SitesBLAST
Comparing AZOBR_RS22375 FitnessBrowser__azobra:AZOBR_RS22375 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
64% identity, 92% coverage: 38:513/519 of query aligns to 29:505/506 of 4gxqA
- active site: T163 (= T173), N183 (= N193), H207 (= H217), T303 (= T313), E304 (= E314), I403 (= I413), N408 (= N418), A491 (≠ K499)
- binding adenosine-5'-triphosphate: T163 (= T173), S164 (= S174), G165 (= G175), T166 (= T176), T167 (= T177), H207 (= H217), S277 (= S287), A278 (= A288), P279 (= P289), E298 (= E308), M302 (= M312), T303 (= T313), D382 (= D392), R397 (= R407)
- binding carbonate ion: H207 (= H217), S277 (= S287), R299 (= R309), G301 (= G311)
Q4G176 Malonate--CoA ligase ACSF3, mitochondrial; Acyl-CoA synthetase family member 3; EC 6.2.1.76 from Homo sapiens (Human) (see 2 papers)
34% identity, 95% coverage: 19:509/519 of query aligns to 40:574/576 of Q4G176
- R354 (= R309) mutation to A: Impairs malonyl-CoA synthase activity.; mutation to L: Impairs malonyl-CoA synthase activity.
- V372 (≠ D326) to M: in dbSNP:rs3743979
Sites not aligning to the query:
- 2 L → P: in dbSNP:rs7188200
- 17 A → P: in dbSNP:rs11547019
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)
33% identity, 93% coverage: 25:507/519 of query aligns to 36:551/561 of P69451
- Y213 (= Y172) mutation to A: Loss of activity.
- T214 (= T173) mutation to A: 10% of wild-type activity.
- G216 (= G175) mutation to A: Decreases activity.
- T217 (= T176) mutation to A: Decreases activity.
- G219 (= G178) mutation to A: Decreases activity.
- K222 (= K181) mutation to A: Decreases activity.
- E361 (= E314) mutation to A: Loss of 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)
32% identity, 97% coverage: 8:510/519 of query aligns to 3:498/503 of P9WQ37
- R9 (= R14) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (= R23) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K181) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ Q204) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ D206) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ T218) 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 (≠ G220) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ N226) 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 (≠ T254) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G311) 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 (≠ F387) 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 (= D392) 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 (= R407) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S414) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G416) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K499) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
3nyrA Malonyl-coa ligase ternary product complex with malonyl-coa and amp bound (see paper)
37% identity, 83% coverage: 64:494/519 of query aligns to 44:460/460 of 3nyrA
- active site: T137 (= T173), T157 (≠ N193), H181 (= H217), T281 (= T313), E282 (= E314), K379 (≠ I413), K384 (≠ N418)
- binding adenosine monophosphate: S255 (= S287), A256 (= A288), A257 (≠ P289), R277 (= R309), Y278 (= Y310), G279 (= G311), M280 (= M312), T281 (= T313), D357 (= D392), K379 (≠ I413), K384 (≠ N418)
- binding malonyl-coenzyme a: P178 (= P214), H181 (= H217), T226 (= T261), R230 (= R265), S255 (= S287), R277 (= R309), G279 (= G311), G381 (= G415), G382 (= G416), Y383 (≠ F417)
3nyqA Malonyl-coa ligase ternary product complex with methylmalonyl-coa and amp bound (see paper)
37% identity, 83% coverage: 64:494/519 of query aligns to 44:460/460 of 3nyqA
- active site: T137 (= T173), T157 (≠ N193), H181 (= H217), T281 (= T313), E282 (= E314), K379 (≠ I413), K384 (≠ N418)
- binding adenosine monophosphate: S255 (= S287), A256 (= A288), A257 (≠ P289), R277 (= R309), Y278 (= Y310), G279 (= G311), M280 (= M312), T281 (= T313), D357 (= D392), K379 (≠ I413), K384 (≠ N418)
- binding methylmalonyl-coenzyme a: P178 (= P214), H181 (= H217), H183 (= H219), T226 (= T261), R230 (= R265), S255 (= S287), R277 (= R309), G279 (= G311), M280 (= M312), M285 (= M317), G381 (= G415), G382 (= G416), Y383 (≠ F417)
5ie2A Crystal structure of a plant enzyme (see paper)
34% identity, 90% coverage: 38:505/519 of query aligns to 31:501/506 of 5ie2A
- active site: T165 (= T173), S185 (≠ N193), H209 (= H217), T310 (= T313), E311 (= E314), N410 (≠ I413), K415 (≠ N418), K495 (= K499)
- binding adenosine-5'-triphosphate: T165 (= T173), S166 (= S174), G167 (= G175), T168 (= T176), T169 (= T177), S284 (= S287), A285 (= A288), S286 (≠ P289), Y307 (= Y310), A308 (≠ G311), M309 (= M312), T310 (= T313), D389 (= D392), L401 (≠ I404), R404 (= R407), K495 (= K499)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
32% identity, 97% coverage: 8:509/519 of query aligns to 6:497/502 of 3r44A
Sites not aligning to the query:
5ie3A Crystal structure of a plant enzyme (see paper)
34% identity, 90% coverage: 38:505/519 of query aligns to 31:499/504 of 5ie3A
- active site: T163 (= T173), S183 (≠ N193), H207 (= H217), T308 (= T313), E309 (= E314), N408 (≠ I413), K413 (≠ N418), K493 (= K499)
- binding adenosine monophosphate: S164 (= S174), S282 (= S287), A283 (= A288), S284 (≠ P289), Y305 (= Y310), A306 (≠ G311), M307 (= M312), T308 (= T313), D387 (= D392), L399 (≠ I404), R402 (= R407), K493 (= K499)
- binding oxalic acid: V208 (≠ T218), S282 (= S287), A306 (≠ G311), M307 (= M312), H312 (≠ G316), K493 (= K499)
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)
34% identity, 90% coverage: 38:505/519 of query aligns to 31:506/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 173:177) binding
- H214 (= H217) binding ; mutation to A: Abolished activity.
- S289 (= S287) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ SAP 287:289) binding
- EA 310:311 (≠ ER 308:309) binding
- M314 (= M312) binding
- T315 (= T313) binding
- H319 (≠ G316) binding ; mutation to A: Abolished activity.
- D394 (= D392) binding
- R409 (= R407) binding ; mutation to A: Abolished activity.
- K500 (= K499) binding ; binding ; mutation to A: Abolished activity.
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
32% identity, 88% coverage: 38:494/519 of query aligns to 31:494/504 of 6qjzA
- active site: T169 (= T173), S189 (≠ N193), H213 (= H217), T314 (= T313), E315 (= E314), N414 (≠ I413), K419 (≠ N418)
- binding adenosine monophosphate: H213 (= H217), S288 (= S287), A289 (= A288), S290 (≠ P289), A312 (≠ G311), M313 (= M312), T314 (= T313), D393 (= D392), L405 (≠ I404), K410 (= K409), K419 (≠ N418)
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)
31% identity, 90% coverage: 39:506/519 of query aligns to 61:542/559 of Q67W82
- G395 (= G358) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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)
29% identity, 93% coverage: 38:519/519 of query aligns to 28:511/512 of O74976
- S283 (= S287) modified: Phosphoserine
- S284 (≠ A288) modified: Phosphoserine
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
29% identity, 91% coverage: 34:507/519 of query aligns to 42:527/528 of 3ni2A
- active site: S182 (≠ T173), S202 (≠ N193), H230 (= H217), T329 (= T313), E330 (= E314), K434 (≠ I413), Q439 (≠ N418), K519 (= K499)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ H219), S236 (≠ V223), G302 (≠ S287), A303 (= A288), P304 (= P289), G325 (≠ R309), G327 (= G311), T329 (= T313), P333 (≠ M317), V334 (≠ L318), D413 (= D392), K430 (= K409), K434 (≠ I413), Q439 (≠ N418)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
29% identity, 91% coverage: 34:507/519 of query aligns to 42:527/528 of 3a9vA
- active site: S182 (≠ T173), S202 (≠ N193), H230 (= H217), T329 (= T313), E330 (= E314), K434 (≠ I413), Q439 (≠ N418), K519 (= K499)
- binding adenosine monophosphate: H230 (= H217), G302 (≠ S287), A303 (= A288), P304 (= P289), Y326 (= Y310), G327 (= G311), M328 (= M312), T329 (= T313), D413 (= D392), K430 (= K409), K434 (≠ I413), Q439 (≠ N418)
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, 90% coverage: 39:506/519 of query aligns to 65:547/556 of Q9S725
- K211 (= K181) mutation to S: Drastically reduces the activity.
- M293 (= M257) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V284) mutation K->L,A: Affects the substrate specificity.
- E401 (≠ I359) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ E361) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R407) mutation to Q: Drastically reduces the activity.
- K457 (≠ G415) mutation to S: Drastically reduces the activity.
- K540 (= K499) mutation to N: Abolishes the activity.
7kydA Drosophila melanogaster long-chain fatty-acyl-coa synthetase cg6178 (see paper)
28% identity, 95% coverage: 16:510/519 of query aligns to 28:534/534 of 7kydA
- binding 5'-O-[(S)-hydroxy(octanoyloxy)phosphoryl]adenosine: H240 (= H217), F242 (≠ H219), A311 (≠ S287), A312 (= A288), P313 (= P289), G334 (vs. gap), Y335 (= Y310), G336 (= G311), L337 (≠ M312), S338 (≠ T313), S343 (≠ L318), D416 (= D392), I428 (= I404)
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)
31% identity, 93% coverage: 32:516/519 of query aligns to 42:541/541 of Q5SKN9
- T184 (= T173) binding
- G302 (= G286) binding
- Q322 (≠ E308) binding
- G323 (≠ R309) binding
- T327 (= T313) binding
- E328 (= E314) binding
- D418 (= D392) binding
- K435 (= K409) binding
- K439 (≠ I413) binding
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, 93% coverage: 32:514/519 of query aligns to 33:538/539 of P0DX84
- H231 (= H217) mutation to A: Retains 74% of wild-type activity.
- W235 (≠ L221) mutation to A: Almost completely abolishes the activity.
- G302 (= G286) mutation to P: Almost completely abolishes the activity.
- G303 (≠ S287) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y310) mutation to A: Retains 7.7% of wild-type activity.
- P333 (≠ M317) mutation to A: Retains 69% of wild-type activity.
- R432 (= R407) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K409) mutation to A: Retains 36% of wild-type activity.
- D435 (= D410) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I413) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G415) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G416) mutation to P: Retains 2.7% of wild-type activity.
- E442 (≠ F417) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N418) mutation to A: Retains 60% of wild-type activity.
- E474 (= E449) mutation to A: Retains 33% of wild-type activity.
- K523 (= K499) 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 (= K502) mutation to A: Retains 48% of wild-type activity.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
29% identity, 91% coverage: 34:506/519 of query aligns to 41:525/528 of 5bsrA
- active site: S181 (≠ T173), S201 (≠ N193), H229 (= H217), T328 (= T313), E329 (= E314), K433 (≠ I413), Q438 (≠ N418), K518 (= K499)
- binding adenosine monophosphate: A301 (≠ S287), G326 (= G311), T328 (= T313), D412 (= D392), K429 (= K409), K433 (≠ I413), Q438 (≠ N418)
- binding coenzyme a: L102 (≠ A95), P226 (= P214), H229 (= H217), Y231 (≠ H219), F253 (= F241), K435 (≠ G415), G436 (= G416), F437 (= F417), F498 (≠ N479)
Query Sequence
>AZOBR_RS22375 FitnessBrowser__azobra:AZOBR_RS22375
VSGNVGGNLFELFRSRFPADRSRPFAETEPGTDNARTVTYGDLEALTGRYANLLADLGLK
KGDRVAVQVEKSVENIILYLATVRAGGVFLPLNPAYTKAEVEYFLTDAEPHVFVARPESA
DALREVADKAKVAHLLTLGTHGEGTLPEQAAGKGTDFTTVPAEADDLAAILYTSGTTGRS
KGAMMSHRNLGSNALTLHKYWGFQPDDVLLHALPIFHTHGLFVATNCVLLNGSSMLFLPK
FDAEQVMGLLPRATVMMGVPTFYTRLLAHPGLTREATAHMRLFVSGSAPLLADTHKEFSA
RTGHAILERYGMTETGMLTSNPLDGDRIPGTVGFPLPEVSVRVVNPETGASLGTDEIGII
EVAGPNVFSGYWRMPEKTTQEIKPDGFFITGDVGKVDGRGYVHIVGRAKDLIISGGFNVY
PKEVETVIDGIDGVVESAVVGVPHPDFGEAVTAVVLRKPGSATPDEAAVIAVCKEQLANF
KVPKRVFFMDELPRNAMGKVQKNLLRDAHKDLFTAAKAR
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