SitesBLAST
Comparing WP_013841103.1 NCBI__GCF_000215085.1:WP_013841103.1 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)
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)
40% identity, 97% coverage: 7:543/554 of query aligns to 37:577/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
31% identity, 96% coverage: 9:538/554 of query aligns to 4:496/503 of P9WQ37
- R9 (≠ D14) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ E22) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K206) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ S229) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R231) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C243) 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 (≠ C246) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ G249) 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 (= R279) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G339) 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 (= W418) 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 (= D423) 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 (= R438) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R445) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G447) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K529) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 91% coverage: 34:537/554 of query aligns to 28:499/506 of 4gxqA
- active site: T163 (= T198), N183 (= N218), H207 (= H242), T303 (= T341), E304 (= E342), I403 (= I444), N408 (= N449), A491 (≠ K529)
- binding adenosine-5'-triphosphate: T163 (= T198), S164 (= S199), G165 (= G200), T166 (= T201), T167 (= T202), H207 (= H242), S277 (≠ G314), A278 (≠ S315), P279 (= P316), E298 (≠ I336), M302 (≠ Q340), T303 (= T341), D382 (= D423), R397 (= R438)
- binding carbonate ion: H207 (= H242), S277 (≠ G314), R299 (≠ T337), G301 (= G339)
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)
33% identity, 94% coverage: 27:547/554 of query aligns to 52:542/542 of O24146
- S189 (≠ T198) binding ATP
- S190 (= S199) binding ATP
- G191 (= G200) binding ATP
- T192 (= T201) binding ATP
- T193 (= T202) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K206) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H242) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F244) 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 (≠ L248) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ V265) binding CoA
- A309 (≠ G314) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ I336) binding ATP
- G332 (≠ T337) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T341) 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 (≠ A346) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (= M349) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D423) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R438) 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 (= K440) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ I444) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G446) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G447) binding CoA
- Q446 (≠ N449) binding AMP
- K526 (= K529) binding ATP; mutation to A: Abolished activity against 4-coumarate.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
30% identity, 96% coverage: 9:538/554 of query aligns to 7:496/502 of 3r44A
Sites not aligning to the query:
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, 95% coverage: 12:539/554 of query aligns to 28:553/561 of P69451
- Y213 (= Y197) mutation to A: Loss of activity.
- T214 (= T198) mutation to A: 10% of wild-type activity.
- G216 (= G200) mutation to A: Decreases activity.
- T217 (= T201) mutation to A: Decreases activity.
- G219 (= G203) mutation to A: Decreases activity.
- K222 (= K206) mutation to A: Decreases activity.
- E361 (= E342) 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)
30% identity, 92% coverage: 36:547/554 of query aligns to 65:556/556 of Q9S725
- K211 (= K206) mutation to S: Drastically reduces the activity.
- M293 (≠ H284) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I311) mutation K->L,A: Affects the substrate specificity.
- E401 (= E390) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C392) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R438) mutation to Q: Drastically reduces the activity.
- K457 (≠ G446) mutation to S: Drastically reduces the activity.
- K540 (= K529) mutation to N: Abolishes the activity.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
33% identity, 92% coverage: 27:538/554 of query aligns to 44:527/528 of 5bsrA
- active site: S181 (≠ T198), S201 (≠ N218), H229 (= H242), T328 (= T341), E329 (= E342), K433 (≠ I444), Q438 (≠ N449), K518 (= K529)
- binding adenosine monophosphate: A301 (≠ G314), G326 (= G339), T328 (= T341), D412 (= D423), K429 (= K440), K433 (≠ I444), Q438 (≠ N449)
- binding coenzyme a: L102 (≠ N92), P226 (= P239), H229 (= H242), Y231 (≠ F244), F253 (= F266), K435 (≠ G446), G436 (= G447), F437 (≠ E448), F498 (≠ K509)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
33% identity, 92% coverage: 27:538/554 of query aligns to 44:524/527 of 5u95B
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
33% identity, 92% coverage: 27:538/554 of query aligns to 45:528/530 of 5bsmA
- active site: S182 (≠ T198), S202 (≠ N218), H230 (= H242), T329 (= T341), E330 (= E342), K434 (≠ I444), Q439 (≠ N449), K519 (= K529)
- binding adenosine-5'-triphosphate: S182 (≠ T198), S183 (= S199), G184 (= G200), T185 (= T201), T186 (= T202), K190 (= K206), H230 (= H242), A302 (≠ G314), A303 (≠ S315), P304 (= P316), Y326 (= Y338), G327 (= G339), M328 (≠ Q340), T329 (= T341), D413 (= D423), I425 (= I435), R428 (= R438), K519 (= K529)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
33% identity, 92% coverage: 27:538/554 of query aligns to 45:528/529 of 5bsvA
- active site: S182 (≠ T198), S202 (≠ N218), H230 (= H242), T329 (= T341), E330 (= E342), K434 (≠ I444), Q439 (≠ N449), K519 (= K529)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H242), Y232 (≠ F244), S236 (≠ L248), A302 (≠ G314), A303 (≠ S315), P304 (= P316), G325 (≠ T337), G327 (= G339), M328 (≠ Q340), T329 (= T341), P333 (= P345), V334 (≠ A346), D413 (= D423), K430 (= K440), K434 (≠ I444), Q439 (≠ N449)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
33% identity, 92% coverage: 27:538/554 of query aligns to 45:528/529 of 5bsuA
- active site: S182 (≠ T198), S202 (≠ N218), H230 (= H242), T329 (= T341), E330 (= E342), K434 (≠ I444), Q439 (≠ N449), K519 (= K529)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H242), Y232 (≠ F244), S236 (≠ L248), M299 (≠ I311), A302 (≠ G314), A303 (≠ S315), P304 (= P316), G325 (≠ T337), G327 (= G339), M328 (≠ Q340), T329 (= T341), P333 (= P345), D413 (= D423), K430 (= K440), K434 (≠ I444), Q439 (≠ N449)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
33% identity, 92% coverage: 27:538/554 of query aligns to 45:528/529 of 5bstA
- active site: S182 (≠ T198), S202 (≠ N218), H230 (= H242), T329 (= T341), E330 (= E342), K434 (≠ I444), Q439 (≠ N449), K519 (= K529)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H242), Y232 (≠ F244), S236 (≠ L248), A302 (≠ G314), A303 (≠ S315), P304 (= P316), G325 (≠ T337), Y326 (= Y338), G327 (= G339), M328 (≠ Q340), T329 (= T341), P333 (= P345), V334 (≠ A346), D413 (= D423), K430 (= K440), K434 (≠ I444), Q439 (≠ N449)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
31% identity, 94% coverage: 15:537/554 of query aligns to 29:535/539 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 (= H242), F245 (= F244), T249 (≠ C246), G314 (= G314), A315 (≠ S315), P316 (= P316), G337 (≠ T337), Y338 (= Y338), G339 (= G339), L340 (≠ Q340), T341 (= T341), S345 (≠ P345), A346 (= A346), D420 (= D423), I432 (= I435), K527 (= K529)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F244), R335 (≠ T335), G337 (≠ T337), G339 (= G339), L340 (≠ Q340), A346 (= A346)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
31% identity, 94% coverage: 15:537/554 of query aligns to 29:535/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H242), F245 (= F244), T249 (≠ C246), G314 (= G314), A315 (≠ S315), P316 (= P316), G337 (≠ T337), Y338 (= Y338), G339 (= G339), L340 (≠ Q340), T341 (= T341), A346 (= A346), D420 (= D423), I432 (= I435), K527 (= K529)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
31% identity, 92% coverage: 27:538/554 of query aligns to 45:528/528 of 3ni2A
- active site: S182 (≠ T198), S202 (≠ N218), H230 (= H242), T329 (= T341), E330 (= E342), K434 (≠ I444), Q439 (≠ N449), K519 (= K529)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F244), S236 (≠ L248), G302 (= G314), A303 (≠ S315), P304 (= P316), G325 (≠ T337), G327 (= G339), T329 (= T341), P333 (= P345), V334 (≠ A346), D413 (= D423), K430 (= K440), K434 (≠ I444), Q439 (≠ N449)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
31% identity, 92% coverage: 27:538/554 of query aligns to 45:528/528 of 3a9vA
- active site: S182 (≠ T198), S202 (≠ N218), H230 (= H242), T329 (= T341), E330 (= E342), K434 (≠ I444), Q439 (≠ N449), K519 (= K529)
- binding adenosine monophosphate: H230 (= H242), G302 (= G314), A303 (≠ S315), P304 (= P316), Y326 (= Y338), G327 (= G339), M328 (≠ Q340), T329 (= T341), D413 (= D423), K430 (= K440), K434 (≠ I444), Q439 (≠ N449)
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, 94% coverage: 36:553/554 of query aligns to 61:559/559 of Q67W82
- G395 (= G389) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
Q5SKN9 Long-chain-fatty-acid--CoA ligase; Long-chain fatty acyl-CoA synthetase; LC-FACS; EC 6.2.1.3 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
31% identity, 95% coverage: 12:538/554 of query aligns to 23:533/541 of Q5SKN9
- T184 (= T198) binding Mg(2+)
- G302 (= G314) binding tetradecanoyl-AMP
- Q322 (≠ I336) binding tetradecanoyl-AMP
- G323 (≠ T337) binding tetradecanoyl-AMP
- T327 (= T341) binding tetradecanoyl-AMP
- E328 (= E342) binding Mg(2+)
- D418 (= D423) binding tetradecanoyl-AMP
- K435 (= K440) binding tetradecanoyl-AMP
- K439 (≠ I444) binding tetradecanoyl-AMP
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)
29% identity, 90% coverage: 35:535/554 of query aligns to 58:536/546 of Q84P21
- K530 (= K529) mutation to N: Lossed enzymatic activity.
Query Sequence
>WP_013841103.1 NCBI__GCF_000215085.1:WP_013841103.1
MQKLDRITVGALLDRTAAQFPENDALVYNHRDLRLSYQEFNRLCRKVAKGLMALGIQKGE
HIAIWATNVPEWVTLQFTTGKMGAVLVTVNTNYKSFEVEYLLQQSDATTLVMIGGTKTTN
YLKIINELCPELKDCPPGQLNSARLPLLKNIIFIGEEAQPGMLNWNDLLELANQITDEEL
DARQASLDPDDCINMQYTSGTTGFPKGVMLTHTNLVNNAHSIANCMAFSERDRLLITVPF
FHCFGCVLGTMTCVVSGATMVPLEVFNPVRVLEIVDQERCTALHGVPTMFIMELEELAKG
NYDVSSLRTGIMAGSPCPIEVMKAVVDRMGMKEITITYGQTEASPAITMTRTDDPIELRV
ATVGKVIPNVEAKIVDPETGEDCPPGIQGEICSRGYNVMKGYYKMPEATAQAIDQDGWLH
TGDLGIMDEKGYFKITGRLKDMIIRGGENVYPREIEEFLYTHPLIKDVQVVGVPSMKYGE
EVLAYVQLREGVTLTKEEIQDYCRDKIAKYKIPSYVLFIDHYPITASGKIQKYKLREQAI
TALGLENLTKIETA
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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