SitesBLAST
Comparing CCNA_01017 FitnessBrowser__Caulo:CCNA_01017 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)
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, 97% coverage: 10:521/530 of query aligns to 1:497/503 of P9WQ37
- R9 (= R18) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D26) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K184) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ G211) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ S213) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I225) 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 (≠ G227) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ W230) 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 (= R260) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G319) 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 (= W400) 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 (= D405) 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 (= R420) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S427) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G429) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K511) 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)
35% identity, 97% coverage: 8:521/530 of query aligns to 2:497/502 of 3r44A
5upsA Acyl-coa synthetase ptma2 from streptomyces platensis in complex with sbnp663 ligand (see paper)
33% identity, 94% coverage: 11:510/530 of query aligns to 2:494/520 of 5upsA
- active site: T169 (= T176), M189 (= M196), H213 (= H224), T312 (= T321), E313 (= E322), K410 (≠ I426), N415 (= N431)
- binding 5'-O-[(R)-hydroxy{[(7beta,8alpha,9beta,10alpha,11beta,13alpha)-7-hydroxy-19-oxo-11,16-epoxykauran-19-yl]oxy}phosphoryl]adenosine: Y309 (= Y318), G310 (= G319), Q311 (≠ M320), T312 (= T321), G316 (= G325), F317 (vs. gap), D389 (= D405), F401 (≠ I417), K410 (≠ I426), N415 (= N431)
Sites not aligning to the query:
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
34% identity, 92% coverage: 34:521/530 of query aligns to 26:501/506 of 4gxqA
- active site: T163 (= T176), N183 (= N203), H207 (= H224), T303 (= T321), E304 (= E322), I403 (= I426), N408 (= N431), A491 (≠ K511)
- binding adenosine-5'-triphosphate: T163 (= T176), S164 (= S177), G165 (= G178), T166 (= T179), T167 (= T180), H207 (= H224), S277 (≠ A295), A278 (= A296), P279 (= P297), E298 (≠ Q316), M302 (= M320), T303 (= T321), D382 (= D405), R397 (= R420)
- binding carbonate ion: H207 (= H224), S277 (≠ A295), R299 (≠ Q317), G301 (= G319)
5uptA Acyl-coa synthetase ptma2 from streptomyces platensis in complex with sbnp468 ligand (see paper)
33% identity, 94% coverage: 11:510/530 of query aligns to 6:498/515 of 5uptA
- active site: T173 (= T176), M193 (= M196), H217 (= H224), T316 (= T321), E317 (= E322), K414 (≠ I426), N419 (= N431)
- binding (7alpha,8alpha,10alpha,13alpha)-7,16-dihydroxykauran-18-oic acid: Y87 (≠ G92), R89 (= R94), R89 (= R94), P214 (= P221), F216 (≠ A223), H217 (= H224), V241 (≠ F247), G314 (= G319)
Sites not aligning to the query:
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: 26:518/530 of query aligns to 54:570/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
30% identity, 91% coverage: 38:518/530 of query aligns to 50:534/539 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 (= H224), F245 (≠ G226), T249 (≠ W230), G314 (≠ A295), A315 (= A296), P316 (= P297), G337 (≠ Q317), Y338 (= Y318), G339 (= G319), L340 (≠ M320), T341 (= T321), S345 (≠ G325), A346 (≠ T326), D420 (= D405), I432 (= I417), K527 (= K511)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ G226), R335 (≠ V315), G337 (≠ Q317), G339 (= G319), L340 (≠ M320), A346 (≠ T326)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
30% identity, 91% coverage: 38:518/530 of query aligns to 50:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H224), F245 (≠ G226), T249 (≠ W230), G314 (≠ A295), A315 (= A296), P316 (= P297), G337 (≠ Q317), Y338 (= Y318), G339 (= G319), L340 (≠ M320), T341 (= T321), A346 (≠ T326), D420 (= D405), I432 (= I417), K527 (= K511)
5upqA Acyl-coa synthetase ptma2 from streptomyces platensis in complex with sbnp465 ligand (see paper)
33% identity, 94% coverage: 11:510/530 of query aligns to 5:495/512 of 5upqA
- active site: T172 (= T176), M190 (= M196), H214 (= H224), T313 (= T321), E314 (= E322), K411 (≠ I426)
- binding 5'-O-[(R)-{[(7beta,8alpha,9beta,10alpha,13alpha,16beta)-7,16-dihydroxy-18-oxokauran-18-yl]oxy}(hydroxy)phosphoryl]adenosine: H214 (= H224), F256 (= F265), G309 (= G313), Y310 (= Y318), G311 (= G319), Q312 (≠ M320), T313 (= T321), G317 (= G325), F318 (vs. gap), D390 (= D405), F402 (≠ I417)
Sites not aligning to the query:
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)
32% identity, 94% coverage: 21:518/530 of query aligns to 12:477/485 of 5x8fB
- active site: T151 (= T176), S171 (≠ M196), H195 (= H224), T288 (= T321), E289 (= E322), I387 (= I426), N392 (= N431), K470 (= K511)
- binding magnesium ion: Y23 (≠ F32), E24 (= E33), H70 (≠ L79), N178 (= N203), L202 (≠ G231), L214 (≠ V243), T296 (≠ Y329), L297 (= L330), S298 (≠ P331)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R94), L191 (≠ M220), P192 (= P221), H195 (= H224), I196 (= I225), S197 (≠ G226), A237 (= A269), V238 (≠ A270), L260 (= L292), G262 (= G294), G286 (= G319), M287 (= M320), S292 (≠ G325), Q293 (≠ T326), S388 (= S427), G389 (= G428), G390 (= G429), E391 (= E430), K420 (= K459), W421 (= W460), K450 (≠ H491), Y451 (≠ F492)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
31% identity, 94% coverage: 21:518/530 of query aligns to 12:477/484 of 5gtdA
- active site: T151 (= T176), S171 (≠ M196), H195 (= H224), T288 (= T321), E289 (= E322)
- binding adenosine-5'-monophosphate: G263 (≠ A295), G264 (≠ A296), Y285 (= Y318), G286 (= G319), M287 (= M320), T288 (= T321), D366 (= D405), V378 (≠ I417)
- binding magnesium ion: F314 (≠ P351), S315 (≠ G352)
- binding 2-succinylbenzoate: H195 (= H224), S197 (≠ G226), A237 (= A269), L260 (= L292), G262 (= G294), G263 (≠ A295), G286 (= G319), M287 (= M320), S292 (≠ G325), Q293 (≠ T326)
Q17577 Acyl-CoA synthetase 7; EC 6.2.1.- from Caenorhabditis elegans (see paper)
28% identity, 97% coverage: 18:529/530 of query aligns to 24:540/540 of Q17577
- SS 186:187 (≠ TS 176:177) mutation to AA: Loss of catalytic activity; when associated with A-339.
- E339 (= E322) mutation to A: Severe loss of catalytic activity. Loss of catalytic activity; when associated with 186-A-A-187.
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)
30% identity, 91% coverage: 34:517/530 of query aligns to 55:536/546 of Q84P21
- K530 (= K511) mutation to N: Lossed enzymatic activity.
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
31% identity, 94% coverage: 21:518/530 of query aligns to 11:474/481 of 5busA
- active site: T150 (= T176), S170 (≠ M196), H194 (= H224), T287 (= T321), E288 (= E322)
- binding adenosine monophosphate: H194 (= H224), G262 (≠ A295), G263 (≠ A296), S283 (≠ Q317), M286 (= M320), T287 (= T321), D365 (= D405), V377 (≠ I417), R380 (= R420), K467 (= K511)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
31% identity, 94% coverage: 21:518/530 of query aligns to 11:474/475 of 5burA
- active site: T150 (= T176), S170 (≠ M196), H194 (= H224), T287 (= T321), E288 (= E322)
- binding adenosine-5'-triphosphate: T150 (= T176), S151 (= S177), T153 (= T179), T154 (= T180), K158 (= K184), G263 (≠ A296), S283 (≠ Q317), T287 (= T321), D365 (= D405), V377 (≠ I417), R380 (= R420)
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
29% identity, 94% coverage: 23:518/530 of query aligns to 31:532/539 of 2d1sA
- active site: S194 (≠ T176), R214 (= R197), H241 (= H224), T339 (= T321), E340 (= E322), K439 (≠ I426), Q444 (≠ N431), K525 (= K511)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S194 (≠ T176), S195 (= S177), H241 (= H224), F243 (≠ G226), T247 (≠ W230), I282 (≠ F265), G312 (≠ A295), A313 (= A296), P314 (= P297), Q334 (= Q316), G335 (≠ Q317), Y336 (= Y318), G337 (= G319), L338 (≠ M320), T339 (= T321), S343 (≠ G325), A344 (≠ T326), D418 (= D405), R433 (= R420), K525 (= K511)
2d1rA Crystal structure of the thermostable japanese firefly luciferase complexed with oxyluciferin and amp (see paper)
29% identity, 94% coverage: 23:518/530 of query aligns to 31:532/539 of 2d1rA
- active site: S194 (≠ T176), R214 (= R197), H241 (= H224), T339 (= T321), E340 (= E322), K439 (≠ I426), Q444 (≠ N431), K525 (= K511)
- binding adenosine monophosphate: S194 (≠ T176), S195 (= S177), H241 (= H224), G312 (≠ A295), A313 (= A296), P314 (= P297), G335 (≠ Q317), Y336 (= Y318), G337 (= G319), L338 (≠ M320), T339 (= T321), D418 (= D405), K525 (= K511)
- binding 2-(6-hydroxy-1,3-benzothiazol-2-yl)-1,3-thiazol-4(5h)-one: H241 (= H224), F243 (≠ G226), T247 (≠ W230), G335 (≠ Q317), G337 (= G319), L338 (≠ M320), A344 (≠ T326)
6q2mA Crystal structure of photinus pyralis luciferase pps6 mutant in complex with dlsa (see paper)
30% identity, 93% coverage: 25:518/530 of query aligns to 36:535/544 of 6q2mA
- active site: S197 (≠ T176), R217 (= R197), H244 (= H224), T342 (= T321), E343 (= E322), K442 (≠ I426), Q447 (≠ N431), K528 (= K511)
- binding (2S,5S)-hexane-2,5-diol: D186 (≠ I165), R187 (≠ Q166), R260 (≠ K240), Y279 (≠ D259)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S198 (= S177), H244 (= H224), F246 (≠ G226), T250 (≠ W230), G315 (≠ A295), A316 (= A296), P317 (= P297), G338 (≠ Q317), Y339 (= Y318), G340 (= G319), L341 (≠ M320), T342 (= T321), S346 (≠ G325), A347 (≠ T326), D421 (= D405), K528 (= K511)
Sites not aligning to the query:
5ie2A Crystal structure of a plant enzyme (see paper)
32% identity, 95% coverage: 11:515/530 of query aligns to 4:499/506 of 5ie2A
- active site: T165 (= T176), S185 (≠ A200), H209 (= H224), T310 (= T321), E311 (= E322), N410 (≠ I426), K415 (≠ N431), K495 (= K511)
- binding adenosine-5'-triphosphate: T165 (= T176), S166 (= S177), G167 (= G178), T168 (= T179), T169 (= T180), S284 (≠ A295), A285 (= A296), S286 (≠ P297), Y307 (= Y318), A308 (≠ G319), M309 (= M320), T310 (= T321), D389 (= D405), L401 (≠ I417), R404 (= R420), K495 (= K511)
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)
31% identity, 97% coverage: 11:523/530 of query aligns to 4:512/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 176:180) binding
- H214 (= H224) binding ; mutation to A: Abolished activity.
- S289 (≠ A295) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ AAP 295:297) binding
- EA 310:311 (≠ QQ 316:317) binding
- M314 (= M320) binding
- T315 (= T321) binding
- H319 (≠ G325) binding ; mutation to A: Abolished activity.
- D394 (= D405) binding
- R409 (= R420) binding ; mutation to A: Abolished activity.
- K500 (= K511) binding ; binding ; mutation to A: Abolished activity.
Query Sequence
>CCNA_01017 FitnessBrowser__Caulo:CCNA_01017
MSDAIDFDRMNTLGDVPRYHAEARPDAVAFSFEGRETTFAQLDRHTNQVANALLAAGLST
GDRIAYVGKNSDHYFELLLGAAKAGVVTTPIGWRLAAPEIAYIVGDSEAKLVFVGRELIG
HVDAVAAELTHRPVVIAMEAEGAGDYQTFEGWRDAASDVDPHKPIQISDIAIQLYTSGTT
GRPKGAMLTHHNLLGMRREAAKNPLEWNQWGPSDVSLVAMPVAHIGGTGWGLVGLINGAK
GVVAREFDPTKVLDFIEKDRISKMFMVPAALQIVVRLPRAREVDYSRLTHILYGAAPIPL
DLLRECMEVFGCGFVQQYGMTETTGTVVYLPPEDHDPAGNKRMRAAGLPMPGVELKIIDE
AGKSLPPNTVGEVAVRSSANMAGYWKLDEATAKTMDADGWLRTGDAGYLDEDGYLFIHDR
VKDMIISGGENIYPAEVESAVYGHPHVAEVAVIGVPDDKWGEAVKAVVAPKPGVTPDADD
IIAFARTRIAHFKAPKSVDFIPALPRNASGKILRRELRAPYWEGRERQVN
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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