SitesBLAST
Comparing RR42_RS31975 FitnessBrowser__Cup4G11:RR42_RS31975 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)
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, 90% coverage: 53:545/546 of query aligns to 28:495/503 of P9WQ37
- K172 (= K215) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ E238) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ G240) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ T252) 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 (≠ G254) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ A257) 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 (= R288) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G348) 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 (= W426) 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 (= D431) 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 (= R446) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V453) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G455) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K537) 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)
31% identity, 96% coverage: 20:545/546 of query aligns to 28:571/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
34% identity, 90% coverage: 53:545/546 of query aligns to 31:495/502 of 3r44A
Sites not aligning to the query:
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: 24:545/546 of query aligns to 10:551/561 of P69451
- Y213 (≠ F206) mutation to A: Loss of activity.
- T214 (= T207) mutation to A: 10% of wild-type activity.
- G216 (= G209) mutation to A: Decreases activity.
- T217 (= T210) mutation to A: Decreases activity.
- G219 (= G212) mutation to A: Decreases activity.
- K222 (= K215) mutation to A: Decreases activity.
- E361 (= E351) mutation to A: Loss of activity.
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)
31% identity, 95% coverage: 26:545/546 of query aligns to 7:531/539 of P0DX84
- H231 (= H251) mutation to A: Retains 74% of wild-type activity.
- W235 (≠ Y255) mutation to A: Almost completely abolishes the activity.
- G302 (= G322) mutation to P: Almost completely abolishes the activity.
- G303 (≠ A323) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y347) mutation to A: Retains 7.7% of wild-type activity.
- P333 (vs. gap) mutation to A: Retains 69% of wild-type activity.
- R432 (= R446) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K448) mutation to A: Retains 36% of wild-type activity.
- D435 (= D449) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I452) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G454) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G455) mutation to P: Retains 2.7% of wild-type activity.
- E442 (≠ F456) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N457) mutation to A: Retains 60% of wild-type activity.
- E474 (= E488) mutation to A: Retains 33% of wild-type activity.
- K523 (= K537) 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 (= K540) mutation to A: Retains 48% of wild-type activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 90% coverage: 52:545/546 of query aligns to 26:499/506 of 4gxqA
- active site: T163 (= T207), N183 (≠ Q223), H207 (= H251), T303 (= T350), E304 (= E351), I403 (= I452), N408 (= N457), A491 (≠ K537)
- binding adenosine-5'-triphosphate: T163 (= T207), S164 (= S208), G165 (= G209), T166 (= T210), T167 (= T211), H207 (= H251), S277 (≠ A323), A278 (≠ S324), P279 (≠ A325), E298 (≠ T345), M302 (≠ L349), T303 (= T350), D382 (= D431), R397 (= R446)
- binding carbonate ion: H207 (= H251), S277 (≠ A323), R299 (≠ G346), G301 (= G348)
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
31% identity, 95% coverage: 26:545/546 of query aligns to 7:531/538 of 6ijbB
- active site: T185 (= T207), H205 (= H229), H231 (= H251), S329 (≠ T350), E330 (= E351), K438 (≠ I452), W443 (≠ N457), A523 (≠ K537)
- binding 3-(methylsulfanyl)propanoic acid: W235 (≠ Y255), G303 (≠ A323), A325 (≠ G346), W326 (≠ Y347), G327 (= G348), M328 (≠ L349)
- binding adenosine monophosphate: G303 (≠ A323), A304 (≠ S324), A305 (= A325), H324 (≠ T345), W326 (≠ Y347), G327 (= G348), M328 (≠ L349), S329 (≠ T350), Q359 (≠ S372), D417 (= D431)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
30% identity, 92% coverage: 45:545/546 of query aligns to 18:478/484 of 5gtdA
- active site: T151 (= T207), S171 (≠ A227), H195 (= H251), T288 (= T350), E289 (= E351)
- binding adenosine-5'-monophosphate: G263 (≠ A323), G264 (≠ S324), Y285 (= Y347), G286 (= G348), M287 (≠ L349), T288 (= T350), D366 (= D431), V378 (≠ I443)
- binding magnesium ion: F314 (≠ P377), S315 (≠ G378)
- binding 2-succinylbenzoate: H195 (= H251), S197 (≠ F253), A237 (≠ G294), L260 (≠ V320), G262 (= G322), G263 (≠ A323), G286 (= G348), M287 (≠ L349), S292 (≠ A356), Q293 (≠ T357)
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, 92% coverage: 45:545/546 of query aligns to 18:478/485 of 5x8fB
- active site: T151 (= T207), S171 (≠ A227), H195 (= H251), T288 (= T350), E289 (= E351), I387 (= I452), N392 (= N457), K470 (= K537)
- binding magnesium ion: Y23 (≠ E50), E24 (≠ D51), H70 (≠ L97), N178 (≠ I234), L202 (≠ W259), L214 (≠ P271), T296 (≠ R360), L297 (≠ A361), S298 (≠ A362)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R112), L191 (≠ N247), P192 (= P248), H195 (= H251), I196 (≠ T252), S197 (≠ F253), A237 (≠ G294), V238 (≠ P295), L260 (≠ V320), G262 (= G322), G286 (= G348), M287 (≠ L349), S292 (≠ A356), Q293 (≠ T357), S388 (≠ V453), G389 (= G454), G390 (= G455), E391 (≠ F456), K420 (≠ R485), W421 (≠ L486), K450 (≠ N517), Y451 (= Y518)
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)
29% identity, 87% coverage: 71:544/546 of query aligns to 80:547/556 of Q9S725
- K211 (= K215) mutation to S: Drastically reduces the activity.
- M293 (≠ P293) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V320) mutation K->L,A: Affects the substrate specificity.
- E401 (= E398) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ T400) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R446) mutation to Q: Drastically reduces the activity.
- K457 (≠ G454) mutation to S: Drastically reduces the activity.
- K540 (= K537) 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)
30% identity, 92% coverage: 45:545/546 of query aligns to 17:475/475 of 5burA
- active site: T150 (= T207), S170 (≠ A227), H194 (= H251), T287 (= T350), E288 (= E351)
- binding adenosine-5'-triphosphate: T150 (= T207), S151 (= S208), T153 (= T210), T154 (= T211), K158 (= K215), G263 (≠ S324), S283 (≠ G346), T287 (= T350), D365 (= D431), V377 (≠ I443), R380 (= R446)
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, 93% coverage: 38:543/546 of query aligns to 39:536/546 of Q84P21
- K530 (= K537) mutation to N: Lossed enzymatic activity.
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
30% identity, 92% coverage: 45:545/546 of query aligns to 17:475/481 of 5busA
- active site: T150 (= T207), S170 (≠ A227), H194 (= H251), T287 (= T350), E288 (= E351)
- binding adenosine monophosphate: H194 (= H251), G262 (≠ A323), G263 (≠ S324), S283 (≠ G346), M286 (≠ L349), T287 (= T350), D365 (= D431), V377 (≠ I443), R380 (= R446), K467 (= K537)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
29% identity, 95% coverage: 27:545/546 of query aligns to 14:527/528 of 3ni2A
- active site: S182 (≠ T207), S202 (vs. gap), H230 (= H251), T329 (= T350), E330 (= E351), K434 (≠ I452), Q439 (≠ N457), K519 (= K537)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F253), S236 (≠ A257), G302 (≠ A323), A303 (≠ S324), P304 (≠ A325), G325 (= G346), G327 (= G348), T329 (= T350), P333 (≠ G354), V334 (≠ F355), D413 (= D431), K430 (= K448), K434 (≠ I452), Q439 (≠ N457)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
29% identity, 95% coverage: 27:545/546 of query aligns to 14:527/528 of 3a9vA
- active site: S182 (≠ T207), S202 (vs. gap), H230 (= H251), T329 (= T350), E330 (= E351), K434 (≠ I452), Q439 (≠ N457), K519 (= K537)
- binding adenosine monophosphate: H230 (= H251), G302 (≠ A323), A303 (≠ S324), P304 (≠ A325), Y326 (= Y347), G327 (= G348), M328 (≠ L349), T329 (= T350), D413 (= D431), K430 (= K448), K434 (≠ I452), Q439 (≠ N457)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
31% identity, 95% coverage: 26:545/546 of query aligns to 7:528/533 of 6ihkB
- active site: T185 (= T207), H202 (= H229), H228 (= H251), S326 (≠ T350), E327 (= E351), K435 (≠ I452), W440 (≠ N457), K520 (= K537)
- binding adenosine-5'-diphosphate: H228 (= H251), G300 (≠ A323), A301 (≠ S324), A302 (= A325), H321 (≠ T345), A322 (≠ G346), W323 (≠ Y347), G324 (= G348), M325 (≠ L349), S326 (≠ T350), Q356 (≠ S372), D414 (= D431), R429 (= R446), K520 (= K537)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 89% coverage: 58:544/546 of query aligns to 50:525/528 of 5bsrA
- active site: S181 (≠ T207), S201 (≠ Q223), H229 (= H251), T328 (= T350), E329 (= E351), K433 (≠ I452), Q438 (≠ N457), K518 (= K537)
- binding adenosine monophosphate: A301 (= A323), G326 (= G348), T328 (= T350), D412 (= D431), K429 (= K448), K433 (≠ I452), Q438 (≠ N457)
- binding coenzyme a: L102 (≠ R112), P226 (= P248), H229 (= H251), Y231 (≠ F253), F253 (= F275), K435 (≠ G454), G436 (= G455), F437 (= F456), F498 (≠ N517)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
30% identity, 89% coverage: 58:544/546 of query aligns to 51:526/530 of 5bsmA
- active site: S182 (≠ T207), S202 (≠ Q223), H230 (= H251), T329 (= T350), E330 (= E351), K434 (≠ I452), Q439 (≠ N457), K519 (= K537)
- binding adenosine-5'-triphosphate: S182 (≠ T207), S183 (= S208), G184 (= G209), T185 (= T210), T186 (= T211), K190 (= K215), H230 (= H251), A302 (= A323), A303 (≠ S324), P304 (≠ A325), Y326 (= Y347), G327 (= G348), M328 (≠ L349), T329 (= T350), D413 (= D431), I425 (= I443), R428 (= R446), K519 (= K537)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 89% coverage: 58:544/546 of query aligns to 51:526/529 of 5bsvA
- active site: S182 (≠ T207), S202 (≠ Q223), H230 (= H251), T329 (= T350), E330 (= E351), K434 (≠ I452), Q439 (≠ N457), K519 (= K537)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H251), Y232 (≠ F253), S236 (≠ A257), A302 (= A323), A303 (≠ S324), P304 (≠ A325), G325 (= G346), G327 (= G348), M328 (≠ L349), T329 (= T350), P333 (≠ G354), V334 (≠ F355), D413 (= D431), K430 (= K448), K434 (≠ I452), Q439 (≠ N457)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 89% coverage: 58:544/546 of query aligns to 51:526/529 of 5bsuA
- active site: S182 (≠ T207), S202 (≠ Q223), H230 (= H251), T329 (= T350), E330 (= E351), K434 (≠ I452), Q439 (≠ N457), K519 (= K537)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H251), Y232 (≠ F253), S236 (≠ A257), M299 (≠ V320), A302 (= A323), A303 (≠ S324), P304 (≠ A325), G325 (= G346), G327 (= G348), M328 (≠ L349), T329 (= T350), P333 (≠ G354), D413 (= D431), K430 (= K448), K434 (≠ I452), Q439 (≠ N457)
Query Sequence
>RR42_RS31975 FitnessBrowser__Cup4G11:RR42_RS31975
MMTTDTIETEPRLAGAASAGQAIPATIPATIPELVRTAAARHGARIAIQEDGLRLSFTEL
DTLRAQAGRALLALGLLPGDRVAVWAPNLSEWIVAALAAHSIGAALVPINTRMKGMEAGA
ILADSGARVLFCIDNFLGESYPEMLAPHRPGTLERIVVLRGRAGRQMAPDELAWADFLAL
AAQTGEAAFRACESAVSGDTLMDIMFTSGTTGRPKGVMTAHAQNLQAIHGWASITGVEAG
DRYLIVNPFFHTFGYKAGWLAALASGATILPHLVFDAEAVMTRIENERITVLPGPPTLYQ
TLLNHPRLREFDLSSLRVAVTGASAIPPVLIQRMRRELGFRDIFTGYGLTESCGFATLTR
AADDADIVALTSGRAMPGVELRCVDGAGYPVPAGEPGEVTVRGYNVMRGYFQLPEATTEA
IDAGGWLRTGDIGTLDVRGNLRITDRIKDMFIVGGFNCYPAEIEKLLVSHPAIAQVAVVG
VPHERLGEAGKAFVVLRHGSKVGADELIDWARRHMANYKVPREVVFVQTLPTSAAGKILK
YRLREG
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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