SitesBLAST
Comparing WP_011914062.1 NCBI__GCF_000013785.1:WP_011914062.1 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)
53% identity, 99% coverage: 4:562/562 of query aligns to 3:553/561 of P69451
- Y213 (= Y214) mutation to A: Loss of activity.
- T214 (= T215) mutation to A: 10% of wild-type activity.
- G216 (= G217) mutation to A: Decreases activity.
- T217 (= T218) mutation to A: Decreases activity.
- G219 (= G220) mutation to A: Decreases activity.
- K222 (= K223) mutation to A: Decreases activity.
- E361 (= E369) mutation to A: Loss of activity.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
32% identity, 97% coverage: 14:559/562 of query aligns to 14:526/530 of 5bsmA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473), K519 (= K552)
- binding adenosine-5'-triphosphate: S182 (≠ T215), S183 (≠ G216), G184 (= G217), T185 (= T218), T186 (= T219), K190 (= K223), H230 (= H269), A302 (≠ G342), A303 (≠ T343), P304 (≠ A344), Y326 (= Y365), G327 (= G366), M328 (≠ L367), T329 (= T368), D413 (= D447), I425 (= I459), R428 (= R462), K519 (= K552)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
32% identity, 97% coverage: 14:559/562 of query aligns to 13:525/528 of 5bsrA
- active site: S181 (≠ T215), S201 (≠ N235), H229 (= H269), T328 (= T368), E329 (= E369), K433 (≠ I468), Q438 (≠ N473), K518 (= K552)
- binding adenosine monophosphate: A301 (≠ G342), G326 (= G366), T328 (= T368), D412 (= D447), K429 (= K464), K433 (≠ I468), Q438 (≠ N473)
- binding coenzyme a: L102 (= L108), P226 (= P266), H229 (= H269), Y231 (= Y271), F253 (≠ R294), K435 (≠ S470), G436 (= G471), F437 (= F472), F498 (≠ G532)
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, 97% coverage: 14:559/562 of query aligns to 21:533/542 of O24146
- S189 (≠ T215) binding ATP
- S190 (≠ G216) binding ATP
- G191 (= G217) binding ATP
- T192 (= T218) binding ATP
- T193 (= T219) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K223) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H269) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (= Y271) 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 (≠ V275) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ P293) binding CoA
- A309 (≠ G342) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E363) binding ATP
- G332 (= G364) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T368) 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 (= V373) 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 (= D447) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R462) 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 (= K464) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ I468) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S470) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G471) binding CoA
- Q446 (≠ N473) binding AMP
- K526 (= K552) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
32% identity, 97% coverage: 14:559/562 of query aligns to 14:526/529 of 5bsvA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473), K519 (= K552)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H269), Y232 (= Y271), S236 (≠ V275), A302 (≠ G342), A303 (≠ T343), P304 (≠ A344), G325 (= G364), G327 (= G366), M328 (≠ L367), T329 (= T368), P333 (= P372), V334 (= V373), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
32% identity, 97% coverage: 14:559/562 of query aligns to 14:526/529 of 5bsuA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473), K519 (= K552)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H269), Y232 (= Y271), S236 (≠ V275), M299 (≠ N339), A302 (≠ G342), A303 (≠ T343), P304 (≠ A344), G325 (= G364), G327 (= G366), M328 (≠ L367), T329 (= T368), P333 (= P372), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
32% identity, 97% coverage: 14:559/562 of query aligns to 14:526/529 of 5bstA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473), K519 (= K552)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H269), Y232 (= Y271), S236 (≠ V275), A302 (≠ G342), A303 (≠ T343), P304 (≠ A344), G325 (= G364), Y326 (= Y365), G327 (= G366), M328 (≠ L367), T329 (= T368), P333 (= P372), V334 (= V373), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
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, 97% coverage: 14:559/562 of query aligns to 32:547/556 of Q9S725
- K211 (= K223) mutation to S: Drastically reduces the activity.
- M293 (≠ L312) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ N339) mutation K->L,A: Affects the substrate specificity.
- E401 (= E414) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C416) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R462) mutation to Q: Drastically reduces the activity.
- K457 (≠ S470) mutation to S: Drastically reduces the activity.
- K540 (= K552) mutation to N: Abolishes the activity.
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)
32% identity, 93% coverage: 43:562/562 of query aligns to 58:573/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
31% identity, 97% coverage: 14:559/562 of query aligns to 13:522/527 of 5u95B
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
29% identity, 97% coverage: 14:560/562 of query aligns to 14:527/528 of 3ni2A
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473), K519 (= K552)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (= Y271), S236 (≠ V275), G302 (= G342), A303 (≠ T343), P304 (≠ A344), G325 (= G364), G327 (= G366), T329 (= T368), P333 (= P372), V334 (= V373), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
29% identity, 97% coverage: 14:560/562 of query aligns to 14:527/528 of 3a9vA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473), K519 (= K552)
- binding adenosine monophosphate: H230 (= H269), G302 (= G342), A303 (≠ T343), P304 (≠ A344), Y326 (= Y365), G327 (= G366), M328 (≠ L367), T329 (= T368), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 92% coverage: 47:561/562 of query aligns to 26:500/506 of 4gxqA
- active site: T163 (= T215), N183 (= N235), H207 (= H269), T303 (= T368), E304 (= E369), I403 (= I468), N408 (= N473), A491 (≠ K552)
- binding adenosine-5'-triphosphate: T163 (= T215), S164 (≠ G216), G165 (= G217), T166 (= T218), T167 (= T219), H207 (= H269), S277 (≠ G342), A278 (≠ T343), P279 (≠ A344), E298 (= E363), M302 (≠ L367), T303 (= T368), D382 (= D447), R397 (= R462)
- binding carbonate ion: H207 (= H269), S277 (≠ G342), R299 (≠ G364), G301 (= G366)
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)
27% identity, 99% coverage: 5:558/562 of query aligns to 17:536/546 of Q84P21
- K530 (= K552) 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)
28% identity, 97% coverage: 14:559/562 of query aligns to 28:542/559 of Q67W82
- G395 (= G413) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
30% identity, 95% coverage: 28:560/562 of query aligns to 22:535/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H269), F245 (= F273), T249 (≠ C277), G314 (= G342), A315 (≠ T343), P316 (≠ A344), G337 (= G364), Y338 (= Y365), G339 (= G366), L340 (= L367), T341 (= T368), A346 (≠ V373), D420 (= D447), I432 (= I459), K527 (= K552)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
30% identity, 95% coverage: 28:560/562 of query aligns to 22:535/539 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 (= H269), F245 (= F273), T249 (≠ C277), G314 (= G342), A315 (≠ T343), P316 (≠ A344), G337 (= G364), Y338 (= Y365), G339 (= G366), L340 (= L367), T341 (= T368), S345 (≠ P372), A346 (≠ V373), D420 (= D447), I432 (= I459), K527 (= K552)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F273), R335 (≠ V362), G337 (= G364), G339 (= G366), L340 (= L367), A346 (≠ V373)
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)
27% identity, 94% coverage: 29:556/562 of query aligns to 9:504/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 215:219) binding ATP
- H214 (= H269) binding ATP; mutation to A: Abolished activity.
- S289 (≠ G342) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ GTA 342:344) binding ATP
- EA 310:311 (≠ EG 363:364) binding ATP
- M314 (≠ L367) binding oxalate
- T315 (= T368) binding ATP
- H319 (≠ P372) binding oxalate; mutation to A: Abolished activity.
- D394 (= D447) binding ATP
- R409 (= R462) binding ATP; mutation to A: Abolished activity.
- K500 (= K552) binding ATP; binding oxalate; mutation to A: Abolished activity.
5ie2A Crystal structure of a plant enzyme (see paper)
27% identity, 94% coverage: 29:556/562 of query aligns to 9:499/506 of 5ie2A
- active site: T165 (= T215), S185 (≠ N235), H209 (= H269), T310 (= T368), E311 (= E369), N410 (≠ I468), K415 (≠ N473), K495 (= K552)
- binding adenosine-5'-triphosphate: T165 (= T215), S166 (≠ G216), G167 (= G217), T168 (= T218), T169 (= T219), S284 (≠ G342), A285 (≠ T343), S286 (≠ A344), Y307 (= Y365), A308 (≠ G366), M309 (≠ L367), T310 (= T368), D389 (= D447), L401 (≠ I459), R404 (= R462), K495 (= K552)
5ie3A Crystal structure of a plant enzyme (see paper)
27% identity, 94% coverage: 29:556/562 of query aligns to 9:497/504 of 5ie3A
- active site: T163 (= T215), S183 (≠ N235), H207 (= H269), T308 (= T368), E309 (= E369), N408 (≠ I468), K413 (≠ N473), K493 (= K552)
- binding adenosine monophosphate: S164 (≠ G216), S282 (≠ G342), A283 (≠ T343), S284 (≠ A344), Y305 (= Y365), A306 (≠ G366), M307 (≠ L367), T308 (= T368), D387 (= D447), L399 (≠ I459), R402 (= R462), K493 (= K552)
- binding oxalic acid: V208 (≠ I270), S282 (≠ G342), A306 (≠ G366), M307 (≠ L367), H312 (≠ P372), K493 (= K552)
Query Sequence
>WP_011914062.1 NCBI__GCF_000013785.1:WP_011914062.1
MQPEFWNDKRPAGVPNDIDLAAYRSVVEVFERACKAHADRPAFSNMGVTLSYSDLERYSA
AFAAWLQHHTDLQPGDRIAIQMPNLLQYPVAVFGALRAGLIVVNTNPLYTAREMRHQFQD
SGARALVYLNTFGNHVQEVLADTVIEHLIEVQIGDMLPTLRGALVNAAVKHLKKMVPDYS
LPQAVAFKNLLRDGARHSLKPTPLSLDDIAVLQYTGGTTGVAKGAMLTHGNLVANMQQVR
ANMQQLDAQGHPVIREGQEVMIAPLPLYHIYAFTVNCMCMMVTGNHNVLITNPRDINGFV
KELQRWQFSAFLGLNTLFVALMAHPQFKKVDFSRLKGTNSGGTALVSAVAERWKSMTGCT
VVEGYGLTETSPVVCANPHGEHSRLGTVGLPVPGTTLKVIDDEGNALPLGERGELCVKGP
QVMKGYWQRPEATAEVLDEEGWLRTGDIAVIDQDGFVSIVDRKKDLIIVSGFNVYPNEIE
DVVMAHPKVAACAAIGVADEKSGEAVKLFVVPSDPTLTQEELHAYCRENFTGYKMPRHYV
FRDALPMTPVGKILRRELRESA
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