SitesBLAST
Comparing GFF2429 FitnessBrowser__psRCH2:GFF2429 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)
32% identity, 89% coverage: 39:522/542 of query aligns to 29:500/503 of P9WQ37
- K172 (= K188) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ K211) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ S213) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ S225) 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 (≠ Q227) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V230) 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 (≠ Q261) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G321) 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 (= W398) 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 (= D403) 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 (= R418) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ T425) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G427) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K509) 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)
31% identity, 89% coverage: 39:522/542 of query aligns to 32:500/502 of 3r44A
Sites not aligning to the query:
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 91% coverage: 25:519/542 of query aligns to 13:501/506 of 4gxqA
- active site: T163 (= T180), N183 (≠ E200), H207 (= H224), T303 (≠ S323), E304 (= E324), I403 (≠ N424), N408 (≠ L429), A491 (≠ K509)
- binding adenosine-5'-triphosphate: T163 (= T180), S164 (= S181), G165 (= G182), T166 (= T183), T167 (= T184), H207 (= H224), S277 (≠ A296), A278 (≠ S297), P279 (≠ I298), E298 (≠ N318), M302 (≠ Q322), T303 (≠ S323), D382 (= D403), R397 (= R418)
- binding carbonate ion: H207 (= H224), S277 (≠ A296), R299 (≠ C319), G301 (= G321)
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)
28% identity, 95% coverage: 3:516/542 of query aligns to 14:550/561 of P69451
- Y213 (= Y179) mutation to A: Loss of activity.
- T214 (= T180) mutation to A: 10% of wild-type activity.
- G216 (= G182) mutation to A: Decreases activity.
- T217 (= T183) mutation to A: Decreases activity.
- G219 (≠ S185) mutation to A: Decreases activity.
- K222 (= K188) mutation to A: Decreases activity.
- E361 (= E324) mutation to A: Loss of activity.
Q5SKN9 Long-chain-fatty-acid--CoA ligase; Long-chain fatty acyl-CoA synthetase; LC-FACS; EC 6.2.1.3 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
29% identity, 89% coverage: 39:519/542 of query aligns to 47:534/541 of Q5SKN9
- T184 (= T180) binding
- G302 (≠ A296) binding
- Q322 (≠ N318) binding
- G323 (≠ C319) binding
- T327 (≠ S323) binding
- E328 (= E324) binding
- D418 (= D403) binding
- K435 (= K420) binding
- K439 (≠ N424) binding
5ie2A Crystal structure of a plant enzyme (see paper)
30% identity, 93% coverage: 14:519/542 of query aligns to 4:505/506 of 5ie2A
- active site: T165 (= T180), S185 (≠ E200), H209 (= H224), T310 (≠ S323), E311 (= E324), N410 (= N424), K415 (≠ L429), K495 (= K509)
- binding adenosine-5'-triphosphate: T165 (= T180), S166 (= S181), G167 (= G182), T168 (= T183), T169 (= T184), S284 (≠ G295), A285 (= A296), S286 (= S297), Y307 (= Y320), A308 (≠ G321), M309 (≠ Q322), T310 (≠ S323), D389 (= D403), L401 (≠ I415), R404 (= R418), K495 (= K509)
5ie3A Crystal structure of a plant enzyme (see paper)
29% identity, 93% coverage: 14:519/542 of query aligns to 4:503/504 of 5ie3A
- active site: T163 (= T180), S183 (≠ E200), H207 (= H224), T308 (≠ S323), E309 (= E324), N408 (= N424), K413 (≠ L429), K493 (= K509)
- binding adenosine monophosphate: S164 (= S181), S282 (≠ G295), A283 (= A296), S284 (= S297), Y305 (= Y320), A306 (≠ G321), M307 (≠ Q322), T308 (≠ S323), D387 (= D403), L399 (≠ I415), R402 (= R418), K493 (= K509)
- binding oxalic acid: V208 (vs. gap), S282 (≠ G295), A306 (≠ G321), M307 (≠ Q322), H312 (≠ P327), K493 (= K509)
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)
28% identity, 92% coverage: 20:516/542 of query aligns to 9:477/485 of 5x8fB
- active site: T151 (= T180), S171 (≠ E200), H195 (= H224), T288 (≠ S323), E289 (= E324), I387 (≠ N424), N392 (≠ L429), K470 (= K509)
- binding magnesium ion: Y23 (= Y35), E24 (≠ R36), H70 (≠ L82), N178 (≠ H207), L202 (≠ F231), L214 (= L244), T296 (≠ V331), L297 (= L332), S298 (≠ T333)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ S97), L191 (= L220), P192 (= P221), H195 (= H224), I196 (≠ S225), S197 (≠ A226), A237 (= A267), V238 (≠ P268), L260 (≠ Y293), G262 (= G295), G286 (= G321), M287 (≠ Q322), S292 (≠ P327), Q293 (≠ L328), S388 (≠ T425), G389 (= G426), G390 (= G427), E391 (≠ V428), K420 (= K457), W421 (= W458), K450 (≠ P489), Y451 (≠ F490)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
28% identity, 92% coverage: 20:516/542 of query aligns to 9:477/484 of 5gtdA
- active site: T151 (= T180), S171 (≠ E200), H195 (= H224), T288 (≠ S323), E289 (= E324)
- binding adenosine-5'-monophosphate: G263 (≠ A296), G264 (≠ S297), Y285 (= Y320), G286 (= G321), M287 (≠ Q322), T288 (≠ S323), D366 (= D403), V378 (≠ I415)
- binding magnesium ion: F314 (≠ S349), S315 (≠ N350)
- binding 2-succinylbenzoate: H195 (= H224), S197 (≠ A226), A237 (= A267), L260 (≠ Y293), G262 (= G295), G263 (≠ A296), G286 (= G321), M287 (≠ Q322), S292 (≠ P327), Q293 (≠ L328)
Q9SMT7 Oxalate--CoA ligase; 4-coumarate--CoA ligase isoform 8; At4CL8; 4-coumarate--CoA ligase-like 10; Acyl-activating enzyme 3; Adenosine monophosphate binding protein 3; AtMPBP3; Oxalyl-CoA synthetase; EC 6.2.1.8 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 93% coverage: 14:519/542 of query aligns to 4:510/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 180:184) binding
- H214 (= H224) binding ; mutation to A: Abolished activity.
- S289 (≠ G295) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ GAS 295:297) binding
- EA 310:311 (≠ QS 313:314) binding
- M314 (≠ Q322) binding
- T315 (≠ S323) binding
- H319 (≠ P327) binding ; mutation to A: Abolished activity.
- D394 (= D403) binding
- R409 (= R418) binding ; mutation to A: Abolished activity.
- K500 (= K509) binding ; binding ; mutation to A: Abolished activity.
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
28% identity, 92% coverage: 19:516/542 of query aligns to 27:534/539 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 (= H224), F245 (≠ A226), T249 (= T232), G314 (≠ A296), A315 (≠ S297), P316 (≠ I298), G337 (≠ C319), Y338 (= Y320), G339 (= G321), L340 (≠ Q322), T341 (≠ S323), S345 (≠ P327), A346 (= A329), D420 (= D403), I432 (= I415), K527 (= K509)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ A226), R335 (≠ Y317), G337 (≠ C319), G339 (= G321), L340 (≠ Q322), A346 (= A329)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
28% identity, 92% coverage: 19:516/542 of query aligns to 27:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H224), F245 (≠ A226), T249 (= T232), G314 (≠ A296), A315 (≠ S297), P316 (≠ I298), G337 (≠ C319), Y338 (= Y320), G339 (= G321), L340 (≠ Q322), T341 (≠ S323), A346 (= A329), D420 (= D403), I432 (= I415), K527 (= K509)
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)
28% identity, 94% coverage: 7:516/542 of query aligns to 30:570/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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, 87% coverage: 49:519/542 of query aligns to 49:533/539 of P0DX84
- H231 (= H224) mutation to A: Retains 74% of wild-type activity.
- W235 (≠ F231) mutation to A: Almost completely abolishes the activity.
- G302 (= G295) mutation to P: Almost completely abolishes the activity.
- G303 (≠ A296) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y320) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P327) mutation to A: Retains 69% of wild-type activity.
- R432 (= R418) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K420) mutation to A: Retains 36% of wild-type activity.
- D435 (= D421) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ N424) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G426) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G427) mutation to P: Retains 2.7% of wild-type activity.
- E442 (≠ V428) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ L429) mutation to A: Retains 60% of wild-type activity.
- E474 (= E460) mutation to A: Retains 33% of wild-type activity.
- K523 (= K509) 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 (= K512) mutation to A: Retains 48% of wild-type activity.
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
27% identity, 92% coverage: 20:516/542 of query aligns to 8:474/481 of 5busA
- active site: T150 (= T180), S170 (≠ E200), H194 (= H224), T287 (≠ S323), E288 (= E324)
- binding adenosine monophosphate: H194 (= H224), G262 (≠ A296), G263 (≠ S297), S283 (≠ C319), M286 (≠ Q322), T287 (≠ S323), D365 (= D403), V377 (≠ I415), R380 (= R418), K467 (= K509)
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
29% identity, 87% coverage: 49:519/542 of query aligns to 49:533/538 of 6ijbB
- active site: T185 (= T180), H205 (≠ M198), H231 (= H224), S329 (= S323), E330 (= E324), K438 (≠ N424), W443 (≠ L429), A523 (≠ K509)
- binding 3-(methylsulfanyl)propanoic acid: W235 (≠ F231), G303 (≠ A296), A325 (≠ C319), W326 (≠ Y320), G327 (= G321), M328 (≠ Q322)
- binding adenosine monophosphate: G303 (≠ A296), A304 (≠ S297), A305 (≠ I298), H324 (≠ Y317), W326 (≠ Y320), G327 (= G321), M328 (≠ Q322), S329 (= S323), Q359 (≠ C344), D417 (= D403)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
27% identity, 92% coverage: 20:516/542 of query aligns to 8:474/475 of 5burA
- active site: T150 (= T180), S170 (≠ E200), H194 (= H224), T287 (≠ S323), E288 (= E324)
- binding adenosine-5'-triphosphate: T150 (= T180), S151 (= S181), T153 (= T183), T154 (= T184), K158 (= K188), G263 (≠ S297), S283 (≠ C319), T287 (≠ S323), D365 (= D403), V377 (≠ I415), R380 (= R418)
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)
26% identity, 89% coverage: 40:522/542 of query aligns to 60:548/559 of Q67W82
- G395 (= G370) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
29% identity, 90% coverage: 15:504/542 of query aligns to 5:494/504 of 6qjzA
- active site: T169 (= T180), S189 (≠ E200), H213 (= H224), T314 (≠ S323), E315 (= E324), N414 (= N424), K419 (≠ L429)
- binding adenosine monophosphate: H213 (= H224), S288 (≠ G295), A289 (= A296), S290 (= S297), A312 (≠ G321), M313 (≠ Q322), T314 (≠ S323), D393 (= D403), L405 (≠ I415), K410 (= K420), K419 (≠ L429)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
29% identity, 87% coverage: 49:519/542 of query aligns to 49:530/533 of 6ihkB
- active site: T185 (= T180), H202 (≠ M198), H228 (= H224), S326 (= S323), E327 (= E324), K435 (≠ N424), W440 (≠ L429), K520 (= K509)
- binding adenosine-5'-diphosphate: H228 (= H224), G300 (≠ A296), A301 (≠ S297), A302 (≠ I298), H321 (≠ Y317), A322 (≠ C319), W323 (≠ Y320), G324 (= G321), M325 (≠ Q322), S326 (= S323), Q356 (≠ C344), D414 (= D403), R429 (= R418), K520 (= K509)
Query Sequence
>GFF2429 FitnessBrowser__psRCH2:GFF2429
MRPTVEVHPSIHRNTIGDALQRIAMRSPEQIALQYRERRWSFQALDRAANRVANHLLALG
LSKADRVAAYGKNSDAYLILWLACTRAGLIHVPVNYSLTEHELAYVLDQSGARALFVDDS
LKGLVDRIPAQRQLAIRGSLHSNETTSDRSDILRIATGSACDLPPEVDIAETDVVQILYT
SGTTSDPKGAMHSHRSLMTEYSSCLLHLDIKASDRCLAALPLYHSAQMHVFTMPALLAGA
FSCLTDTPTPEEILRLLKTEQLNSFFAPPTVWIALLRHEQFVEAQLRHVQKLYYGASIMP
EPIARELGARLPQSGLYNCYGQSEIAPLATVLTPEEHRERPTSCGRPVSNVLTRIIDPST
GEECAPGVAGELVHRSPQLMVGYWEKPAETAEAFADGWFHSGDLGYRDAQGYIWIVDRIK
DIVNTGGVLVASRDVEEALYRHPHVAEVAVIGVPDQKWIEAIAAVVVLKQNATLDAQALL
HHARAHLAPFKVPKHVHFVEQLPKNSSGKLLKRVLRVQFGASARSSLGEAGDNLQQSEAS
AR
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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