SitesBLAST
Comparing AZOBR_RS31155 AZOBR_RS31155 AMP-dependent synthetase 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)
37% identity, 96% coverage: 14:559/567 of query aligns to 5:552/561 of P69451
- Y213 (= Y219) mutation to A: Loss of activity.
- T214 (= T220) mutation to A: 10% of wild-type activity.
- G216 (= G222) mutation to A: Decreases activity.
- T217 (= T223) mutation to A: Decreases activity.
- G219 (= G225) mutation to A: Decreases activity.
- K222 (= K228) mutation to A: Decreases activity.
- E361 (= E365) 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, 93% coverage: 32:556/567 of query aligns to 37:546/556 of Q9S725
- K211 (= K228) mutation to S: Drastically reduces the activity.
- M293 (≠ P308) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ L335) mutation K->L,A: Affects the substrate specificity.
- E401 (= E412) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C414) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R459) mutation to Q: Drastically reduces the activity.
- K457 (≠ S467) mutation to S: Drastically reduces the activity.
- K540 (= K550) 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)
30% identity, 94% coverage: 27:557/567 of query aligns to 23:537/546 of Q84P21
- K530 (= K550) mutation to N: Lossed enzymatic activity.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
33% identity, 93% coverage: 32:556/567 of query aligns to 19:525/528 of 3ni2A
- active site: S182 (≠ T220), S202 (≠ N240), H230 (= H266), T329 (≠ S364), E330 (= E365), K434 (≠ L465), Q439 (≠ N470), K519 (= K550)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F268), S236 (≠ V272), G302 (= G338), A303 (= A339), P304 (= P340), G325 (= G360), G327 (= G362), T329 (≠ S364), P333 (= P368), V334 (= V369), D413 (= D444), K430 (= K461), K434 (≠ L465), Q439 (≠ N470)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
33% identity, 93% coverage: 32:556/567 of query aligns to 19:525/528 of 3a9vA
- active site: S182 (≠ T220), S202 (≠ N240), H230 (= H266), T329 (≠ S364), E330 (= E365), K434 (≠ L465), Q439 (≠ N470), K519 (= K550)
- binding adenosine monophosphate: H230 (= H266), G302 (= G338), A303 (= A339), P304 (= P340), Y326 (= Y361), G327 (= G362), M328 (≠ L363), T329 (≠ S364), D413 (= D444), K430 (= K461), K434 (≠ L465), Q439 (≠ N470)
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, 90% coverage: 45:556/567 of query aligns to 46:541/559 of Q67W82
- G395 (= G411) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 89% coverage: 54:556/567 of query aligns to 26:497/506 of 4gxqA
- active site: T163 (= T220), N183 (= N240), H207 (= H266), T303 (≠ S364), E304 (= E365), I403 (≠ L465), N408 (= N470), A491 (≠ K550)
- binding adenosine-5'-triphosphate: T163 (= T220), S164 (≠ G221), G165 (= G222), T166 (= T223), T167 (= T224), H207 (= H266), S277 (≠ G338), A278 (= A339), P279 (= P340), E298 (= E359), M302 (≠ L363), T303 (≠ S364), D382 (= D444), R397 (= R459)
- binding carbonate ion: H207 (= H266), S277 (≠ G338), R299 (≠ G360), G301 (= G362)
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)
31% identity, 93% coverage: 32:556/567 of query aligns to 26:532/542 of O24146
- S189 (≠ T220) binding
- S190 (≠ G221) binding
- G191 (= G222) binding
- T192 (= T223) binding
- T193 (= T224) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K228) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H266) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F268) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ V272) binding ; binding ; binding
- K260 (≠ R289) binding
- A309 (≠ G338) binding ; binding ; binding
- Q331 (≠ E359) binding
- G332 (= G360) binding ; binding ; binding ; binding ; binding
- T336 (≠ S364) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V369) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ A372) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D444) binding ; binding ; binding ; binding ; binding
- R435 (= R459) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K461) binding ; binding ; binding ; binding
- K441 (≠ L465) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S467) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G468) binding
- Q446 (≠ N470) binding
- K526 (= K550) binding ; 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)
31% identity, 93% coverage: 32:556/567 of query aligns to 18:524/528 of 5bsrA
- active site: S181 (≠ T220), S201 (≠ N240), H229 (= H266), T328 (≠ S364), E329 (= E365), K433 (≠ L465), Q438 (≠ N470), K518 (= K550)
- binding adenosine monophosphate: A301 (≠ G338), G326 (= G362), T328 (≠ S364), D412 (= D444), K429 (= K461), K433 (≠ L465), Q438 (≠ N470)
- binding coenzyme a: L102 (= L114), P226 (= P263), H229 (= H266), Y231 (≠ F268), F253 (= F290), K435 (≠ S467), G436 (= G468), F437 (= F469), F498 (≠ P530)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
31% identity, 93% coverage: 32:556/567 of query aligns to 19:525/529 of 5bsvA
- active site: S182 (≠ T220), S202 (≠ N240), H230 (= H266), T329 (≠ S364), E330 (= E365), K434 (≠ L465), Q439 (≠ N470), K519 (= K550)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H266), Y232 (≠ F268), S236 (≠ V272), A302 (≠ G338), A303 (= A339), P304 (= P340), G325 (= G360), G327 (= G362), M328 (≠ L363), T329 (≠ S364), P333 (= P368), V334 (= V369), D413 (= D444), K430 (= K461), K434 (≠ L465), Q439 (≠ N470)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
31% identity, 93% coverage: 32:556/567 of query aligns to 19:525/529 of 5bsuA
- active site: S182 (≠ T220), S202 (≠ N240), H230 (= H266), T329 (≠ S364), E330 (= E365), K434 (≠ L465), Q439 (≠ N470), K519 (= K550)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H266), Y232 (≠ F268), S236 (≠ V272), M299 (≠ L335), A302 (≠ G338), A303 (= A339), P304 (= P340), G325 (= G360), G327 (= G362), M328 (≠ L363), T329 (≠ S364), P333 (= P368), D413 (= D444), K430 (= K461), K434 (≠ L465), Q439 (≠ N470)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
31% identity, 93% coverage: 32:556/567 of query aligns to 19:525/529 of 5bstA
- active site: S182 (≠ T220), S202 (≠ N240), H230 (= H266), T329 (≠ S364), E330 (= E365), K434 (≠ L465), Q439 (≠ N470), K519 (= K550)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H266), Y232 (≠ F268), S236 (≠ V272), A302 (≠ G338), A303 (= A339), P304 (= P340), G325 (= G360), Y326 (= Y361), G327 (= G362), M328 (≠ L363), T329 (≠ S364), P333 (= P368), V334 (= V369), D413 (= D444), K430 (= K461), K434 (≠ L465), Q439 (≠ N470)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
31% identity, 93% coverage: 32:556/567 of query aligns to 19:525/530 of 5bsmA
- active site: S182 (≠ T220), S202 (≠ N240), H230 (= H266), T329 (≠ S364), E330 (= E365), K434 (≠ L465), Q439 (≠ N470), K519 (= K550)
- binding adenosine-5'-triphosphate: S182 (≠ T220), S183 (≠ G221), G184 (= G222), T185 (= T223), T186 (= T224), K190 (= K228), H230 (= H266), A302 (≠ G338), A303 (= A339), P304 (= P340), Y326 (= Y361), G327 (= G362), M328 (≠ L363), T329 (≠ S364), D413 (= D444), I425 (= I456), R428 (= R459), K519 (= K550)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
31% identity, 88% coverage: 58:556/567 of query aligns to 50:533/539 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 (= H266), F245 (= F268), T249 (≠ V272), G314 (= G338), A315 (= A339), P316 (= P340), G337 (= G360), Y338 (= Y361), G339 (= G362), L340 (= L363), T341 (≠ S364), S345 (≠ P368), A346 (≠ V369), D420 (= D444), I432 (= I456), K527 (= K550)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F268), R335 (≠ V358), G337 (= G360), G339 (= G362), L340 (= L363), A346 (≠ V369)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
31% identity, 88% coverage: 58:556/567 of query aligns to 50:533/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H266), F245 (= F268), T249 (≠ V272), G314 (= G338), A315 (= A339), P316 (= P340), G337 (= G360), Y338 (= Y361), G339 (= G362), L340 (= L363), T341 (≠ S364), A346 (≠ V369), D420 (= D444), I432 (= I456), K527 (= K550)
5ie2A Crystal structure of a plant enzyme (see paper)
31% identity, 92% coverage: 33:554/567 of query aligns to 6:499/506 of 5ie2A
- active site: T165 (= T220), S185 (≠ N240), H209 (= H266), T310 (≠ S364), E311 (= E365), N410 (≠ L465), K415 (≠ N470), K495 (= K550)
- binding adenosine-5'-triphosphate: T165 (= T220), S166 (≠ G221), G167 (= G222), T168 (= T223), T169 (= T224), S284 (≠ L335), A285 (≠ S336), S286 (≠ G337), Y307 (= Y361), A308 (≠ G362), M309 (≠ L363), T310 (≠ S364), D389 (= D444), L401 (≠ I456), R404 (= R459), K495 (= K550)
5ie3A Crystal structure of a plant enzyme (see paper)
30% identity, 92% coverage: 33:554/567 of query aligns to 6:497/504 of 5ie3A
- active site: T163 (= T220), S183 (≠ N240), H207 (= H266), T308 (≠ S364), E309 (= E365), N408 (≠ L465), K413 (≠ N470), K493 (= K550)
- binding adenosine monophosphate: S164 (≠ G221), S282 (≠ L335), A283 (≠ S336), S284 (≠ G337), Y305 (= Y361), A306 (≠ G362), M307 (≠ L363), T308 (≠ S364), D387 (= D444), L399 (≠ I456), R402 (= R459), K493 (= K550)
- binding oxalic acid: V208 (= V267), S282 (≠ L335), A306 (≠ G362), M307 (≠ L363), H312 (≠ P368), K493 (= K550)
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
30% identity, 91% coverage: 33:550/567 of query aligns to 6:499/504 of 6qjzA
- active site: T169 (= T220), S189 (≠ N240), H213 (= H266), T314 (≠ S364), E315 (= E365), N414 (≠ L465), K419 (≠ N470)
- binding adenosine monophosphate: H213 (= H266), S288 (≠ L335), A289 (≠ S336), S290 (≠ G337), A312 (≠ G362), M313 (≠ L363), T314 (≠ S364), D393 (= D444), L405 (≠ I456), K410 (= K461), K419 (≠ N470)
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)
31% identity, 92% coverage: 33:554/567 of query aligns to 6:504/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 220:224) binding
- H214 (= H266) binding ; mutation to A: Abolished activity.
- S289 (≠ L335) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ LSG 335:337) binding
- EA 310:311 (≠ EG 359:360) binding
- M314 (≠ L363) binding
- T315 (≠ S364) binding
- H319 (≠ P368) binding ; mutation to A: Abolished activity.
- D394 (= D444) binding
- R409 (= R459) binding ; mutation to A: Abolished activity.
- K500 (= K550) binding ; binding ; mutation to A: Abolished activity.
6q2mA Crystal structure of photinus pyralis luciferase pps6 mutant in complex with dlsa (see paper)
29% identity, 90% coverage: 58:566/567 of query aligns to 51:544/544 of 6q2mA
- active site: S197 (≠ T220), R217 (≠ N240), H244 (= H266), T342 (≠ S364), E343 (= E365), K442 (≠ L465), Q447 (≠ N470), K528 (= K550)
- binding (2S,5S)-hexane-2,5-diol: D186 (= D209), R187 (≠ P210), R260 (≠ E283), Y279 (≠ R302)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S198 (≠ G221), H244 (= H266), F246 (= F268), T250 (≠ V272), G315 (= G338), A316 (= A339), P317 (= P340), G338 (= G360), Y339 (= Y361), G340 (= G362), L341 (= L363), T342 (≠ S364), S346 (≠ P368), A347 (≠ V369), D421 (= D444), K528 (= K550)
Sites not aligning to the query:
Query Sequence
>AZOBR_RS31155 AZOBR_RS31155 AMP-dependent synthetase
MMGDAARTLPDQSWTLGYPPDVDWNAPIPVKPLTALLEDAAARFAERPFLDFMGKRSTYA
EVARMVDRAARGFQAIGVSKGVRVGLFLPNTPYFVICYFAILKAGGTVVNFNPLYAEREL
HHQITDSGVELMVTLDLKVLYGKMARMLAESGLKRLVICPMADILPFPKNWLFPIVKRAE
VARIPADDRHLSFRRLVANDGAPKPVAIDPTEDVAVLQYTGGTTGVPKGAMLTHANLFAN
TEQCSLWFVGARQGEERMLGVLPFFHVFAMTVVMNFSIRIGAEIVMLPRFELDQVMETIH
ARKPTLFPAVPTIYTAINHHRHLEKYDLSSIRYCLSGGAPLPVEVKEAFERNTGCVLVEG
YGLSESSPVATANPITGLNKAGSIGLPLPGTLIEIVSLEEPRRVLPVGEKGEVCIRGPQV
MKGYWNKPSETALTLVDGRLHTGDVGYMDEDGYTHIVDRIKDMILCSGFNVYPRNVEEAI
YLHPAVAECVVAGLPDEYRGQTVKAYIRVDDGKTLTREELIGFLKDKLSPIEMPKAIEFR
GELPKTMIGKLSRKALLDEEAERRKGS
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