to 47:526/530 of 5bsmA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H262), T329 (= T361), E330 (= E362), K434 (≠ L460), Q439 (≠ N465), K519 (= K544)
- binding adenosine-5'-triphosphate: S182 (≠ T215), S183 (≠ G216), G184 (= G217), T185 (= T218), T186 (= T219), K190 (= K223), H230 (= H262), A302 (≠ G335), A303 (≠ M336), P304 (≠ A337), Y326 (= Y358), G327 (= G359), M328 (≠ L360), T329 (= T361), D413 (= D439), I425 (= I451), R428 (= R454), K519 (= K544)
O24146 4-coumarate--CoA ligase 2; 4CL 2; Nt4CL-19; Nt4CL-2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; Cinnamate--CoA ligase; Ferulate--CoA ligase; EC 6.2.1.12; EC 6.2.1.-; EC 6.2.1.-; EC 6.2.1.34 from Nicotiana tabacum (Common tobacco) (see paper)
30% identity, 90% coverage: 51:551/559 of query aligns to 54:533/542 of O24146
- S189 (≠ T215) binding
- S190 (≠ G216) binding
- G191 (= G217) binding
- T192 (= T218) binding
- T193 (= T219) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K223) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H262) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F264) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ V268) binding ; binding ; binding
- K260 (≠ P286) binding
- A309 (≠ G335) binding ; binding ; binding
- Q331 (≠ E356) binding
- G332 (= G357) binding ; binding ; binding ; binding ; binding
- T336 (= T361) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V366) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ C368) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D439) binding ; binding ; binding ; binding ; binding
- R435 (= R454) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K456) binding ; binding ; binding ; binding
- K441 (≠ L460) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S462) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G463) binding
- Q446 (≠ N465) binding
- K526 (= K544) binding ; mutation to A: Abolished activity against 4-coumarate.
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)
27% identity, 95% coverage: 25:557/559 of query aligns to 5:513/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 215:219) binding
- H214 (= H262) binding ; mutation to A: Abolished activity.
- S289 (≠ G335) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ GMA 335:337) binding
- EA 310:311 (≠ EG 356:357) binding
- M314 (≠ L360) binding
- T315 (= T361) binding
- H319 (≠ P365) binding ; mutation to A: Abolished activity.
- D394 (= D439) binding
- R409 (= R454) binding ; mutation to A: Abolished activity.
- K500 (= K544) binding ; binding ; mutation to A: Abolished activity.
5ie2A Crystal structure of a plant enzyme (see paper)
28% identity, 94% coverage: 25:552/559 of query aligns to 5:503/506 of 5ie2A
- active site: T165 (= T215), S185 (≠ N235), H209 (= H262), T310 (= T361), E311 (= E362), N410 (≠ L460), K415 (≠ N465), K495 (= K544)
- binding adenosine-5'-triphosphate: T165 (= T215), S166 (≠ G216), G167 (= G217), T168 (= T218), T169 (= T219), S284 (≠ G335), A285 (≠ M336), S286 (≠ A337), Y307 (= Y358), A308 (≠ G359), M309 (≠ L360), T310 (= T361), D389 (= D439), L401 (≠ I451), R404 (= R454), K495 (= K544)
5ie3A Crystal structure of a plant enzyme (see paper)
28% identity, 94% coverage: 25:552/559 of query aligns to 5:501/504 of 5ie3A
- active site: T163 (= T215), S183 (≠ N235), H207 (= H262), T308 (= T361), E309 (= E362), N408 (≠ L460), K413 (≠ N465), K493 (= K544)
- binding adenosine monophosphate: S164 (≠ G216), S282 (≠ G335), A283 (≠ M336), S284 (≠ A337), Y305 (= Y358), A306 (≠ G359), M307 (≠ L360), T308 (= T361), D387 (= D439), L399 (≠ I451), R402 (= R454), K493 (= K544)
- binding oxalic acid: V208 (≠ I263), S282 (≠ G335), A306 (≠ G359), M307 (≠ L360), H312 (≠ P365), K493 (= K544)
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)
28% identity, 91% coverage: 49:554/559 of query aligns to 29:497/503 of P9WQ37
- K172 (= K223) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ E249) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ E251) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I263) 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 (= A265) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V268) 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 (≠ K300) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G359) 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 (= W434) 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 (= D439) 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 (= R454) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V461) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G463) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K544) 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.
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
28% identity, 92% coverage: 40:552/559 of query aligns to 20:478/484 of 5gtdA
- active site: T151 (= T215), S171 (≠ Q237), H195 (= H262), T288 (= T361), E289 (= E362)
- binding adenosine-5'-monophosphate: G263 (= G334), G264 (= G335), Y285 (= Y358), G286 (= G359), M287 (≠ L360), T288 (= T361), D366 (= D439), V378 (≠ I451)
- binding magnesium ion: F314 (≠ P386), S315 (≠ N387)
- binding 2-succinylbenzoate: H195 (= H262), S197 (≠ F264), A237 (≠ G306), L260 (≠ S331), G262 (= G333), G263 (= G334), G286 (= G359), M287 (≠ L360), S292 (= S364), Q293 (≠ P365)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
29% identity, 90% coverage: 51:551/559 of query aligns to 46:522/527 of 5u95B
Query Sequence
>Echvi_2567 FitnessBrowser__Cola:Echvi_2567
MKDFPWFKFYPKSVPQEVDVEAYSSVVGLFEESVQKYGEAVAYECMGKKISFHEVDRLSK
DFASYLQNELKLKKGDRIAIQMPNLLQYPVAMFGALRAGLIVVNTNPLYTPHEMEHQFKD
ADISAVVIVANFASNLEEILPRLDVKHIILTEIGDMLGGLKGGIVNLVVKYIKKMVPAYN
LPNAVKFNDALDIGSHLDLQPVTLDLNDTAYLQYTGGTTGVSKGAALTHGNIIANMQQIS
AWMRPKLKEGEELVITALPMYHIFALTVNCLAMLKIGAHNLLITNPRDMKAFCKDLRKHK
FSVITGVNTLFNGLLNQESFRNLDFSYLKISVGGGMAVQKYVAEKWNAVTGTPLAEGYGL
TETSPVACCNPIDGTERIGTIGLPLPNTEVKIIDDEGNELPNGEKGELCIKGPQVMKGYW
NKPKETNDVMLGEWLKTGDIGIITNDGFIKIVDRKKEMILVSGFNVYPNEVEDAIATHDK
VMEVGVIGMPDEHSTEKVIAYVVANDPSVTASEIIKHCRESLTNYKVPREVYFVDELPKS
NVGKILRRIIKEDHIKKSA
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory