SitesBLAST
Comparing WP_039653934.1 NCBI__GCF_000816635.1:WP_039653934.1 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)
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
30% identity, 96% coverage: 15:482/489 of query aligns to 19:479/486 of 8wevA
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)
35% identity, 71% coverage: 141:488/489 of query aligns to 140:478/485 of 5x8fB
- active site: T151 (= T151), S171 (≠ N171), H195 (≠ Y195), T288 (= T294), E289 (= E295), I387 (≠ K394), N392 (≠ R399), K470 (= K480)
- binding magnesium ion: N178 (≠ Y178), L202 (= L202), L214 (≠ I214), T296 (≠ Y302), L297 (= L303), S298 (≠ P304)
- binding o-succinylbenzoyl-N-coenzyme A: L191 (= L191), P192 (= P192), H195 (≠ Y195), I196 (≠ C196), S197 (≠ Y197), A237 (≠ G238), V238 (= V239), L260 (≠ T264), G262 (≠ A266), G286 (= G292), M287 (≠ Q293), S292 (≠ A298), Q293 (≠ R299), S388 (≠ C395), G389 (≠ A396), G390 (= G397), E391 (≠ N398), K420 (≠ M427), W421 (≠ L428), K450 (= K460), Y451 (= Y461)
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)
35% identity, 71% coverage: 141:488/489 of query aligns to 140:478/484 of 5gtdA
- active site: T151 (= T151), S171 (≠ N171), H195 (≠ Y195), T288 (= T294), E289 (= E295)
- binding adenosine-5'-monophosphate: G263 (= G267), G264 (= G268), Y285 (= Y291), G286 (= G292), M287 (≠ Q293), T288 (= T294), D366 (= D373), V378 (≠ I385)
- binding magnesium ion: F314 (≠ P320), S315 (≠ G321)
- binding 2-succinylbenzoate: H195 (≠ Y195), S197 (≠ Y197), A237 (≠ G238), L260 (≠ T264), G262 (≠ A266), G263 (= G267), G286 (= G292), M287 (≠ Q293), S292 (≠ A298), Q293 (≠ R299)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
35% identity, 71% coverage: 141:488/489 of query aligns to 139:475/475 of 5burA
- active site: T150 (= T151), S170 (≠ N171), H194 (≠ Y195), T287 (= T294), E288 (= E295)
- binding adenosine-5'-triphosphate: T150 (= T151), S151 (= S152), T153 (≠ S154), T154 (= T155), K158 (= K159), G263 (= G268), S283 (≠ M290), T287 (= T294), D365 (= D373), V377 (≠ I385), R380 (= R388)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
35% identity, 71% coverage: 141:488/489 of query aligns to 139:475/481 of 5busA
- active site: T150 (= T151), S170 (≠ N171), H194 (≠ Y195), T287 (= T294), E288 (= E295)
- binding adenosine monophosphate: H194 (≠ Y195), G262 (= G267), G263 (= G268), S283 (≠ M290), M286 (≠ Q293), T287 (= T294), D365 (= D373), V377 (≠ I385), R380 (= R388), K467 (= K480)
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
27% identity, 96% coverage: 8:475/489 of query aligns to 17:494/504 of 6qjzA
- active site: T169 (= T151), S189 (≠ N171), H213 (≠ Y195), T314 (= T294), E315 (= E295), N414 (≠ K394), K419 (≠ R399)
- binding adenosine monophosphate: H213 (≠ Y195), S288 (≠ G267), A289 (≠ G268), S290 (≠ K269), A312 (≠ G292), M313 (≠ Q293), T314 (= T294), D393 (= D373), L405 (≠ I385), K410 (= K390), K419 (≠ R399)
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)
30% identity, 99% coverage: 7:488/489 of query aligns to 28:551/561 of P69451
- Y213 (≠ F150) mutation to A: Loss of activity.
- T214 (= T151) mutation to A: 10% of wild-type activity.
- G216 (= G153) mutation to A: Decreases activity.
- T217 (≠ S154) mutation to A: Decreases activity.
- G219 (≠ S156) mutation to A: Decreases activity.
- K222 (= K159) mutation to A: Decreases activity.
- E361 (= E295) mutation to A: Loss of activity.
5ie3A Crystal structure of a plant enzyme (see paper)
28% identity, 93% coverage: 29:481/489 of query aligns to 38:494/504 of 5ie3A
- active site: T163 (= T151), S183 (≠ N171), H207 (≠ Y195), T308 (= T294), E309 (= E295), N408 (≠ K394), K413 (≠ R399), K493 (= K480)
- binding adenosine monophosphate: S164 (= S152), S282 (≠ G267), A283 (≠ G268), S284 (≠ K269), Y305 (= Y291), A306 (≠ G292), M307 (≠ Q293), T308 (= T294), D387 (= D373), L399 (≠ I385), R402 (= R388), K493 (= K480)
- binding oxalic acid: V208 (≠ C196), S282 (≠ G267), A306 (≠ G292), M307 (≠ Q293), H312 (≠ A298), K493 (= K480)
5ie2A Crystal structure of a plant enzyme (see paper)
28% identity, 93% coverage: 29:481/489 of query aligns to 38:496/506 of 5ie2A
- active site: T165 (= T151), S185 (≠ N171), H209 (≠ Y195), T310 (= T294), E311 (= E295), N410 (≠ K394), K415 (≠ R399), K495 (= K480)
- binding adenosine-5'-triphosphate: T165 (= T151), S166 (= S152), G167 (= G153), T168 (≠ S154), T169 (= T155), S284 (≠ G267), A285 (≠ G268), S286 (≠ K269), Y307 (= Y291), A308 (≠ G292), M309 (≠ Q293), T310 (= T294), D389 (= D373), L401 (≠ I385), R404 (= R388), K495 (= K480)
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, 93% coverage: 29:481/489 of query aligns to 38:501/514 of Q9SMT7
- TSGTT 170:174 (≠ TSGST 151:155) binding ATP
- H214 (≠ Y195) binding ATP; mutation to A: Abolished activity.
- S289 (≠ G267) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ GGK 267:269) binding ATP
- EA 310:311 (≠ IM 289:290) binding ATP
- M314 (≠ Q293) binding oxalate
- T315 (= T294) binding ATP
- H319 (≠ A298) binding oxalate; mutation to A: Abolished activity.
- D394 (= D373) binding ATP
- R409 (= R388) binding ATP; mutation to A: Abolished activity.
- K500 (= K480) binding ATP; binding oxalate; mutation to A: Abolished activity.
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)
27% identity, 94% coverage: 25:482/489 of query aligns to 30:489/503 of P9WQ37
- K172 (= K159) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T182) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ K184) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C196) 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 (≠ G198) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ S200) 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 (≠ Y231) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G292) 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 (≠ L368) 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 (= D373) 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 (= R388) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ C395) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G397) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K480) 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.
P38137 Oxalate--CoA ligase; Acyl-activating enzyme 3; Oxalyl-CoA synthetase; Peroxisomal-coenzyme A synthetase; EC 6.2.1.8 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
28% identity, 89% coverage: 48:481/489 of query aligns to 61:524/543 of P38137
Sites not aligning to the query:
- 541:543 C-terminal peroxisome targeting signal (PTS1)
5buqB Unliganded form of o-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, solved at 1.98 angstroms (see paper)
34% identity, 71% coverage: 141:488/489 of query aligns to 139:466/473 of 5buqB
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
29% identity, 95% coverage: 25:489/489 of query aligns to 49:536/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (≠ Y195), F245 (≠ Y197), T249 (≠ L201), G314 (= G267), A315 (≠ G268), P316 (≠ K269), G337 (≠ M290), Y338 (= Y291), G339 (= G292), L340 (≠ Q293), T341 (= T294), A346 (≠ R299), D420 (= D373), I432 (= I385), K527 (= K480)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
29% identity, 95% coverage: 25:489/489 of query aligns to 49:536/539 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 (≠ Y195), F245 (≠ Y197), T249 (≠ L201), G314 (= G267), A315 (≠ G268), P316 (≠ K269), G337 (≠ M290), Y338 (= Y291), G339 (= G292), L340 (≠ Q293), T341 (= T294), S345 (≠ A298), A346 (≠ R299), D420 (= D373), I432 (= I385), K527 (= K480)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ Y197), R335 (≠ Y288), G337 (≠ M290), G339 (= G292), L340 (≠ Q293), A346 (≠ R299)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
26% identity, 94% coverage: 25:482/489 of query aligns to 33:489/502 of 3r44A
Sites not aligning to the query:
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, 94% coverage: 25:486/489 of query aligns to 58:536/546 of Q84P21
- K530 (= K480) mutation to N: Lossed enzymatic activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
26% identity, 98% coverage: 2:481/489 of query aligns to 4:492/506 of 4gxqA
- active site: T163 (= T151), N183 (= N171), H207 (≠ Y195), T303 (= T294), E304 (= E295), I403 (≠ K394), N408 (≠ R399), A491 (≠ K480)
- binding adenosine-5'-triphosphate: T163 (= T151), S164 (= S152), G165 (= G153), T166 (≠ S154), T167 (= T155), H207 (≠ Y195), S277 (≠ G267), A278 (≠ G268), P279 (≠ K269), E298 (≠ I289), M302 (≠ Q293), T303 (= T294), D382 (= D373), R397 (= R388)
- binding carbonate ion: H207 (≠ Y195), S277 (≠ G267), R299 (≠ M290), G301 (= G292)
O74976 Oxalate--CoA ligase; Oxalyl-CoA synthetase; Peroxisomal-coenzyme A synthetase; EC 6.2.1.8 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 94% coverage: 22:481/489 of query aligns to 25:495/512 of O74976
- S283 (≠ G267) modified: Phosphoserine
- S284 (≠ G268) modified: Phosphoserine
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)
28% identity, 99% coverage: 1:486/489 of query aligns to 36:546/556 of Q9S725
- K211 (= K159) mutation to S: Drastically reduces the activity.
- M293 (≠ A237) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ T264) mutation K->L,A: Affects the substrate specificity.
- E401 (= E341) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ A343) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R388) mutation to Q: Drastically reduces the activity.
- K457 (≠ A396) mutation to S: Drastically reduces the activity.
- K540 (= K480) mutation to N: Abolishes the activity.
Query Sequence
>WP_039653934.1 NCBI__GCF_000816635.1:WP_039653934.1
MNFTDYIFEKSKGLNKTAVIDNGEIIYSEIYERVCSIACLLQYKNYSKEDSVLVISENST
FFIETYFGIIKNGSICVPVNPSMDKKDIAYIAKILNIRLVFCQYKYKTEMKDCFGENVEI
CTERYICEKQSNLKLKIDVDMKKDTALIMFTSGSTSKPKGVMLTHYNLIYNTDSIIQYLN
LTDKDRIEVVLPFYYCYGTSLLNTHFRCGGSLVINNRFMFPQTVIDDINKYKCTGFAGVP
TTYQILLRMTNFKDSQFSSLRYVTQAGGKLPKIFISELYKILKGVDIYIMYGQTEATARL
SYLPPQHIMDKLGSIGKGVPGTELMILNRNGMPVNTGEIGEIAARGGNIMKGYFNDEYET
KKVIKNGLLYTGDIAYKDKEGYIFIVSREKNIIKCAGNRISPGEIENTVASIKQVVECAV
IGVEDEMLGEAVKVFVVLNGNYKDIDEKYIINYCSSRLPKYKTPKYIKFLSSLPKNSSGK
VLFKQLSNM
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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