SitesBLAST
Comparing WP_093395276.1 NCBI__GCF_900114975.1:WP_093395276.1 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)
40% identity, 98% coverage: 4:553/562 of query aligns to 1:552/561 of P69451
- Y213 (= Y213) mutation to A: Loss of activity.
- T214 (= T214) mutation to A: 10% of wild-type activity.
- G216 (= G216) mutation to A: Decreases activity.
- T217 (= T217) mutation to A: Decreases activity.
- G219 (= G219) mutation to A: Decreases activity.
- K222 (= K222) mutation to A: Decreases activity.
- E361 (= E359) 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)
31% identity, 95% coverage: 16:551/562 of query aligns to 32:547/556 of Q9S725
- K211 (= K222) mutation to S: Drastically reduces the activity.
- M293 (≠ P302) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I329) mutation K->L,A: Affects the substrate specificity.
- E401 (= E406) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ V408) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R453) mutation to Q: Drastically reduces the activity.
- K457 (≠ G461) mutation to S: Drastically reduces the activity.
- K540 (= K544) 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)
33% identity, 94% coverage: 23:550/562 of query aligns to 25:536/546 of Q84P21
- K530 (= K544) mutation to N: Lossed enzymatic 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)
33% identity, 95% coverage: 16:551/562 of query aligns to 28:542/559 of Q67W82
- G395 (= G405) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
32% identity, 94% coverage: 26:553/562 of query aligns to 19:528/528 of 3ni2A
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H260), T329 (= T358), E330 (= E359), K434 (≠ I459), Q439 (≠ N464), K519 (= K544)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F262), S236 (≠ A266), G302 (≠ S332), A303 (= A333), P304 (= P334), G325 (= G354), G327 (= G356), T329 (= T358), P333 (= P362), V334 (= V363), D413 (= D438), K430 (= K455), K434 (≠ I459), Q439 (≠ N464)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
32% identity, 94% coverage: 26:553/562 of query aligns to 19:528/528 of 3a9vA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H260), T329 (= T358), E330 (= E359), K434 (≠ I459), Q439 (≠ N464), K519 (= K544)
- binding adenosine monophosphate: H230 (= H260), G302 (≠ S332), A303 (= A333), P304 (= P334), Y326 (≠ F355), G327 (= G356), M328 (≠ L357), T329 (= T358), D413 (= D438), K430 (= K455), K434 (≠ I459), Q439 (≠ N464)
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)
32% identity, 95% coverage: 16:551/562 of query aligns to 21:533/542 of O24146
- S189 (≠ T214) binding ATP
- S190 (≠ G215) binding ATP
- G191 (= G216) binding ATP
- T192 (= T217) binding ATP
- T193 (= T218) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K222) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H260) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F262) 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 (≠ A266) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ R283) binding CoA
- A309 (≠ S332) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E353) binding ATP
- G332 (= G354) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T358) 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 (= V363) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ H365) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D438) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R453) 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 (= K455) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ I459) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G461) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G462) binding CoA
- Q446 (≠ N464) binding AMP
- K526 (= K544) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
32% identity, 95% coverage: 16:551/562 of query aligns to 13:525/528 of 5bsrA
- active site: S181 (≠ T214), S201 (≠ N234), H229 (= H260), T328 (= T358), E329 (= E359), K433 (≠ I459), Q438 (≠ N464), K518 (= K544)
- binding adenosine monophosphate: A301 (≠ S332), G326 (= G356), T328 (= T358), D412 (= D438), K429 (= K455), K433 (≠ I459), Q438 (≠ N464)
- binding coenzyme a: L102 (≠ M108), P226 (= P257), H229 (= H260), Y231 (≠ F262), F253 (= F284), K435 (≠ G461), G436 (= G462), F437 (≠ Y463), F498 (≠ A524)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
32% identity, 95% coverage: 16:551/562 of query aligns to 14:526/530 of 5bsmA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H260), T329 (= T358), E330 (= E359), K434 (≠ I459), Q439 (≠ N464), K519 (= K544)
- binding adenosine-5'-triphosphate: S182 (≠ T214), S183 (≠ G215), G184 (= G216), T185 (= T217), T186 (= T218), K190 (= K222), H230 (= H260), A302 (≠ S332), A303 (= A333), P304 (= P334), Y326 (≠ F355), G327 (= G356), M328 (≠ L357), T329 (= T358), D413 (= D438), I425 (= I450), R428 (= R453), K519 (= K544)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
32% identity, 95% coverage: 16:551/562 of query aligns to 14:526/529 of 5bsvA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H260), T329 (= T358), E330 (= E359), K434 (≠ I459), Q439 (≠ N464), 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 (= H260), Y232 (≠ F262), S236 (≠ A266), A302 (≠ S332), A303 (= A333), P304 (= P334), G325 (= G354), G327 (= G356), M328 (≠ L357), T329 (= T358), P333 (= P362), V334 (= V363), D413 (= D438), K430 (= K455), K434 (≠ I459), Q439 (≠ N464)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
32% identity, 95% coverage: 16:551/562 of query aligns to 14:526/529 of 5bsuA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H260), T329 (= T358), E330 (= E359), K434 (≠ I459), Q439 (≠ N464), K519 (= K544)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H260), Y232 (≠ F262), S236 (≠ A266), M299 (≠ I329), A302 (≠ S332), A303 (= A333), P304 (= P334), G325 (= G354), G327 (= G356), M328 (≠ L357), T329 (= T358), P333 (= P362), D413 (= D438), K430 (= K455), K434 (≠ I459), Q439 (≠ N464)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
32% identity, 95% coverage: 16:551/562 of query aligns to 14:526/529 of 5bstA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H260), T329 (= T358), E330 (= E359), K434 (≠ I459), Q439 (≠ N464), K519 (= K544)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H260), Y232 (≠ F262), S236 (≠ A266), A302 (≠ S332), A303 (= A333), P304 (= P334), G325 (= G354), Y326 (≠ F355), G327 (= G356), M328 (≠ L357), T329 (= T358), P333 (= P362), V334 (= V363), D413 (= D438), K430 (= K455), K434 (≠ I459), Q439 (≠ N464)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
32% identity, 96% coverage: 16:553/562 of query aligns to 13:524/527 of 5u95B
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
32% identity, 91% coverage: 40:552/562 of query aligns to 17:499/506 of 4gxqA
- active site: T163 (= T214), N183 (= N234), H207 (= H260), T303 (= T358), E304 (= E359), I403 (= I459), N408 (= N464), A491 (≠ K544)
- binding adenosine-5'-triphosphate: T163 (= T214), S164 (≠ G215), G165 (= G216), T166 (= T217), T167 (= T218), H207 (= H260), S277 (= S332), A278 (= A333), P279 (= P334), E298 (= E353), M302 (≠ L357), T303 (= T358), D382 (= D438), R397 (= R453)
- binding carbonate ion: H207 (= H260), S277 (= S332), R299 (≠ G354), G301 (= G356)
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)
34% identity, 90% coverage: 51:557/562 of query aligns to 31:513/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 214:218) binding ATP
- H214 (= H260) binding ATP; mutation to A: Abolished activity.
- S289 (≠ I329) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ ITG 329:331) binding ATP
- EA 310:311 (≠ EG 353:354) binding ATP
- M314 (≠ L357) binding oxalate
- T315 (= T358) binding ATP
- H319 (≠ P362) binding oxalate; mutation to A: Abolished activity.
- D394 (= D438) binding ATP
- R409 (= R453) binding ATP; mutation to A: Abolished activity.
- K500 (= K544) binding ATP; binding oxalate; mutation to A: Abolished activity.
5ie2A Crystal structure of a plant enzyme (see paper)
35% identity, 89% coverage: 51:548/562 of query aligns to 31:499/506 of 5ie2A
- active site: T165 (= T214), S185 (≠ N234), H209 (= H260), T310 (= T358), E311 (= E359), N410 (≠ I459), K415 (≠ N464), K495 (= K544)
- binding adenosine-5'-triphosphate: T165 (= T214), S166 (≠ G215), G167 (= G216), T168 (= T217), T169 (= T218), S284 (≠ I329), A285 (≠ T330), S286 (≠ G331), Y307 (≠ F355), A308 (≠ G356), M309 (≠ L357), T310 (= T358), D389 (= D438), L401 (≠ I450), R404 (= R453), K495 (= K544)
5ie3A Crystal structure of a plant enzyme (see paper)
34% identity, 89% coverage: 51:548/562 of query aligns to 31:497/504 of 5ie3A
- active site: T163 (= T214), S183 (≠ N234), H207 (= H260), T308 (= T358), E309 (= E359), N408 (≠ I459), K413 (≠ N464), K493 (= K544)
- binding adenosine monophosphate: S164 (≠ G215), S282 (≠ I329), A283 (≠ T330), S284 (≠ G331), Y305 (≠ F355), A306 (≠ G356), M307 (≠ L357), T308 (= T358), D387 (= D438), L399 (≠ I450), R402 (= R453), K493 (= K544)
- binding oxalic acid: V208 (= V261), S282 (≠ I329), A306 (≠ G356), M307 (≠ L357), H312 (≠ P362), 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)
31% identity, 90% coverage: 51:553/562 of query aligns to 30:496/503 of P9WQ37
- K172 (= K222) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ A248) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R249) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V261) 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 (≠ G263) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ A266) 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 (= R297) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G356) 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 (= W433) 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 (= D438) 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 (= R453) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ A460) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G462) 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.
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
32% identity, 88% coverage: 51:544/562 of query aligns to 31:499/504 of 6qjzA
- active site: T169 (= T214), S189 (≠ N234), H213 (= H260), T314 (= T358), E315 (= E359), N414 (≠ I459), K419 (≠ N464)
- binding adenosine monophosphate: H213 (= H260), S288 (≠ I329), A289 (≠ T330), S290 (≠ G331), A312 (≠ G356), M313 (≠ L357), T314 (= T358), D393 (= D438), L405 (≠ I450), K410 (= K455), K419 (≠ N464)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
30% identity, 93% coverage: 31:552/562 of query aligns to 24:535/539 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 (= H260), F245 (= F262), T249 (≠ A266), G314 (≠ S332), A315 (= A333), P316 (= P334), G337 (= G354), Y338 (≠ F355), G339 (= G356), L340 (= L357), T341 (= T358), S345 (≠ P362), A346 (≠ V363), D420 (= D438), I432 (= I450), K527 (= K544)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F262), R335 (≠ V352), G337 (= G354), G339 (= G356), L340 (= L357), A346 (≠ V363)
Query Sequence
>WP_093395276.1 NCBI__GCF_900114975.1:WP_093395276.1
MSALEELWLKHYDEGVPRHAAYPEEPLPSILHRNVQKWAHKPITNFYGAVLTYGDLWRQI
SRMAEALSRLGVKKGDRVAIMLPNCPQYVVSYYATLWLGAVVVNTNPMYVEREIEHQWSD
AGVKVAVVLDHLFPRVEKVYSKIGVEYVIVTSFRDALPRHLALLYPLKARKQKLFTAVPY
SDRVLPYGKLLKSNPPTEVQCPATLDDIALLQYTGGTTGISKGVILTHRNIMANVVQITK
WFPDLEWARERIVCILPFFHVFGMTACMNWALYTGSYMLLIPRFEINEFLKLLHKFRPTI
FPGVPTIYVAIVNHPDIKKFDLSSVKFCITGSAPMPVEVINRFEKMTGSIIVEGFGLTES
SPVTHCNPLHGLRKPGSVGIPVSDTECKIVDIETGERELPIGEEGELVVRGPQVMKGYWN
KPEETAQALRNGWLYTGDIAKMDEDGYTYIVDRKKDMIIAGGYNIYPREIDEVLYSHPKV
LDAVTVGVPDPYRGETVKVFVVPKPGETLTPEEVISFCRERLAAYKVPKLVEIRESLPKS
AVGKVLRKELREEELRKQKQAS
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