SitesBLAST
Comparing WP_110806073.1 NCBI__GCF_003217355.1:WP_110806073.1 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)
29% identity, 90% coverage: 12:579/630 of query aligns to 7:561/561 of P69451
- Y213 (≠ H225) mutation to A: Loss of activity.
- T214 (= T226) mutation to A: 10% of wild-type activity.
- G216 (= G228) mutation to A: Decreases activity.
- T217 (= T229) mutation to A: Decreases activity.
- G219 (= G231) mutation to A: Decreases activity.
- K222 (= K234) mutation to A: Decreases activity.
- E361 (= E372) mutation to A: Loss of activity.
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
30% identity, 80% coverage: 61:563/630 of query aligns to 31:501/504 of 6qjzA
- active site: T169 (= T226), S189 (≠ M243), H213 (= H269), T314 (= T371), E315 (= E372), N414 (≠ I475), K419 (≠ N480)
- binding adenosine monophosphate: H213 (= H269), S288 (= S345), A289 (= A346), S290 (≠ P347), A312 (≠ G369), M313 (≠ L370), T314 (= T371), D393 (= D454), L405 (≠ I466), K410 (= K471), K419 (≠ N480)
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)
30% identity, 78% coverage: 73:562/630 of query aligns to 44:501/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 226:230) binding ATP
- H214 (= H269) binding ATP; mutation to A: Abolished activity.
- S289 (= S345) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ SAP 345:347) binding ATP
- EA 310:311 (≠ EG 366:367) binding ATP
- M314 (≠ L370) binding oxalate
- T315 (= T371) binding ATP
- H319 (≠ C375) binding oxalate; mutation to A: Abolished activity.
- D394 (= D454) binding ATP
- R409 (= R469) binding ATP; mutation to A: Abolished activity.
- K500 (= K561) binding ATP; binding oxalate; mutation to A: Abolished activity.
5ie3A Crystal structure of a plant enzyme (see paper)
30% identity, 78% coverage: 73:562/630 of query aligns to 44:494/504 of 5ie3A
- active site: T163 (= T226), S183 (≠ M243), H207 (= H269), T308 (= T371), E309 (= E372), N408 (≠ I475), K413 (≠ N480), K493 (= K561)
- binding adenosine monophosphate: S164 (≠ G227), S282 (= S345), A283 (= A346), S284 (≠ P347), Y305 (= Y368), A306 (≠ G369), M307 (≠ L370), T308 (= T371), D387 (= D454), L399 (≠ I466), R402 (= R469), K493 (= K561)
- binding oxalic acid: V208 (= V270), S282 (= S345), A306 (≠ G369), M307 (≠ L370), H312 (≠ C375), K493 (= K561)
5ie2A Crystal structure of a plant enzyme (see paper)
30% identity, 78% coverage: 73:562/630 of query aligns to 44:496/506 of 5ie2A
- active site: T165 (= T226), S185 (≠ M243), H209 (= H269), T310 (= T371), E311 (= E372), N410 (≠ I475), K415 (≠ N480), K495 (= K561)
- binding adenosine-5'-triphosphate: T165 (= T226), S166 (≠ G227), G167 (= G228), T168 (= T229), T169 (= T230), S284 (= S345), A285 (= A346), S286 (≠ P347), Y307 (= Y368), A308 (≠ G369), M309 (≠ L370), T310 (= T371), D389 (= D454), L401 (≠ I466), R404 (= R469), K495 (= K561)
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)
28% identity, 86% coverage: 29:570/630 of query aligns to 38:549/556 of Q9S725
- K211 (= K234) mutation to S: Drastically reduces the activity.
- M293 (≠ I317) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I342) mutation K->L,A: Affects the substrate specificity.
- E401 (= E420) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C422) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R469) mutation to Q: Drastically reduces the activity.
- K457 (≠ G477) mutation to S: Drastically reduces the activity.
- K540 (= K561) 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)
28% identity, 91% coverage: 14:584/630 of query aligns to 26:585/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
5x8fB Ternary complex structure of a double mutant i454ra456k of o- succinylbenzoate coa synthetase (mene) from bacillus subtilis bound with amp and its product analogue osb-ncoa at 1.76 angstrom (see paper)
32% identity, 56% coverage: 216:568/630 of query aligns to 141:477/485 of 5x8fB
- active site: T151 (= T226), S171 (≠ N246), H195 (= H269), T288 (= T371), E289 (= E372), I387 (= I475), N392 (= N480), K470 (= K561)
- binding magnesium ion: N178 (≠ T252), L202 (≠ I276), L214 (≠ F289), T296 (≠ S378), L297 (≠ I379), S298 (≠ N380)
- binding o-succinylbenzoyl-N-coenzyme A: L191 (= L265), P192 (= P266), H195 (= H269), I196 (≠ V270), S197 (≠ F271), A237 (≠ T318), V238 (= V319), L260 (≠ I342), G262 (= G344), G286 (= G369), M287 (≠ L370), S292 (vs. gap), Q293 (vs. gap), S388 (≠ R476), G389 (= G477), G390 (= G478), E391 (≠ H479), K420 (≠ F508), W421 (≠ A509), K450 (≠ R541), Y451 (≠ A542)
Sites not aligning to the query:
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
32% identity, 56% coverage: 216:568/630 of query aligns to 141:477/484 of 5gtdA
- active site: T151 (= T226), S171 (≠ N246), H195 (= H269), T288 (= T371), E289 (= E372)
- binding adenosine-5'-monophosphate: G263 (≠ S345), G264 (≠ A346), Y285 (= Y368), G286 (= G369), M287 (≠ L370), T288 (= T371), D366 (= D454), V378 (≠ I466)
- binding magnesium ion: F314 (≠ P396), S315 (≠ Y397)
- binding 2-succinylbenzoate: H195 (= H269), S197 (≠ F271), A237 (≠ T318), L260 (≠ I342), G262 (= G344), G263 (≠ S345), G286 (= G369), M287 (≠ L370), S292 (vs. gap), Q293 (vs. gap)
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
29% identity, 81% coverage: 61:570/630 of query aligns to 30:486/486 of 8wevA
Sites not aligning to the query:
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
32% identity, 56% coverage: 216:568/630 of query aligns to 140:474/475 of 5burA
- active site: T150 (= T226), S170 (≠ N246), H194 (= H269), T287 (= T371), E288 (= E372)
- binding adenosine-5'-triphosphate: T150 (= T226), S151 (≠ G227), T153 (= T229), T154 (= T230), K158 (= K234), G263 (≠ A346), S283 (≠ G367), T287 (= T371), D365 (= D454), V377 (≠ I466), R380 (= R469)
P38137 Oxalate--CoA ligase; Acyl-activating enzyme 3; Oxalyl-CoA synthetase; Peroxisomal-coenzyme A synthetase; EC 6.2.1.8 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
28% identity, 77% coverage: 81:562/630 of query aligns to 58:524/543 of P38137
Sites not aligning to the query:
- 541:543 C-terminal peroxisome targeting signal (PTS1)
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)
29% identity, 81% coverage: 62:570/630 of query aligns to 54:535/542 of O24146
- S189 (≠ T226) binding ATP
- S190 (≠ G227) binding ATP
- G191 (= G228) binding ATP
- T192 (= T229) binding ATP
- T193 (= T230) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K234) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H269) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F271) 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 (≠ P275) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ P292) binding CoA
- A309 (≠ S345) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E366) binding ATP
- G332 (= G367) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T371) 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 (≠ T374) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D454) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R469) 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 (= K471) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ I475) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G477) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G478) binding CoA
- Q446 (≠ N480) binding AMP
- K526 (= K561) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
29% identity, 81% coverage: 62:570/630 of query aligns to 47:528/529 of 5bsvA
- active site: S182 (≠ T226), S202 (≠ N246), H230 (= H269), T329 (= T371), E330 (= E372), K434 (≠ I475), Q439 (≠ N480), K519 (= K561)
- 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 (≠ F271), S236 (≠ P275), A302 (≠ S345), A303 (= A346), P304 (= P347), G325 (= G367), G327 (= G369), M328 (≠ L370), T329 (= T371), P333 (vs. gap), V334 (vs. gap), D413 (= D454), K430 (= K471), K434 (≠ I475), Q439 (≠ N480)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
29% identity, 81% coverage: 62:570/630 of query aligns to 47:528/529 of 5bsuA
- active site: S182 (≠ T226), S202 (≠ N246), H230 (= H269), T329 (= T371), E330 (= E372), K434 (≠ I475), Q439 (≠ N480), K519 (= K561)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H269), Y232 (≠ F271), S236 (≠ P275), M299 (≠ I342), A302 (≠ S345), A303 (= A346), P304 (= P347), G325 (= G367), G327 (= G369), M328 (≠ L370), T329 (= T371), P333 (vs. gap), D413 (= D454), K430 (= K471), K434 (≠ I475), Q439 (≠ N480)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
29% identity, 81% coverage: 62:570/630 of query aligns to 47:528/529 of 5bstA
- active site: S182 (≠ T226), S202 (≠ N246), H230 (= H269), T329 (= T371), E330 (= E372), K434 (≠ I475), Q439 (≠ N480), K519 (= K561)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H269), Y232 (≠ F271), S236 (≠ P275), A302 (≠ S345), A303 (= A346), P304 (= P347), G325 (= G367), Y326 (= Y368), G327 (= G369), M328 (≠ L370), T329 (= T371), P333 (vs. gap), V334 (vs. gap), D413 (= D454), K430 (= K471), K434 (≠ I475), Q439 (≠ N480)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
29% identity, 81% coverage: 62:570/630 of query aligns to 46:527/528 of 5bsrA
- active site: S181 (≠ T226), S201 (≠ N246), H229 (= H269), T328 (= T371), E329 (= E372), K433 (≠ I475), Q438 (≠ N480), K518 (= K561)
- binding adenosine monophosphate: A301 (≠ S345), G326 (= G369), T328 (= T371), D412 (= D454), K429 (= K471), K433 (≠ I475), Q438 (≠ N480)
- binding coenzyme a: L102 (= L117), P226 (= P266), H229 (= H269), Y231 (≠ F271), F253 (= F301), K435 (≠ G477), G436 (= G478), F437 (≠ H479), F498 (vs. gap)
5wm6A Crystal structure of cahj in complex with benzoyl adenylate (see paper)
31% identity, 81% coverage: 62:570/630 of query aligns to 55:533/535 of 5wm6A
- active site: S193 (≠ T226), N213 (= N246), H237 (= H269), A336 (≠ T371), E337 (= E372), N437 (≠ I475), K442 (≠ N480), K524 (= K561)
- binding magnesium ion: S301 (= S336), L303 (= L338), G326 (= G361)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: F239 (= F271), G310 (≠ S345), S311 (≠ A346), K312 (≠ P347), V332 (≠ G367), F333 (≠ Y368), G334 (= G369), M335 (≠ L370), A336 (≠ T371), D416 (= D454), K433 (= K471), K442 (≠ N480)
5wm3A Crystal structure of cahj in complex with salicyl adenylate (see paper)
32% identity, 79% coverage: 72:570/630 of query aligns to 66:533/537 of 5wm3A
- active site: S193 (≠ T226), N213 (= N246), H237 (= H269), A336 (≠ T371), E337 (= E372), N437 (≠ I475), K442 (≠ N480), K524 (= K561)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxybenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: N238 (≠ V270), F239 (= F271), G310 (≠ S345), S311 (≠ A346), K312 (≠ P347), V332 (≠ G367), F333 (≠ Y368), G334 (= G369), M335 (≠ L370), A336 (≠ T371), D416 (= D454), K433 (= K471), K442 (≠ N480)
- binding magnesium ion: S301 (= S336), L303 (= L338), G326 (= G361)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
29% identity, 81% coverage: 62:570/630 of query aligns to 47:528/530 of 5bsmA
- active site: S182 (≠ T226), S202 (≠ N246), H230 (= H269), T329 (= T371), E330 (= E372), K434 (≠ I475), Q439 (≠ N480), K519 (= K561)
- binding adenosine-5'-triphosphate: S182 (≠ T226), S183 (≠ G227), G184 (= G228), T185 (= T229), T186 (= T230), K190 (= K234), H230 (= H269), A302 (≠ S345), A303 (= A346), P304 (= P347), Y326 (= Y368), G327 (= G369), M328 (≠ L370), T329 (= T371), D413 (= D454), I425 (= I466), R428 (= R469), K519 (= K561)
Query Sequence
>WP_110806073.1 NCBI__GCF_003217355.1:WP_110806073.1
MTETYATVADRDRVEGQMPWEDRDRAITMYDFLSRVTAKHGARPALTFQITSGPKDHSVT
MTWEQVLARVTQAANLLRRMGVGEKDTVAYLLPNSLETAVVLLAGTTAGIVNPINPLLEP
EQIAAILRETKAKVLVTLKSFPKSDIAQKAAEAVKHAPNVKTILEVDLNRYLTAPKSWIV
PFLRPKTHFRHHADVYDFNTACDGQPADKLVFEDAKTDRVAAYFHTGGTTGMPKVAQHKY
SGMVYNGWLGGTLLFRHTDVMICPLPLFHVFAAYPILMSAIHSGAHVVFPTPAGYRGEGV
FDNFWKLIERWQVTFLITVPTAIAALMQRKVDADISSLRTAISGSAPLPVELYNRFKDAT
GVEICEGYGLTEATCLVSINPVDGPKKVGSVGIPLPYSHVRILRKTEAGFLECAADEVGE
ICVANPGVFEGSTYTEVDKNHDLFAEERFLRTGDLGRIDPDGYLWITGRAKDLIIRGGHN
IDPAEIEEALLAHPAIAFAGAIGQPDAFAGELPCAYVELVKDATITPDELMAHAKRHIHE
RAAVPKHIEVLDELPKTAVGKIFKPELRKRAIVRVLDAALAEAAVPVHVVAVVEDKKRGL
VAQLATTGDHDAAKLGQVLGQFTVPWDWAE
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