SitesBLAST
Comparing WP_041314143.1 NCBI__GCF_000019165.1:WP_041314143.1 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)
42% identity, 97% coverage: 1:539/555 of query aligns to 34:572/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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, 97% coverage: 5:540/555 of query aligns to 3:497/503 of P9WQ37
- R9 (≠ D11) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ E19) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K207) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T230) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ E232) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C244) 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 (≠ C247) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ S250) 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 (= R280) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G340) 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 (= W419) 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 (= D424) 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 (= R439) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R446) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G448) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K530) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
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)
31% identity, 96% coverage: 5:538/555 of query aligns to 24:551/561 of P69451
- Y213 (= Y198) mutation to A: Loss of activity.
- T214 (= T199) mutation to A: 10% of wild-type activity.
- G216 (= G201) mutation to A: Decreases activity.
- T217 (= T202) mutation to A: Decreases activity.
- G219 (= G204) mutation to A: Decreases activity.
- K222 (= K207) mutation to A: Decreases activity.
- E361 (= E343) mutation to A: Loss of activity.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
32% identity, 97% coverage: 5:540/555 of query aligns to 6:497/502 of 3r44A
Sites not aligning to the query:
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 92% coverage: 32:540/555 of query aligns to 28:501/506 of 4gxqA
- active site: T163 (= T199), N183 (= N219), H207 (= H243), T303 (= T342), E304 (= E343), I403 (= I445), N408 (= N450), A491 (≠ K530)
- binding adenosine-5'-triphosphate: T163 (= T199), S164 (= S200), G165 (= G201), T166 (= T202), T167 (= T203), H207 (= H243), S277 (≠ G315), A278 (≠ S316), P279 (= P317), E298 (≠ I337), M302 (≠ Q341), T303 (= T342), D382 (= D424), R397 (= R439)
- binding carbonate ion: H207 (= H243), S277 (≠ G315), R299 (≠ A338), G301 (= G340)
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, 94% coverage: 34:554/555 of query aligns to 61:559/559 of Q67W82
- G395 (= G390) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
Q5SKN9 Long-chain-fatty-acid--CoA ligase; Long-chain fatty acyl-CoA synthetase; LC-FACS; EC 6.2.1.3 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
29% identity, 97% coverage: 3:540/555 of query aligns to 17:534/541 of Q5SKN9
- T184 (= T199) binding Mg(2+)
- G302 (= G315) binding tetradecanoyl-AMP
- Q322 (≠ I337) binding tetradecanoyl-AMP
- G323 (≠ A338) binding tetradecanoyl-AMP
- T327 (= T342) binding tetradecanoyl-AMP
- E328 (= E343) binding Mg(2+)
- D418 (= D424) binding tetradecanoyl-AMP
- K435 (= K441) binding tetradecanoyl-AMP
- K439 (≠ I445) binding tetradecanoyl-AMP
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, 91% coverage: 34:537/555 of query aligns to 65:547/556 of Q9S725
- K211 (= K207) mutation to S: Drastically reduces the activity.
- M293 (≠ Y285) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I312) mutation K->L,A: Affects the substrate specificity.
- E401 (= E391) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C393) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R439) mutation to Q: Drastically reduces the activity.
- K457 (≠ G447) mutation to S: Drastically reduces the activity.
- K540 (= K530) mutation to N: Abolishes the activity.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
30% identity, 91% coverage: 34:538/555 of query aligns to 47:527/528 of 3ni2A
- active site: S182 (≠ T199), S202 (≠ N219), H230 (= H243), T329 (= T342), E330 (= E343), K434 (≠ I445), Q439 (≠ N450), K519 (= K530)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F245), S236 (≠ M249), G302 (= G315), A303 (≠ S316), P304 (= P317), G325 (≠ A338), G327 (= G340), T329 (= T342), P333 (= P346), V334 (= V347), D413 (= D424), K430 (= K441), K434 (≠ I445), Q439 (≠ N450)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
30% identity, 91% coverage: 34:538/555 of query aligns to 47:527/528 of 3a9vA
- active site: S182 (≠ T199), S202 (≠ N219), H230 (= H243), T329 (= T342), E330 (= E343), K434 (≠ I445), Q439 (≠ N450), K519 (= K530)
- binding adenosine monophosphate: H230 (= H243), G302 (= G315), A303 (≠ S316), P304 (= P317), Y326 (= Y339), G327 (= G340), M328 (≠ Q341), T329 (= T342), D413 (= D424), K430 (= K441), K434 (≠ I445), Q439 (≠ N450)
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)
30% identity, 91% coverage: 34:537/555 of query aligns to 54:533/542 of O24146
- S189 (≠ T199) binding ATP
- S190 (= S200) binding ATP
- G191 (= G201) binding ATP
- T192 (= T202) binding ATP
- T193 (= T203) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K207) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H243) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F245) 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 (= S250) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ Y266) binding CoA
- A309 (≠ G315) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ I337) binding ATP
- G332 (≠ A338) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T342) 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 (= V347) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ Q350) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D424) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R439) 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 (= K441) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ I445) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G447) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G448) binding CoA
- Q446 (≠ N450) binding AMP
- K526 (= K530) 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)
30% identity, 91% coverage: 34:537/555 of query aligns to 47:526/530 of 5bsmA
- active site: S182 (≠ T199), S202 (≠ N219), H230 (= H243), T329 (= T342), E330 (= E343), K434 (≠ I445), Q439 (≠ N450), K519 (= K530)
- binding adenosine-5'-triphosphate: S182 (≠ T199), S183 (= S200), G184 (= G201), T185 (= T202), T186 (= T203), K190 (= K207), H230 (= H243), A302 (≠ G315), A303 (≠ S316), P304 (= P317), Y326 (= Y339), G327 (= G340), M328 (≠ Q341), T329 (= T342), D413 (= D424), I425 (= I436), R428 (= R439), K519 (= K530)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 91% coverage: 34:537/555 of query aligns to 47:526/529 of 5bsvA
- active site: S182 (≠ T199), S202 (≠ N219), H230 (= H243), T329 (= T342), E330 (= E343), K434 (≠ I445), Q439 (≠ N450), K519 (= K530)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H243), Y232 (≠ F245), S236 (= S250), A302 (≠ G315), A303 (≠ S316), P304 (= P317), G325 (≠ A338), G327 (= G340), M328 (≠ Q341), T329 (= T342), P333 (= P346), V334 (= V347), D413 (= D424), K430 (= K441), K434 (≠ I445), Q439 (≠ N450)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 91% coverage: 34:537/555 of query aligns to 47:526/529 of 5bsuA
- active site: S182 (≠ T199), S202 (≠ N219), H230 (= H243), T329 (= T342), E330 (= E343), K434 (≠ I445), Q439 (≠ N450), K519 (= K530)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H243), Y232 (≠ F245), S236 (= S250), M299 (≠ I312), A302 (≠ G315), A303 (≠ S316), P304 (= P317), G325 (≠ A338), G327 (= G340), M328 (≠ Q341), T329 (= T342), P333 (= P346), D413 (= D424), K430 (= K441), K434 (≠ I445), Q439 (≠ N450)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
30% identity, 91% coverage: 34:537/555 of query aligns to 47:526/529 of 5bstA
- active site: S182 (≠ T199), S202 (≠ N219), H230 (= H243), T329 (= T342), E330 (= E343), K434 (≠ I445), Q439 (≠ N450), K519 (= K530)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H243), Y232 (≠ F245), S236 (= S250), A302 (≠ G315), A303 (≠ S316), P304 (= P317), G325 (≠ A338), Y326 (= Y339), G327 (= G340), M328 (≠ Q341), T329 (= T342), P333 (= P346), V334 (= V347), D413 (= D424), K430 (= K441), K434 (≠ I445), Q439 (≠ N450)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 91% coverage: 34:537/555 of query aligns to 46:525/528 of 5bsrA
- active site: S181 (≠ T199), S201 (≠ N219), H229 (= H243), T328 (= T342), E329 (= E343), K433 (≠ I445), Q438 (≠ N450), K518 (= K530)
- binding adenosine monophosphate: A301 (≠ G315), G326 (= G340), T328 (= T342), D412 (= D424), K429 (= K441), K433 (≠ I445), Q438 (≠ N450)
- binding coenzyme a: L102 (≠ N90), P226 (= P240), H229 (= H243), Y231 (≠ F245), F253 (= F267), K435 (≠ G447), G436 (= G448), F437 (≠ E449), F498 (≠ R510)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
31% identity, 96% coverage: 8:538/555 of query aligns to 14:510/518 of 4wv3B
- active site: S175 (≠ T199), T320 (= T342), E321 (= E343), K418 (≠ I445), W423 (≠ N450), K502 (= K530)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H243), T221 (≠ C244), F222 (= F245), A293 (= A314), S294 (≠ G315), E295 (≠ S316), A296 (≠ P317), G316 (≠ A338), I317 (≠ Y339), G318 (= G340), C319 (≠ Q341), T320 (= T342), D397 (= D424), H409 (≠ I436), R412 (= R439), K502 (= K530)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
30% identity, 91% coverage: 34:537/555 of query aligns to 46:522/527 of 5u95B
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
29% identity, 97% coverage: 5:542/555 of query aligns to 19:539/539 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 (= H243), F245 (= F245), T249 (≠ S250), G314 (= G315), A315 (≠ S316), P316 (= P317), G337 (≠ A338), Y338 (= Y339), G339 (= G340), L340 (≠ Q341), T341 (= T342), S345 (≠ P346), A346 (≠ V347), D420 (= D424), I432 (= I436), K527 (= K530)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F245), R335 (≠ T336), G337 (≠ A338), G339 (= G340), L340 (≠ Q341), A346 (≠ V347)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
29% identity, 97% coverage: 5:540/555 of query aligns to 19:537/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H243), F245 (= F245), T249 (≠ S250), G314 (= G315), A315 (≠ S316), P316 (= P317), G337 (≠ A338), Y338 (= Y339), G339 (= G340), L340 (≠ Q341), T341 (= T342), A346 (≠ V347), D420 (= D424), I432 (= I436), K527 (= K530)
Query Sequence
>WP_041314143.1 NCBI__GCF_000019165.1:WP_041314143.1
MLQITIGDLLDQTAARYPEKEALVYTDDRNLRLTYAQFRQKADEVAKGLMALGVQKGEHI
ALWATNYPEWLYTQFGSAKMGAVLVTVNTNYRSFELEYLLRQSDATTLFLIDGFRDNNFV
EIINELCPGLGDSEPGRLSLRRLPKLKNIIFIGRDPQAKHPGMYSWQELIDMGRSVSDAE
LAERQRSLHFDEVINMQYTSGTTGFPKGVMLSHANIINNANMVADCQKWTHEDRLCFPVP
LFHCFGCVMSSLACVCKGATMVPLEYFTAKGVLEAVQRERCTVLYGVPTMFIAELDHPDF
DKYDLSSLRTGIMAGSPCPIEVMRKVIDRMGIGEITIAYGQTEFSPVITQTRTDDSLERR
VCTVGKALPHVEVKIVHPDTGLEIPRGTQGELCARGFGTMKGYYNNPEATEAAIDAEGWL
HTGDLATMDEEGYCRITGRAKDMIIRGGENIYPREVEEFLFTHPKVKDVQVVGVPDPKYG
EEALACIILKDGEEATEEEIRYFCRGKISRYKIPKYVRFVDHFPMTASGKIQKFKLREIF
IKELGLEDAAKIETA
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