SitesBLAST
Comparing WP_013076344.1 NCBI__GCF_000092905.1:WP_013076344.1 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)
41% identity, 98% coverage: 11:518/521 of query aligns to 24:551/561 of P69451
- Y213 (= Y178) mutation to A: Loss of activity.
- T214 (= T179) mutation to A: 10% of wild-type activity.
- G216 (= G181) mutation to A: Decreases activity.
- T217 (= T182) mutation to A: Decreases activity.
- G219 (= G184) mutation to A: Decreases activity.
- K222 (= K187) mutation to A: Decreases activity.
- E361 (= E325) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
36% identity, 93% coverage: 36:521/521 of query aligns to 29:502/506 of 4gxqA
- active site: T163 (= T179), N183 (= N199), H207 (= H226), T303 (= T324), E304 (= E325), I403 (= I425), N408 (= N430), A491 (≠ K510)
- binding adenosine-5'-triphosphate: T163 (= T179), S164 (≠ G180), G165 (= G181), T166 (= T182), T167 (= T183), H207 (= H226), S277 (= S298), A278 (= A299), P279 (= P300), E298 (= E319), M302 (≠ L323), T303 (= T324), D382 (= D404), R397 (= R419)
- binding carbonate ion: H207 (= H226), S277 (= S298), R299 (≠ G320), G301 (= G322)
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)
35% identity, 92% coverage: 37:517/521 of query aligns to 65:547/556 of Q9S725
- K211 (= K187) mutation to S: Drastically reduces the activity.
- M293 (≠ P268) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ N295) mutation K->L,A: Affects the substrate specificity.
- E401 (= E372) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ V374) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R419) mutation to Q: Drastically reduces the activity.
- K457 (≠ S427) mutation to S: Drastically reduces the activity.
- K540 (= K510) 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)
36% identity, 92% coverage: 36:516/521 of query aligns to 58:536/546 of Q84P21
- K530 (= K510) mutation to N: Lossed enzymatic activity.
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)
36% identity, 98% coverage: 7:517/521 of query aligns to 16:533/542 of O24146
- S189 (≠ T179) binding ATP
- S190 (≠ G180) binding ATP
- G191 (= G181) binding ATP
- T192 (= T182) binding ATP
- T193 (= T183) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K187) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H226) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (= Y228) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ V232) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ R249) binding CoA
- A309 (≠ S298) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E319) binding ATP
- G332 (= G320) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T324) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V329) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (vs. gap) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D404) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R419) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding ATP; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K421) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ I425) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S427) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G428) binding CoA
- Q446 (≠ N430) binding AMP
- K526 (= K510) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
36% identity, 98% coverage: 7:517/521 of query aligns to 9:526/530 of 5bsmA
- active site: S182 (≠ T179), S202 (≠ N199), H230 (= H226), T329 (= T324), E330 (= E325), K434 (≠ I425), Q439 (≠ N430), K519 (= K510)
- binding adenosine-5'-triphosphate: S182 (≠ T179), S183 (≠ G180), G184 (= G181), T185 (= T182), T186 (= T183), K190 (= K187), H230 (= H226), A302 (≠ S298), A303 (= A299), P304 (= P300), Y326 (= Y321), G327 (= G322), M328 (≠ L323), T329 (= T324), D413 (= D404), I425 (= I416), R428 (= R419), K519 (= K510)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
36% identity, 98% coverage: 7:517/521 of query aligns to 9:526/529 of 5bsvA
- active site: S182 (≠ T179), S202 (≠ N199), H230 (= H226), T329 (= T324), E330 (= E325), K434 (≠ I425), Q439 (≠ N430), K519 (= K510)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H226), Y232 (= Y228), S236 (≠ V232), A302 (≠ S298), A303 (= A299), P304 (= P300), G325 (= G320), G327 (= G322), M328 (≠ L323), T329 (= T324), P333 (= P328), V334 (= V329), D413 (= D404), K430 (= K421), K434 (≠ I425), Q439 (≠ N430)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
36% identity, 98% coverage: 7:517/521 of query aligns to 9:526/529 of 5bsuA
- active site: S182 (≠ T179), S202 (≠ N199), H230 (= H226), T329 (= T324), E330 (= E325), K434 (≠ I425), Q439 (≠ N430), K519 (= K510)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H226), Y232 (= Y228), S236 (≠ V232), M299 (≠ N295), A302 (≠ S298), A303 (= A299), P304 (= P300), G325 (= G320), G327 (= G322), M328 (≠ L323), T329 (= T324), P333 (= P328), D413 (= D404), K430 (= K421), K434 (≠ I425), Q439 (≠ N430)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
36% identity, 98% coverage: 7:517/521 of query aligns to 9:526/529 of 5bstA
- active site: S182 (≠ T179), S202 (≠ N199), H230 (= H226), T329 (= T324), E330 (= E325), K434 (≠ I425), Q439 (≠ N430), K519 (= K510)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H226), Y232 (= Y228), S236 (≠ V232), A302 (≠ S298), A303 (= A299), P304 (= P300), G325 (= G320), Y326 (= Y321), G327 (= G322), M328 (≠ L323), T329 (= T324), P333 (= P328), V334 (= V329), D413 (= D404), K430 (= K421), K434 (≠ I425), Q439 (≠ N430)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
36% identity, 98% coverage: 7:517/521 of query aligns to 8:525/528 of 5bsrA
- active site: S181 (≠ T179), S201 (≠ N199), H229 (= H226), T328 (= T324), E329 (= E325), K433 (≠ I425), Q438 (≠ N430), K518 (= K510)
- binding adenosine monophosphate: A301 (≠ S298), G326 (= G322), T328 (= T324), D412 (= D404), K429 (= K421), K433 (≠ I425), Q438 (≠ N430)
- binding coenzyme a: L102 (≠ M93), P226 (= P223), H229 (= H226), Y231 (= Y228), F253 (= F250), K435 (≠ S427), G436 (= G428), F437 (= F429), F498 (≠ H490)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
35% identity, 93% coverage: 37:518/521 of query aligns to 47:527/528 of 3ni2A
- active site: S182 (≠ T179), S202 (≠ N199), H230 (= H226), T329 (= T324), E330 (= E325), K434 (≠ I425), Q439 (≠ N430), K519 (= K510)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (= Y228), S236 (≠ V232), G302 (≠ S298), A303 (= A299), P304 (= P300), G325 (= G320), G327 (= G322), T329 (= T324), P333 (= P328), V334 (= V329), D413 (= D404), K430 (= K421), K434 (≠ I425), Q439 (≠ N430)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
35% identity, 93% coverage: 37:518/521 of query aligns to 47:527/528 of 3a9vA
- active site: S182 (≠ T179), S202 (≠ N199), H230 (= H226), T329 (= T324), E330 (= E325), K434 (≠ I425), Q439 (≠ N430), K519 (= K510)
- binding adenosine monophosphate: H230 (= H226), G302 (≠ S298), A303 (= A299), P304 (= P300), Y326 (= Y321), G327 (= G322), M328 (≠ L323), T329 (= T324), D413 (= D404), K430 (= K421), K434 (≠ I425), Q439 (≠ N430)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
36% identity, 98% coverage: 7:517/521 of query aligns to 8:522/527 of 5u95B
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)
35% identity, 98% coverage: 7:517/521 of query aligns to 23:542/559 of Q67W82
- G395 (= G371) 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)
33% identity, 97% coverage: 11:514/521 of query aligns to 5:497/504 of 5ie3A
- active site: T163 (= T179), S183 (≠ N199), H207 (= H226), T308 (= T324), E309 (= E325), N408 (≠ I425), K413 (≠ N430), K493 (= K510)
- binding adenosine monophosphate: S164 (≠ G180), S282 (≠ N295), A283 (≠ S296), S284 (≠ G297), Y305 (= Y321), A306 (≠ G322), M307 (≠ L323), T308 (= T324), D387 (= D404), L399 (≠ I416), R402 (= R419), K493 (= K510)
- binding oxalic acid: V208 (= V227), S282 (≠ N295), A306 (≠ G322), M307 (≠ L323), H312 (≠ P328), K493 (= K510)
5ie2A Crystal structure of a plant enzyme (see paper)
33% identity, 97% coverage: 11:514/521 of query aligns to 5:499/506 of 5ie2A
- active site: T165 (= T179), S185 (≠ N199), H209 (= H226), T310 (= T324), E311 (= E325), N410 (≠ I425), K415 (≠ N430), K495 (= K510)
- binding adenosine-5'-triphosphate: T165 (= T179), S166 (≠ G180), G167 (= G181), T168 (= T182), T169 (= T183), S284 (≠ N295), A285 (≠ S296), S286 (≠ G297), Y307 (= Y321), A308 (≠ G322), M309 (≠ L323), T310 (= T324), D389 (= D404), L401 (≠ I416), R404 (= R419), K495 (= K510)
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)
33% identity, 97% coverage: 11:514/521 of query aligns to 5:504/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 179:183) binding ATP
- H214 (= H226) binding ATP; mutation to A: Abolished activity.
- S289 (≠ N295) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ NSG 295:297) binding ATP
- EA 310:311 (≠ EG 319:320) binding ATP
- M314 (≠ L323) binding oxalate
- T315 (= T324) binding ATP
- H319 (≠ P328) binding oxalate; mutation to A: Abolished activity.
- D394 (= D404) binding ATP
- R409 (= R419) binding ATP; mutation to A: Abolished activity.
- K500 (= K510) binding ATP; binding oxalate; mutation to A: Abolished 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, 93% coverage: 34:518/521 of query aligns to 28:495/503 of P9WQ37
- K172 (= K187) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R208) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R212) 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 (≠ V232) 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 (≠ K263) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G322) 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 (= W399) 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 (= D404) 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 (= R419) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ A426) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G428) 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.
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
31% identity, 96% coverage: 11:510/521 of query aligns to 5:499/504 of 6qjzA
- active site: T169 (= T179), S189 (≠ N199), H213 (= H226), T314 (= T324), E315 (= E325), N414 (≠ I425), K419 (≠ N430)
- binding adenosine monophosphate: H213 (= H226), S288 (= S298), A289 (= A299), S290 (≠ P300), A312 (≠ G322), M313 (≠ L323), T314 (= T324), D393 (= D404), L405 (≠ I416), K410 (= K421), K419 (≠ N430)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
32% identity, 98% coverage: 14:521/521 of query aligns to 22:538/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H226), F245 (≠ Y228), T249 (≠ V232), G314 (≠ S298), A315 (= A299), P316 (= P300), G337 (= G320), Y338 (= Y321), G339 (= G322), L340 (= L323), T341 (= T324), A346 (≠ V329), D420 (= D404), I432 (= I416), K527 (= K510)
Query Sequence
>WP_013076344.1 NCBI__GCF_000092905.1:WP_013076344.1
MGGTFSFPQISLPEMLRDTAKRFSGRPAVSFYHVTLTYEQVWWMVQRAAVGLAAAGVRKG
DRVAIMLPNCPHYVIAYYAVLVAGGIVVQVNPMYTGAELEHLLVDADPKVIVAYEPLWGK
IEAVWENTHLERAYLVQFPGPVQTPATERVQPVEALLGAQGDPPSVAISPEDTAVLQYTG
GTTGYSKGAMLTHRNLVANVYQSLADFRDGLRDGEEVILLVLPLFHVYGMTVGMNLGIAV
GANLVMLPRFQVDEVLDAIKAAKPTMFPGVPTMYVAVNSHPKAREYGIDSIRICNSGSAP
LPVEVLRAFEAKTGAKILEGYGLTEASPVTHTNPYHGVRKVGSIGLPVAGTEARIVDVAT
GLQELPPGEPGELVVRGPQVMKGYWNRPEETAQVLRNGWLHTGDIATRDEDGYYYIVDRK
KDIIIASGFNVYPREVEEVLYTHPGIQEAAVVGVPDPYRGETVKAYVVCKPGVTLTRDEV
IAFCRERMAHYKAPTEVEFREELPKSSVGKILRRALRDSQQ
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