SitesBLAST
Comparing WP_011423856.1 NCBI__GCF_000092045.1:WP_011423856.1 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.
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)
31% identity, 95% coverage: 30:565/566 of query aligns to 32:570/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
30% identity, 96% coverage: 22:566/566 of query aligns to 28:548/556 of Q9S725
- K211 (= K232) mutation to S: Drastically reduces the activity.
- M293 (≠ P318) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ L345) 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.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% 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)
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, 98% coverage: 12:566/566 of query aligns to 7:534/542 of O24146
- S189 (≠ T224) binding ATP
- S190 (≠ G225) binding ATP
- G191 (= G226) binding ATP
- T192 (= T227) binding ATP
- T193 (= T228) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K232) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H275) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F277) 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 (≠ V281) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ P299) binding CoA
- A309 (≠ G348) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E369) binding ATP
- G332 (= G370) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (≠ S374) 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 (= 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 (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D453) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R468) 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 (= K470) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ L474) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S476) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G477) binding CoA
- Q446 (≠ N479) binding AMP
- K526 (= K558) 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)
30% identity, 96% coverage: 22:566/566 of query aligns to 9:526/528 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)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
30% identity, 96% coverage: 22:566/566 of query aligns to 10:527/530 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)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
31% identity, 90% coverage: 58:565/566 of query aligns to 43:526/528 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)
31% identity, 90% coverage: 58:565/566 of query aligns to 43:526/528 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)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 96% coverage: 22:566/566 of query aligns to 10:527/529 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, 96% coverage: 22:566/566 of query aligns to 10:527/529 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 (≠ L345), 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, 96% coverage: 22:566/566 of query aligns to 10:527/529 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)
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
31% identity, 91% coverage: 52:565/566 of query aligns to 21:484/486 of 8wevA
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, 96% coverage: 21:564/566 of query aligns to 18:536/546 of Q84P21
- K530 (= K558) 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)
30% 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.
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
30% identity, 96% coverage: 22:566/566 of query aligns to 9:523/527 of 5u95B
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
28% identity, 96% coverage: 24:565/566 of query aligns to 1:509/518 of 4wv3B
- active site: S175 (≠ T224), T320 (≠ S374), E321 (= E375), K418 (≠ L474), W423 (≠ N479), K502 (= K558)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H275), T221 (≠ I276), F222 (= F277), A293 (≠ G347), S294 (≠ G348), E295 (≠ M349), A296 (= A350), G316 (= G370), I317 (≠ Y371), G318 (= G372), C319 (≠ L373), T320 (≠ S374), D397 (= D453), H409 (≠ I465), R412 (= R468), K502 (= K558)
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)
29% identity, 89% coverage: 61:565/566 of query aligns to 30:494/503 of P9WQ37
- K172 (= K232) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R258) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ K260) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I276) 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 (= A278) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V281) 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 (≠ N313) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G372) 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 (≠ Y448) 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 (= D453) 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 (= R468) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V475) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G477) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K558) 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.
4zjzA Crystal structure of a benzoate coenzyme a ligase with benzoyl-amp (see paper)
29% identity, 95% coverage: 30:565/566 of query aligns to 3:514/517 of 4zjzA
- active site: S176 (≠ T224), T196 (≠ L252), T324 (≠ S374), E325 (= E375), K422 (≠ L474), Y427 (≠ N479), K507 (= K558)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: A222 (≠ I276), Y223 (≠ F277), A297 (≠ G347), G298 (= G348), E299 (≠ M349), A300 (= A350), G320 (= G370), I321 (≠ Y371), G322 (= G372), S323 (≠ L373), T324 (≠ S374), H328 (≠ P378), I329 (≠ V379), D401 (= D453), R416 (= R468), K422 (≠ L474), Y427 (≠ N479)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
29% identity, 95% coverage: 30:565/566 of query aligns to 3:514/518 of 4rmnA
- active site: S176 (≠ T224), T196 (≠ L252), T324 (≠ S374), E325 (= E375), K422 (≠ L474), Y427 (≠ N479), K507 (= K558)
- binding thiophene-2-carboxylic acid: A217 (≠ L271), F221 (≠ H275), Y223 (≠ F277), G269 (= G319), A270 (≠ L320), A297 (≠ G347), G298 (= G348), G322 (= G372), S323 (≠ L373), H328 (≠ P378), I329 (≠ V379), K422 (≠ L474), G425 (= G477)
Query Sequence
>WP_011423856.1 NCBI__GCF_000092045.1:WP_011423856.1
MTSISVHPNGAKTDKPWLATYPDMVPAELPPLEHASLAELLEKSCARYADRTVFSSMGKS
MSYRDLESQTRKVAAWLQSIGLEKGDRVAVMMPNVLQNPVATYAILRAGLVVVNVNPLYT
PRELEHQLRDSGAKAIFVLENFARTVEQVLNKTDLRHVVVTSLGEMLGPKGLMVNFVVRK
VKKLVPSWSIPQHKSFSQVLREGAKKSLQPVTLAGGHIAFLQYTGGTTGVAKGAVLTHQN
LLANKLQLSLWLRSAFQRKKQPEVLNFLCALPLYHIFALTVNSLMGMSLGAHNILIANPR
DIPGLVKEFGKSNIHIFPGLNTLFNALMNNAEFAKLDFSSLIMSLGGGMAVQRPVAERWL
KTTGTAITEGYGLSETSPVATANRFDSIEFTGSIGLPIPSTELDIRDEEGRSLPLGEIGE
ICIRGPQVMAGYWQKPEETARVMTADGYFRSGDMGFMDERGYTKIVDRKKDMILVSGFNV
YPNEIEEVAAMHAGILEAAAVGVPDGHSGEAVKLFVVRKDPNLTEAEVRAHCIANLTNYK
RPRFIEFRTELPKSPVGKILRKDLRG
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