SitesBLAST
Comparing SMc02162 FitnessBrowser__Smeli:SMc02162 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)
56% identity, 97% coverage: 15:565/566 of query aligns to 3:550/561 of P69451
- Y213 (= Y223) mutation to A: Loss of activity.
- T214 (= T224) mutation to A: 10% of wild-type activity.
- G216 (= G226) mutation to A: Decreases activity.
- T217 (= T227) mutation to A: Decreases activity.
- G219 (= G229) mutation to A: Decreases activity.
- K222 (= K232) mutation to A: Decreases activity.
- E361 (= E375) 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)
29% identity, 93% coverage: 39:566/566 of query aligns to 40:548/556 of Q9S725
- K211 (= K232) mutation to S: Drastically reduces the activity.
- M293 (≠ P318) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ F345) 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 (= R468) mutation to Q: Drastically reduces the activity.
- K457 (≠ S476) mutation to S: Drastically reduces the activity.
- K540 (= K558) mutation to N: Abolishes the activity.
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)
30% identity, 92% coverage: 45:566/566 of query aligns to 35:534/542 of O24146
- S189 (≠ T224) binding
- S190 (≠ G225) binding
- G191 (= G226) binding
- T192 (= T227) binding
- T193 (= T228) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K232) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H275) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F277) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ V281) binding ; binding ; binding
- K260 (≠ P299) binding
- A309 (≠ G348) binding ; binding ; binding
- Q331 (≠ E369) binding
- G332 (= G370) binding ; binding ; binding ; binding ; binding
- T336 (≠ S374) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V379) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ T381) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D453) binding ; binding ; binding ; binding ; binding
- R435 (= R468) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K470) binding ; binding ; binding ; binding
- K441 (≠ L474) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S476) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G477) binding
- Q446 (≠ N479) binding
- K526 (= K558) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
30% identity, 92% coverage: 45:566/566 of query aligns to 28:527/530 of 5bsmA
- active site: S182 (≠ T224), S202 (≠ N244), H230 (= H275), T329 (≠ S374), E330 (= E375), K434 (≠ L474), Q439 (≠ N479), K519 (= K558)
- binding adenosine-5'-triphosphate: S182 (≠ T224), S183 (≠ G225), G184 (= G226), T185 (= T227), T186 (= T228), K190 (= K232), H230 (= H275), A302 (≠ G348), A303 (≠ M349), P304 (≠ A350), Y326 (= Y371), G327 (= G372), M328 (≠ L373), T329 (≠ S374), D413 (= D453), I425 (= I465), R428 (= R468), K519 (= K558)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 92% coverage: 45:566/566 of query aligns to 27:526/528 of 5bsrA
- active site: S181 (≠ T224), S201 (≠ N244), H229 (= H275), T328 (≠ S374), E329 (= E375), K433 (≠ L474), Q438 (≠ N479), K518 (= K558)
- binding adenosine monophosphate: A301 (≠ G348), G326 (= G372), T328 (≠ S374), D412 (= D453), K429 (= K470), K433 (≠ L474), Q438 (≠ N479)
- binding coenzyme a: L102 (= L118), P226 (= P272), H229 (= H275), Y231 (≠ F277), F253 (≠ R300), K435 (≠ S476), G436 (= G477), F437 (= F478), F498 (≠ N538)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 92% coverage: 45:566/566 of query aligns to 28:527/529 of 5bsvA
- active site: S182 (≠ T224), S202 (≠ N244), H230 (= H275), T329 (≠ S374), E330 (= E375), K434 (≠ L474), Q439 (≠ N479), K519 (= K558)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H275), Y232 (≠ F277), S236 (≠ V281), A302 (≠ G348), A303 (≠ M349), P304 (≠ A350), G325 (= G370), G327 (= G372), M328 (≠ L373), T329 (≠ S374), P333 (= P378), V334 (= V379), D413 (= D453), K430 (= K470), K434 (≠ L474), Q439 (≠ N479)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 92% coverage: 45:566/566 of query aligns to 28:527/529 of 5bsuA
- active site: S182 (≠ T224), S202 (≠ N244), H230 (= H275), T329 (≠ S374), E330 (= E375), K434 (≠ L474), Q439 (≠ N479), K519 (= K558)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H275), Y232 (≠ F277), S236 (≠ V281), M299 (≠ F345), A302 (≠ G348), A303 (≠ M349), P304 (≠ A350), G325 (= G370), G327 (= G372), M328 (≠ L373), T329 (≠ S374), P333 (= P378), D413 (= D453), K430 (= K470), K434 (≠ L474), Q439 (≠ N479)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
30% identity, 92% coverage: 45:566/566 of query aligns to 28:527/529 of 5bstA
- active site: S182 (≠ T224), S202 (≠ N244), H230 (= H275), T329 (≠ S374), E330 (= E375), K434 (≠ L474), Q439 (≠ N479), K519 (= K558)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H275), Y232 (≠ F277), S236 (≠ V281), A302 (≠ G348), A303 (≠ M349), P304 (≠ A350), G325 (= G370), Y326 (= Y371), G327 (= G372), M328 (≠ L373), T329 (≠ S374), P333 (= P378), V334 (= V379), D413 (= D453), K430 (= K470), K434 (≠ L474), Q439 (≠ N479)
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)
31% identity, 90% coverage: 58:565/566 of query aligns to 57:542/559 of Q67W82
- G395 (= G419) 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, 90% coverage: 55:565/566 of query aligns to 23:498/506 of 4gxqA
- active site: T163 (= T224), N183 (= N244), H207 (= H275), T303 (≠ S374), E304 (= E375), I403 (≠ L474), N408 (= N479), A491 (≠ K558)
- binding adenosine-5'-triphosphate: T163 (= T224), S164 (≠ G225), G165 (= G226), T166 (= T227), T167 (= T228), H207 (= H275), S277 (≠ G348), A278 (≠ M349), P279 (≠ A350), E298 (= E369), M302 (≠ L373), T303 (≠ S374), D382 (= D453), R397 (= R468)
- binding carbonate ion: H207 (= H275), S277 (≠ G348), R299 (≠ G370), G301 (= G372)
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)
29% identity, 94% coverage: 32:565/566 of query aligns to 43:570/590 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
30% identity, 92% coverage: 45:566/566 of query aligns to 27:523/527 of 5u95B
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
28% identity, 92% coverage: 45:565/566 of query aligns to 28:526/528 of 3ni2A
- active site: S182 (≠ T224), S202 (≠ N244), H230 (= H275), T329 (≠ S374), E330 (= E375), K434 (≠ L474), Q439 (≠ N479), K519 (= K558)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F277), S236 (≠ V281), G302 (= G348), A303 (≠ M349), P304 (≠ A350), G325 (= G370), G327 (= G372), T329 (≠ S374), P333 (= P378), V334 (= V379), D413 (= D453), K430 (= K470), K434 (≠ L474), Q439 (≠ N479)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
28% identity, 92% coverage: 45:565/566 of query aligns to 28:526/528 of 3a9vA
- active site: S182 (≠ T224), S202 (≠ N244), H230 (= H275), T329 (≠ S374), E330 (= E375), K434 (≠ L474), Q439 (≠ N479), K519 (= K558)
- binding adenosine monophosphate: H230 (= H275), G302 (= G348), A303 (≠ M349), P304 (≠ A350), Y326 (= Y371), G327 (= G372), M328 (≠ L373), T329 (≠ S374), D413 (= D453), K430 (= K470), K434 (≠ L474), Q439 (≠ N479)
6e97B Crystal structure of the aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with dhb-adenylate
30% identity, 95% coverage: 28:565/566 of query aligns to 15:529/537 of 6e97B
- active site: S190 (≠ T224), S210 (≠ N244), H234 (= H275), A336 (≠ S374), E337 (= E375), N437 (≠ L474), K442 (≠ N479), K522 (= K558)
- binding 5'-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine: H234 (= H275), N235 (≠ I276), F236 (= F277), S240 (≠ V281), G310 (= G348), A311 (≠ M349), K312 (≠ A350), V332 (≠ G370), F333 (≠ Y371), G334 (= G372), M335 (≠ L373), A336 (≠ S374), D416 (= D453), K433 (= K470), K442 (≠ N479)
6e8oA Crystal structure of aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with amp
30% identity, 95% coverage: 28:565/566 of query aligns to 15:528/536 of 6e8oA
- active site: S190 (≠ T224), S210 (≠ N244), H234 (= H275), A336 (≠ S374), E337 (= E375), N437 (≠ L474), K442 (≠ N479), K521 (= K558)
- binding adenosine monophosphate: H234 (= H275), G310 (= G348), A311 (≠ M349), K312 (≠ A350), V332 (≠ G370), F333 (≠ Y371), G334 (= G372), M335 (≠ L373), A336 (≠ S374), D416 (= D453), V428 (≠ I465), K442 (≠ N479)
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)
28% identity, 90% coverage: 58:564/566 of query aligns to 55:536/546 of Q84P21
- K530 (= K558) mutation to N: Lossed enzymatic activity.
5wm3A Crystal structure of cahj in complex with salicyl adenylate (see paper)
31% identity, 90% coverage: 58:564/566 of query aligns to 51:530/537 of 5wm3A
- active site: S193 (≠ T224), N213 (= N244), H237 (= H275), A336 (≠ S374), E337 (= E375), N437 (≠ L474), K442 (≠ N479), K524 (= K558)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxybenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: N238 (≠ I276), F239 (= F277), G310 (= G348), S311 (≠ M349), K312 (≠ A350), V332 (≠ G370), F333 (≠ Y371), G334 (= G372), M335 (≠ L373), A336 (≠ S374), D416 (= D453), K433 (= K470), K442 (≠ N479)
- binding magnesium ion: S301 (= S339), L303 (= L341), G326 (= G364)
5wm6A Crystal structure of cahj in complex with benzoyl adenylate (see paper)
31% identity, 90% coverage: 58:564/566 of query aligns to 51:530/535 of 5wm6A
- active site: S193 (≠ T224), N213 (= N244), H237 (= H275), A336 (≠ S374), E337 (= E375), N437 (≠ L474), K442 (≠ N479), K524 (= K558)
- binding magnesium ion: S301 (= S339), L303 (= L341), G326 (= G364)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: F239 (= F277), G310 (= G348), S311 (≠ M349), K312 (≠ A350), V332 (≠ G370), F333 (≠ Y371), G334 (= G372), M335 (≠ L373), A336 (≠ S374), D416 (= D453), K433 (= K470), K442 (≠ N479)
5wm2A Crystal structure of cahj in complex with salicylic acid and amp (see paper)
31% identity, 90% coverage: 58:564/566 of query aligns to 51:530/536 of 5wm2A
- active site: S193 (≠ T224), N213 (= N244), H237 (= H275), A336 (≠ S374), E337 (= E375), N437 (≠ L474), K442 (≠ N479), K524 (= K558)
- binding adenosine monophosphate: G310 (= G348), S311 (≠ M349), K312 (≠ A350), V332 (≠ G370), F333 (≠ Y371), G334 (= G372), M335 (≠ L373), A336 (≠ S374), E337 (= E375), D416 (= D453), V428 (≠ I465), K433 (= K470), K442 (≠ N479)
Query Sequence
>SMc02162 FitnessBrowser__Smeli:SMc02162
MAEASTQQAGSSTAKIWLGSYPPGVPAEIGPLTYRSIGEFFDHAVAQYSWRPAFTCMGKA
LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYT
PRELEHQLVDAGAKAIFVLENFAHTVEQVLARTEVKHVVVASMGDMLGAKGAIVNLVVRR
VKKLVPAWSIPGHLSFKTVLAKGATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHAN
LLSNMAQMELWLNTAFLRKPRPESLTFMCALPLYHIFALTVNSLMGLATGGNNILIPNPR
DIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWL
ELTGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGE
ICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNV
FPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKDPNLTEEEVKRHCAASLTNYK
RPRYVEFRTELPKSNVGKILRKDLRG
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