SitesBLAST
Comparing GFF2964 FitnessBrowser__WCS417:GFF2964 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)
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)
53% identity, 98% coverage: 10:567/567 of query aligns to 2:550/561 of P69451
- Y213 (= Y222) mutation to A: Loss of activity.
- T214 (= T223) mutation to A: 10% of wild-type activity.
- G216 (= G225) mutation to A: Decreases activity.
- T217 (= T226) mutation to A: Decreases activity.
- G219 (= G228) mutation to A: Decreases activity.
- K222 (= K231) mutation to A: Decreases activity.
- E361 (= E371) 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)
32% identity, 91% coverage: 51:567/567 of query aligns to 20:494/503 of P9WQ37
- K172 (= K231) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ D258) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ Q260) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I272) 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 (≠ S274) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V277) 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 (= R309) 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 (= W449) 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 (= D454) 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 (= R469) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V476) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G478) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K560) 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.
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)
29% identity, 92% coverage: 48:567/567 of query aligns to 54:570/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
31% identity, 91% coverage: 51:567/567 of query aligns to 23:494/502 of 3r44A
Sites not aligning to the query:
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
29% identity, 91% coverage: 53:567/567 of query aligns to 23:498/506 of 4gxqA
- active site: T163 (= T223), N183 (= N243), H207 (= H271), T303 (= T370), E304 (= E371), I403 (≠ L475), N408 (= N480), A491 (≠ K560)
- binding adenosine-5'-triphosphate: T163 (= T223), S164 (≠ G224), G165 (= G225), T166 (= T226), T167 (= T227), H207 (= H271), S277 (≠ G344), A278 (≠ M345), P279 (≠ A346), E298 (= E365), M302 (≠ L369), T303 (= T370), D382 (= D454), R397 (= R469)
- binding carbonate ion: H207 (= H271), S277 (≠ G344), R299 (≠ G366), G301 (= G368)
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)
29% identity, 92% coverage: 48:567/567 of query aligns to 17:477/485 of 5x8fB
- active site: T151 (= T223), S171 (≠ N243), H195 (= H271), T288 (= T370), E289 (= E371), I387 (≠ L475), N392 (= N480), K470 (= K560)
- binding magnesium ion: Y23 (≠ S54), E24 (≠ I55), H70 (≠ L101), N178 (≠ W250), L202 (= L280), L214 (≠ I292), T296 (≠ S377), L297 (≠ I378), S298 (= S379)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ L116), L191 (= L267), P192 (= P268), H195 (= H271), I196 (= I272), S197 (≠ F273), A237 (≠ G315), V238 (= V316), L260 (≠ I341), G262 (= G343), G286 (= G368), M287 (≠ L369), S292 (= S373), Q293 (≠ P374), S388 (≠ V476), G389 (≠ S477), G390 (= G478), E391 (≠ F479), K420 (≠ V508), W421 (≠ T509), K450 (≠ G539), Y451 (= Y540)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
29% identity, 92% coverage: 48:567/567 of query aligns to 17:477/484 of 5gtdA
- active site: T151 (= T223), S171 (≠ N243), H195 (= H271), T288 (= T370), E289 (= E371)
- binding adenosine-5'-monophosphate: G263 (= G344), G264 (≠ M345), Y285 (= Y367), G286 (= G368), M287 (≠ L369), T288 (= T370), D366 (= D454), V378 (≠ L466)
- binding magnesium ion: F314 (≠ P400), S315 (= S401)
- binding 2-succinylbenzoate: H195 (= H271), S197 (≠ F273), A237 (≠ G315), L260 (≠ I341), G262 (= G343), G263 (= G344), G286 (= G368), M287 (≠ L369), S292 (= S373), Q293 (≠ P374)
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)
26% identity, 96% coverage: 26:567/567 of query aligns to 29:547/556 of Q9S725
- K211 (= K231) mutation to S: Drastically reduces the activity.
- M293 (≠ A314) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I341) mutation K->L,A: Affects the substrate specificity.
- E401 (= E421) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ Q423) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R469) mutation to Q: Drastically reduces the activity.
- K457 (≠ S477) mutation to S: Drastically reduces the activity.
- K540 (= K560) mutation to N: Abolishes the activity.
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
29% identity, 92% coverage: 48:567/567 of query aligns to 16:474/475 of 5burA
- active site: T150 (= T223), S170 (≠ N243), H194 (= H271), T287 (= T370), E288 (= E371)
- binding adenosine-5'-triphosphate: T150 (= T223), S151 (≠ G224), T153 (= T226), T154 (= T227), K158 (= K231), G263 (≠ M345), S283 (≠ G366), T287 (= T370), D365 (= D454), V377 (≠ L466), R380 (= R469)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
29% identity, 92% coverage: 48:567/567 of query aligns to 16:474/481 of 5busA
- active site: T150 (= T223), S170 (≠ N243), H194 (= H271), T287 (= T370), E288 (= E371)
- binding adenosine monophosphate: H194 (= H271), G262 (= G344), G263 (≠ M345), S283 (≠ G366), M286 (≠ L369), T287 (= T370), D365 (= D454), V377 (≠ L466), R380 (= R469), K467 (= K560)
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)
28% identity, 94% coverage: 33:566/567 of query aligns to 30:536/546 of Q84P21
- K530 (= K560) mutation to N: Lossed enzymatic activity.
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)
28% identity, 96% coverage: 26:567/567 of query aligns to 25:542/559 of Q67W82
- G395 (= G420) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
28% identity, 92% coverage: 49:567/567 of query aligns to 26:509/518 of 4wv3B
- active site: S175 (≠ T223), T320 (= T370), E321 (= E371), K418 (≠ L475), W423 (≠ N480), K502 (= K560)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H271), T221 (≠ I272), F222 (= F273), A293 (≠ G343), S294 (≠ G344), E295 (≠ M345), A296 (= A346), G316 (= G366), I317 (≠ Y367), G318 (= G368), C319 (≠ L369), T320 (= T370), D397 (= D454), H409 (≠ L466), R412 (= R469), K502 (= K560)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
27% identity, 94% coverage: 35:567/567 of query aligns to 20:526/528 of 3ni2A
- active site: S182 (≠ T223), S202 (≠ N243), H230 (= H271), T329 (= T370), E330 (= E371), K434 (≠ L475), Q439 (≠ N480), K519 (= K560)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F273), S236 (≠ C279), G302 (= G344), A303 (≠ M345), P304 (≠ A346), G325 (= G366), G327 (= G368), T329 (= T370), P333 (= P374), V334 (= V375), D413 (= D454), K430 (= K471), K434 (≠ L475), Q439 (≠ N480)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
27% identity, 94% coverage: 35:567/567 of query aligns to 20:526/528 of 3a9vA
- active site: S182 (≠ T223), S202 (≠ N243), H230 (= H271), T329 (= T370), E330 (= E371), K434 (≠ L475), Q439 (≠ N480), K519 (= K560)
- binding adenosine monophosphate: H230 (= H271), G302 (= G344), A303 (≠ M345), P304 (≠ A346), Y326 (= Y367), G327 (= G368), M328 (≠ L369), T329 (= T370), D413 (= D454), K430 (= K471), K434 (≠ L475), Q439 (≠ N480)
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)
26% identity, 96% coverage: 26:567/567 of query aligns to 18:533/542 of O24146
- S189 (≠ T223) binding
- S190 (≠ G224) binding
- G191 (= G225) binding
- T192 (= T226) binding
- T193 (= T227) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K231) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H271) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F273) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ V277) binding ; binding ; binding
- K260 (≠ P295) binding
- A309 (vs. gap) binding ; binding ; binding
- Q331 (≠ E365) binding
- G332 (= G366) 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 (≠ I378) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D454) binding ; binding ; binding ; binding ; binding
- R435 (= R469) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K471) binding ; binding ; binding ; binding
- K441 (≠ L475) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S477) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G478) binding
- Q446 (≠ N480) binding
- K526 (= K560) 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)
26% identity, 96% coverage: 26:567/567 of query aligns to 11:526/530 of 5bsmA
- active site: S182 (≠ T223), S202 (≠ N243), H230 (= H271), T329 (= T370), E330 (= E371), K434 (≠ L475), Q439 (≠ N480), K519 (= K560)
- binding adenosine-5'-triphosphate: S182 (≠ T223), S183 (≠ G224), G184 (= G225), T185 (= T226), T186 (= T227), K190 (= K231), H230 (= H271), A302 (vs. gap), A303 (vs. gap), P304 (vs. gap), Y326 (= Y367), G327 (= G368), M328 (≠ L369), T329 (= T370), D413 (= D454), I425 (≠ L466), R428 (= R469), K519 (= K560)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
26% identity, 96% coverage: 26:567/567 of query aligns to 11:526/529 of 5bsvA
- active site: S182 (≠ T223), S202 (≠ N243), H230 (= H271), T329 (= T370), E330 (= E371), K434 (≠ L475), Q439 (≠ N480), K519 (= K560)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H271), Y232 (≠ F273), S236 (≠ V277), A302 (vs. gap), A303 (vs. gap), P304 (vs. gap), G325 (= G366), G327 (= G368), M328 (≠ L369), T329 (= T370), P333 (= P374), V334 (= V375), D413 (= D454), K430 (= K471), K434 (≠ L475), Q439 (≠ N480)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
26% identity, 96% coverage: 26:567/567 of query aligns to 11:526/529 of 5bsuA
- active site: S182 (≠ T223), S202 (≠ N243), H230 (= H271), T329 (= T370), E330 (= E371), K434 (≠ L475), Q439 (≠ N480), K519 (= K560)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H271), Y232 (≠ F273), S236 (≠ V277), M299 (≠ I341), A302 (vs. gap), A303 (vs. gap), P304 (vs. gap), G325 (= G366), G327 (= G368), M328 (≠ L369), T329 (= T370), P333 (= P374), D413 (= D454), K430 (= K471), K434 (≠ L475), Q439 (≠ N480)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
26% identity, 96% coverage: 26:567/567 of query aligns to 11:526/529 of 5bstA
- active site: S182 (≠ T223), S202 (≠ N243), H230 (= H271), T329 (= T370), E330 (= E371), K434 (≠ L475), Q439 (≠ N480), K519 (= K560)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H271), Y232 (≠ F273), S236 (≠ V277), A302 (vs. gap), A303 (vs. gap), P304 (vs. gap), G325 (= G366), Y326 (= Y367), G327 (= G368), M328 (≠ L369), T329 (= T370), P333 (= P374), V334 (= V375), D413 (= D454), K430 (= K471), K434 (≠ L475), Q439 (≠ N480)
Query Sequence
>GFF2964 FitnessBrowser__WCS417:GFF2964
MNAVSLEHTERIWLNAYLPGVPADIDAGIEDYPSLREVFLEHLEKFRERVAYVSIGTEMT
YADWQVQGVAFAAWLQGQGVRKGERVALMMPNCLQYPICLLGTILAGAVVVNVNPLYTSH
ELKHLLKDSGAETVVIFENFAHTLEKVITGSSVKRVVIAAIGDLLGTFKGAAMNFILRRV
QKQVPAFNLPGSVRFNQVLKQGRALNHFPVEMHLDALAFLQYTGGTTGDAKGVMLSHRNI
IANLLQAKAWVGDQLDQDKQETNVTLLPLYHIFSLTVNCLMFMCLGGRNILIANPRDVKR
VQMILRKERFNGIAGVNTLFNGLLENEAFCARDFSDLRMVIAGGMATHTAVAKRWKEVTG
LPIIEGYGLTECSPVVSISPIDIARMREMEFTGSIGVPLPSTWVRFVREDGELAEIGEQG
ELQVRGPQVMQGYWQRPEATAEVLDAEGWLSTGDIGVMDARGYIRLVDRKKDMILVSGFN
VYPNEIEDVVALHPAVAEVAAIGVEDGVTGEKVKIIVVRKDPNLTQEQILAHCREYLTGY
KMPKYVEFRTTELPKTTVGKVLRRALR
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