SitesBLAST
Comparing Ac3H11_964 FitnessBrowser__acidovorax_3H11:Ac3H11_964 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)
55% identity, 99% coverage: 5:516/517 of query aligns to 4:505/506 of 4gxqA
- active site: T163 (= T170), N183 (= N190), H207 (= H214), T303 (≠ S310), E304 (= E311), I403 (= I417), N408 (= N422), A491 (≠ K502)
- binding adenosine-5'-triphosphate: T163 (= T170), S164 (= S171), G165 (= G172), T166 (= T173), T167 (= T174), H207 (= H214), S277 (= S284), A278 (= A285), P279 (= P286), E298 (= E305), M302 (= M309), T303 (≠ S310), D382 (= D396), R397 (= R411)
- binding carbonate ion: H207 (= H214), S277 (= S284), R299 (= R306), G301 (= G308)
Q4G176 Malonate--CoA ligase ACSF3, mitochondrial; Acyl-CoA synthetase family member 3; EC 6.2.1.76 from Homo sapiens (Human) (see 2 papers)
33% identity, 92% coverage: 35:512/517 of query aligns to 66:574/576 of Q4G176
- R354 (= R306) mutation to A: Impairs malonyl-CoA synthase activity.; mutation to L: Impairs malonyl-CoA synthase activity.
- V372 (≠ K324) 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)
30% identity, 94% coverage: 31:514/517 of query aligns to 39:555/561 of P69451
- Y213 (= Y169) mutation to A: Loss of activity.
- T214 (= T170) mutation to A: 10% of wild-type activity.
- G216 (= G172) mutation to A: Decreases activity.
- T217 (= T173) mutation to A: Decreases activity.
- G219 (= G175) mutation to A: Decreases activity.
- K222 (= K178) mutation to A: Decreases activity.
- E361 (= E311) mutation to A: Loss of activity.
3nyrA Malonyl-coa ligase ternary product complex with malonyl-coa and amp bound (see paper)
35% identity, 85% coverage: 61:497/517 of query aligns to 44:460/460 of 3nyrA
- active site: T137 (= T170), T157 (≠ N190), H181 (= H214), T281 (≠ S310), E282 (= E311), K379 (≠ I417), K384 (≠ N422)
- binding adenosine monophosphate: S255 (= S284), A256 (= A285), A257 (≠ P286), R277 (= R306), Y278 (= Y307), G279 (= G308), M280 (= M309), T281 (≠ S310), D357 (= D396), K379 (≠ I417), K384 (≠ N422)
- binding malonyl-coenzyme a: P178 (= P211), H181 (= H214), T226 (= T258), R230 (= R262), S255 (= S284), R277 (= R306), G279 (= G308), G381 (= G419), G382 (= G420), Y383 (= Y421)
3nyqA Malonyl-coa ligase ternary product complex with methylmalonyl-coa and amp bound (see paper)
35% identity, 85% coverage: 61:497/517 of query aligns to 44:460/460 of 3nyqA
- active site: T137 (= T170), T157 (≠ N190), H181 (= H214), T281 (≠ S310), E282 (= E311), K379 (≠ I417), K384 (≠ N422)
- binding adenosine monophosphate: S255 (= S284), A256 (= A285), A257 (≠ P286), R277 (= R306), Y278 (= Y307), G279 (= G308), M280 (= M309), T281 (≠ S310), D357 (= D396), K379 (≠ I417), K384 (≠ N422)
- binding methylmalonyl-coenzyme a: P178 (= P211), H181 (= H214), H183 (= H216), T226 (= T258), R230 (= R262), S255 (= S284), R277 (= R306), G279 (= G308), M280 (= M309), M285 (= M314), G381 (= G419), G382 (= G420), Y383 (= Y421)
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, 92% coverage: 36:512/517 of query aligns to 31:497/503 of P9WQ37
- K172 (= K178) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ K201) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ G203) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V215) 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 (≠ G217) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V220) 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 (≠ T251) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G308) 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 (= W391) 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 (= D396) 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 (= R411) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S418) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G420) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K502) 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.
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)
29% identity, 92% coverage: 35:510/517 of query aligns to 65:571/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
31% identity, 92% coverage: 36:512/517 of query aligns to 34:497/502 of 3r44A
Sites not aligning to the query:
5ie2A Crystal structure of a plant enzyme (see paper)
30% identity, 91% coverage: 40:511/517 of query aligns to 40:504/506 of 5ie2A
- active site: T165 (= T170), S185 (≠ N190), H209 (= H214), T310 (≠ S310), E311 (= E311), N410 (≠ I417), K415 (≠ N422), K495 (= K502)
- binding adenosine-5'-triphosphate: T165 (= T170), S166 (= S171), G167 (= G172), T168 (= T173), T169 (= T174), S284 (= S284), A285 (= A285), S286 (≠ P286), Y307 (= Y307), A308 (≠ G308), M309 (= M309), T310 (≠ S310), D389 (= D396), L401 (≠ I408), R404 (= R411), K495 (= K502)
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, 91% coverage: 40:511/517 of query aligns to 40:509/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 170:174) binding
- H214 (= H214) binding ; mutation to A: Abolished activity.
- S289 (= S284) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ SAP 284:286) binding
- EA 310:311 (≠ ER 305:306) binding
- M314 (= M309) binding
- T315 (≠ S310) binding
- H319 (≠ I313) binding ; mutation to A: Abolished activity.
- D394 (= D396) binding
- R409 (= R411) binding ; mutation to A: Abolished activity.
- K500 (= K502) binding ; binding ; mutation to A: Abolished activity.
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
29% identity, 90% coverage: 36:502/517 of query aligns to 32:499/504 of 6qjzA
- active site: T169 (= T170), S189 (≠ N190), H213 (= H214), T314 (≠ S310), E315 (= E311), N414 (≠ I417), K419 (≠ N422)
- binding adenosine monophosphate: H213 (= H214), S288 (= S284), A289 (= A285), S290 (≠ P286), A312 (≠ G308), M313 (= M309), T314 (≠ S310), D393 (= D396), L405 (≠ I408), K410 (= K413), K419 (≠ N422)
5ie3A Crystal structure of a plant enzyme (see paper)
29% identity, 91% coverage: 40:511/517 of query aligns to 40:502/504 of 5ie3A
- active site: T163 (= T170), S183 (≠ N190), H207 (= H214), T308 (≠ S310), E309 (= E311), N408 (≠ I417), K413 (≠ N422), K493 (= K502)
- binding adenosine monophosphate: S164 (= S171), S282 (= S284), A283 (= A285), S284 (≠ P286), Y305 (= Y307), A306 (≠ G308), M307 (= M309), T308 (≠ S310), D387 (= D396), L399 (≠ I408), R402 (= R411), K493 (= K502)
- binding oxalic acid: V208 (= V215), S282 (= S284), A306 (≠ G308), M307 (= M309), H312 (≠ I313), K493 (= K502)
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)
27% identity, 97% coverage: 7:508/517 of query aligns to 3:500/512 of O74976
- S283 (= S284) modified: Phosphoserine
- S284 (≠ A285) modified: Phosphoserine
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
31% identity, 93% coverage: 36:514/517 of query aligns to 29:482/484 of 5gtdA
- active site: T151 (= T170), S171 (≠ N190), H195 (= H214), T288 (≠ S310), E289 (= E311)
- binding adenosine-5'-monophosphate: G263 (≠ S284), G264 (≠ A285), Y285 (= Y307), G286 (= G308), M287 (= M309), T288 (≠ S310), D366 (= D396), V378 (≠ I408)
- binding magnesium ion: F314 (≠ P342), S315 (≠ G343)
- binding 2-succinylbenzoate: H195 (= H214), S197 (≠ H216), A237 (≠ G255), L260 (≠ I281), G262 (= G283), G263 (≠ S284), G286 (= G308), M287 (= M309), S292 (vs. gap), 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)
31% identity, 93% coverage: 36:514/517 of query aligns to 29:482/485 of 5x8fB
- active site: T151 (= T170), S171 (≠ N190), H195 (= H214), T288 (≠ S310), E289 (= E311), I387 (= I417), N392 (= N422), K470 (= K502)
- binding magnesium ion: H70 (≠ L77), N178 (≠ Y197), L202 (≠ I222), L214 (≠ W234), T296 (≠ L315), L297 (≠ T316), S298 (= S317)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ A92), L191 (= L210), P192 (= P211), H195 (= H214), I196 (≠ V215), S197 (≠ H216), A237 (≠ G255), V238 (= V256), L260 (≠ I281), G262 (= G283), G286 (= G308), M287 (= M309), S292 (vs. gap), Q293 (vs. gap), S388 (= S418), G389 (= G419), G390 (= G420), E391 (≠ Y421), K420 (≠ D450), W421 (≠ F451), K450 (≠ N482), Y451 (≠ F483)
Sites not aligning to the query:
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
31% identity, 93% coverage: 36:514/517 of query aligns to 28:479/481 of 5busA
- active site: T150 (= T170), S170 (≠ N190), H194 (= H214), T287 (≠ S310), E288 (= E311)
- binding adenosine monophosphate: H194 (= H214), G262 (≠ S284), G263 (≠ A285), S283 (≠ R306), M286 (= M309), T287 (≠ S310), D365 (= D396), V377 (≠ I408), R380 (= R411), K467 (= K502)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
31% identity, 92% coverage: 36:510/517 of query aligns to 28:475/475 of 5burA
- active site: T150 (= T170), S170 (≠ N190), H194 (= H214), T287 (≠ S310), E288 (= E311)
- binding adenosine-5'-triphosphate: T150 (= T170), S151 (= S171), T153 (= T173), T154 (= T174), K158 (= K178), G263 (≠ A285), S283 (≠ R306), T287 (≠ S310), D365 (= D396), V377 (≠ I408), R380 (= R411)
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, 93% coverage: 36:516/517 of query aligns to 49:538/541 of Q5SKN9
- T184 (= T170) binding
- G302 (vs. gap) binding
- Q322 (≠ E305) binding
- G323 (≠ R306) binding
- T327 (≠ S310) binding
- E328 (= E311) binding
- D418 (= D396) binding
- K435 (= K413) binding
- K439 (≠ I417) binding
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)
27% identity, 87% coverage: 62:510/517 of query aligns to 65:531/543 of P38137
Sites not aligning to the query:
- 541:543 C-terminal peroxisome targeting signal (PTS1)
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)
28% identity, 99% coverage: 1:513/517 of query aligns to 6:534/539 of P0DX84
- H231 (= H214) mutation to A: Retains 74% of wild-type activity.
- W235 (≠ F219) mutation to A: Almost completely abolishes the activity.
- G302 (≠ A282) mutation to P: Almost completely abolishes the activity.
- G303 (= G283) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y307) mutation to A: Retains 7.7% of wild-type activity.
- P333 (≠ M314) mutation to A: Retains 69% of wild-type activity.
- R432 (= R411) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K413) mutation to A: Retains 36% of wild-type activity.
- D435 (= D414) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I417) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G419) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G420) mutation to P: Retains 2.7% of wild-type activity.
- E442 (≠ Y421) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N422) mutation to A: Retains 60% of wild-type activity.
- E474 (= E453) mutation to A: Retains 33% of wild-type activity.
- K523 (= K502) 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 (= K505) mutation to A: Retains 48% of wild-type activity.
Query Sequence
>Ac3H11_964 FitnessBrowser__acidovorax_3H11:Ac3H11_964
MSQQNLFSALRAAFPADLSSTAVETTAPDGSPLFYTWGDLDRASARMANLLASLKLPEGS
RVAVQVEKSVEAMVLYLATLRAGYVFLPLNTAYQSAEIEYFIGNAEPGVVVCTPGNFGWV
SKIAFTQGTGHVFTLGDDRTGSLLERAAHHSDVHTPVQKSADDLAAILYTSGTTGRSKGA
MLTHGNLLSNAVTLKDYWGWKAGDVLIHALPIFHVHGLFVAIHGALINGSKMIWFAKFDP
KAVLAAMPRATVFMGVPTLYVRLLAEAGLTKEAAKNMRLFIAGSAPLLIETFTEWQQRTG
HTILERYGMSETIMLTSNPYAADKRHAGQTERRGATVGFPLPGVGLRVVDDANKPLPVGE
IGSIQVKGPNVFKGYWRMPEKTAEEFTQDGWFKTGDVGKVDARDYVSIVGRSKDLIISGG
YNVYPAEIEGYINDMPGVAESALVGVPHPDFGEVGVAVVIAKPGASLNPDAIVAQLKSQL
ANFKIPKKCFVVPELPRNTMGKVQKNLLREQHKGLFA
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