SitesBLAST
Comparing GFF1020 FitnessBrowser__Marino:GFF1020 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)
42% identity, 98% coverage: 3:540/548 of query aligns to 34:573/590 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)
31% identity, 97% coverage: 7:538/548 of query aligns to 24:551/561 of P69451
- Y213 (≠ F196) mutation to A: Loss of activity.
- T214 (= T197) mutation to A: 10% of wild-type activity.
- G216 (= G199) mutation to A: Decreases activity.
- T217 (= T200) mutation to A: Decreases activity.
- G219 (= G202) mutation to A: Decreases activity.
- K222 (= K205) 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)
31% identity, 92% coverage: 33:538/548 of query aligns to 28:499/506 of 4gxqA
- active site: T163 (= T197), N183 (= N217), H207 (= H241), T303 (= T341), E304 (= E342), I403 (= I444), N408 (= N449), A491 (≠ K530)
- binding adenosine-5'-triphosphate: T163 (= T197), S164 (= S198), G165 (= G199), T166 (= T200), T167 (= T201), H207 (= H241), S277 (≠ G314), A278 (≠ S315), P279 (≠ I316), E298 (≠ Q335), M302 (= M340), T303 (= T341), D382 (= D423), R397 (= R438)
- binding carbonate ion: H207 (= H241), S277 (≠ G314), R299 (≠ A337), 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, 97% coverage: 8:538/548 of query aligns to 4:495/503 of P9WQ37
- R9 (≠ D13) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D21) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K205) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T228) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ K230) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C242) 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 (≠ G244) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ M247) 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 (≠ K279) 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 (= K530) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
29% identity, 97% coverage: 8:538/548 of query aligns to 7:495/502 of 3r44A
Sites not aligning to the query:
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
28% identity, 98% coverage: 2:539/548 of query aligns to 14:536/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H241), F245 (= F243), T249 (≠ M247), G314 (= G314), A315 (≠ S315), P316 (≠ I316), G337 (≠ A337), Y338 (= Y338), G339 (= G339), L340 (≠ M340), T341 (= T341), A346 (≠ V346), D420 (= D423), I432 (= I435), K527 (= K530)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
28% identity, 98% coverage: 2:539/548 of query aligns to 14:536/539 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 (= H241), F245 (= F243), T249 (≠ M247), G314 (= G314), A315 (≠ S315), P316 (≠ I316), G337 (≠ A337), Y338 (= Y338), G339 (= G339), L340 (≠ M340), T341 (= T341), S345 (≠ P345), A346 (≠ V346), D420 (= D423), I432 (= I435), K527 (= K530)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F243), R335 (≠ Q335), G337 (≠ A337), G339 (= G339), L340 (≠ M340), A346 (≠ V346)
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)
30% identity, 93% coverage: 23:533/548 of query aligns to 17:497/512 of O74976
- S283 (≠ G314) modified: Phosphoserine
- S284 (= S315) modified: Phosphoserine
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, 92% coverage: 35:540/548 of query aligns to 59:540/546 of Q84P21
- K530 (= K530) mutation to N: Lossed enzymatic activity.
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
29% identity, 95% coverage: 7:524/548 of query aligns to 5:493/504 of 6qjzA
- active site: T169 (= T197), S189 (≠ N217), H213 (= H241), T314 (= T341), E315 (= E342), N414 (≠ I444), K419 (≠ N449)
- binding adenosine monophosphate: H213 (= H241), S288 (≠ P318), A289 (= A319), S290 (≠ E320), A312 (≠ G339), M313 (= M340), 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)
30% identity, 96% coverage: 7:533/548 of query aligns to 5:503/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 197:201) binding
- H214 (= H241) binding ; mutation to A: Abolished activity.
- S289 (≠ A313) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ AGS 313:315) binding
- E-A 310:311 (≠ QIA 335:337) binding
- M314 (= M340) binding
- T315 (= T341) binding
- H319 (≠ Q349) binding ; mutation to A: Abolished activity.
- D394 (= D423) binding
- R409 (= R438) binding ; mutation to A: Abolished activity.
- K500 (= K530) binding ; binding ; mutation to A: Abolished 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: 6:538/548 of query aligns to 18:532/541 of Q5SKN9
- T184 (= T197) binding
- G302 (= G314) binding
- Q322 (≠ I336) binding
- G323 (≠ A337) binding
- T327 (= T341) binding
- E328 (= E342) binding
- D418 (= D423) binding
- K435 (= K440) binding
- K439 (≠ I444) binding
5ie2A Crystal structure of a plant enzyme (see paper)
30% identity, 96% coverage: 7:533/548 of query aligns to 5:498/506 of 5ie2A
- active site: T165 (= T197), S185 (≠ N217), H209 (= H241), T310 (= T341), E311 (= E342), N410 (≠ I444), K415 (≠ N449), K495 (= K530)
- binding adenosine-5'-triphosphate: T165 (= T197), S166 (= S198), G167 (= G199), T168 (= T200), T169 (= T201), S284 (≠ A313), A285 (≠ G314), S286 (= S315), Y307 (= Y338), A308 (≠ G339), M309 (= M340), T310 (= T341), D389 (= D423), L401 (≠ I435), R404 (= R438), K495 (= K530)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
29% identity, 97% coverage: 10:538/548 of query aligns to 14:510/518 of 4wv3B
- active site: S175 (≠ T197), T320 (= T343), E321 (≠ S344), K418 (≠ I444), W423 (≠ N449), K502 (= K530)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H241), T221 (≠ C242), F222 (= F243), A293 (= A313), S294 (≠ G314), E295 (≠ S315), A296 (≠ I316), G316 (= G339), I317 (≠ M340), G318 (≠ T341), C319 (≠ E342), T320 (= T343), D397 (= D423), H409 (≠ I435), R412 (= R438), K502 (= K530)
5ie3A Crystal structure of a plant enzyme (see paper)
30% identity, 96% coverage: 7:533/548 of query aligns to 5:496/504 of 5ie3A
- active site: T163 (= T197), S183 (≠ N217), H207 (= H241), T308 (= T341), E309 (= E342), N408 (≠ I444), K413 (≠ N449), K493 (= K530)
- binding adenosine monophosphate: S164 (= S198), S282 (≠ A313), A283 (≠ G314), S284 (= S315), Y305 (= Y338), A306 (≠ G339), M307 (= M340), T308 (= T341), D387 (= D423), L399 (≠ I435), R402 (= R438), K493 (= K530)
- binding oxalic acid: V208 (≠ C242), S282 (≠ A313), A306 (≠ G339), M307 (= M340), H312 (≠ Q349), K493 (= K530)
1md9A Crystal structure of dhbe in complex with dhb and amp (see paper)
27% identity, 99% coverage: 5:544/548 of query aligns to 24:533/536 of 1md9A
- active site: S190 (≠ T197), S210 (≠ N217), H234 (= H241), A333 (≠ T341), E334 (= E342), N434 (≠ I444), K439 (≠ N449), K519 (= K530)
- binding adenosine monophosphate: G191 (≠ S198), G307 (= G314), A308 (≠ S315), K309 (≠ I316), V329 (≠ A337), F330 (≠ Y338), G331 (= G339), M332 (= M340), D413 (= D423), V425 (≠ I435), R428 (= R438), K519 (= K530)
- binding 2,3-dihydroxy-benzoic acid: H234 (= H241), N235 (≠ C242), Y236 (≠ F243), S240 (≠ M247), G307 (= G314), V329 (≠ A337), G331 (= G339), M332 (= M340), K519 (= K530)
P40871 2,3-dihydroxybenzoate-AMP ligase; Dihydroxybenzoic acid-activating enzyme; EC 6.2.1.71 from Bacillus subtilis (strain 168) (see paper)
28% identity, 99% coverage: 5:548/548 of query aligns to 24:539/539 of P40871
- G191 (≠ S198) binding
- HN 234:235 (≠ HC 241:242) binding
- S240 (≠ M247) binding
- G307 (= G314) binding
- V329 (≠ A337) binding
- D413 (= D423) binding
- R428 (= R438) binding
- K519 (= K530) binding ; binding
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, 92% coverage: 34:537/548 of query aligns to 64:547/556 of Q9S725
- K211 (= K205) mutation to S: Drastically reduces the activity.
- M293 (≠ Y284) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I311) 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 (= K530) mutation to N: Abolishes the activity.
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)
30% identity, 94% coverage: 21:533/548 of query aligns to 19:526/543 of P38137
Sites not aligning to the query:
- 541:543 C-terminal peroxisome targeting signal (PTS1)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
28% identity, 96% coverage: 12:538/548 of query aligns to 8:478/484 of 5gtdA
- active site: T151 (= T197), S171 (≠ V221), H195 (= H241), T288 (= T341), E289 (= E342)
- binding adenosine-5'-monophosphate: G263 (= G314), G264 (≠ S315), Y285 (= Y338), G286 (= G339), M287 (= M340), T288 (= T341), D366 (= D423), V378 (≠ I435)
- binding magnesium ion: F314 (≠ L370), S315 (≠ E371)
- binding 2-succinylbenzoate: H195 (= H241), S197 (≠ F243), A237 (≠ G285), L260 (≠ I311), G262 (≠ A313), G263 (= G314), G286 (= G339), M287 (= M340), S292 (≠ T348), Q293 (= Q349)
Query Sequence
>GFF1020 FitnessBrowser__Marino:GFF1020
MPLLGMTIGEMLDRTAEKYPDNEALVCLHQDIRWTYKEFVEKVDEAARAFMAIGVKRGDR
VGIWSPNRYEWTVTQFATAKVGAILVNINPAYGVHELQYALNLAGITTLVTADSFKASNY
REMIYELAPELKRSSPGKLKADHVPELRAVINVHEDKHDGMWTWKEFLGFSSDVSQDDLV
KRQGELQFDDPINIQFTSGTTGNPKGATLTHHNILNNGYFVGESQLLTEKDRLVIPVPLY
HCFGMVMGNLGCITHGSTMIYPGEGFEPKSVLQAVHQEKATALYGVPTMFIAELAEPEFE
TYDLSSLRTGIMAGSICPAEVMKKVNGKMNMKEVQIAYGMTETSPVSTQTSSLDPFEKQV
TTVGRTQPHLETKIVDPGTGNVVPRGEIGELCTRGYSVMLKYWNNEEKTREAIDSAGWMH
TGDLATMDEEGYVQIVGRIKDMVIRGGENIYPKEIEEFLYTHPAIEEVQVTGIPDDKYGE
ELIAWVKLAPDAAPVTAEDLQAFCKGKIAHFKIPKNYKFVDEFPMTVTGKIQKFKMREIS
IEEMGLKK
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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