SitesBLAST
Comparing RR42_RS28980 FitnessBrowser__Cup4G11:RR42_RS28980 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)
32% identity, 90% coverage: 55:577/580 of query aligns to 43:572/590 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)
32% identity, 88% coverage: 72:580/580 of query aligns to 27:499/503 of P9WQ37
- K172 (= K232) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ L257) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R259) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V284) 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 (≠ G286) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ A289) 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 (= R320) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G380) 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 (= W456) 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 (= D461) 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 (= R476) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R483) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G485) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K568) 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)
32% identity, 88% coverage: 72:580/580 of query aligns to 30:499/502 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)
31% identity, 90% coverage: 55:575/580 of query aligns to 8:477/484 of 5gtdA
- active site: T151 (= T224), S171 (≠ V244), H195 (= H283), T288 (= T382), E289 (= E383)
- binding adenosine-5'-monophosphate: G263 (= G355), G264 (≠ A356), Y285 (≠ W379), G286 (= G380), M287 (= M381), T288 (= T382), D366 (= D461), V378 (≠ I473)
- binding magnesium ion: F314 (≠ P408), S315 (≠ I409)
- binding 2-succinylbenzoate: H195 (= H283), S197 (≠ T285), A237 (≠ G326), L260 (≠ N352), G262 (= G354), G263 (= G355), G286 (= G380), M287 (= M381), S292 (≠ A386), Q293 (≠ T387)
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)
31% identity, 90% coverage: 55:575/580 of query aligns to 8:477/485 of 5x8fB
- active site: T151 (= T224), S171 (≠ V244), H195 (= H283), T288 (= T382), E289 (= E383), I387 (= I482), N392 (= N487), K470 (= K568)
- binding magnesium ion: Y23 (= Y70), E24 (= E71), H70 (≠ Y117), N178 (≠ R258), L202 (≠ V290), L214 (= L303), T296 (≠ S390), L297 (≠ H391), S298 (= S392)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ W132), L191 (≠ V279), P192 (= P280), H195 (= H283), I196 (≠ V284), S197 (≠ T285), A237 (≠ G326), V238 (= V327), L260 (≠ N352), G262 (= G354), G286 (= G380), M287 (= M381), S292 (≠ A386), Q293 (≠ T387), S388 (≠ R483), G389 (= G484), G390 (= G485), E391 (= E486), K420 (≠ T515), W421 (≠ L516), K450 (≠ A547), Y451 (≠ F548)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
31% identity, 90% coverage: 55:575/580 of query aligns to 7:474/475 of 5burA
- active site: T150 (= T224), S170 (≠ V244), H194 (= H283), T287 (= T382), E288 (= E383)
- binding adenosine-5'-triphosphate: T150 (= T224), S151 (= S225), T153 (= T227), T154 (= T228), K158 (= K232), G263 (≠ A356), S283 (≠ G378), T287 (= T382), D365 (= D461), V377 (≠ I473), R380 (= R476)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
31% identity, 90% coverage: 55:575/580 of query aligns to 7:474/481 of 5busA
- active site: T150 (= T224), S170 (≠ V244), H194 (= H283), T287 (= T382), E288 (= E383)
- binding adenosine monophosphate: H194 (= H283), G262 (= G355), G263 (≠ A356), S283 (≠ G378), M286 (= M381), T287 (= T382), D365 (= D461), V377 (≠ I473), R380 (= R476), K467 (= K568)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
31% identity, 84% coverage: 87:575/580 of query aligns to 58:526/529 of 5bsvA
- active site: S182 (≠ T224), S202 (≠ V244), H230 (= H283), T329 (= T382), E330 (= E383), K434 (≠ I482), Q439 (≠ N487), K519 (= K568)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H283), Y232 (≠ T285), S236 (≠ A289), A302 (≠ G355), A303 (= A356), P304 (= P357), G325 (= G378), G327 (= G380), M328 (= M381), T329 (= T382), P333 (vs. gap), V334 (vs. gap), D413 (= D461), K430 (= K478), K434 (≠ I482), Q439 (≠ N487)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
31% identity, 84% coverage: 87:575/580 of query aligns to 58:526/529 of 5bsuA
- active site: S182 (≠ T224), S202 (≠ V244), H230 (= H283), T329 (= T382), E330 (= E383), K434 (≠ I482), Q439 (≠ N487), K519 (= K568)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H283), Y232 (≠ T285), S236 (≠ A289), M299 (≠ N352), A302 (≠ G355), A303 (= A356), P304 (= P357), G325 (= G378), G327 (= G380), M328 (= M381), T329 (= T382), P333 (vs. gap), D413 (= D461), K430 (= K478), K434 (≠ I482), Q439 (≠ N487)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
31% identity, 84% coverage: 87:575/580 of query aligns to 58:526/529 of 5bstA
- active site: S182 (≠ T224), S202 (≠ V244), H230 (= H283), T329 (= T382), E330 (= E383), K434 (≠ I482), Q439 (≠ N487), K519 (= K568)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H283), Y232 (≠ T285), S236 (≠ A289), A302 (≠ G355), A303 (= A356), P304 (= P357), G325 (= G378), Y326 (≠ W379), G327 (= G380), M328 (= M381), T329 (= T382), P333 (vs. gap), V334 (vs. gap), D413 (= D461), K430 (= K478), K434 (≠ I482), Q439 (≠ N487)
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)
31% identity, 84% coverage: 87:575/580 of query aligns to 65:533/542 of O24146
- S189 (≠ T224) binding
- S190 (= S225) binding
- G191 (= G226) binding
- T192 (= T227) binding
- T193 (= T228) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K232) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H283) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ T285) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ A289) binding ; binding ; binding
- K260 (≠ R306) binding
- A309 (≠ G355) binding ; binding ; binding
- Q331 (≠ I377) binding
- G332 (= G378) binding ; binding ; binding ; binding ; binding
- T336 (= T382) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (vs. gap) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ T387) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D461) binding ; binding ; binding ; binding ; binding
- R435 (= R476) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K478) binding ; binding ; binding ; binding
- K441 (≠ I482) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G484) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G485) binding
- Q446 (≠ N487) binding
- K526 (= K568) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
31% identity, 84% coverage: 87:575/580 of query aligns to 57:525/528 of 5bsrA
- active site: S181 (≠ T224), S201 (≠ V244), H229 (= H283), T328 (= T382), E329 (= E383), K433 (≠ I482), Q438 (≠ N487), K518 (= K568)
- binding adenosine monophosphate: A301 (≠ G355), G326 (= G380), T328 (= T382), D412 (= D461), K429 (= K478), K433 (≠ I482), Q438 (≠ N487)
- binding coenzyme a: L102 (≠ W132), P226 (= P280), H229 (= H283), Y231 (≠ T285), F253 (≠ W307), K435 (≠ G484), G436 (= G485), F437 (≠ E486), F498 (≠ A547)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
31% identity, 84% coverage: 87:575/580 of query aligns to 58:526/530 of 5bsmA
- active site: S182 (≠ T224), S202 (≠ V244), H230 (= H283), T329 (= T382), E330 (= E383), K434 (≠ I482), Q439 (≠ N487), K519 (= K568)
- binding adenosine-5'-triphosphate: S182 (≠ T224), S183 (= S225), G184 (= G226), T185 (= T227), T186 (= T228), K190 (= K232), H230 (= H283), A302 (≠ G355), A303 (= A356), P304 (= P357), Y326 (≠ W379), G327 (= G380), M328 (= M381), T329 (= T382), D413 (= D461), I425 (= I473), R428 (= R476), K519 (= K568)
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)
29% identity, 87% coverage: 73:577/580 of query aligns to 56:539/546 of Q84P21
- K530 (= K568) mutation to N: Lossed enzymatic activity.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
31% identity, 86% coverage: 76:576/580 of query aligns to 47:527/528 of 3ni2A
- active site: S182 (≠ T224), S202 (≠ V244), H230 (= H283), T329 (= T382), E330 (= E383), K434 (≠ I482), Q439 (≠ N487), K519 (= K568)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ T285), S236 (≠ A289), G302 (= G355), A303 (= A356), P304 (= P357), G325 (= G378), G327 (= G380), T329 (= T382), P333 (vs. gap), V334 (vs. gap), D413 (= D461), K430 (= K478), K434 (≠ I482), Q439 (≠ N487)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
31% identity, 86% coverage: 76:576/580 of query aligns to 47:527/528 of 3a9vA
- active site: S182 (≠ T224), S202 (≠ V244), H230 (= H283), T329 (= T382), E330 (= E383), K434 (≠ I482), Q439 (≠ N487), K519 (= K568)
- binding adenosine monophosphate: H230 (= H283), G302 (= G355), A303 (= A356), P304 (= P357), Y326 (≠ W379), G327 (= G380), M328 (= M381), T329 (= T382), D413 (= D461), K430 (= K478), K434 (≠ I482), Q439 (≠ N487)
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)
32% identity, 84% coverage: 87:575/580 of query aligns to 76:547/556 of Q9S725
- K211 (= K232) mutation to S: Drastically reduces the activity.
- M293 (≠ G325) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ N352) mutation K->L,A: Affects the substrate specificity.
- E401 (= E429) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ M431) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R476) mutation to Q: Drastically reduces the activity.
- K457 (≠ G484) mutation to S: Drastically reduces the activity.
- K540 (= K568) mutation to N: Abolishes the activity.
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
30% identity, 88% coverage: 70:578/580 of query aligns to 44:537/539 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 (= H283), F245 (≠ T285), T249 (≠ A289), G314 (= G355), A315 (= A356), P316 (= P357), G337 (= G378), Y338 (≠ W379), G339 (= G380), L340 (≠ M381), T341 (= T382), S345 (≠ A386), A346 (≠ T387), D420 (= D461), I432 (= I473), K527 (= K568)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ T285), R335 (vs. gap), G337 (= G378), G339 (= G380), L340 (≠ M381), A346 (≠ T387)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
30% identity, 88% coverage: 70:578/580 of query aligns to 44:537/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H283), F245 (≠ T285), T249 (≠ A289), G314 (= G355), A315 (= A356), P316 (= P357), G337 (= G378), Y338 (≠ W379), G339 (= G380), L340 (≠ M381), T341 (= T382), A346 (≠ T387), D420 (= D461), I432 (= I473), K527 (= K568)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
31% identity, 84% coverage: 87:575/580 of query aligns to 57:522/527 of 5u95B
Query Sequence
>RR42_RS28980 FitnessBrowser__Cup4G11:RR42_RS28980
MSNNPQSATTWPAISLAEAHARLTAPGAPFETETRVIRGIATVVWKNAPPTLRDLFLQAR
ALGDKTFVVYEDERVSYDAFARAALTIAHALIRDGVTKGDRVALAMRNLPEWPAVFYGAL
LTGAIVTPLNAWWTGAELEYGLADSGSKIAIVDDERLGRIIEHLPGCPALEKIYVSRANA
PASDARISQLESLIGTPDQWASLPALPVPVVAIDADDDATIFYTSGTTGKPKGALGTHRN
ATNVAVAAAFSPMRNCLRRGETIPAPDPGAPQKGMLLSVPFFHVTGCMAVLNGALASGTK
IVLMRRWDAVRAMGLIERERCTAAGGVPTIAWQIIEHPERERFDLSSLENVNYGGAPASA
ELVRRIKEVFPHSAPGIGWGMTETSATFTSHSAEEYVERPESGGPALPIGEMKVVDGRGH
SLPTGETGELMVRGANVVRGYWNKPEATAQTFIDGWLKTGDIARLDEEGFVYIVDRMKDM
LIRGGENIYSIEVESALYDHPAIMDAALVGIPHRTLGEEPAAVVSLKPGAQATEAELQAF
VGERLAAFKVPVRIVFCPDMLPRNANGKILKSTLRKMFDA
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