SitesBLAST
Comparing WP_010960838.1 NCBI__GCF_000008325.1:WP_010960838.1 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)
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, 98% coverage: 4:501/510 of query aligns to 24:552/561 of P69451
- Y213 (= Y166) mutation to A: Loss of activity.
- T214 (= T167) mutation to A: 10% of wild-type activity.
- G216 (= G169) mutation to A: Decreases activity.
- T217 (= T170) mutation to A: Decreases activity.
- G219 (= G172) mutation to A: Decreases activity.
- K222 (= K175) mutation to A: Decreases activity.
- E361 (= E311) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
37% identity, 93% coverage: 28:499/510 of query aligns to 28:498/506 of 4gxqA
- active site: T163 (= T167), N183 (= N187), H207 (= H212), T303 (= T310), E304 (= E311), I403 (= I409), N408 (= N414), A491 (≠ K492)
- binding adenosine-5'-triphosphate: T163 (= T167), S164 (= S168), G165 (= G169), T166 (= T170), T167 (= T171), H207 (= H212), S277 (≠ G284), A278 (= A285), P279 (≠ A286), E298 (= E305), M302 (≠ P309), T303 (= T310), D382 (= D388), R397 (= R403)
- binding carbonate ion: H207 (= H212), S277 (≠ G284), R299 (≠ G306), G301 (= G308)
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)
36% identity, 93% coverage: 28:501/510 of query aligns to 29:496/503 of P9WQ37
- K172 (= K175) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R198) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ E201) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ A213) 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 (= A215) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V218) 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 (= R249) 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 (= W383) 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 (= D388) 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 (= R403) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V410) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G412) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K492) 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.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
36% identity, 93% coverage: 28:501/510 of query aligns to 32:496/502 of 3r44A
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)
33% identity, 95% coverage: 21:504/510 of query aligns to 20:484/484 of 5gtdA
- active site: T151 (= T167), S171 (≠ T189), H195 (= H212), T288 (= T310), E289 (= E311)
- binding adenosine-5'-monophosphate: G263 (= G284), G264 (≠ A285), Y285 (≠ D307), G286 (= G308), M287 (≠ P309), T288 (= T310), D366 (= D388), V378 (≠ I400)
- binding magnesium ion: F314 (≠ P335), S315 (≠ G336)
- binding 2-succinylbenzoate: H195 (= H212), S197 (≠ A215), A237 (≠ G255), L260 (≠ V281), G262 (= G283), G263 (= G284), G286 (= G308), M287 (≠ P309), S292 (= S313), Q293 (≠ P314)
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)
33% identity, 95% coverage: 21:504/510 of query aligns to 20:484/485 of 5x8fB
- active site: T151 (= T167), S171 (≠ T189), H195 (= H212), T288 (= T310), E289 (= E311), I387 (= I409), N392 (= N414), K470 (= K492)
- binding magnesium ion: Y23 (≠ T24), E24 (≠ D25), H70 (≠ A71), N178 (≠ D196), L202 (≠ M220), L214 (≠ P232), T296 (≠ C317), L297 (≠ V318), S298 (≠ N319)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ L86), L191 (= L208), P192 (= P209), H195 (= H212), I196 (≠ F214), S197 (≠ A215), A237 (≠ G255), V238 (= V256), L260 (≠ V281), G262 (= G283), G286 (= G308), M287 (≠ P309), S292 (= S313), Q293 (≠ P314), S388 (≠ V410), G389 (≠ N411), G390 (= G412), E391 (≠ M413), K420 (≠ L442), W421 (≠ H443), K450 (≠ R472), Y451 (≠ H473)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
33% identity, 95% coverage: 21:504/510 of query aligns to 19:481/481 of 5busA
- active site: T150 (= T167), S170 (≠ T189), H194 (= H212), T287 (= T310), E288 (= E311)
- binding adenosine monophosphate: H194 (= H212), G262 (= G284), G263 (≠ A285), S283 (≠ G306), M286 (≠ P309), T287 (= T310), D365 (= D388), V377 (≠ I400), R380 (= R403), K467 (= K492)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
33% identity, 94% coverage: 21:499/510 of query aligns to 19:474/475 of 5burA
- active site: T150 (= T167), S170 (≠ T189), H194 (= H212), T287 (= T310), E288 (= E311)
- binding adenosine-5'-triphosphate: T150 (= T167), S151 (= S168), T153 (= T170), T154 (= T171), K158 (= K175), G263 (≠ A285), S283 (≠ G306), T287 (= T310), D365 (= D388), V377 (≠ I400), R380 (= R403)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
31% identity, 95% coverage: 21:504/510 of query aligns to 28:514/518 of 4wv3B
- active site: S175 (≠ T167), T320 (= T310), E321 (= E311), K418 (≠ I409), W423 (≠ N414), K502 (= K492)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H212), T221 (≠ A213), F222 (= F214), A293 (≠ G283), S294 (≠ G284), E295 (≠ A285), A296 (= A286), G316 (= G306), I317 (≠ D307), G318 (= G308), C319 (≠ P309), T320 (= T310), D397 (= D388), H409 (≠ I400), R412 (= R403), K502 (= K492)
5ie2A Crystal structure of a plant enzyme (see paper)
33% identity, 88% coverage: 49:496/510 of query aligns to 52:499/506 of 5ie2A
- active site: T165 (= T167), S185 (≠ N187), H209 (= H212), T310 (= T310), E311 (= E311), N410 (≠ I409), K415 (≠ N414), K495 (= K492)
- binding adenosine-5'-triphosphate: T165 (= T167), S166 (= S168), G167 (= G169), T168 (= T170), T169 (= T171), S284 (≠ G284), A285 (= A285), S286 (≠ A286), Y307 (≠ D307), A308 (≠ G308), M309 (≠ P309), T310 (= T310), D389 (= D388), L401 (≠ I400), R404 (= R403), K495 (= K492)
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)
33% identity, 88% coverage: 49:496/510 of query aligns to 52:504/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 167:171) binding ATP
- H214 (= H212) binding ATP; mutation to A: Abolished activity.
- S289 (≠ G284) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ GAA 284:286) binding ATP
- EA 310:311 (≠ EG 305:306) binding ATP
- M314 (≠ P309) binding oxalate
- T315 (= T310) binding ATP
- H319 (≠ P314) binding oxalate; mutation to A: Abolished activity.
- D394 (= D388) binding ATP
- R409 (= R403) binding ATP; mutation to A: Abolished activity.
- K500 (= K492) binding ATP; binding oxalate; mutation to A: Abolished activity.
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, 97% coverage: 5:501/510 of query aligns to 28:544/559 of Q67W82
- G395 (= G355) 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)
33% identity, 88% coverage: 49:496/510 of query aligns to 52:497/504 of 5ie3A
- active site: T163 (= T167), S183 (≠ N187), H207 (= H212), T308 (= T310), E309 (= E311), N408 (≠ I409), K413 (≠ N414), K493 (= K492)
- binding adenosine monophosphate: S164 (= S168), S282 (≠ G284), A283 (= A285), S284 (≠ A286), Y305 (≠ D307), A306 (≠ G308), M307 (≠ P309), T308 (= T310), D387 (= D388), L399 (≠ I400), R402 (= R403), K493 (= K492)
- binding oxalic acid: V208 (≠ A213), S282 (≠ G284), A306 (≠ G308), M307 (≠ P309), H312 (≠ P314), K493 (= K492)
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)
30% identity, 93% coverage: 28:500/510 of query aligns to 64:571/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
5buqB Unliganded form of o-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, solved at 1.98 angstroms (see paper)
32% identity, 95% coverage: 21:504/510 of query aligns to 19:472/473 of 5buqB
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)
33% identity, 92% coverage: 31:499/510 of query aligns to 66:547/556 of Q9S725
- K211 (= K175) mutation to S: Drastically reduces the activity.
- M293 (≠ L254) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V281) mutation K->L,A: Affects the substrate specificity.
- E401 (= E356) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ A358) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R403) mutation to Q: Drastically reduces the activity.
- K457 (≠ N411) mutation to S: Drastically reduces the activity.
- K540 (= K492) mutation to N: Abolishes the activity.
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
29% identity, 95% coverage: 4:487/510 of query aligns to 5:494/504 of 6qjzA
- active site: T169 (= T167), S189 (≠ N187), H213 (= H212), T314 (= T310), E315 (= E311), N414 (≠ I409), K419 (≠ N414)
- binding adenosine monophosphate: H213 (= H212), S288 (≠ G284), A289 (= A285), S290 (≠ A286), A312 (≠ G308), M313 (≠ P309), T314 (= T310), D393 (= D388), L405 (≠ I400), K410 (= K405), K419 (≠ N414)
Q4G176 Malonate--CoA ligase ACSF3, mitochondrial; Acyl-CoA synthetase family member 3; EC 6.2.1.76 from Homo sapiens (Human) (see 2 papers)
30% identity, 89% coverage: 47:501/510 of query aligns to 89:572/576 of Q4G176
- R354 (≠ G306) mutation to A: Impairs malonyl-CoA synthase activity.; mutation to L: Impairs malonyl-CoA synthase activity.
- V372 (= V325) to M: in dbSNP:rs3743979
Sites not aligning to the query:
- 2 L → P: in dbSNP:rs7188200
- 17 A → P: in dbSNP:rs11547019
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)
31% identity, 92% coverage: 29:496/510 of query aligns to 28:498/512 of O74976
- S283 (≠ V281) modified: Phosphoserine
- S284 (= S282) modified: Phosphoserine
4rlfB Crystal structure of a benzoate coenzyme a ligase with p-toluic acid and o-toluic acid (see paper)
30% identity, 94% coverage: 21:499/510 of query aligns to 26:514/519 of 4rlfB
- active site: S176 (≠ T167), T196 (vs. gap), T324 (= T310), E325 (= E311), K422 (≠ I409), Y427 (≠ N414), K507 (= K492)
- binding 2-methylbenzoic acid: A222 (= A213), Y223 (vs. gap), G298 (= G284), I321 (≠ D307), G322 (= G308), S323 (≠ P309), H328 (≠ P314)
- binding 4-methylbenzoic acid: A216 (≠ V207), P246 (≠ L230), P248 (= P232), G269 (= G255), A270 (≠ V256), G273 (≠ M259)
Query Sequence
>WP_010960838.1 NCBI__GCF_000008325.1:WP_010960838.1
MQASLPAALRLAADRFSSLPAILTDERRVDFAEFDRASDAIAAGLAVRGVAKGERIGLYC
INSVEFTLAYAGIVKAGAVVVPINLLLSAEEVHYNLADAGVSGLIYHGQVSANAAAVADR
LSGLKVRAGIGLDDQDGDVWRALLEESAEPPSIEFDAVEDLAAILYTSGTTGHPKGAMLT
HGNLLANTTSVREALDWRPGEDRVLVVLPMFHAFAATVGMLTPLLHGCALIPLAKFEPDR
VADTIGRHRATLFLGVPSMYALLCRLGEERIARFGTVRLCVSGGAALPPSVMEQFQARFG
LPIHEGDGPTECSPVTCVNPVAGPVKRGTVGLPVPGVEMKILGEDGVELPRGELGEIAVR
GANVFKGYWNQPEATRECFRDGWFLTGDLGQVDDDGYFSIVDRKKDLIIVNGMNVYPRVI
EEVLCRHPAVREVAVVGDPDPLHGERVVAYVVLDAPASEAEIRAWCKPYLGRHEIPRQVK
ALQQLPRNAAGKIVKRQLRRQGEVERGVDA
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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