SitesBLAST
Comparing Ga0059261_0835 FitnessBrowser__Korea:Ga0059261_0835 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)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
34% identity, 89% coverage: 56:573/582 of query aligns to 7:477/484 of 5gtdA
- active site: T151 (= T226), S171 (≠ N246), H195 (= H281), T288 (= T379), E289 (= E380)
- binding adenosine-5'-monophosphate: G263 (= G353), G264 (≠ A354), Y285 (≠ W376), G286 (= G377), M287 (= M378), T288 (= T379), D366 (= D459), V378 (≠ I471)
- binding magnesium ion: F314 (≠ P405), S315 (≠ V406)
- binding 2-succinylbenzoate: H195 (= H281), S197 (≠ T283), A237 (≠ G324), L260 (≠ A350), G262 (= G352), G263 (= G353), G286 (= G377), M287 (= M378), S292 (≠ A383), Q293 (≠ T384)
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)
34% identity, 89% coverage: 56:573/582 of query aligns to 7:477/485 of 5x8fB
- active site: T151 (= T226), S171 (≠ N246), H195 (= H281), T288 (= T379), E289 (= E380), I387 (= I480), N392 (= N485), K470 (= K566)
- binding magnesium ion: Y23 (≠ H72), E24 (= E73), H70 (≠ F119), N178 (≠ R260), L202 (= L289), L214 (≠ F301), T296 (≠ Q387), L297 (≠ H388), S298 (= S389)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ W134), L191 (≠ I277), P192 (= P278), H195 (= H281), I196 (≠ V282), S197 (≠ T283), A237 (≠ G324), V238 (= V325), L260 (≠ A350), G262 (= G352), G286 (= G377), M287 (= M378), S292 (≠ A383), Q293 (≠ T384), S388 (≠ R481), G389 (= G482), G390 (= G483), E391 (= E484), K420 (≠ T513), W421 (≠ L514), K450 (≠ A545), Y451 (≠ F546)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
34% identity, 89% coverage: 56:573/582 of query aligns to 6:474/475 of 5burA
- active site: T150 (= T226), S170 (≠ N246), H194 (= H281), T287 (= T379), E288 (= E380)
- binding adenosine-5'-triphosphate: T150 (= T226), S151 (= S227), T153 (= T229), T154 (= T230), K158 (= K234), G263 (≠ A354), S283 (≠ G375), T287 (= T379), D365 (= D459), V377 (≠ I471), R380 (= R474)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
33% identity, 89% coverage: 56:573/582 of query aligns to 6:474/481 of 5busA
- active site: T150 (= T226), S170 (≠ N246), H194 (= H281), T287 (= T379), E288 (= E380)
- binding adenosine monophosphate: H194 (= H281), G262 (= G353), G263 (≠ A354), S283 (≠ G375), M286 (= M378), T287 (= T379), D365 (= D459), V377 (≠ I471), R380 (= R474), K467 (= K566)
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)
33% identity, 87% coverage: 74:577/582 of query aligns to 27:498/503 of P9WQ37
- K172 (= K234) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ P257) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ L259) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V282) 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 (= A284) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ A287) 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 (≠ K318) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G377) 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 (= W454) 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 (= D459) 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 (= R474) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R481) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G483) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K566) 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.
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, 88% coverage: 59:573/582 of query aligns to 31:550/561 of P69451
- Y213 (= Y225) 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 (= E380) mutation to A: Loss of activity.
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: 88:578/582 of query aligns to 75:552/556 of Q9S725
- K211 (= K234) mutation to S: Drastically reduces the activity.
- M293 (≠ G323) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ A350) mutation K->L,A: Affects the substrate specificity.
- E401 (= E427) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ W429) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R474) mutation to Q: Drastically reduces the activity.
- K457 (≠ G482) mutation to S: Drastically reduces the activity.
- K540 (= K566) mutation to N: Abolishes the activity.
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, 84% coverage: 88:577/582 of query aligns to 76:574/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
33% identity, 84% coverage: 88:577/582 of query aligns to 71:546/559 of Q67W82
- G395 (= G426) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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)
31% identity, 88% coverage: 60:572/582 of query aligns to 39:536/546 of Q84P21
- K530 (= K566) mutation to N: Lossed enzymatic activity.
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
31% identity, 87% coverage: 72:576/582 of query aligns to 44:537/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H281), F245 (≠ T283), T249 (≠ A287), G314 (= G353), A315 (= A354), P316 (= P355), G337 (= G375), Y338 (≠ W376), G339 (= G377), L340 (≠ M378), T341 (= T379), A346 (≠ T384), D420 (= D459), I432 (= I471), K527 (= K566)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
31% identity, 87% coverage: 72:578/582 of query aligns to 44:539/539 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 (= H281), F245 (≠ T283), T249 (≠ A287), G314 (= G353), A315 (= A354), P316 (= P355), G337 (= G375), Y338 (≠ W376), G339 (= G377), L340 (≠ M378), T341 (= T379), S345 (≠ A383), A346 (≠ T384), D420 (= D459), I432 (= I471), K527 (= K566)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ T283), R335 (vs. gap), G337 (= G375), G339 (= G377), L340 (≠ M378), A346 (≠ T384)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
33% identity, 87% coverage: 74:577/582 of query aligns to 30:498/502 of 3r44A
Sites not aligning to the query:
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
33% identity, 84% coverage: 88:573/582 of query aligns to 57:526/528 of 3ni2A
- active site: S182 (≠ T226), S202 (≠ N246), H230 (= H281), T329 (= T379), E330 (= E380), K434 (≠ I480), Q439 (≠ N485), K519 (= K566)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ T283), S236 (≠ A287), G302 (= G353), A303 (= A354), P304 (= P355), G325 (= G375), G327 (= G377), T329 (= T379), P333 (vs. gap), V334 (≠ T381), D413 (= D459), K430 (= K476), K434 (≠ I480), Q439 (≠ N485)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
33% identity, 84% coverage: 88:573/582 of query aligns to 57:526/528 of 3a9vA
- active site: S182 (≠ T226), S202 (≠ N246), H230 (= H281), T329 (= T379), E330 (= E380), K434 (≠ I480), Q439 (≠ N485), K519 (= K566)
- binding adenosine monophosphate: H230 (= H281), G302 (= G353), A303 (= A354), P304 (= P355), Y326 (≠ W376), G327 (= G377), M328 (= M378), T329 (= T379), D413 (= D459), K430 (= K476), K434 (≠ I480), Q439 (≠ N485)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
33% identity, 87% coverage: 75:578/582 of query aligns to 27:503/506 of 4gxqA
- active site: T163 (= T226), N183 (= N246), H207 (= H281), T303 (= T379), E304 (= E380), I403 (= I480), N408 (= N485), A491 (≠ K566)
- binding adenosine-5'-triphosphate: T163 (= T226), S164 (= S227), G165 (= G228), T166 (= T229), T167 (= T230), H207 (= H281), S277 (≠ G353), A278 (= A354), P279 (= P355), E298 (vs. gap), M302 (= M378), T303 (= T379), D382 (= D459), R397 (= R474)
- binding carbonate ion: H207 (= H281), S277 (≠ G353), R299 (vs. gap), G301 (= G377)
5buqB Unliganded form of o-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, solved at 1.98 angstroms (see paper)
32% identity, 89% coverage: 56:573/582 of query aligns to 6:465/473 of 5buqB
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: 88:577/582 of query aligns to 64:537/542 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 (= H281) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ T283) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ A287) binding ; binding ; binding
- K260 (= K304) binding
- A309 (≠ G353) binding ; binding ; binding
- Q331 (≠ N374) binding
- G332 (= G375) binding ; binding ; binding ; binding ; binding
- T336 (= T379) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ T381) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ T384) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D459) binding ; binding ; binding ; binding ; binding
- R435 (= R474) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K476) binding ; binding ; binding ; binding
- K441 (≠ I480) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G482) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G483) binding
- Q446 (≠ N485) binding
- K526 (= K566) 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)
31% identity, 84% coverage: 88:577/582 of query aligns to 57:530/530 of 5bsmA
- active site: S182 (≠ T226), S202 (≠ N246), H230 (= H281), T329 (= T379), E330 (= E380), K434 (≠ I480), Q439 (≠ N485), K519 (= K566)
- binding adenosine-5'-triphosphate: S182 (≠ T226), S183 (= S227), G184 (= G228), T185 (= T229), T186 (= T230), K190 (= K234), H230 (= H281), A302 (≠ G353), A303 (= A354), P304 (= P355), Y326 (≠ W376), G327 (= G377), M328 (= M378), T329 (= T379), D413 (= D459), I425 (= I471), R428 (= R474), K519 (= K566)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
31% identity, 84% coverage: 88:574/582 of query aligns to 56:526/528 of 5bsrA
- active site: S181 (≠ T226), S201 (≠ N246), H229 (= H281), T328 (= T379), E329 (= E380), K433 (≠ I480), Q438 (≠ N485), K518 (= K566)
- binding adenosine monophosphate: A301 (≠ G353), G326 (= G377), T328 (= T379), D412 (= D459), K429 (= K476), K433 (≠ I480), Q438 (≠ N485)
- binding coenzyme a: L102 (≠ W134), P226 (= P278), H229 (= H281), Y231 (≠ T283), F253 (≠ W305), K435 (≠ G482), G436 (= G483), F437 (≠ E484), F498 (≠ A545)
Query Sequence
>Ga0059261_0835 FitnessBrowser__Korea:Ga0059261_0835
VAAEPIIPLDPNWPKMTLGQAQALMTAPGQKFEMDEVEIRGVRTRVWKNAPPSLAWLIQA
SRMHGDRIFTIHEDERVSFEANFRAVARLATQLREMGVGKGDRVALAMRNLPEWPVVFFA
AVSIGAILVPLNAWWTSGELDYGLRDSGSVVLFTDGERYDRLADALPGLPDLKHIVVSRA
RGPLGEGVRQLEDLIGKPGDWAELPDAPLPAEPSLVPDDDATIFYTSGTTGHPKGALGTH
RNLITNILSSGYCGARPYLRRGEMPPDPTPRVGLMVIPLFHVTACSASLMGAVFAGHTTI
FMRKWDVEQAMEIIQREKVNLTGGVPTIAWQLLEHPARAKYDLSSLEMIAYGGAPSAPEL
VKRIYTEFGALPGNGWGMTETMATVTQHSAEDYLNRPTSAGPPVPVAELKIMDAEGEHEL
PIGEVGELWAKGPMIVKGYWNKPEETAESFRDGWVRTGDLARVDEEGFLFIVDRAKDIII
RGGENIYSSEVEDVLYAHPAVTDAALIGIPHRTLGEEPVAVVHLAPGKQASEAELQQWVR
DRLAAFKVPVAIRFTRDTLPRNANGKILKKDLKGLFAEEAAA
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