SitesBLAST
Comparing Dsui_3212 FitnessBrowser__PS:Dsui_3212 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)
60% identity, 100% coverage: 1:555/555 of query aligns to 1:553/561 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.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
36% identity, 63% coverage: 202:553/555 of query aligns to 150:499/506 of 4gxqA
- active site: T163 (= T215), N183 (= N235), H207 (= H262), T303 (= T361), E304 (= E362), I403 (≠ L461), N408 (= N466), A491 (≠ K545)
- 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 (= D440), R397 (= R455)
- binding carbonate ion: H207 (= H262), S277 (≠ G335), R299 (≠ A357), G301 (= G359)
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, 94% coverage: 31:552/555 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 (≠ L332) 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 (= R455) mutation to Q: Drastically reduces the activity.
- K457 (≠ S463) mutation to S: Drastically reduces the activity.
- K540 (= K545) mutation to N: Abolishes the 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, 94% coverage: 32:555/555 of query aligns to 39:540/546 of Q84P21
- K530 (= K545) mutation to N: Lossed enzymatic 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)
28% identity, 96% coverage: 22:553/555 of query aligns to 1:495/503 of P9WQ37
- R9 (≠ E30) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D38) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K223) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ K249) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ Q251) 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 (≠ S265) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ A268) 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 (≠ F435) 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 (= D440) 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 (= R455) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V462) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G464) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K545) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
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, 98% coverage: 14:555/555 of query aligns to 32:573/590 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)
29% identity, 91% coverage: 46:552/555 of query aligns to 57:542/559 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.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
30% identity, 91% coverage: 50:552/555 of query aligns to 47:526/530 of 5bsmA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H262), T329 (= T361), E330 (= E362), K434 (≠ L461), Q439 (≠ N466), K519 (= K545)
- 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 (= D440), I425 (= I452), R428 (= R455), K519 (= K545)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 91% coverage: 50:552/555 of query aligns to 47:526/529 of 5bsvA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H262), T329 (= T361), E330 (= E362), K434 (≠ L461), Q439 (≠ N466), K519 (= K545)
- 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 (≠ A268), A302 (≠ G335), A303 (≠ M336), P304 (≠ A337), G325 (≠ A357), G327 (= G359), M328 (≠ L360), T329 (= T361), P333 (= P365), V334 (≠ A366), D413 (= D440), K430 (= K457), K434 (≠ L461), Q439 (≠ N466)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 91% coverage: 50:552/555 of query aligns to 47:526/529 of 5bsuA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H262), T329 (= T361), E330 (= E362), K434 (≠ L461), Q439 (≠ N466), K519 (= K545)
- 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 (≠ A268), M299 (≠ L332), A302 (≠ G335), A303 (≠ M336), P304 (≠ A337), G325 (≠ A357), G327 (= G359), M328 (≠ L360), T329 (= T361), P333 (= P365), D413 (= D440), K430 (= K457), K434 (≠ L461), Q439 (≠ N466)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
30% identity, 91% coverage: 50:552/555 of query aligns to 47:526/529 of 5bstA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H262), T329 (= T361), E330 (= E362), K434 (≠ L461), Q439 (≠ N466), K519 (= K545)
- 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 (≠ A268), A302 (≠ G335), A303 (≠ M336), P304 (≠ A337), G325 (≠ A357), Y326 (= Y358), G327 (= G359), M328 (≠ L360), T329 (= T361), P333 (= P365), V334 (≠ A366), D413 (= D440), K430 (= K457), K434 (≠ L461), Q439 (≠ N466)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 91% coverage: 50:552/555 of query aligns to 46:525/528 of 5bsrA
- active site: S181 (≠ T215), S201 (≠ N235), H229 (= H262), T328 (= T361), E329 (= E362), K433 (≠ L461), Q438 (≠ N466), K518 (= K545)
- binding adenosine monophosphate: A301 (≠ G335), G326 (= G359), T328 (= T361), D412 (= D440), K429 (= K457), K433 (≠ L461), Q438 (≠ N466)
- binding coenzyme a: L102 (= L107), P226 (= P259), H229 (= H262), Y231 (≠ F264), F253 (≠ R287), K435 (≠ S463), G436 (= G464), F437 (= F465), F498 (≠ G525)
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, 91% coverage: 50:552/555 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 (≠ A268) binding ; binding ; binding
- K260 (≠ P286) binding
- A309 (≠ G335) binding ; binding ; binding
- Q331 (≠ E356) binding
- G332 (≠ A357) binding ; binding ; binding ; binding ; binding
- T336 (= T361) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ A366) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ I369) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D440) binding ; binding ; binding ; binding ; binding
- R435 (= R455) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K457) binding ; binding ; binding ; binding
- K441 (≠ L461) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S463) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G464) binding
- Q446 (≠ N466) binding
- K526 (= K545) binding ; mutation to A: Abolished activity against 4-coumarate.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
29% identity, 94% coverage: 31:553/555 of query aligns to 26:527/528 of 3ni2A
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H262), T329 (= T361), E330 (= E362), K434 (≠ L461), Q439 (≠ N466), K519 (= K545)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F264), S236 (≠ A268), G302 (= G335), A303 (≠ M336), P304 (≠ A337), G325 (≠ A357), G327 (= G359), T329 (= T361), P333 (= P365), V334 (vs. gap), D413 (= D440), K430 (= K457), K434 (≠ L461), Q439 (≠ N466)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
29% identity, 94% coverage: 31:553/555 of query aligns to 26:527/528 of 3a9vA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H262), T329 (= T361), E330 (= E362), K434 (≠ L461), Q439 (≠ N466), K519 (= K545)
- binding adenosine monophosphate: H230 (= H262), G302 (= G335), A303 (≠ M336), P304 (≠ A337), Y326 (= Y358), G327 (= G359), M328 (≠ L360), T329 (= T361), D413 (= D440), K430 (= K457), K434 (≠ L461), Q439 (≠ N466)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
27% identity, 96% coverage: 20:553/555 of query aligns to 2:495/502 of 3r44A
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
30% identity, 91% coverage: 50:552/555 of query aligns to 46:522/527 of 5u95B
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
29% identity, 91% coverage: 49:553/555 of query aligns to 49:535/539 of 6k4dA
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (4S)-2-(6-oxidanyl-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylate: H243 (= H262), F245 (= F264), T249 (≠ A268), G314 (= G335), A315 (≠ M336), P316 (≠ A337), G337 (≠ A357), Y338 (= Y358), G339 (= G359), L340 (= L360), T341 (= T361), S345 (≠ P365), A346 (= A366), D420 (= D440), I432 (= I452), K527 (= K545)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F264), R335 (vs. gap), G337 (≠ A357), G339 (= G359), L340 (= L360), A346 (= A366)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
29% identity, 91% coverage: 49:553/555 of query aligns to 49:535/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H262), F245 (= F264), T249 (≠ A268), G314 (= G335), A315 (≠ M336), P316 (≠ A337), G337 (≠ A357), Y338 (= Y358), G339 (= G359), L340 (= L360), T341 (= T361), A346 (= A366), D420 (= D440), I432 (= I452), K527 (= K545)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
28% identity, 87% coverage: 74:555/555 of query aligns to 60:512/518 of 4wv3B
- active site: S175 (≠ T215), T320 (= T361), E321 (= E362), K418 (≠ L461), W423 (≠ N466), K502 (= K545)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H262), T221 (≠ I263), F222 (= F264), A293 (≠ G334), S294 (≠ G335), E295 (≠ M336), A296 (= A337), G316 (≠ A357), I317 (≠ Y358), G318 (= G359), C319 (≠ L360), T320 (= T361), D397 (= D440), H409 (≠ I452), R412 (= R455), K502 (= K545)
Query Sequence
>Dsui_3212 FitnessBrowser__PS:Dsui_3212
MEKIWLRSYPQGVPEFVDVNEFKSLGQLFEQSCAQYRDRVAYINMGVGITYGELDRLSRD
FAAYLQDVLKLPQGARVALMMPNLLQYPVCMFGALRAGYVVVNCNPLYTHRELEHQLKDS
GAEAIVIVENFAHTLEQALPLVPGLKHVIVTSLGDMLGALKGTVVNLVVRHVKKMVPAWK
LPRHVKFKAAMARGKGATLRPVQVGHEDIAYLQYTGGTTGVAKGAMLLHRNIIANLQQAH
AWIEPFLHKDQQLIITALPLYHIFSLTANCLTFLKIGATNVLITNPRDIPGFVKELAQYK
FTVITGVNTLFNALLNNPDFAKLDFSALRAALGGGMAVQKSVAQKWRQVTGKPLIEAYGL
TETSPAATINPLDLGEFNGAIGLPISSTEIVIRDDLGNDLPVGQAGEICIRGPQVMKGYW
LRPDETATVFYADGFLRTGDVGVMDEKGFVRIVDRKKDMILVSGFNVYPNEVEAVVAMHP
AVMEVAAVGVPSEHSGEAVKIFVVLKDKSVTKEQLIAHCKENLTGYKVPHLVEFRDDLPK
TNVGKILRRALKEAA
Or try a new SitesBLAST search
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