SitesBLAST
Comparing 5210149 FitnessBrowser__PV4:5210149 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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, 96% coverage: 14:562/574 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)
32% identity, 95% coverage: 17:561/574 of query aligns to 6:551/561 of P69451
- Y213 (≠ F221) mutation to A: Loss of activity.
- T214 (= T222) mutation to A: 10% of wild-type activity.
- G216 (= G224) mutation to A: Decreases activity.
- T217 (= T225) mutation to A: Decreases activity.
- G219 (= G227) mutation to A: Decreases activity.
- K222 (= K230) mutation to A: Decreases activity.
- E361 (= E367) 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)
30% identity, 93% coverage: 31:561/574 of query aligns to 2:495/503 of P9WQ37
- R9 (≠ D38) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D46) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K230) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ G253) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ E255) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C267) 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 (≠ G269) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ L272) 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 (= R304) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G364) 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 (= W442) 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 (= D447) 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 (= R462) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R469) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G471) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K553) 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, 93% coverage: 35:567/574 of query aligns to 40:554/556 of Q9S725
- K211 (= K230) mutation to S: Drastically reduces the activity.
- M293 (≠ H309) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V336) mutation K->L,A: Affects the substrate specificity.
- E401 (= E414) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C416) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R462) mutation to Q: Drastically reduces the activity.
- K457 (≠ G470) mutation to S: Drastically reduces the activity.
- K540 (= K553) mutation to N: Abolishes the activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
29% identity, 91% coverage: 45:569/574 of query aligns to 16:506/506 of 4gxqA
- active site: T163 (= T222), N183 (= N242), H207 (= H266), T303 (= T366), E304 (= E367), I403 (= I468), N408 (= N473), A491 (≠ K553)
- binding adenosine-5'-triphosphate: T163 (= T222), S164 (= S223), G165 (= G224), T166 (= T225), T167 (= T226), H207 (= H266), S277 (≠ G339), A278 (= A340), P279 (≠ T341), E298 (≠ I361), M302 (≠ Q365), T303 (= T366), D382 (= D447), R397 (= R462)
- binding carbonate ion: H207 (= H266), S277 (≠ G339), R299 (≠ G362), G301 (= G364)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
29% identity, 93% coverage: 31:561/574 of query aligns to 5:495/502 of 3r44A
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
29% identity, 90% coverage: 32:547/574 of query aligns to 5:493/504 of 6qjzA
- active site: T169 (= T222), S189 (≠ N242), H213 (= H266), T314 (= T366), E315 (= E367), N414 (≠ I468), K419 (≠ N473)
- binding adenosine monophosphate: H213 (= H266), S288 (≠ G339), A289 (= A340), S290 (≠ T341), A312 (≠ G364), M313 (≠ Q365), T314 (= T366), D393 (= D447), L405 (≠ I459), K410 (= K464), K419 (≠ N473)
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: 31:569/574 of query aligns to 4:512/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 222:226) binding
- H214 (= H266) binding ; mutation to A: Abolished activity.
- S289 (≠ G339) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ GAT 339:341) binding
- EA 310:311 (≠ IG 361:362) binding
- M314 (≠ Q365) binding
- T315 (= T366) binding
- H319 (≠ P370) binding ; mutation to A: Abolished activity.
- D394 (= D447) binding
- R409 (= R462) binding ; mutation to A: Abolished activity.
- K500 (= K553) binding ; binding ; mutation to A: Abolished activity.
6e97B Crystal structure of the aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with dhb-adenylate
29% identity, 94% coverage: 31:567/574 of query aligns to 22:536/537 of 6e97B
- active site: S190 (≠ T222), S210 (≠ N242), H234 (= H266), A336 (≠ T366), E337 (= E367), N437 (≠ I468), K442 (≠ N473), K522 (= K553)
- binding 5'-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine: H234 (= H266), N235 (≠ C267), F236 (= F268), S240 (≠ L272), G310 (= G339), A311 (= A340), K312 (≠ T341), V332 (= V359), F333 (≠ Y363), G334 (= G364), M335 (≠ Q365), A336 (≠ T366), D416 (= D447), K433 (= K464), K442 (≠ N473)
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, 87% coverage: 59:560/574 of query aligns to 53:533/542 of O24146
- S189 (≠ T222) binding
- S190 (= S223) binding
- G191 (= G224) binding
- T192 (= T225) binding
- T193 (= T226) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K230) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H266) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F268) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ L272) binding ; binding ; binding
- K260 (≠ S290) binding
- A309 (≠ G339) binding ; binding ; binding
- Q331 (≠ I361) binding
- G332 (= G362) binding ; binding ; binding ; binding ; binding
- T336 (= T366) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ I371) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (= M374) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D447) binding ; binding ; binding ; binding ; binding
- R435 (= R462) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K464) binding ; binding ; binding ; binding
- K441 (≠ I468) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G470) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G471) binding
- Q446 (≠ N473) binding
- K526 (= K553) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
29% identity, 87% coverage: 59:560/574 of query aligns to 46:526/530 of 5bsmA
- active site: S182 (≠ T222), S202 (≠ A247), H230 (= H266), T329 (= T366), E330 (= E367), K434 (≠ I468), Q439 (≠ N473), K519 (= K553)
- binding adenosine-5'-triphosphate: S182 (≠ T222), S183 (= S223), G184 (= G224), T185 (= T225), T186 (= T226), K190 (= K230), H230 (= H266), A302 (≠ G339), A303 (= A340), P304 (≠ T341), Y326 (= Y363), G327 (= G364), M328 (≠ Q365), T329 (= T366), D413 (= D447), I425 (= I459), R428 (= R462), K519 (= K553)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
29% identity, 87% coverage: 59:560/574 of query aligns to 46:526/529 of 5bsvA
- active site: S182 (≠ T222), S202 (≠ A247), H230 (= H266), T329 (= T366), E330 (= E367), K434 (≠ I468), Q439 (≠ N473), K519 (= K553)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H266), Y232 (≠ F268), S236 (≠ L272), A302 (≠ G339), A303 (= A340), P304 (≠ T341), G325 (= G362), G327 (= G364), M328 (≠ Q365), T329 (= T366), P333 (= P370), V334 (≠ I371), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
29% identity, 87% coverage: 59:560/574 of query aligns to 46:526/529 of 5bsuA
- active site: S182 (≠ T222), S202 (≠ A247), H230 (= H266), T329 (= T366), E330 (= E367), K434 (≠ I468), Q439 (≠ N473), K519 (= K553)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H266), Y232 (≠ F268), S236 (≠ L272), M299 (≠ V336), A302 (≠ G339), A303 (= A340), P304 (≠ T341), G325 (= G362), G327 (= G364), M328 (≠ Q365), T329 (= T366), P333 (= P370), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
29% identity, 87% coverage: 59:560/574 of query aligns to 46:526/529 of 5bstA
- active site: S182 (≠ T222), S202 (≠ A247), H230 (= H266), T329 (= T366), E330 (= E367), K434 (≠ I468), Q439 (≠ N473), K519 (= K553)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H266), Y232 (≠ F268), S236 (≠ L272), A302 (≠ G339), A303 (= A340), P304 (≠ T341), G325 (= G362), Y326 (= Y363), G327 (= G364), M328 (≠ Q365), T329 (= T366), P333 (= P370), V334 (≠ I371), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
29% identity, 88% coverage: 59:563/574 of query aligns to 45:528/528 of 5bsrA
- active site: S181 (≠ T222), S201 (≠ A247), H229 (= H266), T328 (= T366), E329 (= E367), K433 (≠ I468), Q438 (≠ N473), K518 (= K553)
- binding adenosine monophosphate: A301 (≠ G339), G326 (= G364), T328 (= T366), D412 (= D447), K429 (= K464), K433 (≠ I468), Q438 (≠ N473)
- binding coenzyme a: L102 (≠ A116), P226 (= P263), H229 (= H266), Y231 (≠ F268), F253 (= F291), K435 (≠ G470), G436 (= G471), F437 (≠ E472), F498 (≠ Y533)
5ie2A Crystal structure of a plant enzyme (see paper)
28% identity, 92% coverage: 31:556/574 of query aligns to 4:498/506 of 5ie2A
- active site: T165 (= T222), S185 (≠ N242), H209 (= H266), T310 (= T366), E311 (= E367), N410 (≠ I468), K415 (≠ N473), K495 (= K553)
- binding adenosine-5'-triphosphate: T165 (= T222), S166 (= S223), G167 (= G224), T168 (= T225), T169 (= T226), S284 (≠ G339), A285 (= A340), S286 (≠ T341), Y307 (= Y363), A308 (≠ G364), M309 (≠ Q365), T310 (= T366), D389 (= D447), L401 (≠ I459), R404 (= R462), K495 (= K553)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
28% identity, 92% coverage: 36:561/574 of query aligns to 23:527/528 of 3ni2A
- active site: S182 (≠ T222), S202 (≠ A247), H230 (= H266), T329 (= T366), E330 (= E367), K434 (≠ I468), Q439 (≠ N473), K519 (= K553)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F268), S236 (≠ L272), G302 (= G339), A303 (= A340), P304 (≠ T341), G325 (= G362), G327 (= G364), T329 (= T366), P333 (= P370), V334 (≠ I371), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
28% identity, 92% coverage: 36:561/574 of query aligns to 23:527/528 of 3a9vA
- active site: S182 (≠ T222), S202 (≠ A247), H230 (= H266), T329 (= T366), E330 (= E367), K434 (≠ I468), Q439 (≠ N473), K519 (= K553)
- binding adenosine monophosphate: H230 (= H266), G302 (= G339), A303 (= A340), P304 (≠ T341), Y326 (= Y363), G327 (= G364), M328 (≠ Q365), T329 (= T366), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
5wm6A Crystal structure of cahj in complex with benzoyl adenylate (see paper)
28% identity, 91% coverage: 37:559/574 of query aligns to 33:530/535 of 5wm6A
- active site: S193 (≠ T222), N213 (= N242), H237 (= H266), A336 (≠ T366), E337 (= E367), N437 (≠ I468), K442 (≠ N473), K524 (= K553)
- binding magnesium ion: S301 (= S330), L303 (= L332), G326 (vs. gap)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: F239 (= F268), G310 (= G339), S311 (≠ A340), K312 (≠ T341), V332 (= V359), F333 (≠ Y363), G334 (= G364), M335 (≠ Q365), A336 (≠ T366), D416 (= D447), K433 (= K464), K442 (≠ N473)
5wm2A Crystal structure of cahj in complex with salicylic acid and amp (see paper)
28% identity, 91% coverage: 37:559/574 of query aligns to 33:530/536 of 5wm2A
- active site: S193 (≠ T222), N213 (= N242), H237 (= H266), A336 (≠ T366), E337 (= E367), N437 (≠ I468), K442 (≠ N473), K524 (= K553)
- binding adenosine monophosphate: G310 (= G339), S311 (≠ A340), K312 (≠ T341), V332 (= V359), F333 (≠ Y363), G334 (= G364), M335 (≠ Q365), A336 (≠ T366), E337 (= E367), D416 (= D447), V428 (≠ I459), K433 (= K464), K442 (≠ N473)
Query Sequence
>5210149 FitnessBrowser__PV4:5210149
MSAVTTFATENQFPLQLSQFDGDTSTPLIEQTIGDYLDQMAASHPDQLAIVMHHQGIRWS
YQEYQSHIDELAAGLLAIGIKPGDRVGIWSPNNIEWCLTQFATAKIGAIMVCINPAYRPE
ELQYALNNVGCRAIICAEKFKSSHYLSMLYELAPELKQCLPGQLESANLPSLEFVIRMGD
EASPGMLNFNHLKRPLTESDRKALKDTAAQLSPFDAINIQFTSGTTGSPKGATLSHHNIL
NNGLLVAKAMRLGLEDRLCIPVPLYHCFGMVLGNLSCISVGASAIYPSDSFDPLTTLEVV
EAERCTALHGVPTMFIAQLEHPEFKRFDLSSLRTGVMAGATCPEEVMRRVQDLMYMKEVL
IGYGQTECSPINNMTEIGSSLEKRVTTVGRALAHTQVKIVDEFGEVLPVGQPGEVCSRGY
CVMQFYWNDAEKTAATIDSEGWLHSGDLGEMDSEGYVKIVGRIKDMIIRGGENIYPREIE
EKLYTHPDVQDAAIFGVKSEKYGEEVCAWIKVQPGASVTEEEIRHFLTEKFAYFKVPRYI
KFVEQYPMTVTGKIQKFKMREMMYQELYEAINCN
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