SitesBLAST
Comparing WP_012756293.1 NCBI__GCF_000023185.1:WP_012756293.1 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)
66% identity, 94% coverage: 29:501/504 of query aligns to 30:505/506 of 4gxqA
- active site: T163 (= T162), N183 (= N182), H207 (= H206), T303 (= T302), E304 (= E303), I403 (= I402), N408 (= N407), A491 (≠ K487)
- binding adenosine-5'-triphosphate: T163 (= T162), S164 (= S163), G165 (= G164), T166 (= T165), T167 (= T166), H207 (= H206), S277 (= S276), A278 (= A277), P279 (= P278), E298 (= E297), M302 (= M301), T303 (= T302), D382 (= D381), R397 (= R396)
- binding carbonate ion: H207 (= H206), S277 (= S276), R299 (= R298), G301 (= G300)
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
37% identity, 93% coverage: 29:496/504 of query aligns to 31:486/486 of 8wevA
Sites not aligning to the query:
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)
35% identity, 93% coverage: 29:498/504 of query aligns to 31:498/503 of P9WQ37
- K172 (= K170) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T193) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ D195) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ T207) 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 (≠ G209) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V212) 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 (≠ T243) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G300) 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 (≠ F376) 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 (= D381) 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 (= R396) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S403) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G405) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K487) 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)
35% identity, 93% coverage: 29:498/504 of query aligns to 34:498/502 of 3r44A
Sites not aligning to the query:
3nyrA Malonyl-coa ligase ternary product complex with malonyl-coa and amp bound (see paper)
37% identity, 95% coverage: 5:482/504 of query aligns to 1:460/460 of 3nyrA
- active site: T137 (= T162), T157 (≠ N182), H181 (= H206), T281 (= T302), E282 (= E303), K379 (≠ I402), K384 (≠ N407)
- binding adenosine monophosphate: S255 (= S276), A256 (= A277), A257 (≠ P278), R277 (= R298), Y278 (= Y299), G279 (= G300), M280 (= M301), T281 (= T302), D357 (= D381), K379 (≠ I402), K384 (≠ N407)
- binding malonyl-coenzyme a: P178 (= P203), H181 (= H206), T226 (= T250), R230 (= R254), S255 (= S276), R277 (= R298), G279 (= G300), G381 (= G404), G382 (= G405), Y383 (= Y406)
3nyqA Malonyl-coa ligase ternary product complex with methylmalonyl-coa and amp bound (see paper)
37% identity, 95% coverage: 5:482/504 of query aligns to 1:460/460 of 3nyqA
- active site: T137 (= T162), T157 (≠ N182), H181 (= H206), T281 (= T302), E282 (= E303), K379 (≠ I402), K384 (≠ N407)
- binding adenosine monophosphate: S255 (= S276), A256 (= A277), A257 (≠ P278), R277 (= R298), Y278 (= Y299), G279 (= G300), M280 (= M301), T281 (= T302), D357 (= D381), K379 (≠ I402), K384 (≠ N407)
- binding methylmalonyl-coenzyme a: P178 (= P203), H181 (= H206), H183 (= H208), T226 (= T250), R230 (= R254), S255 (= S276), R277 (= R298), G279 (= G300), M280 (= M301), M285 (= M306), G381 (= G404), G382 (= G405), Y383 (= Y406)
Q4G176 Malonate--CoA ligase ACSF3, mitochondrial; Acyl-CoA synthetase family member 3; EC 6.2.1.76 from Homo sapiens (Human) (see 2 papers)
32% identity, 97% coverage: 10:497/504 of query aligns to 49:573/576 of Q4G176
- R354 (= R298) mutation to A: Impairs malonyl-CoA synthase activity.; mutation to L: Impairs malonyl-CoA synthase activity.
- V372 (≠ K315) to M: in dbSNP:rs3743979
Sites not aligning to the query:
- 2 L → P: in dbSNP:rs7188200
- 17 A → P: in dbSNP:rs11547019
5ie2A Crystal structure of a plant enzyme (see paper)
33% identity, 89% coverage: 48:497/504 of query aligns to 52:505/506 of 5ie2A
- active site: T165 (= T162), S185 (≠ N182), H209 (= H206), T310 (= T302), E311 (= E303), N410 (≠ I402), K415 (≠ N407), K495 (= K487)
- binding adenosine-5'-triphosphate: T165 (= T162), S166 (= S163), G167 (= G164), T168 (= T165), T169 (= T166), S284 (= S276), A285 (= A277), S286 (≠ P278), Y307 (= Y299), A308 (≠ G300), M309 (= M301), T310 (= T302), D389 (= D381), L401 (≠ I393), R404 (= R396), K495 (= K487)
5ie3A Crystal structure of a plant enzyme (see paper)
33% identity, 89% coverage: 48:497/504 of query aligns to 52:503/504 of 5ie3A
- active site: T163 (= T162), S183 (≠ N182), H207 (= H206), T308 (= T302), E309 (= E303), N408 (≠ I402), K413 (≠ N407), K493 (= K487)
- binding adenosine monophosphate: S164 (= S163), S282 (= S276), A283 (= A277), S284 (≠ P278), Y305 (= Y299), A306 (≠ G300), M307 (= M301), T308 (= T302), D387 (= D381), L399 (≠ I393), R402 (= R396), K493 (= K487)
- binding oxalic acid: V208 (≠ T207), S282 (= S276), A306 (≠ G300), M307 (= M301), H312 (≠ N305), K493 (= K487)
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, 89% coverage: 48:497/504 of query aligns to 52:510/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 162:166) binding ATP
- H214 (= H206) binding ATP; mutation to A: Abolished activity.
- S289 (= S276) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ SAP 276:278) binding ATP
- EA 310:311 (≠ ER 297:298) binding ATP
- M314 (= M301) binding oxalate
- T315 (= T302) binding ATP
- H319 (≠ N305) binding oxalate; mutation to A: Abolished activity.
- D394 (= D381) binding ATP
- R409 (= R396) binding ATP; mutation to A: Abolished activity.
- K500 (= K487) binding ATP; binding oxalate; mutation to A: Abolished activity.
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
32% identity, 86% coverage: 48:482/504 of query aligns to 51:494/504 of 6qjzA
- active site: T169 (= T162), S189 (≠ N182), H213 (= H206), T314 (= T302), E315 (= E303), N414 (≠ I402), K419 (≠ N407)
- binding adenosine monophosphate: H213 (= H206), S288 (= S276), A289 (= A277), S290 (≠ P278), A312 (≠ G300), M313 (= M301), T314 (= T302), D393 (= D381), L405 (≠ I393), K410 (= K398), K419 (≠ N407)
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, 89% coverage: 46:493/504 of query aligns to 46:500/512 of O74976
- S283 (= S276) modified: Phosphoserine
- S284 (≠ A277) 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)
29% identity, 95% coverage: 15:494/504 of query aligns to 45:538/546 of Q84P21
- K530 (= K487) mutation to N: Lossed enzymatic activity.
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)
29% identity, 89% coverage: 47:496/504 of query aligns to 69:552/561 of P69451
- Y213 (= Y161) mutation to A: Loss of activity.
- T214 (= T162) mutation to A: 10% of wild-type activity.
- G216 (= G164) mutation to A: Decreases activity.
- T217 (= T165) mutation to A: Decreases activity.
- G219 (= G167) mutation to A: Decreases activity.
- K222 (= K170) mutation to A: Decreases activity.
- E361 (= E303) mutation to A: Loss of 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)
30% identity, 94% coverage: 27:498/504 of query aligns to 59:546/559 of Q67W82
- G395 (= G347) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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: 26:494/504 of query aligns to 26:477/485 of 5x8fB
- active site: T151 (= T162), S171 (≠ N182), H195 (= H206), T288 (= T302), E289 (= E303), I387 (= I402), N392 (= N407), K470 (= K487)
- binding magnesium ion: H70 (≠ L70), N178 (≠ Y189), L202 (≠ T214), L214 (= L226), T296 (= T308), L297 (≠ S309), S298 (≠ N310)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ A85), L191 (= L202), P192 (= P203), H195 (= H206), I196 (≠ T207), S197 (≠ H208), A237 (≠ G247), V238 (= V248), L260 (= L271), G262 (≠ I273), G286 (= G300), M287 (= M301), S292 (vs. gap), Q293 (≠ N305), S388 (= S403), G389 (= G404), G390 (= G405), E391 (≠ Y406), K420 (≠ D435), W421 (≠ F436), K450 (≠ R467), Y451 (= Y468)
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)
31% identity, 93% coverage: 26:494/504 of query aligns to 26:477/484 of 5gtdA
- active site: T151 (= T162), S171 (≠ N182), H195 (= H206), T288 (= T302), E289 (= E303)
- binding adenosine-5'-monophosphate: G263 (≠ S274), G264 (= G275), Y285 (= Y299), G286 (= G300), M287 (= M301), T288 (= T302), D366 (= D381), V378 (≠ I393)
- binding magnesium ion: F314 (≠ P326), S315 (≠ D327)
- binding 2-succinylbenzoate: H195 (= H206), S197 (≠ H208), A237 (≠ G247), L260 (= L271), G262 (≠ I273), G263 (≠ S274), G286 (= G300), M287 (= M301), S292 (vs. gap), Q293 (≠ N305)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
28% identity, 98% coverage: 4:495/504 of query aligns to 23:535/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H206), F245 (≠ H208), T249 (≠ V212), G314 (≠ S276), A315 (= A277), P316 (= P278), G337 (≠ R298), Y338 (= Y299), G339 (= G300), L340 (≠ M301), T341 (= T302), A346 (≠ N307), D420 (= D381), I432 (= I393), K527 (= K487)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
28% identity, 98% coverage: 4:495/504 of query aligns to 23:535/539 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 (= H206), F245 (≠ H208), T249 (≠ V212), G314 (≠ S276), A315 (= A277), P316 (= P278), G337 (≠ R298), Y338 (= Y299), G339 (= G300), L340 (≠ M301), T341 (= T302), S345 (≠ M306), A346 (≠ N307), D420 (= D381), I432 (= I393), K527 (= K487)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ H208), R335 (≠ L296), G337 (≠ R298), G339 (= G300), L340 (≠ M301), A346 (≠ N307)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
31% identity, 93% coverage: 26:494/504 of query aligns to 25:474/475 of 5burA
- active site: T150 (= T162), S170 (≠ N182), H194 (= H206), T287 (= T302), E288 (= E303)
- binding adenosine-5'-triphosphate: T150 (= T162), S151 (= S163), T153 (= T165), T154 (= T166), K158 (= K170), G263 (= G275), S283 (≠ R298), T287 (= T302), D365 (= D381), V377 (≠ I393), R380 (= R396)
Query Sequence
>WP_012756293.1 NCBI__GCF_000023185.1:WP_012756293.1
MSNHLFDAMRAAAPGDAPFIRIDSTRTWTYDDAFALSGRIAGAMDTLGIRPGDRVAVQVE
KSAEALILYLACLRTGAVYLPLNTAYTLAELDYFIGDAEPRLVVVASAARGGVETIAKPH
GAIVETLDADGSGSLLDLARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLL
SNALTLRDYWRVTADDRLIHALPIFHTHGLFVATNVTLLAGASMFLLTKFDADEVVSLMP
QATMLMGVPTFYVRLLQSPRLDEQAVANIRLFISGSAPLLAETHTEFQARTGHAILERYG
MTETNMNTSNPYEGKRIAGTVGFPLPDVTVRVTDPATGLVLSPEETGMIEIKGPNVFKGY
WRMPEKTAAEFTADGFFISGDLGKIDREGYVHIVGRGKDLVISGGYNIYPKEVEGEIDQI
EGVVESAVIGVPHPDFGEGVTAVVVCKPGAVLDEKTIVSALQDRLARYKQPKRIIFADDL
PRNTMGKVQKNILRQQYADLYTRR
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