SitesBLAST
Comparing 7025315 FitnessBrowser__ANA3:7025315 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, 96% coverage: 15:563/574 of query aligns to 20:572/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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, 93% coverage: 28:562/574 of query aligns to 27:551/561 of P69451
- Y213 (≠ F222) mutation to A: Loss of activity.
- T214 (= T223) mutation to A: 10% of wild-type activity.
- G216 (= G225) mutation to A: Decreases activity.
- T217 (= T226) mutation to A: Decreases activity.
- G219 (= G228) mutation to A: Decreases activity.
- K222 (= K231) mutation to A: Decreases activity.
- E361 (= E368) 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, 93% coverage: 32:562/574 of query aligns to 2:495/503 of P9WQ37
- R9 (≠ N39) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ E47) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K231) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T254) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ E256) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C268) 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 (≠ V272) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ N275) 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 (= R305) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G365) 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 (= W443) 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 (= D448) 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 (= R463) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R470) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G472) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K554) 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)
29% identity, 91% coverage: 46:570/574 of query aligns to 16:506/506 of 4gxqA
- active site: T163 (= T223), N183 (= N243), H207 (= H267), T303 (= T367), E304 (= E368), I403 (= I469), N408 (= N474), A491 (≠ K554)
- binding adenosine-5'-triphosphate: T163 (= T223), S164 (= S224), G165 (= G225), T166 (= T226), T167 (= T227), H207 (= H267), S277 (≠ G340), A278 (= A341), P279 (≠ T342), E298 (≠ I362), M302 (≠ Q366), T303 (= T367), D382 (= D448), R397 (= R463)
- binding carbonate ion: H207 (= H267), S277 (≠ G340), R299 (≠ G363), G301 (= G365)
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, 85% coverage: 72:561/574 of query aligns to 76:547/556 of Q9S725
- K211 (= K231) mutation to S: Drastically reduces the activity.
- M293 (≠ H310) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V337) mutation K->L,A: Affects the substrate specificity.
- E401 (= E415) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C417) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R463) mutation to Q: Drastically reduces the activity.
- K457 (≠ G471) mutation to S: Drastically reduces the activity.
- K540 (= K554) mutation to N: Abolishes the activity.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
30% identity, 93% coverage: 32:562/574 of query aligns to 5:495/502 of 3r44A
6e97B Crystal structure of the aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with dhb-adenylate
29% identity, 94% coverage: 32:568/574 of query aligns to 22:536/537 of 6e97B
- active site: S190 (≠ T223), S210 (≠ N243), H234 (= H267), A336 (≠ T367), E337 (= E368), N437 (≠ I469), K442 (≠ N474), K522 (= K554)
- binding 5'-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine: H234 (= H267), N235 (≠ C268), F236 (= F269), S240 (≠ L273), G310 (= G340), A311 (= A341), K312 (≠ T342), V332 (= V360), F333 (≠ Y364), G334 (= G365), M335 (≠ Q366), A336 (≠ T367), D416 (= D448), K433 (= K465), K442 (≠ N474)
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, 94% coverage: 33:570/574 of query aligns to 5:512/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 223:227) binding
- H214 (= H267) binding ; mutation to A: Abolished activity.
- S289 (≠ G340) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ GAT 340:342) binding
- EA 310:311 (≠ IG 362:363) binding
- M314 (≠ Q366) binding
- T315 (= T367) binding
- H319 (≠ P371) binding ; mutation to A: Abolished activity.
- D394 (= D448) binding
- R409 (= R463) binding ; mutation to A: Abolished activity.
- K500 (= K554) binding ; binding ; mutation to A: Abolished activity.
5ie2A Crystal structure of a plant enzyme (see paper)
30% identity, 91% coverage: 33:557/574 of query aligns to 5:498/506 of 5ie2A
- active site: T165 (= T223), S185 (≠ N243), H209 (= H267), T310 (= T367), E311 (= E368), N410 (≠ I469), K415 (≠ N474), K495 (= K554)
- binding adenosine-5'-triphosphate: T165 (= T223), S166 (= S224), G167 (= G225), T168 (= T226), T169 (= T227), S284 (≠ G340), A285 (= A341), S286 (≠ T342), Y307 (= Y364), A308 (≠ G365), M309 (≠ Q366), T310 (= T367), D389 (= D448), L401 (≠ I460), R404 (= R463), K495 (= K554)
6e8oA Crystal structure of aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with amp
29% identity, 94% coverage: 32:568/574 of query aligns to 22:535/536 of 6e8oA
- active site: S190 (≠ T223), S210 (≠ N243), H234 (= H267), A336 (≠ T367), E337 (= E368), N437 (≠ I469), K442 (≠ N474), K521 (= K554)
- binding adenosine monophosphate: H234 (= H267), G310 (= G340), A311 (= A341), K312 (≠ T342), V332 (= V360), F333 (≠ Y364), G334 (= G365), M335 (≠ Q366), A336 (≠ T367), D416 (= D448), V428 (≠ I460), K442 (≠ N474)
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: 73:561/574 of query aligns to 73:542/559 of Q67W82
- G395 (= G414) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
5ie3A Crystal structure of a plant enzyme (see paper)
30% identity, 91% coverage: 33:557/574 of query aligns to 5:496/504 of 5ie3A
- active site: T163 (= T223), S183 (≠ N243), H207 (= H267), T308 (= T367), E309 (= E368), N408 (≠ I469), K413 (≠ N474), K493 (= K554)
- binding adenosine monophosphate: S164 (= S224), S282 (≠ G340), A283 (= A341), S284 (≠ T342), Y305 (= Y364), A306 (≠ G365), M307 (≠ Q366), T308 (= T367), D387 (= D448), L399 (≠ I460), R402 (= R463), K493 (= K554)
- binding oxalic acid: V208 (≠ C268), S282 (≠ G340), A306 (≠ G365), M307 (≠ Q366), H312 (≠ P371), K493 (= K554)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
29% identity, 89% coverage: 52:561/574 of query aligns to 45:526/530 of 5bsmA
- active site: S182 (≠ T223), S202 (≠ N243), H230 (= H267), T329 (= T367), E330 (= E368), K434 (≠ I469), Q439 (≠ N474), K519 (= K554)
- binding adenosine-5'-triphosphate: S182 (≠ T223), S183 (= S224), G184 (= G225), T185 (= T226), T186 (= T227), K190 (= K231), H230 (= H267), A302 (≠ G340), A303 (= A341), P304 (≠ T342), Y326 (= Y364), G327 (= G365), M328 (≠ Q366), T329 (= T367), D413 (= D448), I425 (= I460), R428 (= R463), K519 (= K554)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
29% identity, 89% coverage: 52:561/574 of query aligns to 44:525/528 of 5bsrA
- active site: S181 (≠ T223), S201 (≠ N243), H229 (= H267), T328 (= T367), E329 (= E368), K433 (≠ I469), Q438 (≠ N474), K518 (= K554)
- binding adenosine monophosphate: A301 (≠ G340), G326 (= G365), T328 (= T367), D412 (= D448), K429 (= K465), K433 (≠ I469), Q438 (≠ N474)
- binding coenzyme a: L102 (≠ A117), P226 (= P264), H229 (= H267), Y231 (≠ F269), F253 (= F292), K435 (≠ G471), G436 (= G472), F437 (≠ E473), F498 (≠ Y534)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
29% identity, 89% coverage: 52:561/574 of query aligns to 45:526/529 of 5bsvA
- active site: S182 (≠ T223), S202 (≠ N243), H230 (= H267), T329 (= T367), E330 (= E368), K434 (≠ I469), Q439 (≠ N474), K519 (= K554)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H267), Y232 (≠ F269), S236 (≠ G274), A302 (≠ G340), A303 (= A341), P304 (≠ T342), G325 (= G363), G327 (= G365), M328 (≠ Q366), T329 (= T367), P333 (= P371), V334 (≠ L372), D413 (= D448), K430 (= K465), K434 (≠ I469), Q439 (≠ N474)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
29% identity, 89% coverage: 52:561/574 of query aligns to 45:526/529 of 5bsuA
- active site: S182 (≠ T223), S202 (≠ N243), H230 (= H267), T329 (= T367), E330 (= E368), K434 (≠ I469), Q439 (≠ N474), K519 (= K554)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H267), Y232 (≠ F269), S236 (≠ G274), M299 (≠ V337), A302 (≠ G340), A303 (= A341), P304 (≠ T342), G325 (= G363), G327 (= G365), M328 (≠ Q366), T329 (= T367), P333 (= P371), D413 (= D448), K430 (= K465), K434 (≠ I469), Q439 (≠ N474)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
29% identity, 89% coverage: 52:561/574 of query aligns to 45:526/529 of 5bstA
- active site: S182 (≠ T223), S202 (≠ N243), H230 (= H267), T329 (= T367), E330 (= E368), K434 (≠ I469), Q439 (≠ N474), K519 (= K554)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H267), Y232 (≠ F269), S236 (≠ G274), A302 (≠ G340), A303 (= A341), P304 (≠ T342), G325 (= G363), Y326 (= Y364), G327 (= G365), M328 (≠ Q366), T329 (= T367), P333 (= P371), V334 (≠ L372), D413 (= D448), K430 (= K465), K434 (≠ I469), Q439 (≠ N474)
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, 89% coverage: 52:561/574 of query aligns to 52:533/542 of O24146
- S189 (≠ T223) binding
- S190 (= S224) binding
- G191 (= G225) binding
- T192 (= T226) binding
- T193 (= T227) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K231) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H267) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F269) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ G274) binding ; binding ; binding
- K260 (≠ S291) binding
- A309 (≠ G340) binding ; binding ; binding
- Q331 (≠ I362) binding
- G332 (= G363) binding ; binding ; binding ; binding ; binding
- T336 (= T367) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ L372) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (vs. gap) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D448) binding ; binding ; binding ; binding ; binding
- R435 (= R463) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K465) binding ; binding ; binding ; binding
- K441 (≠ I469) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G471) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G472) binding
- Q446 (≠ N474) binding
- K526 (= K554) binding ; mutation to A: Abolished activity against 4-coumarate.
5wm2A Crystal structure of cahj in complex with salicylic acid and amp (see paper)
28% identity, 92% coverage: 32:560/574 of query aligns to 27:530/536 of 5wm2A
- active site: S193 (≠ T223), N213 (= N243), H237 (= H267), A336 (≠ T367), E337 (= E368), N437 (≠ I469), K442 (≠ N474), K524 (= K554)
- binding adenosine monophosphate: G310 (= G340), S311 (≠ A341), K312 (≠ T342), V332 (= V360), F333 (≠ Y364), G334 (= G365), M335 (≠ Q366), A336 (≠ T367), E337 (= E368), D416 (= D448), V428 (≠ I460), K433 (= K465), K442 (≠ N474)
5wm3A Crystal structure of cahj in complex with salicyl adenylate (see paper)
29% identity, 92% coverage: 32:560/574 of query aligns to 27:530/537 of 5wm3A
- active site: S193 (≠ T223), N213 (= N243), H237 (= H267), A336 (≠ T367), E337 (= E368), N437 (≠ I469), K442 (≠ N474), K524 (= K554)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxybenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: N238 (≠ C268), F239 (= F269), G310 (= G340), S311 (≠ A341), K312 (≠ T342), V332 (= V360), F333 (≠ Y364), G334 (= G365), M335 (≠ Q366), A336 (≠ T367), D416 (= D448), K433 (= K465), K442 (≠ N474)
- binding magnesium ion: S301 (= S331), L303 (= L333), G326 (vs. gap)
Query Sequence
>7025315 FitnessBrowser__ANA3:7025315
MSVSTTQATNQATHPLKYSEFRGPNSPELVEKTIGQYLNDIANVYPEQLAVVVNHQDIRW
NYRQYLAQIDALATGLLKLGIGPGDRVGIWSPNNIEWCLTQFATAKIGAIMVCINPAYRP
EELQYALTNVGCRAVICADKFKSSNYLQMLYELAPELKVCAAGQLQAKALPDLQFVIRMG
AEQSPGMLNFDDLLVEVTADDKAALERIAESLSPYDAINIQFTSGTTGSPKGATLSHHNI
LNNGYLVAEAMKFTCEDKLCIPVPLYHCFGMVLGNLVCLAKGAAAVFPGDSFDPLTTLEV
VERERCTALHGVPTMFIAELEHPEFKRFDLSSLRTGVMAGATCPEEVMRRVQNLMYMQEV
LIGYGQTECSPLNHITEIDSPVEKRVLTVGRALPHTEVKIVDEFGEVLPINTPGEVCSRG
YCIMQCYWNDPEKTAATIDSEGWLHSGDIGQMDEQGYVQIVGRIKDMIIRGGENIYPREI
EEKLYTHKDVQDAAVFGVHSDKYGEEVCAWIKIRSGATISEEDIRHFLTEKFAYFKVPRY
IKFVEQYPMTVTGKIQKFKMRELMYQELYEDINA
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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