SitesBLAST
Comparing GFF2497 FitnessBrowser__Phaeo:GFF2497 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)
41% identity, 97% coverage: 18:576/577 of query aligns to 2:551/561 of P69451
- Y213 (= Y237) mutation to A: Loss of activity.
- T214 (= T238) mutation to A: 10% of wild-type activity.
- G216 (= G240) mutation to A: Decreases activity.
- T217 (= T241) mutation to A: Decreases activity.
- G219 (= G243) mutation to A: Decreases activity.
- K222 (= K246) mutation to A: Decreases activity.
- E361 (= E386) mutation to A: Loss of activity.
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
29% identity, 88% coverage: 72:576/577 of query aligns to 29:478/484 of 5gtdA
- active site: T151 (= T238), S171 (≠ E260), H195 (= H288), T288 (= T385), E289 (= E386)
- binding adenosine-5'-monophosphate: G263 (= G359), G264 (= G360), Y285 (= Y382), G286 (= G383), M287 (= M384), T288 (= T385), D366 (= D463), V378 (≠ I475)
- binding magnesium ion: F314 (≠ P410), S315 (≠ G411)
- binding 2-succinylbenzoate: H195 (= H288), S197 (≠ F290), A237 (≠ G332), L260 (≠ A356), G262 (= G358), G263 (= G359), G286 (= G383), M287 (= M384), S292 (≠ C389), Q293 (vs. gap)
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, 88% coverage: 72:576/577 of query aligns to 29:478/485 of 5x8fB
- active site: T151 (= T238), S171 (≠ E260), H195 (= H288), T288 (= T385), E289 (= E386), I387 (≠ L484), N392 (= N489), K470 (= K568)
- binding magnesium ion: H70 (≠ F114), N178 (≠ H267), L202 (≠ M297), L214 (≠ I309), T296 (≠ A392), L297 (= L393), S298 (= S394)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ L129), L191 (≠ I284), P192 (= P285), H195 (= H288), I196 (= I289), S197 (≠ F290), A237 (≠ G332), V238 (= V333), L260 (≠ A356), G262 (= G358), G286 (= G383), M287 (= M384), S292 (≠ C389), Q293 (vs. gap), S388 (≠ V485), G389 (≠ S486), G390 (= G487), E391 (≠ F488), K420 (≠ T517), W421 (≠ R518), K450 (≠ A548), Y451 (= Y549)
Sites not aligning to the query:
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
29% identity, 88% coverage: 72:576/577 of query aligns to 28:475/475 of 5burA
- active site: T150 (= T238), S170 (≠ E260), H194 (= H288), T287 (= T385), E288 (= E386)
- binding adenosine-5'-triphosphate: T150 (= T238), S151 (≠ G239), T153 (= T241), T154 (= T242), K158 (= K246), G263 (= G360), S283 (≠ G381), T287 (= T385), D365 (= D463), V377 (≠ I475), R380 (= R478)
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)
28% identity, 92% coverage: 42:572/577 of query aligns to 6:504/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 238:242) binding
- H214 (= H288) binding ; mutation to A: Abolished activity.
- S289 (≠ G360) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ GTS 360:362) binding
- EA 310:311 (≠ EG 380:381) binding
- M314 (= M384) binding
- T315 (= T385) binding
- H319 (≠ C389) binding ; mutation to A: Abolished activity.
- D394 (= D463) binding
- R409 (= R478) binding ; mutation to A: Abolished activity.
- K500 (= K568) binding ; binding ; mutation to A: Abolished activity.
5ie3A Crystal structure of a plant enzyme (see paper)
28% identity, 92% coverage: 42:572/577 of query aligns to 6:497/504 of 5ie3A
- active site: T163 (= T238), S183 (≠ V258), H207 (= H288), T308 (= T385), E309 (= E386), N408 (≠ L484), K413 (≠ N489), K493 (= K568)
- binding adenosine monophosphate: S164 (≠ G239), S282 (≠ G360), A283 (≠ T361), S284 (= S362), Y305 (= Y382), A306 (≠ G383), M307 (= M384), T308 (= T385), D387 (= D463), L399 (≠ I475), R402 (= R478), K493 (= K568)
- binding oxalic acid: V208 (≠ I289), S282 (≠ G360), A306 (≠ G383), M307 (= M384), H312 (≠ C389), K493 (= K568)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
29% identity, 88% coverage: 72:576/577 of query aligns to 28:475/481 of 5busA
- active site: T150 (= T238), S170 (≠ E260), H194 (= H288), T287 (= T385), E288 (= E386)
- binding adenosine monophosphate: H194 (= H288), G262 (= G359), G263 (= G360), S283 (≠ G381), M286 (= M384), T287 (= T385), D365 (= D463), V377 (≠ I475), R380 (= R478), K467 (= K568)
5ie2A Crystal structure of a plant enzyme (see paper)
28% identity, 92% coverage: 42:572/577 of query aligns to 6:499/506 of 5ie2A
- active site: T165 (= T238), S185 (≠ V258), H209 (= H288), T310 (= T385), E311 (= E386), N410 (≠ L484), K415 (≠ N489), K495 (= K568)
- binding adenosine-5'-triphosphate: T165 (= T238), S166 (≠ G239), G167 (= G240), T168 (= T241), T169 (= T242), S284 (≠ G360), A285 (≠ T361), S286 (= S362), Y307 (= Y382), A308 (≠ G383), M309 (= M384), T310 (= T385), D389 (= D463), L401 (≠ I475), R404 (= R478), K495 (= K568)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
29% identity, 88% coverage: 72:577/577 of query aligns to 30:500/506 of 4gxqA
- active site: T163 (= T238), N183 (≠ G268), H207 (= H288), T303 (= T385), E304 (= E386), I403 (≠ L484), N408 (= N489), A491 (≠ K568)
- binding adenosine-5'-triphosphate: T163 (= T238), S164 (≠ G239), G165 (= G240), T166 (= T241), T167 (= T242), H207 (= H288), S277 (≠ G360), A278 (≠ T361), P279 (≠ S362), E298 (= E380), M302 (= M384), T303 (= T385), D382 (= D463), R397 (= R478)
- binding carbonate ion: H207 (= H288), S277 (≠ G360), R299 (≠ G381), G301 (= G383)
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)
26% identity, 87% coverage: 72:574/577 of query aligns to 59:536/546 of Q84P21
- K530 (= K568) mutation to N: Lossed enzymatic activity.
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
29% identity, 87% coverage: 72:575/577 of query aligns to 50:534/539 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 (= H288), F245 (= F290), T249 (≠ V294), G314 (= G360), A315 (≠ T361), P316 (≠ S362), G337 (= G381), Y338 (= Y382), G339 (= G383), L340 (≠ M384), T341 (= T385), S345 (≠ C389), A346 (≠ M390), D420 (= D463), I432 (= I475), K527 (= K568)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F290), R335 (≠ V379), G337 (= G381), G339 (= G383), L340 (≠ M384), A346 (≠ M390)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
29% identity, 87% coverage: 72:575/577 of query aligns to 50:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H288), F245 (= F290), T249 (≠ V294), G314 (= G360), A315 (≠ T361), P316 (≠ S362), G337 (= G381), Y338 (= Y382), G339 (= G383), L340 (≠ M384), T341 (= T385), A346 (≠ M390), D420 (= D463), I432 (= I475), K527 (= K568)
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)
28% identity, 88% coverage: 72:576/577 of query aligns to 31:495/503 of P9WQ37
- K172 (= K246) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ Q271) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ T273) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I289) 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 (= A291) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (vs. gap) 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 (≠ P312) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G383) 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 (= W458) 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 (= D463) 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 (= R478) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V485) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G487) 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.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
29% identity, 88% coverage: 72:576/577 of query aligns to 47:527/528 of 3ni2A
- active site: S182 (≠ T238), S202 (≠ G268), H230 (= H288), T329 (= T385), E330 (= E386), K434 (≠ L484), Q439 (≠ N489), K519 (= K568)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F290), S236 (≠ N295), G302 (= G360), A303 (≠ T361), P304 (≠ S362), G325 (= G381), G327 (= G383), T329 (= T385), P333 (≠ C389), V334 (≠ M390), D413 (= D463), K430 (= K480), K434 (≠ L484), Q439 (≠ N489)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
29% identity, 88% coverage: 72:576/577 of query aligns to 47:527/528 of 3a9vA
- active site: S182 (≠ T238), S202 (≠ G268), H230 (= H288), T329 (= T385), E330 (= E386), K434 (≠ L484), Q439 (≠ N489), K519 (= K568)
- binding adenosine monophosphate: H230 (= H288), G302 (= G360), A303 (≠ T361), P304 (≠ S362), Y326 (= Y382), G327 (= G383), M328 (= M384), T329 (= T385), D413 (= D463), K430 (= K480), K434 (≠ L484), Q439 (≠ N489)
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
26% identity, 91% coverage: 42:568/577 of query aligns to 6:499/504 of 6qjzA
- active site: T169 (= T238), S189 (≠ V258), H213 (= H288), T314 (= T385), E315 (= E386), N414 (≠ L484), K419 (≠ N489)
- binding adenosine monophosphate: H213 (= H288), S288 (≠ G360), A289 (≠ T361), S290 (= S362), A312 (≠ G383), M313 (= M384), T314 (= T385), D393 (= D463), L405 (≠ I475), K410 (= K480), K419 (≠ N489)
7kydA Drosophila melanogaster long-chain fatty-acyl-coa synthetase cg6178 (see paper)
29% identity, 85% coverage: 86:575/577 of query aligns to 66:530/534 of 7kydA
- binding 5'-O-[(S)-hydroxy(octanoyloxy)phosphoryl]adenosine: H240 (= H288), F242 (= F290), A311 (≠ G360), A312 (≠ T361), P313 (≠ S362), G334 (= G381), Y335 (= Y382), G336 (= G383), L337 (≠ M384), S338 (≠ T385), S343 (≠ M390), D416 (= D463), I428 (= I475)
5buqB Unliganded form of o-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, solved at 1.98 angstroms (see paper)
28% identity, 88% coverage: 72:576/577 of query aligns to 28:466/473 of 5buqB
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
28% identity, 88% coverage: 69:575/577 of query aligns to 45:532/539 of 2d1sA
- active site: S194 (≠ T238), R214 (≠ V258), H241 (= H288), T339 (= T385), E340 (= E386), K439 (≠ L484), Q444 (≠ N489), K525 (= K568)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S194 (≠ T238), S195 (≠ G239), H241 (= H288), F243 (= F290), T247 (≠ V294), I282 (≠ T331), G312 (= G360), A313 (≠ T361), P314 (≠ S362), Q334 (≠ E380), G335 (= G381), Y336 (= Y382), G337 (= G383), L338 (≠ M384), T339 (= T385), S343 (≠ C389), A344 (≠ M390), D418 (= D463), R433 (= R478), K525 (= K568)
2d1rA Crystal structure of the thermostable japanese firefly luciferase complexed with oxyluciferin and amp (see paper)
28% identity, 88% coverage: 69:575/577 of query aligns to 45:532/539 of 2d1rA
- active site: S194 (≠ T238), R214 (≠ V258), H241 (= H288), T339 (= T385), E340 (= E386), K439 (≠ L484), Q444 (≠ N489), K525 (= K568)
- binding adenosine monophosphate: S194 (≠ T238), S195 (≠ G239), H241 (= H288), G312 (= G360), A313 (≠ T361), P314 (≠ S362), G335 (= G381), Y336 (= Y382), G337 (= G383), L338 (≠ M384), T339 (= T385), D418 (= D463), K525 (= K568)
- binding 2-(6-hydroxy-1,3-benzothiazol-2-yl)-1,3-thiazol-4(5h)-one: H241 (= H288), F243 (= F290), T247 (≠ V294), G335 (= G381), G337 (= G383), L338 (≠ M384), A344 (≠ M390)
Query Sequence
>GFF2497 FitnessBrowser__Phaeo:GFF2497
MQQPEATVENTQKIDGNNRFWAEHYAPDIRGYDHQTRRYQRVSDILDTAVRSTPERVGFS
LVLPSGHCLDKTYAEIGRASDAIACYLREDLGLFPGDVAAIQLPNSIHYPVILFGAMKAG
LKVTNLNPLYTPREIVHQLQDSGAKVLFGFNLFADRLQTALRDTAVEQVVIAALWEFFPQ
AASDALRHTITDVAKLVPEYSFDHVPFEDAFAQGMAHGEIHYDLSQIDPGSAAFLQYTGG
TTGVSKGAELTHDNVTHVLEMLNACVHGAMQKTDHGQMSILTVIPYYHIFALIVNLMHFT
AASGRNVLIPNPNPIANLKPAFDNYDIDWLTGVDTLFNGLMAQDWFQQTPPQIGLAIGGG
TSLRPDTARRWSEQIGPIVEGYGMTETTCMIALSPLDGSDKPGTAGQPVPGLEIKITRSD
GAPVGIGEAGELHVRGPNIATAYLNRPDASAETFADGWMATGDIVTMDAEGHLAIVDRKK
DMILVSGFNVYPNELEAVIQSMPGVAEVAVVGEAHPTRGESPAAFVKRADPAVTEEMVIK
YCRANLTAYKVPTQVHFLEELPKSSVGKILRKELRNC
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