SitesBLAST
Comparing Ac3H11_4478 FitnessBrowser__acidovorax_3H11:Ac3H11_4478 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)
33% identity, 96% coverage: 23:536/536 of query aligns to 38:553/561 of P69451
- Y213 (= Y195) mutation to A: Loss of activity.
- T214 (= T196) mutation to A: 10% of wild-type activity.
- G216 (= G198) mutation to A: Decreases activity.
- T217 (= T199) mutation to A: Decreases activity.
- G219 (= G201) mutation to A: Decreases activity.
- K222 (= K204) mutation to A: Decreases activity.
- E361 (= E343) mutation to A: Loss of activity.
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, 98% coverage: 7:533/536 of query aligns to 35:547/556 of Q9S725
- K211 (= K204) mutation to S: Drastically reduces the activity.
- M293 (≠ Y282) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ R307) mutation K->L,A: Affects the substrate specificity.
- E401 (= E388) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ T390) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R435) mutation to Q: Drastically reduces the activity.
- K457 (≠ S443) mutation to S: Drastically reduces the activity.
- K540 (= K526) 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, 98% coverage: 7:533/536 of query aligns to 16:525/528 of 5bsrA
- active site: S181 (≠ T196), S201 (≠ A218), H229 (= H240), T328 (≠ S342), E329 (= E343), K433 (= K441), Q438 (≠ S446), K518 (= K526)
- binding adenosine monophosphate: A301 (≠ G314), G326 (= G340), T328 (≠ S342), D412 (= D420), K429 (= K437), K433 (= K441), Q438 (≠ S446)
- binding coenzyme a: L102 (= L91), P226 (= P237), H229 (= H240), Y231 (≠ A242), F253 (= F264), K435 (≠ S443), G436 (= G444), F437 (≠ Y445), F498 (≠ P506)
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, 98% coverage: 7:533/536 of query aligns to 24:533/542 of O24146
- S189 (≠ T196) binding
- S190 (= S197) binding
- G191 (= G198) binding
- T192 (= T199) binding
- T193 (= T200) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K204) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H240) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ A242) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ M246) binding ; binding ; binding
- K260 (≠ R263) binding
- A309 (≠ G314) binding ; binding ; binding
- Q331 (≠ E336) binding
- G332 (≠ A337) binding ; binding ; binding ; binding ; binding
- T336 (≠ S342) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V347) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (= M351) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D420) binding ; binding ; binding ; binding ; binding
- R435 (= R435) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K437) binding ; binding ; binding ; binding
- K441 (= K441) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S443) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G444) binding
- Q446 (≠ S446) binding
- K526 (= K526) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 98% coverage: 7:533/536 of query aligns to 17:526/529 of 5bsvA
- active site: S182 (≠ T196), S202 (≠ A218), H230 (= H240), T329 (≠ S342), E330 (= E343), K434 (= K441), Q439 (≠ S446), K519 (= K526)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H240), Y232 (≠ A242), S236 (≠ M246), A302 (≠ G314), A303 (≠ I315), P304 (≠ T316), G325 (≠ A337), G327 (= G340), M328 (≠ L341), T329 (≠ S342), P333 (≠ T346), V334 (= V347), D413 (= D420), K430 (= K437), K434 (= K441), Q439 (≠ S446)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 98% coverage: 7:533/536 of query aligns to 17:526/529 of 5bsuA
- active site: S182 (≠ T196), S202 (≠ A218), H230 (= H240), T329 (≠ S342), E330 (= E343), K434 (= K441), Q439 (≠ S446), K519 (= K526)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H240), Y232 (≠ A242), S236 (≠ M246), M299 (≠ T311), A302 (≠ G314), A303 (≠ I315), P304 (≠ T316), G325 (≠ A337), G327 (= G340), M328 (≠ L341), T329 (≠ S342), P333 (≠ T346), D413 (= D420), K430 (= K437), K434 (= K441), Q439 (≠ S446)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
30% identity, 98% coverage: 7:533/536 of query aligns to 17:526/529 of 5bstA
- active site: S182 (≠ T196), S202 (≠ A218), H230 (= H240), T329 (≠ S342), E330 (= E343), K434 (= K441), Q439 (≠ S446), K519 (= K526)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H240), Y232 (≠ A242), S236 (≠ M246), A302 (≠ G314), A303 (≠ I315), P304 (≠ T316), G325 (≠ A337), Y326 (= Y339), G327 (= G340), M328 (≠ L341), T329 (≠ S342), P333 (≠ T346), V334 (= V347), D413 (= D420), K430 (= K437), K434 (= K441), Q439 (≠ S446)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
30% identity, 98% coverage: 7:533/536 of query aligns to 17:526/530 of 5bsmA
- active site: S182 (≠ T196), S202 (≠ K216), H230 (= H240), T329 (≠ S342), E330 (= E343), K434 (= K441), Q439 (≠ S446), K519 (= K526)
- binding adenosine-5'-triphosphate: S182 (≠ T196), S183 (= S197), G184 (= G198), T185 (= T199), T186 (= T200), K190 (= K204), H230 (= H240), A302 (≠ G314), A303 (≠ I315), P304 (≠ T316), Y326 (= Y339), G327 (= G340), M328 (≠ L341), T329 (≠ S342), D413 (= D420), I425 (≠ F432), R428 (= R435), K519 (= K526)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 94% coverage: 31:534/536 of query aligns to 26:499/506 of 4gxqA
- active site: T163 (= T196), N183 (≠ K216), H207 (= H240), T303 (≠ S342), E304 (= E343), I403 (≠ K441), N408 (≠ S446), A491 (≠ K526)
- binding adenosine-5'-triphosphate: T163 (= T196), S164 (= S197), G165 (= G198), T166 (= T199), T167 (= T200), H207 (= H240), S277 (≠ G314), A278 (≠ I315), P279 (≠ T316), E298 (≠ H335), M302 (≠ L341), T303 (≠ S342), D382 (= D420), R397 (= R435)
- binding carbonate ion: H207 (= H240), S277 (≠ G314), R299 (≠ E336), G301 (= G340)
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, 96% coverage: 24:536/536 of query aligns to 46:540/546 of Q84P21
- K530 (= K526) mutation to N: Lossed enzymatic activity.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
29% identity, 99% coverage: 7:534/536 of query aligns to 17:527/528 of 3ni2A
- active site: S182 (≠ T196), S202 (≠ K216), H230 (= H240), T329 (≠ S342), E330 (= E343), K434 (= K441), Q439 (≠ S446), K519 (= K526)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ A242), S236 (≠ M246), G302 (= G314), A303 (≠ I315), P304 (≠ T316), G325 (≠ A337), G327 (= G340), T329 (≠ S342), P333 (≠ T346), V334 (= V347), D413 (= D420), K430 (= K437), K434 (= K441), Q439 (≠ S446)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
29% identity, 99% coverage: 7:534/536 of query aligns to 17:527/528 of 3a9vA
- active site: S182 (≠ T196), S202 (≠ K216), H230 (= H240), T329 (≠ S342), E330 (= E343), K434 (= K441), Q439 (≠ S446), K519 (= K526)
- binding adenosine monophosphate: H230 (= H240), G302 (= G314), A303 (≠ I315), P304 (≠ T316), Y326 (= Y339), G327 (= G340), M328 (≠ L341), T329 (≠ S342), D413 (= D420), K430 (= K437), K434 (= K441), Q439 (≠ S446)
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, 98% coverage: 7:533/536 of query aligns to 27:542/559 of Q67W82
- G395 (= G387) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
30% identity, 98% coverage: 7:533/536 of query aligns to 16:522/527 of 5u95B
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, 96% coverage: 25:536/536 of query aligns to 56:573/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
30% identity, 97% coverage: 14:534/536 of query aligns to 8:495/503 of P9WQ37
- R9 (= R15) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D23) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K204) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T227) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ H229) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I241) 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 (≠ G243) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ M246) 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 (= R277) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G340) 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 (= W415) 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 (= D420) 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 (= R435) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V442) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G444) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K526) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
29% identity, 98% coverage: 12:534/536 of query aligns to 12:515/519 of 4rlfB
- active site: S176 (≠ T196), T196 (≠ K216), T324 (= T344), E325 (vs. gap), K422 (= K441), Y427 (≠ S446), K507 (= K526)
- binding 2-methylbenzoic acid: A222 (≠ I241), Y223 (≠ A242), G298 (= G314), I321 (≠ L341), G322 (≠ S342), S323 (≠ E343), H328 (= H345)
- binding 4-methylbenzoic acid: A216 (≠ V235), P246 (≠ F264), P248 (= P266), G269 (≠ S283), A270 (≠ I284), G273 (≠ M287)
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
29% identity, 98% coverage: 12:534/536 of query aligns to 12:515/516 of 4rm2A
- active site: S176 (≠ T196), T196 (≠ K216), T324 (= T344), E325 (vs. gap), K422 (= K441), Y427 (≠ S446), K507 (= K526)
- binding 2-fluorobenzoic acid: A216 (≠ V235), A222 (≠ I241), Y223 (≠ A242), P246 (≠ F264), T247 (≠ D265), V251 (= V269), F267 (≠ W281), G269 (≠ S283), A270 (≠ I284), G273 (≠ M287), M277 (≠ L291), A297 (≠ F313), G298 (= G314), I321 (≠ L341), G322 (≠ S342), S323 (≠ E343), H328 (= H345), K422 (= K441)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
29% identity, 98% coverage: 12:534/536 of query aligns to 12:515/518 of 4rmnA
- active site: S176 (≠ T196), T196 (≠ K216), T324 (= T344), E325 (vs. gap), K422 (= K441), Y427 (≠ S446), K507 (= K526)
- binding thiophene-2-carboxylic acid: A217 (= A236), F221 (≠ H240), Y223 (≠ A242), G269 (≠ S283), A270 (≠ I284), A297 (≠ F313), G298 (= G314), G322 (≠ S342), S323 (≠ E343), H328 (= H345), I329 (≠ T346), K422 (= K441), G425 (= G444)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
27% identity, 98% coverage: 10:535/536 of query aligns to 24:536/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H240), F245 (≠ M244), T249 (≠ V248), G314 (= G314), A315 (≠ I315), P316 (≠ T316), G337 (≠ A338), Y338 (= Y339), G339 (= G340), L340 (= L341), T341 (≠ S342), A346 (≠ V347), D420 (= D420), I432 (≠ F432), K527 (= K526)
Query Sequence
>Ac3H11_4478 FitnessBrowser__acidovorax_3H11:Ac3H11_4478
MPSAAPQLPLHEHLRRHARETPDRIAYLWYGQPLTWAQLDAASDAFAARLQALGVAKGEP
VALFMNNCPQYVMAHYGIQKIGAIVCPCGPLNKEHELEYQLTDLQTRVIVAADVLLPVVD
KVRAKTALQHVFVVRYAELLPDGTPSIDVPAELLNMRTAMGSVPAGCEDFLAATRTGARP
APVALSMDDISLMTYTSGTTGLPKGAMLSYGNATFKTAASADCNGMTPHETLLAVAPLYH
IAGMVMGVNLPVYTGATAVLLYRFDPLGVAQALERHRVTWWYSIAPMNGALMQVPGARDM
DWSALRRNPVTSFGITFTEALAQQWQQFAPNCIAHEAAYGLSETHTVDTAMPVDAIRWGT
QGQPVPGNTIRIVDPDTGAPLPTGEVGEITIHGPGNFKGYWNKPEATAKTLRDGWVYTGD
MGKIDADGYLTFIGRFKEMIKVSGYSVFPEEVETLLIKHPAVAQAAVIGVPDAEKGEVAR
AFIVKKPGQDLDAAALVAWCRENMAPYKAPREVRFIDALPATGAGKVLRRLLRDIA
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