SitesBLAST
Comparing 3610022 FitnessBrowser__Dino:3610022 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)
41% identity, 94% coverage: 22:564/579 of query aligns to 24:570/590 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, 92% coverage: 36:570/579 of query aligns to 24:552/561 of P69451
- Y213 (≠ F225) mutation to A: Loss of activity.
- T214 (= T226) mutation to A: 10% of wild-type activity.
- G216 (= G228) mutation to A: Decreases activity.
- T217 (= T229) mutation to A: Decreases activity.
- G219 (= G231) mutation to A: Decreases activity.
- K222 (= K234) mutation to A: Decreases activity.
- E361 (= E371) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 89% coverage: 51:564/579 of query aligns to 17:498/506 of 4gxqA
- active site: T163 (= T226), N183 (= N246), H207 (= H270), T303 (= T370), E304 (= E371), I403 (≠ V472), N408 (= N477), A491 (≠ K557)
- binding adenosine-5'-triphosphate: T163 (= T226), S164 (= S227), G165 (= G228), T166 (= T229), T167 (= T230), H207 (= H270), S277 (≠ G343), A278 (= A344), P279 (= P345), E298 (≠ I365), M302 (= M369), T303 (= T370), D382 (= D451), R397 (= R466)
- binding carbonate ion: H207 (= H270), S277 (≠ G343), R299 (≠ A366), G301 (= G368)
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, 91% coverage: 40:566/579 of query aligns to 7:496/503 of P9WQ37
- R9 (≠ V42) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ N50) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K234) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ I257) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ Q259) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C271) 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 (≠ G273) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ M276) 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 (= R308) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G368) 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 (= W446) 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 (= D451) 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 (= R466) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R473) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G475) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K557) 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: 35:571/579 of query aligns to 36:554/556 of Q9S725
- K211 (= K234) mutation to S: Drastically reduces the activity.
- M293 (≠ Y313) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I340) mutation K->L,A: Affects the substrate specificity.
- E401 (= E418) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ L420) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R466) mutation to Q: Drastically reduces the activity.
- K457 (≠ G474) mutation to S: Drastically reduces the activity.
- K540 (= K557) mutation to N: Abolishes the activity.
6e97B Crystal structure of the aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with dhb-adenylate
31% identity, 93% coverage: 36:571/579 of query aligns to 23:536/537 of 6e97B
- active site: S190 (≠ T226), S210 (≠ N246), H234 (= H270), A336 (≠ T370), E337 (= E371), N437 (≠ V472), K442 (≠ N477), K522 (= K557)
- binding 5'-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine: H234 (= H270), N235 (≠ C271), F236 (= F272), S240 (≠ M276), G310 (= G343), A311 (= A344), K312 (≠ P345), V332 (≠ A366), F333 (≠ Y367), G334 (= G368), M335 (= M369), A336 (≠ T370), D416 (= D451), K433 (= K468), K442 (≠ N477)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
29% identity, 91% coverage: 40:566/579 of query aligns to 10:496/502 of 3r44A
Sites not aligning to the query:
P0DX84 3-methylmercaptopropionyl-CoA ligase; MMPA-CoA ligase; EC 6.2.1.44 from Ruegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157) (Silicibacter lacuscaerulensis) (see paper)
29% identity, 92% coverage: 41:571/579 of query aligns to 15:537/539 of P0DX84
- H231 (= H270) mutation to A: Retains 74% of wild-type activity.
- W235 (≠ M274) mutation to A: Almost completely abolishes the activity.
- G302 (≠ A342) mutation to P: Almost completely abolishes the activity.
- G303 (= G343) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y367) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P374) mutation to A: Retains 69% of wild-type activity.
- R432 (= R466) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K468) mutation to A: Retains 36% of wild-type activity.
- D435 (= D469) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ V472) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G474) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G475) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E476) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N477) mutation to A: Retains 60% of wild-type activity.
- E474 (= E508) mutation to A: Retains 33% of wild-type activity.
- K523 (= K557) Plays an important role in catalysis; mutation to A: Retains 1.6% of wild-type activity.; mutation to E: Retains 1.4% of wild-type activity.; mutation to R: Retains 57% of wild-type activity.
- K526 (= K560) mutation to A: Retains 48% of wild-type activity.
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, 93% coverage: 30:569/579 of query aligns to 27:538/546 of Q84P21
- K530 (= K557) mutation to N: Lossed enzymatic activity.
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
29% identity, 92% coverage: 41:571/579 of query aligns to 15:537/538 of 6ijbB
- active site: T185 (= T226), H205 (vs. gap), H231 (= H270), S329 (≠ T370), E330 (= E371), K438 (≠ V472), W443 (≠ N477), A523 (≠ K557)
- binding 3-(methylsulfanyl)propanoic acid: W235 (≠ M274), G303 (= G343), A325 (= A366), W326 (≠ Y367), G327 (= G368), M328 (= M369)
- binding adenosine monophosphate: G303 (= G343), A304 (= A344), A305 (≠ P345), H324 (≠ T364), W326 (≠ Y367), G327 (= G368), M328 (= M369), S329 (≠ T370), Q359 (≠ V392), D417 (= D451)
6e8oA Crystal structure of aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with amp
31% identity, 93% coverage: 36:571/579 of query aligns to 23:531/536 of 6e8oA
- active site: S190 (≠ T226), S210 (≠ N246), H234 (= H270), A336 (≠ T370), E337 (= E371), N437 (≠ V472), K442 (≠ N477), K521 (≠ G556)
- binding adenosine monophosphate: H234 (= H270), G310 (= G343), A311 (= A344), K312 (≠ P345), V332 (≠ A366), F333 (≠ Y367), G334 (= G368), M335 (= M369), A336 (≠ T370), D416 (= D451), V428 (≠ I463), K442 (≠ N477)
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)
28% identity, 91% coverage: 43:567/579 of query aligns to 33:536/542 of O24146
- S189 (≠ T226) binding
- S190 (= S227) binding
- G191 (= G228) binding
- T192 (= T229) binding
- T193 (= T230) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K234) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H270) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F272) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ M276) binding ; binding ; binding
- K260 (≠ G294) binding
- A309 (≠ G343) binding ; binding ; binding
- Q331 (≠ I365) binding
- G332 (≠ A366) binding ; binding ; binding ; binding ; binding
- T336 (= T370) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V375) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ Q378) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D451) binding ; binding ; binding ; binding ; binding
- R435 (= R466) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K468) binding ; binding ; binding ; binding
- K441 (≠ V472) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G474) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G475) binding
- Q446 (≠ N477) binding
- K526 (= K557) 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)
28% identity, 91% coverage: 43:567/579 of query aligns to 26:529/530 of 5bsmA
- active site: S182 (≠ T226), S202 (≠ N246), H230 (= H270), T329 (= T370), E330 (= E371), K434 (≠ V472), Q439 (≠ N477), K519 (= K557)
- binding adenosine-5'-triphosphate: S182 (≠ T226), S183 (= S227), G184 (= G228), T185 (= T229), T186 (= T230), K190 (= K234), H230 (= H270), A302 (≠ G343), A303 (= A344), P304 (= P345), Y326 (= Y367), G327 (= G368), M328 (= M369), T329 (= T370), D413 (= D451), I425 (= I463), R428 (= R466), K519 (= K557)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
28% identity, 91% coverage: 43:567/579 of query aligns to 25:528/528 of 5bsrA
- active site: S181 (≠ T226), S201 (≠ N246), H229 (= H270), T328 (= T370), E329 (= E371), K433 (≠ V472), Q438 (≠ N477), K518 (= K557)
- binding adenosine monophosphate: A301 (≠ G343), G326 (= G368), T328 (= T370), D412 (= D451), K429 (= K468), K433 (≠ V472), Q438 (≠ N477)
- binding coenzyme a: L102 (≠ A120), P226 (= P267), H229 (= H270), Y231 (≠ F272), F253 (= F295), K435 (≠ G474), G436 (= G475), F437 (≠ E476), F498 (≠ H537)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
28% identity, 91% coverage: 43:567/579 of query aligns to 26:529/529 of 5bsvA
- active site: S182 (≠ T226), S202 (≠ N246), H230 (= H270), T329 (= T370), E330 (= E371), K434 (≠ V472), Q439 (≠ N477), K519 (= K557)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H270), Y232 (≠ F272), S236 (≠ M276), A302 (≠ G343), A303 (= A344), P304 (= P345), G325 (≠ A366), G327 (= G368), M328 (= M369), T329 (= T370), P333 (= P374), V334 (= V375), D413 (= D451), K430 (= K468), K434 (≠ V472), Q439 (≠ N477)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
28% identity, 91% coverage: 43:567/579 of query aligns to 26:529/529 of 5bsuA
- active site: S182 (≠ T226), S202 (≠ N246), H230 (= H270), T329 (= T370), E330 (= E371), K434 (≠ V472), Q439 (≠ N477), K519 (= K557)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H270), Y232 (≠ F272), S236 (≠ M276), M299 (≠ I340), A302 (≠ G343), A303 (= A344), P304 (= P345), G325 (≠ A366), G327 (= G368), M328 (= M369), T329 (= T370), P333 (= P374), D413 (= D451), K430 (= K468), K434 (≠ V472), Q439 (≠ N477)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
28% identity, 91% coverage: 43:567/579 of query aligns to 26:529/529 of 5bstA
- active site: S182 (≠ T226), S202 (≠ N246), H230 (= H270), T329 (= T370), E330 (= E371), K434 (≠ V472), Q439 (≠ N477), K519 (= K557)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H270), Y232 (≠ F272), S236 (≠ M276), A302 (≠ G343), A303 (= A344), P304 (= P345), G325 (≠ A366), Y326 (= Y367), G327 (= G368), M328 (= M369), T329 (= T370), P333 (= P374), V334 (= V375), D413 (= D451), K430 (= K468), K434 (≠ V472), Q439 (≠ N477)
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
30% identity, 89% coverage: 36:551/579 of query aligns to 5:493/504 of 6qjzA
- active site: T169 (= T226), S189 (≠ N246), H213 (= H270), T314 (= T370), E315 (= E371), N414 (≠ V472), K419 (≠ N477)
- binding adenosine monophosphate: H213 (= H270), S288 (≠ I340), A289 (≠ M341), S290 (≠ A342), A312 (≠ G368), M313 (= M369), T314 (= T370), D393 (= D451), L405 (≠ I463), K410 (= K468), K419 (≠ N477)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
28% identity, 89% coverage: 58:570/579 of query aligns to 41:528/528 of 3ni2A
- active site: S182 (≠ T226), S202 (≠ N246), H230 (= H270), T329 (= T370), E330 (= E371), K434 (≠ V472), Q439 (≠ N477), K519 (= K557)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F272), S236 (≠ M276), G302 (= G343), A303 (= A344), P304 (= P345), G325 (≠ A366), G327 (= G368), T329 (= T370), P333 (= P374), V334 (= V375), D413 (= D451), K430 (= K468), K434 (≠ V472), Q439 (≠ N477)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
28% identity, 89% coverage: 58:570/579 of query aligns to 41:528/528 of 3a9vA
- active site: S182 (≠ T226), S202 (≠ N246), H230 (= H270), T329 (= T370), E330 (= E371), K434 (≠ V472), Q439 (≠ N477), K519 (= K557)
- binding adenosine monophosphate: H230 (= H270), G302 (= G343), A303 (= A344), P304 (= P345), Y326 (= Y367), G327 (= G368), M328 (= M369), T329 (= T370), D413 (= D451), K430 (= K468), K434 (≠ V472), Q439 (≠ N477)
Query Sequence
>3610022 FitnessBrowser__Dino:3610022
MALEDEGHSGTQLGVAPTNGSSHVLGAQEPPLLELTIPELLVQTAARFPNHVAAIFEAQG
IRWTYRDLIREVDALAGGLLQLGLKPGDRVGVWAPNCAEWLLAQFATARLGIILVNVNPA
YRPFELSYALKKTGCTALILAAQFKNSDYVAMLSEVVPEIAASDPGALHAAELPDLRAVI
VTEAEAPDGMIAFPDLIAKGRAVVAKDLDAITRKLDCHDPINIQFTSGTTGLPKGATLTH
RNIVNNAASVTSAIKLIEQDMLCIPVPFYHCFGMVMGTLGCVTKGAAIVVPGPGFDPITT
LDTVSKHRCTALYGVPTMFVGMLEHPRFAEYDLSSLRTGIMAGAPCPIEIMRQVQSRMHM
SEVTIAYGMTETSPVSFQSATDDPVQKRVSSVGRIQPHVEVKIVDEDSVVVPVGAQGELL
TRGYSVMQGYWDEPDKTAEAIDADGWMHTGDLATLDVDGFCKITGRVKDMIVRGGENVYP
REIEEFLYTHPAISQVQVFGIPDQKFGEIVVAWLVAKPGADPTEAEILDFCRDSIAHFKV
PAMVRFKNSLPMTVTGKPQKFIMRAQMVEELGLEEIETA
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