SitesBLAST
Comparing WP_012592395.1 NCBI__GCF_000021745.1:WP_012592395.1 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)
34% identity, 100% coverage: 2:507/507 of query aligns to 21:561/561 of P69451
- Y213 (= Y160) mutation to A: Loss of activity.
- T214 (= T161) mutation to A: 10% of wild-type activity.
- G216 (= G163) mutation to A: Decreases activity.
- T217 (= T164) mutation to A: Decreases activity.
- G219 (= G166) mutation to A: Decreases activity.
- K222 (= K169) mutation to A: Decreases activity.
- E361 (= E303) mutation to A: Loss of 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)
35% identity, 93% coverage: 31:504/507 of query aligns to 30:502/503 of P9WQ37
- K172 (= K169) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R191) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ A193) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V206) 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 (≠ G208) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V211) 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 (= R241) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G300) 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 (= W378) 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 (= D383) 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 (= R398) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ T405) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G407) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K489) 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.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
35% identity, 93% coverage: 30:502/507 of query aligns to 28:504/506 of 4gxqA
- active site: T163 (= T161), N183 (≠ M182), H207 (= H205), T303 (= T302), E304 (= E303), I403 (= I404), N408 (= N409), A491 (≠ K489)
- binding adenosine-5'-triphosphate: T163 (= T161), S164 (= S162), G165 (= G163), T166 (= T164), T167 (= T165), H207 (= H205), S277 (≠ Q277), A278 (≠ T278), P279 (≠ M279), E298 (= E297), M302 (= M301), T303 (= T302), D382 (= D383), R397 (= R398)
- binding carbonate ion: H207 (= H205), S277 (≠ Q277), R299 (≠ L298), G301 (= G300)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
34% identity, 92% coverage: 31:498/507 of query aligns to 46:528/528 of 3ni2A
- active site: S182 (≠ T161), S202 (= S181), H230 (= H205), T329 (= T302), E330 (= E303), K434 (≠ I404), Q439 (≠ N409), K519 (= K489)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (= Y207), S236 (≠ A214), G302 (= G276), A303 (≠ Q277), P304 (≠ T278), G325 (≠ L298), G327 (= G300), T329 (= T302), P333 (= P307), V334 (vs. gap), D413 (= D383), K430 (= K400), K434 (≠ I404), Q439 (≠ N409)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
34% identity, 92% coverage: 31:498/507 of query aligns to 46:528/528 of 3a9vA
- active site: S182 (≠ T161), S202 (= S181), H230 (= H205), T329 (= T302), E330 (= E303), K434 (≠ I404), Q439 (≠ N409), K519 (= K489)
- binding adenosine monophosphate: H230 (= H205), G302 (= G276), A303 (≠ Q277), P304 (≠ T278), Y326 (≠ W299), G327 (= G300), M328 (= M301), T329 (= T302), D413 (= D383), K430 (= K400), K434 (≠ I404), Q439 (≠ N409)
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)
32% identity, 97% coverage: 5:496/507 of query aligns to 42:547/556 of Q9S725
- K211 (= K169) mutation to S: Drastically reduces the activity.
- M293 (≠ E246) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ T273) mutation K->L,A: Affects the substrate specificity.
- E401 (= E350) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ L352) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R398) mutation to Q: Drastically reduces the activity.
- K457 (≠ A406) mutation to S: Drastically reduces the activity.
- K540 (= K489) 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)
34% identity, 94% coverage: 31:506/507 of query aligns to 60:552/559 of Q67W82
- G395 (= G349) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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)
34% identity, 92% coverage: 31:496/507 of query aligns to 53:533/542 of O24146
- S189 (≠ T161) binding ATP
- S190 (= S162) binding ATP
- G191 (= G163) binding ATP
- T192 (= T164) binding ATP
- T193 (= T165) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K169) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H205) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (= Y207) 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 (≠ A214) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ R227) binding CoA
- A309 (≠ Q277) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (vs. gap) binding ATP
- G332 (vs. gap) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T302) 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 (vs. gap) 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 (= D383) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R398) 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 (= K400) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ I404) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ A406) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G407) binding CoA
- Q446 (≠ N409) binding AMP
- K526 (= K489) 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)
34% identity, 92% coverage: 31:496/507 of query aligns to 46:526/530 of 5bsmA
- active site: S182 (≠ T161), S202 (= S181), H230 (= H205), T329 (= T302), E330 (= E303), K434 (≠ I404), Q439 (≠ N409), K519 (= K489)
- binding adenosine-5'-triphosphate: S182 (≠ T161), S183 (= S162), G184 (= G163), T185 (= T164), T186 (= T165), K190 (= K169), H230 (= H205), A302 (≠ Q277), A303 (≠ T278), P304 (= P280), Y326 (≠ W299), G327 (= G300), M328 (= M301), T329 (= T302), D413 (= D383), I425 (= I395), R428 (= R398), K519 (= K489)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
34% identity, 92% coverage: 31:496/507 of query aligns to 45:525/528 of 5bsrA
- active site: S181 (≠ T161), S201 (= S181), H229 (= H205), T328 (= T302), E329 (= E303), K433 (≠ I404), Q438 (≠ N409), K518 (= K489)
- binding adenosine monophosphate: A301 (≠ Q277), G326 (= G300), T328 (= T302), D412 (= D383), K429 (= K400), K433 (≠ I404), Q438 (≠ N409)
- binding coenzyme a: L102 (= L88), P226 (= P202), H229 (= H205), Y231 (= Y207), F253 (= F228), K435 (≠ A406), G436 (= G407), F437 (≠ Y408), F498 (≠ A469)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
34% identity, 92% coverage: 31:496/507 of query aligns to 46:526/529 of 5bsvA
- active site: S182 (≠ T161), S202 (= S181), H230 (= H205), T329 (= T302), E330 (= E303), K434 (≠ I404), Q439 (≠ N409), K519 (= K489)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H205), Y232 (= Y207), S236 (≠ A214), A302 (≠ Q277), A303 (≠ T278), P304 (= P280), G325 (vs. gap), G327 (= G300), M328 (= M301), T329 (= T302), P333 (= P307), V334 (vs. gap), D413 (= D383), K430 (= K400), K434 (≠ I404), Q439 (≠ N409)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
34% identity, 92% coverage: 31:496/507 of query aligns to 46:526/529 of 5bsuA
- active site: S182 (≠ T161), S202 (= S181), H230 (= H205), T329 (= T302), E330 (= E303), K434 (≠ I404), Q439 (≠ N409), K519 (= K489)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H205), Y232 (= Y207), S236 (≠ A214), M299 (≠ V274), A302 (≠ Q277), A303 (≠ T278), P304 (= P280), G325 (vs. gap), G327 (= G300), M328 (= M301), T329 (= T302), P333 (= P307), D413 (= D383), K430 (= K400), K434 (≠ I404), Q439 (≠ N409)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
34% identity, 92% coverage: 31:496/507 of query aligns to 46:526/529 of 5bstA
- active site: S182 (≠ T161), S202 (= S181), H230 (= H205), T329 (= T302), E330 (= E303), K434 (≠ I404), Q439 (≠ N409), K519 (= K489)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H205), Y232 (= Y207), S236 (≠ A214), A302 (≠ Q277), A303 (≠ T278), P304 (= P280), G325 (vs. gap), Y326 (≠ W299), G327 (= G300), M328 (= M301), T329 (= T302), P333 (= P307), V334 (vs. gap), D413 (= D383), K430 (= K400), K434 (≠ I404), Q439 (≠ N409)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
35% identity, 93% coverage: 31:504/507 of query aligns to 33:502/502 of 3r44A
Sites not aligning to the query:
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
34% identity, 92% coverage: 31:496/507 of query aligns to 45:522/527 of 5u95B
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
32% identity, 93% coverage: 29:497/507 of query aligns to 47:535/539 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 (= H205), F245 (≠ Y207), T249 (≠ V211), G314 (= G276), A315 (≠ Q277), P316 (≠ T278), G337 (≠ L298), Y338 (≠ W299), G339 (= G300), L340 (≠ M301), T341 (= T302), S345 (≠ G306), A346 (= A308), D420 (= D383), I432 (= I395), K527 (= K489)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ Y207), R335 (≠ L296), G337 (≠ L298), G339 (= G300), L340 (≠ M301), A346 (= A308)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
32% identity, 93% coverage: 29:497/507 of query aligns to 47:535/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H205), F245 (≠ Y207), T249 (≠ V211), G314 (= G276), A315 (≠ Q277), P316 (≠ T278), G337 (≠ L298), Y338 (≠ W299), G339 (= G300), L340 (≠ M301), T341 (= T302), A346 (= A308), D420 (= D383), I432 (= I395), K527 (= K489)
5ie2A Crystal structure of a plant enzyme (see paper)
32% identity, 97% coverage: 1:493/507 of query aligns to 1:499/506 of 5ie2A
- active site: T165 (= T161), S185 (= S181), H209 (= H205), T310 (= T302), E311 (= E303), N410 (≠ I404), K415 (≠ N409), K495 (= K489)
- binding adenosine-5'-triphosphate: T165 (= T161), S166 (= S162), G167 (= G163), T168 (= T164), T169 (= T165), S284 (≠ T273), A285 (≠ V274), S286 (≠ G275), Y307 (≠ W299), A308 (≠ G300), M309 (= M301), T310 (= T302), D389 (= D383), L401 (≠ I395), R404 (= R398), K495 (= K489)
5ie3A Crystal structure of a plant enzyme (see paper)
31% identity, 97% coverage: 1:493/507 of query aligns to 1:497/504 of 5ie3A
- active site: T163 (= T161), S183 (= S181), H207 (= H205), T308 (= T302), E309 (= E303), N408 (≠ I404), K413 (≠ N409), K493 (= K489)
- binding adenosine monophosphate: S164 (= S162), S282 (≠ T273), A283 (≠ V274), S284 (≠ G275), Y305 (≠ W299), A306 (≠ G300), M307 (= M301), T308 (= T302), D387 (= D383), L399 (≠ I395), R402 (= R398), K493 (= K489)
- binding oxalic acid: V208 (= V206), S282 (≠ T273), A306 (≠ G300), M307 (= M301), H312 (vs. gap), K493 (= K489)
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)
32% identity, 97% coverage: 1:493/507 of query aligns to 1:504/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 161:165) binding ATP
- H214 (= H205) binding ATP; mutation to A: Abolished activity.
- S289 (≠ T273) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ TVG 273:275) binding ATP
- EA 310:311 (≠ EL 297:298) binding ATP
- M314 (= M301) binding oxalate
- T315 (= T302) binding ATP
- H319 (vs. gap) binding oxalate; mutation to A: Abolished activity.
- D394 (= D383) binding ATP
- R409 (= R398) binding ATP; mutation to A: Abolished activity.
- K500 (= K489) binding ATP; binding oxalate; mutation to A: Abolished activity.
Query Sequence
>WP_012592395.1 NCBI__GCF_000021745.1:WP_012592395.1
MRRGVISNLVQLAAQRYGDGAALTLPGARSFTFRELDELTGRFAGGLRSLGVRAGDRVVL
HLPNGWEWIVSYHAIARIGAVVVPANFLLSAAEVTFAARDSEALALILPAERRSAVAVSE
DVAVITLGSSEGAVEFQRLLAGAYIDPVERGADDLFTIGYTSGTTGRPKGAMLTHGCVYA
SMAATATMHVRHAGDIVLSSLPFPHVYGNVVMNAVFLTGMRLVSTPRFEAGAALKLIEQE
RVTLFEGVPTMYYQMLAHPDIASADLTSLVRCTVGGQTMPLSQIEAVANRFGCPVLELWG
MTEVAGPAVTHSPYWPSRYGSIGLPAPGVHARIVDLEERTRDQPIGEAGELLVRGPMVTR
GYWNDAEATADAIDKDGWLATGDVARADSDGYIFIVDRKKDLIITAGYNVYPAELEQVIA
MHPSVVMVAVAAIADAEKGELAEAFVVRRADATLDETELLIHCRKHLAAYKVPRRVIFVD
DLPKTSTGKIMRRKLRESARDCIPTQA
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