SitesBLAST
Comparing SMc00261 FitnessBrowser__Smeli:SMc00261 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)
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)
33% identity, 93% coverage: 19:527/549 of query aligns to 3:496/503 of P9WQ37
- R9 (≠ S25) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D33) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K191) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T216) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R218) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ G230) 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 (≠ G232) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ Q235) 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 (= R266) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G325) 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 (= W407) 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 (= D412) 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 (= R427) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S434) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G436) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K518) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
33% identity, 93% coverage: 16:527/549 of query aligns to 3:496/502 of 3r44A
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)
31% identity, 89% coverage: 43:531/549 of query aligns to 64:580/590 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, 95% coverage: 16:535/549 of query aligns to 21:558/561 of P69451
- Y213 (= Y182) mutation to A: Loss of activity.
- T214 (= T183) mutation to A: 10% of wild-type activity.
- G216 (= G185) mutation to A: Decreases activity.
- T217 (= T186) mutation to A: Decreases activity.
- G219 (= G188) mutation to A: Decreases activity.
- K222 (= K191) mutation to A: Decreases activity.
- E361 (= E328) mutation to A: Loss of activity.
5x8fB Ternary complex structure of a double mutant i454ra456k of o- succinylbenzoate coa synthetase (mene) from bacillus subtilis bound with amp and its product analogue osb-ncoa at 1.76 angstrom (see paper)
30% identity, 93% coverage: 22:534/549 of query aligns to 6:484/485 of 5x8fB
- active site: T151 (= T183), S171 (≠ V203), H195 (= H229), T288 (≠ G327), E289 (= E328), I387 (= I433), N392 (= N438), K470 (= K522)
- binding magnesium ion: Y23 (≠ H39), E24 (≠ G40), H70 (≠ F87), N178 (≠ D210), L202 (= L236), L214 (= L247), T296 (≠ V335), L297 (= L336), S298 (≠ P337)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R102), L191 (≠ A225), P192 (= P226), H195 (= H229), I196 (≠ G230), S197 (≠ A231), A237 (= A272), V238 (= V273), L260 (≠ I298), G262 (≠ A300), G286 (= G325), M287 (≠ L326), S292 (≠ G331), Q293 (≠ A332), S388 (= S434), G389 (= G435), G390 (= G436), E391 (≠ S437), K420 (≠ V466), W421 (= W467), K450 (≠ R498), Y451 (= Y499)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
30% identity, 93% coverage: 22:534/549 of query aligns to 6:484/484 of 5gtdA
- active site: T151 (= T183), S171 (≠ V203), H195 (= H229), T288 (≠ G327), E289 (= E328)
- binding adenosine-5'-monophosphate: G263 (= G301), G264 (≠ A302), Y285 (≠ F324), G286 (= G325), M287 (≠ L326), T288 (≠ G327), D366 (= D412), V378 (≠ I424)
- binding magnesium ion: F314 (≠ T359), S315 (≠ G360)
- binding 2-succinylbenzoate: H195 (= H229), S197 (≠ A231), A237 (= A272), L260 (≠ I298), G262 (≠ A300), G263 (= G301), G286 (= G325), M287 (≠ L326), S292 (≠ G331), Q293 (≠ A332)
5ie2A Crystal structure of a plant enzyme (see paper)
28% identity, 93% coverage: 19:528/549 of query aligns to 5:505/506 of 5ie2A
- active site: T165 (= T183), S185 (≠ V203), H209 (= H229), T310 (≠ G327), E311 (= E328), N410 (≠ I433), K415 (≠ N438), K495 (= K518)
- binding adenosine-5'-triphosphate: T165 (= T183), S166 (= S184), G167 (= G185), T168 (= T186), T169 (= T187), S284 (≠ G301), A285 (= A302), S286 (≠ P303), Y307 (≠ F324), A308 (≠ G325), M309 (≠ L326), T310 (≠ G327), D389 (= D412), L401 (≠ I424), R404 (= R427), K495 (= K518)
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)
28% identity, 93% coverage: 19:528/549 of query aligns to 5:510/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 183:187) binding
- H214 (= H229) binding ; mutation to A: Abolished activity.
- S289 (≠ G301) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ GAP 301:303) binding
- EA 310:311 (≠ QY 322:323) binding
- M314 (≠ L326) binding
- T315 (≠ G327) binding
- H319 (≠ G331) binding ; mutation to A: Abolished activity.
- D394 (= D412) binding
- R409 (= R427) binding ; mutation to A: Abolished activity.
- K500 (= K518) binding ; binding ; mutation to A: Abolished activity.
5ie3A Crystal structure of a plant enzyme (see paper)
28% identity, 93% coverage: 19:528/549 of query aligns to 5:503/504 of 5ie3A
- active site: T163 (= T183), S183 (≠ V203), H207 (= H229), T308 (≠ G327), E309 (= E328), N408 (≠ I433), K413 (≠ N438), K493 (= K518)
- binding adenosine monophosphate: S164 (= S184), S282 (≠ G301), A283 (= A302), S284 (≠ P303), Y305 (≠ F324), A306 (≠ G325), M307 (≠ L326), T308 (≠ G327), D387 (= D412), L399 (≠ I424), R402 (= R427), K493 (= K518)
- binding oxalic acid: V208 (vs. gap), S282 (≠ G301), A306 (≠ G325), M307 (≠ L326), H312 (≠ G331), K493 (= K518)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
30% identity, 93% coverage: 22:534/549 of query aligns to 5:481/481 of 5busA
- active site: T150 (= T183), S170 (≠ V203), H194 (= H229), T287 (≠ G327), E288 (= E328)
- binding adenosine monophosphate: H194 (= H229), G262 (= G301), G263 (≠ A302), S283 (≠ Y323), M286 (≠ L326), T287 (≠ G327), D365 (= D412), V377 (≠ I424), R380 (= R427), K467 (= K522)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
29% identity, 92% coverage: 22:526/549 of query aligns to 5:475/475 of 5burA
- active site: T150 (= T183), S170 (≠ V203), H194 (= H229), T287 (≠ G327), E288 (= E328)
- binding adenosine-5'-triphosphate: T150 (= T183), S151 (= S184), T153 (= T186), T154 (= T187), K158 (= K191), G263 (≠ A302), S283 (≠ Y323), T287 (≠ G327), D365 (= D412), V377 (≠ I424), R380 (= R427)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 90% coverage: 31:526/549 of query aligns to 15:499/506 of 4gxqA
- active site: T163 (= T183), N183 (= N205), H207 (= H229), T303 (≠ G327), E304 (= E328), I403 (= I433), N408 (= N438), A491 (≠ K518)
- binding adenosine-5'-triphosphate: T163 (= T183), S164 (= S184), G165 (= G185), T166 (= T186), T167 (= T187), H207 (= H229), S277 (≠ G301), A278 (= A302), P279 (= P303), E298 (≠ Q322), M302 (≠ L326), T303 (≠ G327), D382 (= D412), R397 (= R427)
- binding carbonate ion: H207 (= H229), S277 (≠ G301), R299 (≠ Y323), G301 (= G325)
O74976 Oxalate--CoA ligase; Oxalyl-CoA synthetase; Peroxisomal-coenzyme A synthetase; EC 6.2.1.8 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
30% identity, 89% coverage: 36:524/549 of query aligns to 18:500/512 of O74976
- S283 (≠ G301) modified: Phosphoserine
- S284 (≠ A302) modified: Phosphoserine
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, 90% coverage: 36:528/549 of query aligns to 43:536/542 of O24146
- S189 (≠ T183) binding
- S190 (= S184) binding
- G191 (= G185) binding
- T192 (= T186) binding
- T193 (= T187) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K191) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H229) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ A231) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ Q235) binding ; binding ; binding
- K260 (= K252) binding
- A309 (≠ G301) binding ; binding ; binding
- Q331 (= Q322) binding
- G332 (≠ Y323) binding ; binding ; binding ; binding ; binding
- T336 (≠ G327) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ I333) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ L336) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D412) binding ; binding ; binding ; binding ; binding
- R435 (= R427) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (≠ S429) binding ; binding ; binding ; binding
- K441 (≠ I433) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G435) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G436) binding
- Q446 (≠ N438) binding
- K526 (= K518) 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, 90% coverage: 36:528/549 of query aligns to 36:529/530 of 5bsmA
- active site: S182 (≠ T183), S202 (≠ V203), H230 (= H229), T329 (≠ G327), E330 (= E328), K434 (≠ I433), Q439 (≠ N438), K519 (= K518)
- binding adenosine-5'-triphosphate: S182 (≠ T183), S183 (= S184), G184 (= G185), T185 (= T186), T186 (= T187), K190 (= K191), H230 (= H229), A302 (≠ G301), A303 (= A302), P304 (= P303), Y326 (≠ F324), G327 (= G325), M328 (≠ L326), T329 (≠ G327), D413 (= D412), I425 (= I424), R428 (= R427), K519 (= K518)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
29% identity, 90% coverage: 36:528/549 of query aligns to 36:529/529 of 5bsvA
- active site: S182 (≠ T183), S202 (≠ V203), H230 (= H229), T329 (≠ G327), E330 (= E328), K434 (≠ I433), Q439 (≠ N438), K519 (= K518)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H229), Y232 (≠ A231), S236 (≠ Q235), A302 (≠ G301), A303 (= A302), P304 (= P303), G325 (≠ Y323), G327 (= G325), M328 (≠ L326), T329 (≠ G327), P333 (≠ A332), V334 (≠ I333), D413 (= D412), K430 (≠ S429), K434 (≠ I433), Q439 (≠ N438)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
29% identity, 90% coverage: 36:528/549 of query aligns to 36:529/529 of 5bsuA
- active site: S182 (≠ T183), S202 (≠ V203), H230 (= H229), T329 (≠ G327), E330 (= E328), K434 (≠ I433), Q439 (≠ N438), K519 (= K518)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H229), Y232 (≠ A231), S236 (≠ Q235), M299 (≠ I298), A302 (≠ G301), A303 (= A302), P304 (= P303), G325 (≠ Y323), G327 (= G325), M328 (≠ L326), T329 (≠ G327), P333 (≠ A332), D413 (= D412), K430 (≠ S429), K434 (≠ I433), Q439 (≠ N438)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
29% identity, 90% coverage: 36:528/549 of query aligns to 36:529/529 of 5bstA
- active site: S182 (≠ T183), S202 (≠ V203), H230 (= H229), T329 (≠ G327), E330 (= E328), K434 (≠ I433), Q439 (≠ N438), K519 (= K518)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H229), Y232 (≠ A231), S236 (≠ Q235), A302 (≠ G301), A303 (= A302), P304 (= P303), G325 (≠ Y323), Y326 (≠ F324), G327 (= G325), M328 (≠ L326), T329 (≠ G327), P333 (≠ A332), V334 (≠ I333), D413 (= D412), K430 (≠ S429), K434 (≠ I433), Q439 (≠ N438)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
29% identity, 90% coverage: 36:528/549 of query aligns to 35:528/528 of 5bsrA
- active site: S181 (≠ T183), S201 (≠ V203), H229 (= H229), T328 (≠ G327), E329 (= E328), K433 (≠ I433), Q438 (≠ N438), K518 (= K518)
- binding adenosine monophosphate: A301 (≠ G301), G326 (= G325), T328 (≠ G327), D412 (= D412), K429 (≠ S429), K433 (≠ I433), Q438 (≠ N438)
- binding coenzyme a: L102 (≠ R102), P226 (= P226), H229 (= H229), Y231 (≠ A231), F253 (≠ L253), K435 (≠ G435), G436 (= G436), F437 (≠ S437), F498 (≠ R498)
5wm3A Crystal structure of cahj in complex with salicyl adenylate (see paper)
30% identity, 93% coverage: 20:531/549 of query aligns to 29:533/537 of 5wm3A
- active site: S193 (≠ T183), N213 (≠ V203), H237 (= H229), A336 (≠ G327), E337 (= E328), N437 (≠ I433), K442 (≠ N438), K524 (= K518)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxybenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: N238 (≠ G230), F239 (≠ A231), G310 (= G301), S311 (≠ A302), K312 (≠ P303), V332 (≠ Y323), F333 (= F324), G334 (= G325), M335 (≠ L326), A336 (≠ G327), D416 (= D412), K433 (≠ S429), K442 (≠ N438)
- binding magnesium ion: S301 (= S292), L303 (= L294), G326 (= G317)
Query Sequence
>SMc00261 FitnessBrowser__Smeli:SMc00261
MTNNEPKGGVTPVSTRVMNLANFLSQAARRNPDEIALVHGDRRWRWSEMEARVDAMAYAL
VHEFGVRKGDRILVHSANCNQMFESMFAAFRAGAVWVPTNFRQLPEEVAYLAESSGARLV
IFQAAFEAHAEACRAAGEQIGSCIPIGSSRVGEDYDAIVARNLGRSVSPVAVDRDDPCWY
FYTSGTTGRPKAAVLTHGQMAFVINNHIGDLFPATTHRDRSIVVAPLSHGAGIHQLCQVA
RGATTILLPSEKLDIPQFWALVEKWRVNNLFAVPTIVKLLIEDPSVDRYDHSSLRYVIYA
GAPMYRADQKKALEKLGAVLVQYFGLGEVTGAITVLPPAFHSSEDGPDARIGTCGFERTG
MQLQIQDEDGNEVPAGATGEICVIGPAVFAGYYRNPEANAKAFRNGWFRTGDLGHVDAQG
FLYITGRASDMYISGGSNVYPREIEEKLLMHPDISEAAIVGVPDPVWGEVGIAVCVARGG
ATVGAAALREWLDGKIARYKLPKKIVFWSEMPKSAYGKITKKLIREELERRGELDIGSAG
IGERRSAAP
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