SitesBLAST
Comparing WP_011734419.1 NCBI__GCF_000015045.1:WP_011734419.1 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)
39% identity, 95% coverage: 11:548/568 of query aligns to 36:577/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
32% identity, 89% coverage: 39:542/568 of query aligns to 28:499/506 of 4gxqA
- active site: T163 (= T203), N183 (= N223), H207 (= H247), T303 (= T346), E304 (= E347), I403 (= I449), N408 (= N454), A491 (≠ K534)
- binding adenosine-5'-triphosphate: T163 (= T203), S164 (= S204), G165 (= G205), T166 (= T206), T167 (= T207), H207 (= H247), S277 (≠ G319), A278 (≠ S320), P279 (= P321), E298 (≠ I341), M302 (≠ L345), T303 (= T346), D382 (= D428), R397 (= R443)
- binding carbonate ion: H207 (= H247), S277 (≠ G319), R299 (≠ A342), G301 (= G344)
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)
30% identity, 86% coverage: 58:544/568 of query aligns to 68:553/561 of P69451
- Y213 (= Y202) mutation to A: Loss of activity.
- T214 (= T203) mutation to A: 10% of wild-type activity.
- G216 (= G205) mutation to A: Decreases activity.
- T217 (= T206) mutation to A: Decreases activity.
- G219 (= G208) mutation to A: Decreases activity.
- K222 (= K211) mutation to A: Decreases activity.
- E361 (= E347) mutation to A: Loss of 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)
29% identity, 96% coverage: 10:552/568 of query aligns to 30:553/559 of Q67W82
- G395 (= G394) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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)
28% identity, 93% coverage: 13:542/568 of query aligns to 3:495/503 of P9WQ37
- R9 (≠ D19) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D27) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K211) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T234) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ M236) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C248) 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 (≠ G250) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ L253) 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 (≠ K284) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G344) 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 (= W423) 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 (= D428) 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 (= R443) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R450) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G452) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K534) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
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, 92% coverage: 23:546/568 of query aligns to 50:552/556 of Q9S725
- K211 (= K211) mutation to S: Drastically reduces the activity.
- M293 (≠ Y289) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I316) mutation K->L,A: Affects the substrate specificity.
- E401 (= E395) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ I397) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R443) mutation to Q: Drastically reduces the activity.
- K457 (≠ G451) mutation to S: Drastically reduces the activity.
- K540 (= K534) mutation to N: Abolishes the activity.
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)
30% identity, 87% coverage: 49:544/568 of query aligns to 67:540/546 of Q84P21
- K530 (= K534) mutation to N: Lossed enzymatic activity.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
27% identity, 93% coverage: 13:542/568 of query aligns to 6:495/502 of 3r44A
Sites not aligning to the query:
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)
27% identity, 91% coverage: 30:547/568 of query aligns to 43:540/542 of O24146
- S189 (≠ T203) binding ATP
- S190 (= S204) binding ATP
- G191 (= G205) binding ATP
- T192 (= T206) binding ATP
- T193 (= T207) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K211) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H247) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F249) 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 (≠ L253) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ I270) binding CoA
- A309 (≠ G319) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ I341) binding ATP
- G332 (≠ A342) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T346) 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 (= V351) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ Q354) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D428) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R443) 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 (= K445) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ I449) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G451) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G452) binding CoA
- Q446 (≠ N454) binding AMP
- K526 (= K534) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
27% identity, 91% coverage: 30:545/568 of query aligns to 36:530/530 of 5bsmA
- active site: S182 (≠ T203), S202 (vs. gap), H230 (= H247), T329 (= T346), E330 (= E347), K434 (≠ I449), Q439 (≠ N454), K519 (= K534)
- binding adenosine-5'-triphosphate: S182 (≠ T203), S183 (= S204), G184 (= G205), T185 (= T206), T186 (= T207), K190 (= K211), H230 (= H247), A302 (≠ G319), A303 (≠ S320), P304 (= P321), Y326 (= Y343), G327 (= G344), M328 (≠ L345), T329 (= T346), D413 (= D428), I425 (≠ V440), R428 (= R443), K519 (= K534)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
27% identity, 90% coverage: 30:541/568 of query aligns to 36:526/529 of 5bsvA
- active site: S182 (≠ T203), S202 (vs. gap), H230 (= H247), T329 (= T346), E330 (= E347), K434 (≠ I449), Q439 (≠ N454), K519 (= K534)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H247), Y232 (≠ F249), S236 (≠ L253), A302 (≠ G319), A303 (≠ S320), P304 (= P321), G325 (≠ A342), G327 (= G344), M328 (≠ L345), T329 (= T346), P333 (= P350), V334 (= V351), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
27% identity, 90% coverage: 30:541/568 of query aligns to 36:526/529 of 5bsuA
- active site: S182 (≠ T203), S202 (vs. gap), H230 (= H247), T329 (= T346), E330 (= E347), K434 (≠ I449), Q439 (≠ N454), K519 (= K534)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H247), Y232 (≠ F249), S236 (≠ L253), M299 (≠ I316), A302 (≠ G319), A303 (≠ S320), P304 (= P321), G325 (≠ A342), G327 (= G344), M328 (≠ L345), T329 (= T346), P333 (= P350), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
27% identity, 90% coverage: 30:541/568 of query aligns to 36:526/529 of 5bstA
- active site: S182 (≠ T203), S202 (vs. gap), H230 (= H247), T329 (= T346), E330 (= E347), K434 (≠ I449), Q439 (≠ N454), K519 (= K534)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H247), Y232 (≠ F249), S236 (≠ L253), A302 (≠ G319), A303 (≠ S320), P304 (= P321), G325 (≠ A342), Y326 (= Y343), G327 (= G344), M328 (≠ L345), T329 (= T346), P333 (= P350), V334 (= V351), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
27% identity, 90% coverage: 30:541/568 of query aligns to 35:525/528 of 5bsrA
- active site: S181 (≠ T203), S201 (vs. gap), H229 (= H247), T328 (= T346), E329 (= E347), K433 (≠ I449), Q438 (≠ N454), K518 (= K534)
- binding adenosine monophosphate: A301 (≠ G319), G326 (= G344), T328 (= T346), D412 (= D428), K429 (= K445), K433 (≠ I449), Q438 (≠ N454)
- binding coenzyme a: L102 (≠ V97), P226 (= P244), H229 (= H247), Y231 (≠ F249), F253 (= F271), K435 (≠ G451), G436 (= G452), F437 (≠ E453), F498 (≠ R514)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
26% identity, 94% coverage: 11:542/568 of query aligns to 17:527/528 of 3ni2A
- active site: S182 (≠ T203), S202 (≠ N223), H230 (= H247), T329 (= T346), E330 (= E347), K434 (≠ I449), Q439 (≠ N454), K519 (= K534)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F249), S236 (≠ L253), G302 (= G319), A303 (≠ S320), P304 (= P321), G325 (≠ A342), G327 (= G344), T329 (= T346), P333 (= P350), V334 (= V351), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
26% identity, 94% coverage: 11:542/568 of query aligns to 17:527/528 of 3a9vA
- active site: S182 (≠ T203), S202 (≠ N223), H230 (= H247), T329 (= T346), E330 (= E347), K434 (≠ I449), Q439 (≠ N454), K519 (= K534)
- binding adenosine monophosphate: H230 (= H247), G302 (= G319), A303 (≠ S320), P304 (= P321), Y326 (= Y343), G327 (= G344), M328 (≠ L345), T329 (= T346), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
7kydA Drosophila melanogaster long-chain fatty-acyl-coa synthetase cg6178 (see paper)
28% identity, 93% coverage: 13:543/568 of query aligns to 25:532/534 of 7kydA
- binding 5'-O-[(S)-hydroxy(octanoyloxy)phosphoryl]adenosine: H240 (= H247), F242 (= F249), A311 (≠ G319), A312 (≠ S320), P313 (= P321), G334 (≠ A342), Y335 (= Y343), G336 (= G344), L337 (= L345), S338 (≠ T346), S343 (≠ P350), D416 (= D428), I428 (≠ V440)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
27% identity, 91% coverage: 30:545/568 of query aligns to 35:526/527 of 5u95B
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
27% identity, 87% coverage: 52:543/568 of query aligns to 61:536/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H247), F245 (= F249), T249 (≠ G254), G314 (= G319), A315 (≠ S320), P316 (= P321), G337 (≠ A342), Y338 (= Y343), G339 (= G344), L340 (= L345), T341 (= T346), A346 (≠ V351), D420 (= D428), I432 (≠ V440), K527 (= K534)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
27% identity, 87% coverage: 52:543/568 of query aligns to 61:536/539 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 (= H247), F245 (= F249), T249 (≠ G254), G314 (= G319), A315 (≠ S320), P316 (= P321), G337 (≠ A342), Y338 (= Y343), G339 (= G344), L340 (= L345), T341 (= T346), S345 (≠ P350), A346 (≠ V351), D420 (= D428), I432 (≠ V440), K527 (= K534)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F249), R335 (≠ T340), G337 (≠ A342), G339 (= G344), L340 (= L345), A346 (≠ V351)
Query Sequence
>WP_011734419.1 NCBI__GCF_000015045.1:WP_011734419.1
MTKTFKGPFSDLTIGQYFDTVVAAQPDHDCIIYPDRNLRWSWGQFNARVDALAKGLLAIG
LEKGDHLGMWARNVPDWLTFMFATAKIGVVFVTVNPVYKSHELAYVLTQSDMKALCIIDS
FRDVDYVSIVRELVPEAATQERGHLDSAQFPFLKKLIYMGPEKHRGFYTVPELLLLGEHY
SDDDYAAAREGLVADDVINMQYTSGTTGFPKGVMLSSRNILNNGYYIGERQKFTKMDRIC
LPVPLFHCFGCVLGVMAMLTHGSTLVMLEIFDPLMALAAVQKEKCTAIYGVPTMFIAELT
HPMFPLFDTSSLRTGIMAGSPCPIETMKQVMSDMHASEITIAYGLTEGSPVFIQTSTDDT
IERRCETIGTAMPEIEVRVVDPETGQDCPPGVPGELICRGYNVMKGYYKMPEQTAAAIDA
AGWLHSGDLGTVDEHGYYRVTGRIKDMIIRGGENIYPREIEEFLYTMPGVKDVQIVGVPD
EKYGEVVGAFVMRSKGSDISEEDVREFAQTRIARYKCPRHVWFVEEFPMTASNKIQKYKL
REMAAELLGVSDVKVFAGEAAEKGGTDA
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