SitesBLAST
Comparing WP_078717853.1 NCBI__GCF_900167125.1:WP_078717853.1 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)
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)
40% identity, 99% coverage: 3:543/548 of query aligns to 33:577/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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, 97% coverage: 7:539/548 of query aligns to 23:553/561 of P69451
- Y213 (= Y197) mutation to A: Loss of activity.
- T214 (= T198) mutation to A: 10% of wild-type activity.
- G216 (= G200) mutation to A: Decreases activity.
- T217 (= T201) mutation to A: Decreases activity.
- G219 (= G203) mutation to A: Decreases activity.
- K222 (= K206) mutation to A: Decreases activity.
- E361 (= E342) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
28% identity, 93% coverage: 36:543/548 of query aligns to 30:505/506 of 4gxqA
- active site: T163 (= T198), N183 (= N218), H207 (= H242), T303 (= T341), E304 (= E342), I403 (= I444), N408 (= N449), A491 (≠ K529)
- binding adenosine-5'-triphosphate: T163 (= T198), S164 (= S199), G165 (= G200), T166 (= T201), T167 (= T202), H207 (= H242), S277 (≠ G314), A278 (≠ S315), P279 (= P316), E298 (≠ I336), M302 (≠ L340), T303 (= T341), D382 (= D423), R397 (= R438)
- binding carbonate ion: H207 (= H242), S277 (≠ G314), R299 (≠ C337), G301 (= G339)
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)
29% identity, 98% coverage: 7:545/548 of query aligns to 2:503/503 of P9WQ37
- R9 (≠ D14) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D22) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K206) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T229) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ K231) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C243) 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 (≠ C246) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ G249) 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 (= R279) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G339) 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 (= W418) 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 (= D423) 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 (= R438) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R445) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G447) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K529) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
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, 91% coverage: 36:536/548 of query aligns to 65:547/556 of Q9S725
- K211 (= K206) mutation to S: Drastically reduces the activity.
- M293 (≠ Y284) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ M312) mutation K->L,A: Affects the substrate specificity.
- E401 (= E390) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C392) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R438) mutation to Q: Drastically reduces the activity.
- K457 (≠ G446) mutation to S: Drastically reduces the activity.
- K540 (= K529) mutation to N: Abolishes the activity.
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
29% identity, 98% coverage: 4:541/548 of query aligns to 14:537/539 of 2d1sA
- active site: S194 (≠ T198), R214 (≠ N218), H241 (= H242), T339 (= T341), E340 (= E342), K439 (≠ I444), Q444 (≠ N449), K525 (= K529)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S194 (≠ T198), S195 (= S199), H241 (= H242), F243 (= F244), T247 (≠ C246), I282 (≠ Y284), G312 (= G314), A313 (≠ S315), P314 (= P316), Q334 (≠ I336), G335 (≠ C337), Y336 (= Y338), G337 (= G339), L338 (= L340), T339 (= T341), S343 (≠ P345), A344 (≠ V346), D418 (= D423), R433 (= R438), K525 (= K529)
2d1rA Crystal structure of the thermostable japanese firefly luciferase complexed with oxyluciferin and amp (see paper)
29% identity, 98% coverage: 4:541/548 of query aligns to 14:537/539 of 2d1rA
- active site: S194 (≠ T198), R214 (≠ N218), H241 (= H242), T339 (= T341), E340 (= E342), K439 (≠ I444), Q444 (≠ N449), K525 (= K529)
- binding adenosine monophosphate: S194 (≠ T198), S195 (= S199), H241 (= H242), G312 (= G314), A313 (≠ S315), P314 (= P316), G335 (≠ C337), Y336 (= Y338), G337 (= G339), L338 (= L340), T339 (= T341), D418 (= D423), K525 (= K529)
- binding 2-(6-hydroxy-1,3-benzothiazol-2-yl)-1,3-thiazol-4(5h)-one: H241 (= H242), F243 (= F244), T247 (≠ C246), G335 (≠ C337), G337 (= G339), L338 (= L340), A344 (≠ V346)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
28% identity, 98% coverage: 4:541/548 of query aligns to 15:539/539 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 (= H242), F245 (= F244), T249 (≠ C246), G314 (= G314), A315 (≠ S315), P316 (= P316), G337 (≠ C337), Y338 (= Y338), G339 (= G339), L340 (= L340), T341 (= T341), S345 (≠ P345), A346 (≠ V346), D420 (= D423), I432 (= I435), K527 (= K529)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F244), R335 (≠ T335), G337 (≠ C337), G339 (= G339), L340 (= L340), A346 (≠ V346)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
28% identity, 98% coverage: 4:540/548 of query aligns to 15:538/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H242), F245 (= F244), T249 (≠ C246), G314 (= G314), A315 (≠ S315), P316 (= P316), G337 (≠ C337), Y338 (= Y338), G339 (= G339), L340 (= L340), T341 (= T341), A346 (≠ V346), D420 (= D423), I432 (= I435), K527 (= K529)
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
28% identity, 94% coverage: 8:523/548 of query aligns to 5:493/504 of 6qjzA
- active site: T169 (= T198), S189 (≠ N218), H213 (= H242), T314 (= T341), E315 (= E342), N414 (≠ I444), K419 (≠ N449)
- binding adenosine monophosphate: H213 (= H242), S288 (= S315), A289 (≠ P316), S290 (≠ C317), A312 (≠ G339), M313 (≠ L340), T314 (= T341), D393 (= D423), L405 (≠ I435), K410 (= K440), K419 (≠ N449)
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, 96% coverage: 8:532/548 of query aligns to 5:503/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 198:202) binding ATP
- H214 (= H242) binding ATP; mutation to A: Abolished activity.
- S289 (= S315) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ SPC 315:317) binding ATP
- EA 310:311 (≠ IC 336:337) binding ATP
- M314 (≠ L340) binding oxalate
- T315 (= T341) binding ATP
- H319 (≠ P345) binding oxalate; mutation to A: Abolished activity.
- D394 (= D423) binding ATP
- R409 (= R438) binding ATP; mutation to A: Abolished activity.
- K500 (= K529) binding ATP; binding oxalate; mutation to A: Abolished activity.
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)
27% identity, 94% coverage: 26:539/548 of query aligns to 47:540/546 of Q84P21
- K530 (= K529) mutation to N: Lossed enzymatic 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, 97% coverage: 5:537/548 of query aligns to 16:532/541 of Q5SKN9
- T184 (= T198) binding Mg(2+)
- G302 (= G314) binding tetradecanoyl-AMP
- Q322 (≠ I336) binding tetradecanoyl-AMP
- G323 (≠ C337) binding tetradecanoyl-AMP
- T327 (= T341) binding tetradecanoyl-AMP
- E328 (= E342) binding Mg(2+)
- D418 (= D423) binding tetradecanoyl-AMP
- K435 (= K440) binding tetradecanoyl-AMP
- K439 (≠ I444) binding tetradecanoyl-AMP
5ie2A Crystal structure of a plant enzyme (see paper)
29% identity, 96% coverage: 8:532/548 of query aligns to 5:498/506 of 5ie2A
- active site: T165 (= T198), S185 (≠ N218), H209 (= H242), T310 (= T341), E311 (= E342), N410 (≠ I444), K415 (≠ N449), K495 (= K529)
- binding adenosine-5'-triphosphate: T165 (= T198), S166 (= S199), G167 (= G200), T168 (= T201), T169 (= T202), S284 (= S315), A285 (≠ P316), S286 (≠ C317), Y307 (= Y338), A308 (≠ G339), M309 (≠ L340), T310 (= T341), D389 (= D423), L401 (≠ I435), R404 (= R438), K495 (= K529)
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)
30% identity, 91% coverage: 36:536/548 of query aligns to 61:542/559 of Q67W82
- G395 (= G389) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
5ie3A Crystal structure of a plant enzyme (see paper)
28% identity, 96% coverage: 8:532/548 of query aligns to 5:496/504 of 5ie3A
- active site: T163 (= T198), S183 (≠ N218), H207 (= H242), T308 (= T341), E309 (= E342), N408 (≠ I444), K413 (≠ N449), K493 (= K529)
- binding adenosine monophosphate: S164 (= S199), S282 (= S315), A283 (≠ P316), S284 (≠ C317), Y305 (= Y338), A306 (≠ G339), M307 (≠ L340), T308 (= T341), D387 (= D423), L399 (≠ I435), R402 (= R438), K493 (= K529)
- binding oxalic acid: V208 (≠ C243), S282 (= S315), A306 (≠ G339), M307 (≠ L340), H312 (≠ P345), K493 (= K529)
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)
28% identity, 95% coverage: 13:532/548 of query aligns to 6:497/512 of O74976
- S283 (≠ G314) modified: Phosphoserine
- S284 (= S315) modified: Phosphoserine
7kydA Drosophila melanogaster long-chain fatty-acyl-coa synthetase cg6178 (see paper)
28% identity, 97% coverage: 6:538/548 of query aligns to 23:532/534 of 7kydA
- binding 5'-O-[(S)-hydroxy(octanoyloxy)phosphoryl]adenosine: H240 (= H242), F242 (= F244), A311 (≠ G314), A312 (≠ S315), P313 (= P316), G334 (≠ C337), Y335 (= Y338), G336 (= G339), L337 (= L340), S338 (≠ T341), S343 (≠ P345), D416 (= D423), I428 (= I435)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
29% identity, 91% coverage: 36:536/548 of query aligns to 46:522/527 of 5u95B
6q2mA Crystal structure of photinus pyralis luciferase pps6 mutant in complex with dlsa (see paper)
28% identity, 98% coverage: 4:538/548 of query aligns to 16:537/544 of 6q2mA
- active site: S197 (≠ T198), R217 (vs. gap), H244 (= H242), T342 (= T341), E343 (= E342), K442 (≠ I444), Q447 (≠ N449), K528 (= K529)
- binding (2S,5S)-hexane-2,5-diol: D18 (≠ E6), G19 (≠ R7), D186 (= D188), R187 (≠ P189), R260 (≠ T259), Y279 (≠ E278)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S198 (= S199), H244 (= H242), F246 (= F244), T250 (≠ C246), G315 (= G314), A316 (≠ S315), P317 (= P316), G338 (≠ C337), Y339 (= Y338), G340 (= G339), L341 (= L340), T342 (= T341), S346 (≠ P345), A347 (≠ V346), D421 (= D423), K528 (= K529)
Query Sequence
>WP_078717853.1 NCBI__GCF_900167125.1:WP_078717853.1
MSQLKERTLGQLLDEAVENYPDNEAVVYVDRDYRQTYREFAEKVDTLAKGLMALGVKRGE
KVAIWATNVPYWVAFQFATAKIGAVLLTVNTYYRNHELDYLLKQSETENLIIIDGFRDVD
YVSTIYELVPELRTMERGRLKNKTYPHLKRVLFLGQEKHRGMYSMPELEAMSVMISDEEY
QARQDELDPHDVVNMQYTSGTTGFPKGVQLTHYNIGNNGFWIGENQHFTEKDRVCLPVPL
FHCFGCVLGVLACVSHASTMVILEGFDPFLIMASVDSERCTALYGVPTMFIAVLEHRSFS
RFDYSSLRTGIMAGSPCPVPVMRRVMDVMNMKDITICYGLTESSPVMTQTRIGDPIEKMT
ETVGKPMPEVEVSVVDPETGEPCAPGVQGEVCCRGYLVMKGYYNNPEATAKTIDKDGWLH
SGDLGTFDEDGYLVITGRLKDMIIRGGENIYPREIEEFLYTMEGVQDVQVAAVPSRKYGE
EIGAFIILKDGVDMIPEDVRDFCRGKISRYKIPKYIAFVEEYPMTASGKIQKYKLREMAE
ELFPQAMQ
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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