SitesBLAST
Comparing CCNA_03292 FitnessBrowser__Caulo:CCNA_03292 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)
30% identity, 97% coverage: 13:512/517 of query aligns to 3:498/503 of P9WQ37
- R9 (= R19) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (= R28) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K180) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ G202) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ T204) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ N216) 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 (≠ T218) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ C221) 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 (= R251) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G310) 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 (= W388) 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 (= D395) 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 (= R410) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S417) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G419) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K501) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
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, 92% coverage: 34:508/517 of query aligns to 55:542/559 of Q67W82
- G395 (= G357) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
31% identity, 92% coverage: 35:510/517 of query aligns to 42:528/528 of 3ni2A
- active site: S182 (= S172), S202 (≠ H192), H230 (≠ S215), T329 (= T312), E330 (= E313), K434 (≠ I416), Q439 (≠ N421), K519 (= K501)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (vs. gap), S236 (≠ T217), G302 (≠ S286), A303 (= A287), P304 (= P288), G325 (≠ Y308), G327 (= G310), T329 (= T312), P333 (vs. gap), V334 (vs. gap), D413 (≠ T393), K430 (= K412), K434 (≠ I416), Q439 (≠ N421)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
31% identity, 92% coverage: 35:510/517 of query aligns to 42:528/528 of 3a9vA
- active site: S182 (= S172), S202 (≠ H192), H230 (≠ S215), T329 (= T312), E330 (= E313), K434 (≠ I416), Q439 (≠ N421), K519 (= K501)
- binding adenosine monophosphate: H230 (≠ S215), G302 (≠ S286), A303 (= A287), P304 (= P288), Y326 (≠ F309), G327 (= G310), M328 (= M311), T329 (= T312), D413 (≠ T393), K430 (= K412), K434 (≠ I416), Q439 (≠ N421)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
30% identity, 97% coverage: 13:512/517 of query aligns to 6:498/502 of 3r44A
Sites not aligning to the query:
O24146 4-coumarate--CoA ligase 2; 4CL 2; Nt4CL-19; Nt4CL-2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; Cinnamate--CoA ligase; Ferulate--CoA ligase; EC 6.2.1.12; EC 6.2.1.-; EC 6.2.1.-; EC 6.2.1.34 from Nicotiana tabacum (Common tobacco) (see paper)
30% identity, 91% coverage: 40:508/517 of query aligns to 54:533/542 of O24146
- S189 (= S172) binding
- S190 (= S173) binding
- G191 (= G174) binding
- T192 (= T175) binding
- T193 (= T176) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K180) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (≠ S215) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (vs. gap) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ T217) binding ; binding ; binding
- K260 (= K237) binding
- A309 (≠ S286) binding ; binding ; binding
- Q331 (≠ E307) binding
- G332 (≠ Y308) binding ; binding ; binding ; binding ; binding
- T336 (= T312) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (vs. gap) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ T317) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (≠ T393) binding ; binding ; binding ; binding ; binding
- R435 (= R410) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K412) binding ; binding ; binding ; binding
- K441 (≠ I416) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G418) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G419) binding
- Q446 (≠ N421) binding
- K526 (= K501) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
30% identity, 91% coverage: 40:508/517 of query aligns to 47:526/530 of 5bsmA
- active site: S182 (= S172), S202 (vs. gap), H230 (≠ S215), T329 (= T312), E330 (= E313), K434 (≠ I416), Q439 (≠ N421), K519 (= K501)
- binding adenosine-5'-triphosphate: S182 (= S172), S183 (= S173), G184 (= G174), T185 (= T175), T186 (= T176), K190 (= K180), H230 (≠ S215), A302 (≠ S286), A303 (= A287), P304 (= P288), Y326 (≠ F309), G327 (= G310), M328 (= M311), T329 (= T312), D413 (≠ T393), I425 (≠ L405), R428 (= R410), K519 (= K501)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 91% coverage: 40:508/517 of query aligns to 46:525/528 of 5bsrA
- active site: S181 (= S172), S201 (vs. gap), H229 (≠ S215), T328 (= T312), E329 (= E313), K433 (≠ I416), Q438 (≠ N421), K518 (= K501)
- binding adenosine monophosphate: A301 (≠ S286), G326 (= G310), T328 (= T312), D412 (≠ T393), K429 (= K412), K433 (≠ I416), Q438 (≠ N421)
- binding coenzyme a: L102 (≠ S96), P226 (= P212), H229 (≠ S215), Y231 (vs. gap), F253 (= F238), K435 (≠ G418), G436 (= G419), F437 (= F420), F498 (≠ K481)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 91% coverage: 40:508/517 of query aligns to 47:526/529 of 5bsvA
- active site: S182 (= S172), S202 (vs. gap), H230 (≠ S215), T329 (= T312), E330 (= E313), K434 (≠ I416), Q439 (≠ N421), K519 (= K501)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (≠ S215), Y232 (vs. gap), S236 (≠ T217), A302 (≠ S286), A303 (= A287), P304 (= P288), G325 (≠ Y308), G327 (= G310), M328 (= M311), T329 (= T312), P333 (vs. gap), V334 (vs. gap), D413 (≠ T393), K430 (= K412), K434 (≠ I416), Q439 (≠ N421)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 91% coverage: 40:508/517 of query aligns to 47:526/529 of 5bsuA
- active site: S182 (= S172), S202 (vs. gap), H230 (≠ S215), T329 (= T312), E330 (= E313), K434 (≠ I416), Q439 (≠ N421), K519 (= K501)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (≠ S215), Y232 (vs. gap), S236 (≠ T217), M299 (≠ F283), A302 (≠ S286), A303 (= A287), P304 (= P288), G325 (≠ Y308), G327 (= G310), M328 (= M311), T329 (= T312), P333 (vs. gap), D413 (≠ T393), K430 (= K412), K434 (≠ I416), Q439 (≠ N421)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
30% identity, 91% coverage: 40:508/517 of query aligns to 47:526/529 of 5bstA
- active site: S182 (= S172), S202 (vs. gap), H230 (≠ S215), T329 (= T312), E330 (= E313), K434 (≠ I416), Q439 (≠ N421), K519 (= K501)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (≠ S215), Y232 (vs. gap), S236 (≠ T217), A302 (≠ S286), A303 (= A287), P304 (= P288), G325 (≠ Y308), Y326 (≠ F309), G327 (= G310), M328 (= M311), T329 (= T312), P333 (vs. gap), V334 (vs. gap), D413 (≠ T393), K430 (= K412), K434 (≠ I416), Q439 (≠ N421)
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, 97% coverage: 11:510/517 of query aligns to 22:552/561 of P69451
- Y213 (= Y171) mutation to A: Loss of activity.
- T214 (≠ S172) mutation to A: 10% of wild-type activity.
- G216 (= G174) mutation to A: Decreases activity.
- T217 (= T175) mutation to A: Decreases activity.
- G219 (= G177) mutation to A: Decreases activity.
- K222 (= K180) mutation to A: Decreases activity.
- E361 (= E313) mutation to A: Loss of activity.
5wm6A Crystal structure of cahj in complex with benzoyl adenylate (see paper)
32% identity, 95% coverage: 17:507/517 of query aligns to 32:530/535 of 5wm6A
- active site: S193 (= S172), N213 (≠ H192), H237 (≠ S215), A336 (≠ T312), E337 (= E313), N437 (≠ I416), K442 (≠ N421), K524 (= K501)
- binding magnesium ion: S301 (= S277), L303 (≠ T279), G326 (≠ P302)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: F239 (≠ T217), G310 (≠ S286), S311 (≠ A287), K312 (≠ P288), V332 (≠ Y308), F333 (= F309), G334 (= G310), M335 (= M311), A336 (≠ T312), D416 (= D395), K433 (= K412), K442 (≠ N421)
5wm3A Crystal structure of cahj in complex with salicyl adenylate (see paper)
32% identity, 95% coverage: 17:507/517 of query aligns to 32:530/537 of 5wm3A
- active site: S193 (= S172), N213 (≠ H192), H237 (≠ S215), A336 (≠ T312), E337 (= E313), N437 (≠ I416), K442 (≠ N421), K524 (= K501)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxybenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: N238 (= N216), F239 (≠ T217), G310 (≠ S286), S311 (≠ A287), K312 (≠ P288), V332 (≠ Y308), F333 (= F309), G334 (= G310), M335 (= M311), A336 (≠ T312), D416 (= D395), K433 (= K412), K442 (≠ N421)
- binding magnesium ion: S301 (= S277), L303 (≠ T279), G326 (≠ P302)
5wm2A Crystal structure of cahj in complex with salicylic acid and amp (see paper)
32% identity, 95% coverage: 17:507/517 of query aligns to 32:530/536 of 5wm2A
- active site: S193 (= S172), N213 (≠ H192), H237 (≠ S215), A336 (≠ T312), E337 (= E313), N437 (≠ I416), K442 (≠ N421), K524 (= K501)
- binding adenosine monophosphate: G310 (≠ S286), S311 (≠ A287), K312 (≠ P288), V332 (≠ Y308), F333 (= F309), G334 (= G310), M335 (= M311), A336 (≠ T312), E337 (= E313), D416 (= D395), V428 (≠ L407), K433 (= K412), K442 (≠ N421)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
27% identity, 92% coverage: 35:512/517 of query aligns to 45:538/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (≠ S215), F245 (≠ T217), T249 (≠ C221), G314 (≠ S286), A315 (= A287), P316 (= P288), G337 (≠ Y308), Y338 (≠ F309), G339 (= G310), L340 (≠ M311), T341 (= T312), A346 (≠ C318), D420 (= D395), I432 (≠ L407), K527 (= K501)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
27% identity, 92% coverage: 35:512/517 of query aligns to 45:538/539 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 (≠ S215), F245 (≠ T217), T249 (≠ C221), G314 (≠ S286), A315 (= A287), P316 (= P288), G337 (≠ Y308), Y338 (≠ F309), G339 (= G310), L340 (≠ M311), T341 (= T312), S345 (≠ T317), A346 (≠ C318), D420 (= D395), I432 (≠ L407), K527 (= K501)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ T217), R335 (≠ V306), G337 (≠ Y308), G339 (= G310), L340 (≠ M311), A346 (≠ C318)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 95% coverage: 24:513/517 of query aligns to 14:503/506 of 4gxqA
- active site: T163 (≠ S172), N183 (≠ K191), H207 (vs. gap), T303 (= T312), E304 (= E313), I403 (= I416), N408 (= N421), A491 (≠ K501)
- binding adenosine-5'-triphosphate: T163 (≠ S172), S164 (= S173), G165 (= G174), T166 (= T175), T167 (= T176), H207 (vs. gap), S277 (= S286), A278 (= A287), P279 (= P288), E298 (= E307), M302 (= M311), T303 (= T312), D382 (= D395), R397 (= R410)
- binding carbonate ion: H207 (vs. gap), S277 (= S286), R299 (≠ Y308), G301 (= G310)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
31% identity, 91% coverage: 40:508/517 of query aligns to 46:522/527 of 5u95B
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)
30% identity, 93% coverage: 35:513/517 of query aligns to 60:552/556 of Q9S725
- K211 (= K180) mutation to S: Drastically reduces the activity.
- M293 (= M256) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ F283) mutation K->L,A: Affects the substrate specificity.
- E401 (= E358) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ V360) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R410) mutation to Q: Drastically reduces the activity.
- K457 (≠ G418) mutation to S: Drastically reduces the activity.
- K540 (= K501) mutation to N: Abolishes the activity.
Query Sequence
>CCNA_03292 FitnessBrowser__Caulo:CCNA_03292
MTLAAMIAADYGTIGDILRERARENPDRLAVVMETGEAVTYAQFDALVDRVAAALQRDGV
APGEAVAVCALSSIPYAALFLGALRAGVAVAPIAPSSTPESIAGMVADCGAKLFFLDAGV
AEAQKPAPVPVRPIALDGSSAGQAFDAWLAPEDATPTPVEIGPKHPFNIIYSSGTTGTPK
GIIQSHGMRWKHIFVGDAIGYGHTPVSLLSTPLYSNTTLVCFFPTLAGGGTVVLMKKFDV
VRYLELAAKHRITHTMLVPVQYRRLMEHPDFDRYDLSSTRMKFCTSAPFAADLKAQVLKR
WPGGLVEYFGMTEGGGTCILMAHEHPDKLHTVGRPAPGHDIRLVDEDGRQVGPGVVGEIV
GRSASMMNGYHGRPDKTAEATWVSPEGWTFIRTGDVGRFDEEGFLTLMDRKKDMIISGGF
NIYPSDLEAVLVQHPAVFEAAVVGVPSDAWGETPVAFVALKSSQVAEADAIKTFVNGQVG
KTQRLAEVVVVDSLPRSHIGKVLKRELRDSWQNSPSQ
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