SitesBLAST
Comparing BPHYT_RS08270 FitnessBrowser__BFirm:BPHYT_RS08270 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)
55% identity, 93% coverage: 39:597/601 of query aligns to 4:556/561 of P69451
- Y213 (= Y250) mutation to A: Loss of activity.
- T214 (= T251) mutation to A: 10% of wild-type activity.
- G216 (= G253) mutation to A: Decreases activity.
- T217 (= T254) mutation to A: Decreases activity.
- G219 (= G256) mutation to A: Decreases activity.
- K222 (= K259) mutation to A: Decreases activity.
- E361 (= E398) mutation to A: Loss of activity.
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, 86% coverage: 76:593/601 of query aligns to 20:496/503 of P9WQ37
- K172 (= K259) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ G285) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ V287) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I299) 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 (≠ S301) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V304) 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 (≠ K336) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G395) 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 (= W474) 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 (= D479) 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 (= R494) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V501) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G503) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K584) 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.
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)
31% identity, 86% coverage: 72:590/601 of query aligns to 44:536/546 of Q84P21
- K530 (= K584) mutation to N: Lossed enzymatic activity.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
30% identity, 86% coverage: 76:593/601 of query aligns to 23:496/502 of 3r44A
Sites not aligning to the query:
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, 85% coverage: 81:591/601 of query aligns to 57:542/559 of Q67W82
- G395 (= G445) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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, 86% coverage: 73:591/601 of query aligns to 54:570/590 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)
31% identity, 86% coverage: 79:592/601 of query aligns to 24:499/506 of 4gxqA
- active site: T163 (= T251), N183 (= N271), H207 (= H298), T303 (= T397), E304 (= E398), I403 (≠ L500), N408 (= N505), A491 (≠ K584)
- binding adenosine-5'-triphosphate: T163 (= T251), S164 (≠ G252), G165 (= G253), T166 (= T254), T167 (= T255), H207 (= H298), S277 (≠ G371), A278 (≠ M372), P279 (≠ A373), E298 (= E392), M302 (≠ L396), T303 (= T397), D382 (= D479), R397 (= R494)
- binding carbonate ion: H207 (= H298), S277 (≠ G371), R299 (≠ G393), G301 (= G395)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
29% identity, 88% coverage: 66:591/601 of query aligns to 26:526/530 of 5bsmA
- active site: S182 (≠ T251), S202 (≠ N271), H230 (= H298), T329 (= T397), E330 (= E398), K434 (≠ L500), Q439 (≠ N505), K519 (= K584)
- binding adenosine-5'-triphosphate: S182 (≠ T251), S183 (≠ G252), G184 (= G253), T185 (= T254), T186 (= T255), K190 (= K259), H230 (= H298), A302 (≠ G371), A303 (≠ M372), P304 (≠ A373), Y326 (= Y394), G327 (= G395), M328 (≠ L396), T329 (= T397), D413 (= D479), I425 (≠ L491), R428 (= R494), K519 (= K584)
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, 88% coverage: 66:591/601 of query aligns to 33:533/542 of O24146
- S189 (≠ T251) binding
- S190 (≠ G252) binding
- G191 (= G253) binding
- T192 (= T254) binding
- T193 (= T255) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K259) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H298) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (= Y300) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ A306) binding ; binding ; binding
- K260 (≠ P322) binding
- A309 (≠ G371) binding ; binding ; binding
- Q331 (≠ E392) binding
- G332 (= G393) binding ; binding ; binding ; binding ; binding
- T336 (= T397) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ I402) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (= M405) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D479) binding ; binding ; binding ; binding ; binding
- R435 (= R494) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K496) binding ; binding ; binding ; binding
- K441 (≠ L500) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S502) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G503) binding
- Q446 (≠ N505) binding
- K526 (= K584) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
29% identity, 88% coverage: 66:591/601 of query aligns to 26:526/529 of 5bsvA
- active site: S182 (≠ T251), S202 (≠ N271), H230 (= H298), T329 (= T397), E330 (= E398), K434 (≠ L500), Q439 (≠ N505), K519 (= K584)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H298), Y232 (= Y300), S236 (≠ A306), A302 (≠ G371), A303 (≠ M372), P304 (≠ A373), G325 (= G393), G327 (= G395), M328 (≠ L396), T329 (= T397), P333 (= P401), V334 (≠ I402), D413 (= D479), K430 (= K496), K434 (≠ L500), Q439 (≠ N505)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
29% identity, 88% coverage: 66:591/601 of query aligns to 26:526/529 of 5bsuA
- active site: S182 (≠ T251), S202 (≠ N271), H230 (= H298), T329 (= T397), E330 (= E398), K434 (≠ L500), Q439 (≠ N505), K519 (= K584)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H298), Y232 (= Y300), S236 (≠ A306), M299 (= M368), A302 (≠ G371), A303 (≠ M372), P304 (≠ A373), G325 (= G393), G327 (= G395), M328 (≠ L396), T329 (= T397), P333 (= P401), D413 (= D479), K430 (= K496), K434 (≠ L500), Q439 (≠ N505)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
29% identity, 88% coverage: 66:591/601 of query aligns to 26:526/529 of 5bstA
- active site: S182 (≠ T251), S202 (≠ N271), H230 (= H298), T329 (= T397), E330 (= E398), K434 (≠ L500), Q439 (≠ N505), K519 (= K584)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H298), Y232 (= Y300), S236 (≠ A306), A302 (≠ G371), A303 (≠ M372), P304 (≠ A373), G325 (= G393), Y326 (= Y394), G327 (= G395), M328 (≠ L396), T329 (= T397), P333 (= P401), V334 (≠ I402), D413 (= D479), K430 (= K496), K434 (≠ L500), Q439 (≠ N505)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
29% identity, 88% coverage: 66:591/601 of query aligns to 25:525/528 of 5bsrA
- active site: S181 (≠ T251), S201 (≠ N271), H229 (= H298), T328 (= T397), E329 (= E398), K433 (≠ L500), Q438 (≠ N505), K518 (= K584)
- binding adenosine monophosphate: A301 (≠ G371), G326 (= G395), T328 (= T397), D412 (= D479), K429 (= K496), K433 (≠ L500), Q438 (≠ N505)
- binding coenzyme a: L102 (= L141), P226 (= P295), H229 (= H298), Y231 (= Y300), F253 (≠ R323), K435 (≠ S502), G436 (= G503), F437 (= F504), F498 (≠ G564)
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)
27% identity, 88% coverage: 66:591/601 of query aligns to 44:547/556 of Q9S725
- K211 (= K259) mutation to S: Drastically reduces the activity.
- M293 (≠ T341) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ M368) mutation K->L,A: Affects the substrate specificity.
- E401 (= E446) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C448) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R494) mutation to Q: Drastically reduces the activity.
- K457 (≠ S502) mutation to S: Drastically reduces the activity.
- K540 (= K584) mutation to N: Abolishes the activity.
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)
29% identity, 87% coverage: 74:597/601 of query aligns to 21:513/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 251:255) binding
- H214 (= H298) binding ; mutation to A: Abolished activity.
- S289 (≠ G371) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ GMA 371:373) binding
- EA 310:311 (≠ EG 392:393) binding
- M314 (≠ L396) binding
- T315 (= T397) binding
- H319 (≠ P401) binding ; mutation to A: Abolished activity.
- D394 (= D479) binding
- R409 (= R494) binding ; mutation to A: Abolished activity.
- K500 (= K584) binding ; binding ; mutation to A: Abolished activity.
5ie2A Crystal structure of a plant enzyme (see paper)
30% identity, 86% coverage: 74:588/601 of query aligns to 21:499/506 of 5ie2A
- active site: T165 (= T251), S185 (≠ N271), H209 (= H298), T310 (= T397), E311 (= E398), N410 (≠ L500), K415 (≠ N505), K495 (= K584)
- binding adenosine-5'-triphosphate: T165 (= T251), S166 (≠ G252), G167 (= G253), T168 (= T254), T169 (= T255), S284 (≠ G371), A285 (≠ M372), S286 (≠ A373), Y307 (= Y394), A308 (≠ G395), M309 (≠ L396), T310 (= T397), D389 (= D479), L401 (= L491), R404 (= R494), K495 (= K584)
5ie3A Crystal structure of a plant enzyme (see paper)
30% identity, 86% coverage: 74:588/601 of query aligns to 21:497/504 of 5ie3A
- active site: T163 (= T251), S183 (≠ N271), H207 (= H298), T308 (= T397), E309 (= E398), N408 (≠ L500), K413 (≠ N505), K493 (= K584)
- binding adenosine monophosphate: S164 (≠ G252), S282 (≠ G371), A283 (≠ M372), S284 (≠ A373), Y305 (= Y394), A306 (≠ G395), M307 (≠ L396), T308 (= T397), D387 (= D479), L399 (= L491), R402 (= R494), K493 (= K584)
- binding oxalic acid: V208 (≠ I299), S282 (≠ G371), A306 (≠ G395), M307 (≠ L396), H312 (≠ P401), K493 (= K584)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
29% identity, 85% coverage: 81:593/601 of query aligns to 40:528/528 of 3ni2A
- active site: S182 (≠ T251), S202 (≠ N271), H230 (= H298), T329 (= T397), E330 (= E398), K434 (≠ L500), Q439 (≠ N505), K519 (= K584)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (= Y300), S236 (≠ A306), G302 (= G371), A303 (≠ M372), P304 (≠ A373), G325 (= G393), G327 (= G395), T329 (= T397), P333 (= P401), V334 (≠ I402), D413 (= D479), K430 (= K496), K434 (≠ L500), Q439 (≠ N505)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
29% identity, 85% coverage: 81:593/601 of query aligns to 40:528/528 of 3a9vA
- active site: S182 (≠ T251), S202 (≠ N271), H230 (= H298), T329 (= T397), E330 (= E398), K434 (≠ L500), Q439 (≠ N505), K519 (= K584)
- binding adenosine monophosphate: H230 (= H298), G302 (= G371), A303 (≠ M372), P304 (≠ A373), Y326 (= Y394), G327 (= G395), M328 (≠ L396), T329 (= T397), D413 (= D479), K430 (= K496), K434 (≠ L500), Q439 (≠ N505)
Q17577 Acyl-CoA synthetase 7; EC 6.2.1.- from Caenorhabditis elegans (see paper)
28% identity, 88% coverage: 73:599/601 of query aligns to 32:537/540 of Q17577
- SS 186:187 (≠ TG 251:252) mutation to AA: Loss of catalytic activity; when associated with A-339.
- E339 (= E398) mutation to A: Severe loss of catalytic activity. Loss of catalytic activity; when associated with 186-A-A-187.
Query Sequence
>BPHYT_RS08270 FitnessBrowser__BFirm:BPHYT_RS08270
MTQPTQTTLAPGGESAAQNTAPAPTQAHAPHHAPNTDGIWYASYPADVPHEIDVSKYESV
VQFFDECIAQFRERVAYVSVGANLTYGELGRKATAFAAYLQSIGVKPGERVAIMLPNTFQ
YPVSLFGVLKAGGVVVNVNPLYTVRELAHQLKDSGAQTIIVFENFAKTVEDALPGTKVQN
VIVTGLGDLLADGLNLKGRLLNFMLRHVKKMVPAYNLPKAVPLLEALSTGYSRPLTPVRP
THDDIAFLQYTGGTTGVAKGAMLTHKNIIANLLQAKAWSEGQLTGEVETVLTPLPLYHIY
SLTVNALIFMGLGGRNILIANPRDMKRVMMIIRHEKFTGMTAVNTLYNAFLDNEEFCKRD
FSDLKLAMAGGMATQKSVAERFKAVTGKPIIEGYGLTECSPIVSMNPVDLSNMRDFEGSI
GLPAPSTQVRFRKDDGSWANIGEAGELCVKGPQVMKGYWNRPDETAKVIDEDGWLATGDI
GVMDSRGFIRLIDRKKDMILVSGFNVYPNEVEDVIAAHPDVREVAAIGVPDAAQGERVKV
FIVKRNPSLTAEQVIAHCRKNLTGYKVPKLVEFRDELPQTNVGKILRRALRDEELAKQKP
A
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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