SitesBLAST
Comparing PfGW456L13_2521 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2521 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)
35% identity, 93% coverage: 35:521/526 of query aligns to 66:573/590 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)
35% identity, 93% coverage: 31:519/526 of query aligns to 27:495/503 of P9WQ37
- K172 (= K189) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R212) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ G214) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ S226) 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 (≠ G228) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ A231) 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 (= R262) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G322) 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 (= W400) 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 (= D405) 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 (= R420) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ T427) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G429) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K511) 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.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
35% identity, 93% coverage: 31:519/526 of query aligns to 30:495/502 of 3r44A
Sites not aligning to the query:
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
30% identity, 95% coverage: 18:519/526 of query aligns to 12:478/484 of 5gtdA
- active site: T151 (= T181), S171 (≠ I201), H195 (= H225), T288 (= T324), E289 (= E325)
- binding adenosine-5'-monophosphate: G263 (≠ A297), G264 (≠ A298), Y285 (= Y321), G286 (= G322), M287 (≠ L323), T288 (= T324), D366 (= D405), V378 (≠ I417)
- binding magnesium ion: F314 (≠ P351), S315 (≠ G352)
- binding 2-succinylbenzoate: H195 (= H225), S197 (≠ F227), A237 (≠ G268), L260 (≠ V294), G262 (= G296), G263 (≠ A297), G286 (= G322), M287 (≠ L323), S292 (≠ G328), Q293 (≠ F329)
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, 95% coverage: 18:519/526 of query aligns to 12:478/485 of 5x8fB
- active site: T151 (= T181), S171 (≠ I201), H195 (= H225), T288 (= T324), E289 (= E325), I387 (= I426), N392 (= N431), K470 (= K511)
- binding magnesium ion: Y23 (≠ D29), E24 (≠ A30), H70 (≠ G76), N178 (≠ I208), L202 (≠ W233), L214 (≠ P245), T296 (≠ I332), L297 (≠ C333), S298 (≠ R334)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R91), L191 (≠ N221), P192 (= P222), H195 (= H225), I196 (≠ S226), S197 (≠ F227), A237 (≠ G268), V238 (≠ P269), L260 (≠ V294), G262 (= G296), G286 (= G322), M287 (≠ L323), S292 (≠ G328), Q293 (≠ F329), S388 (≠ T427), G389 (= G428), G390 (= G429), E391 (≠ F430), K420 (≠ R459), W421 (≠ L460), K450 (≠ N491), Y451 (= Y492)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
30% identity, 95% coverage: 18:519/526 of query aligns to 11:475/475 of 5burA
- active site: T150 (= T181), S170 (≠ I201), H194 (= H225), T287 (= T324), E288 (= E325)
- binding adenosine-5'-triphosphate: T150 (= T181), S151 (= S182), T153 (= T184), T154 (= T185), K158 (= K189), G263 (≠ A298), S283 (≠ A320), T287 (= T324), D365 (= D405), V377 (≠ I417), R380 (= R420)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
30% identity, 95% coverage: 18:519/526 of query aligns to 11:475/481 of 5busA
- active site: T150 (= T181), S170 (≠ I201), H194 (= H225), T287 (= T324), E288 (= E325)
- binding adenosine monophosphate: H194 (= H225), G262 (≠ A297), G263 (≠ A298), S283 (≠ A320), M286 (≠ L323), T287 (= T324), D365 (= D405), V377 (≠ I417), R380 (= R420), K467 (= K511)
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)
28% identity, 98% coverage: 9:526/526 of query aligns to 24:558/561 of P69451
- Y213 (≠ F180) mutation to A: Loss of activity.
- T214 (= T181) mutation to A: 10% of wild-type activity.
- G216 (= G183) mutation to A: Decreases activity.
- T217 (= T184) mutation to A: Decreases activity.
- G219 (= G186) mutation to A: Decreases activity.
- K222 (= K189) mutation to A: Decreases activity.
- E361 (= E325) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 97% coverage: 11:519/526 of query aligns to 3:499/506 of 4gxqA
- active site: T163 (= T181), N183 (≠ Q197), H207 (= H225), T303 (= T324), E304 (= E325), I403 (= I426), N408 (= N431), A491 (≠ K511)
- binding adenosine-5'-triphosphate: T163 (= T181), S164 (= S182), G165 (= G183), T166 (= T184), T167 (= T185), H207 (= H225), S277 (≠ A297), A278 (= A298), P279 (≠ A299), E298 (≠ T319), M302 (≠ L323), T303 (= T324), D382 (= D405), R397 (= R420)
- binding carbonate ion: H207 (= H225), S277 (≠ A297), R299 (≠ A320), G301 (= G322)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
30% identity, 94% coverage: 23:518/526 of query aligns to 25:509/518 of 4wv3B
- active site: S175 (≠ T181), T320 (= T324), E321 (= E325), K418 (≠ I426), W423 (≠ N431), K502 (= K511)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H225), T221 (≠ S226), F222 (= F227), A293 (≠ G296), S294 (≠ A297), E295 (≠ A298), A296 (= A299), G316 (≠ A320), I317 (≠ Y321), G318 (= G322), C319 (≠ L323), T320 (= T324), D397 (= D405), H409 (≠ I417), R412 (= R420), K502 (= K511)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
29% identity, 96% coverage: 14:518/526 of query aligns to 24:525/528 of 5bsrA
- active site: S181 (≠ T181), S201 (≠ I201), H229 (= H225), T328 (= T324), E329 (= E325), K433 (≠ I426), Q438 (≠ N431), K518 (= K511)
- binding adenosine monophosphate: A301 (= A297), G326 (= G322), T328 (= T324), D412 (= D405), K429 (= K422), K433 (≠ I426), Q438 (≠ N431)
- binding coenzyme a: L102 (= L88), P226 (= P222), H229 (= H225), Y231 (≠ F227), F253 (= F249), K435 (≠ G428), G436 (= G429), F437 (= F430), F498 (≠ N491)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
29% identity, 96% coverage: 14:518/526 of query aligns to 25:526/530 of 5bsmA
- active site: S182 (≠ T181), S202 (≠ I201), H230 (= H225), T329 (= T324), E330 (= E325), K434 (≠ I426), Q439 (≠ N431), K519 (= K511)
- binding adenosine-5'-triphosphate: S182 (≠ T181), S183 (= S182), G184 (= G183), T185 (= T184), T186 (= T185), K190 (= K189), H230 (= H225), A302 (= A297), A303 (= A298), P304 (≠ A299), Y326 (= Y321), G327 (= G322), M328 (≠ L323), T329 (= T324), D413 (= D405), I425 (= I417), R428 (= R420), K519 (= K511)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
29% identity, 96% coverage: 14:518/526 of query aligns to 25:526/529 of 5bsvA
- active site: S182 (≠ T181), S202 (≠ I201), H230 (= H225), T329 (= T324), E330 (= E325), K434 (≠ I426), Q439 (≠ N431), K519 (= K511)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H225), Y232 (≠ F227), S236 (≠ A231), A302 (= A297), A303 (= A298), P304 (≠ A299), G325 (≠ A320), G327 (= G322), M328 (≠ L323), T329 (= T324), P333 (≠ G328), V334 (≠ F329), D413 (= D405), K430 (= K422), K434 (≠ I426), Q439 (≠ N431)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
29% identity, 96% coverage: 14:518/526 of query aligns to 25:526/529 of 5bsuA
- active site: S182 (≠ T181), S202 (≠ I201), H230 (= H225), T329 (= T324), E330 (= E325), K434 (≠ I426), Q439 (≠ N431), K519 (= K511)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H225), Y232 (≠ F227), S236 (≠ A231), M299 (≠ V294), A302 (= A297), A303 (= A298), P304 (≠ A299), G325 (≠ A320), G327 (= G322), M328 (≠ L323), T329 (= T324), P333 (≠ G328), D413 (= D405), K430 (= K422), K434 (≠ I426), Q439 (≠ N431)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
29% identity, 96% coverage: 14:518/526 of query aligns to 25:526/529 of 5bstA
- active site: S182 (≠ T181), S202 (≠ I201), H230 (= H225), T329 (= T324), E330 (= E325), K434 (≠ I426), Q439 (≠ N431), K519 (= K511)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H225), Y232 (≠ F227), S236 (≠ A231), A302 (= A297), A303 (= A298), P304 (≠ A299), G325 (≠ A320), Y326 (= Y321), G327 (= G322), M328 (≠ L323), T329 (= T324), P333 (≠ G328), V334 (≠ F329), D413 (= D405), K430 (= K422), K434 (≠ I426), Q439 (≠ N431)
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, 96% coverage: 14:518/526 of query aligns to 32:533/542 of O24146
- S189 (≠ T181) binding
- S190 (= S182) binding
- G191 (= G183) binding
- T192 (= T184) binding
- T193 (= T185) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K189) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H225) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F227) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ A231) binding ; binding ; binding
- K260 (≠ V248) binding
- A309 (= A297) binding ; binding ; binding
- Q331 (≠ T319) binding
- G332 (≠ A320) binding ; binding ; binding ; binding ; binding
- T336 (= T324) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ F329) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ I332) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D405) binding ; binding ; binding ; binding ; binding
- R435 (= R420) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K422) binding ; binding ; binding ; binding
- K441 (≠ I426) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G428) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G429) binding
- Q446 (≠ N431) binding
- K526 (= K511) binding ; mutation to A: Abolished activity against 4-coumarate.
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)
27% identity, 96% coverage: 17:521/526 of query aligns to 39:540/546 of Q84P21
- K530 (= K511) mutation to N: Lossed enzymatic activity.
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
28% identity, 97% coverage: 9:519/526 of query aligns to 19:535/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H225), F245 (= F227), T249 (≠ A231), G314 (≠ A297), A315 (= A298), P316 (≠ A299), G337 (≠ A320), Y338 (= Y321), G339 (= G322), L340 (= L323), T341 (= T324), A346 (≠ F329), D420 (= D405), I432 (= I417), K527 (= K511)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
28% identity, 97% coverage: 9:519/526 of query aligns to 19:535/539 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 (= H225), F245 (= F227), T249 (≠ A231), G314 (≠ A297), A315 (= A298), P316 (≠ A299), G337 (≠ A320), Y338 (= Y321), G339 (= G322), L340 (= L323), T341 (= T324), S345 (≠ G328), A346 (≠ F329), D420 (= D405), I432 (= I417), K527 (= K511)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F227), R335 (≠ V318), G337 (≠ A320), G339 (= G322), L340 (= L323), A346 (≠ F329)
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, 92% coverage: 35:518/526 of query aligns to 65:547/556 of Q9S725
- K211 (= K189) mutation to S: Drastically reduces the activity.
- M293 (≠ P267) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V294) mutation K->L,A: Affects the substrate specificity.
- E401 (= E372) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ Q374) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R420) mutation to Q: Drastically reduces the activity.
- K457 (≠ G428) mutation to S: Drastically reduces the activity.
- K540 (= K511) mutation to N: Abolishes the activity.
Query Sequence
>PfGW456L13_2521 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2521
MPPVATALTIAQLFANAAQAYGDRPAIEDADHTISYRQLDQLRRQAARALLALDVQVGDR
VAIWAPNVWEWIVAAGALQSVGAALVPLNTRMKGSEAGYILRESGTCVLFAIGEFLGADY
PGMLTPEDLPALRHIVSVRGANSGTLAWERFMDLAADVPQLALRTREQSVGPQALSDVLF
TSGTTGKPKGVMTSHGQNLRIVRDWSDIVGLREGDRYLIVNPFFHSFGYKAGWLAALMRG
CTLLPQQVFDVQAVLECVQRERITVLPGPPTLYQSLLAHPQRSEFDLSSLRVAVTGAAAI
PVEMIHRMRDELGFATIVTAYGLTEVCGFATICRSGDSAELVANTSGRAMPGVQVRCVGN
SGRSQPANIPGEVQIRGYNLMQGYLNNPEASQEILDADGWLHTGDIGMLDEQGYLRITDR
LKDMFITGGFNVYPAEIEQCLLTYPGVAQAAVIGIPDERLGEVAMAFLLPAPGMEIEQTR
FLAWCREQMANYKVPRRVQVLQKMPINAAGKVTKNVLREWALQPVD
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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