SitesBLAST
Comparing WP_066607782.1 NCBI__GCF_001046645.1:WP_066607782.1 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)
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
33% identity, 91% coverage: 39:545/556 of query aligns to 27:484/486 of 8wevA
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)
29% identity, 95% coverage: 17:545/556 of query aligns to 38:570/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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, 92% coverage: 39:552/556 of query aligns to 61:554/556 of Q9S725
- K211 (= K215) mutation to S: Drastically reduces the activity.
- M293 (= M292) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ N321) mutation K->L,A: Affects the substrate specificity.
- E401 (= E400) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ L402) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R448) mutation to Q: Drastically reduces the activity.
- K457 (≠ G456) mutation to S: Drastically reduces the activity.
- K540 (= K538) mutation to N: Abolishes the activity.
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)
31% identity, 91% coverage: 41:545/556 of query aligns to 29:494/503 of P9WQ37
- K172 (= K215) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R233) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R235) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I253) 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 (= A255) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ C258) 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 (= R288) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G349) 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 (= W428) 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 (= D433) 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 (= R448) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V455) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G457) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K538) 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)
31% identity, 91% coverage: 41:545/556 of query aligns to 32:494/502 of 3r44A
Sites not aligning to the query:
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, 93% coverage: 39:556/556 of query aligns to 57:553/559 of Q67W82
- G395 (= G399) 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)
29% identity, 91% coverage: 39:545/556 of query aligns to 43:526/528 of 3ni2A
- active site: S182 (≠ T207), S202 (vs. gap), H230 (= H252), T329 (= T351), E330 (= E352), K434 (= K454), Q439 (≠ N459), K519 (= K538)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ A254), S236 (≠ L257), G302 (≠ F324), A303 (= A325), P304 (≠ F326), G325 (≠ T347), G327 (= G349), T329 (= T351), P333 (= P362), V334 (≠ A363), D413 (= D433), K430 (= K450), K434 (= K454), Q439 (≠ N459)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
29% identity, 91% coverage: 39:545/556 of query aligns to 43:526/528 of 3a9vA
- active site: S182 (≠ T207), S202 (vs. gap), H230 (= H252), T329 (= T351), E330 (= E352), K434 (= K454), Q439 (≠ N459), K519 (= K538)
- binding adenosine monophosphate: H230 (= H252), G302 (≠ F324), A303 (= A325), P304 (≠ F326), Y326 (≠ M348), G327 (= G349), M328 (= M350), T329 (= T351), D413 (= D433), K430 (= K450), K434 (= K454), Q439 (≠ N459)
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)
29% identity, 91% coverage: 43:548/556 of query aligns to 54:536/542 of O24146
- S189 (≠ T207) binding ATP
- S190 (= S208) binding ATP
- G191 (= G209) binding ATP
- T192 (= T210) binding ATP
- T193 (≠ S211) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K215) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H252) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ A254) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ L257) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ H274) binding CoA
- A309 (≠ F324) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ G346) binding ATP
- G332 (≠ T347) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T351) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ A363) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ P366) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D433) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R448) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding ATP; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K450) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (= K454) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G456) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G457) binding CoA
- Q446 (≠ N459) binding AMP
- K526 (= K538) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
29% identity, 91% coverage: 43:548/556 of query aligns to 47:529/530 of 5bsmA
- active site: S182 (≠ T207), S202 (≠ N230), H230 (= H252), T329 (= T351), E330 (= E352), K434 (= K454), Q439 (≠ N459), K519 (= K538)
- binding adenosine-5'-triphosphate: S182 (≠ T207), S183 (= S208), G184 (= G209), T185 (= T210), T186 (≠ S211), K190 (= K215), H230 (= H252), A302 (≠ F324), A303 (= A325), P304 (≠ F326), Y326 (≠ M348), G327 (= G349), M328 (= M350), T329 (= T351), D413 (= D433), I425 (≠ F445), R428 (= R448), K519 (= K538)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
29% identity, 91% coverage: 43:548/556 of query aligns to 47:529/529 of 5bsvA
- active site: S182 (≠ T207), S202 (≠ N230), H230 (= H252), T329 (= T351), E330 (= E352), K434 (= K454), Q439 (≠ N459), K519 (= K538)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H252), Y232 (≠ A254), S236 (≠ L257), A302 (≠ F324), A303 (= A325), P304 (≠ F326), G325 (≠ T347), G327 (= G349), M328 (= M350), T329 (= T351), P333 (= P362), V334 (≠ A363), D413 (= D433), K430 (= K450), K434 (= K454), Q439 (≠ N459)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
29% identity, 91% coverage: 43:548/556 of query aligns to 47:529/529 of 5bsuA
- active site: S182 (≠ T207), S202 (≠ N230), H230 (= H252), T329 (= T351), E330 (= E352), K434 (= K454), Q439 (≠ N459), K519 (= K538)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H252), Y232 (≠ A254), S236 (≠ L257), M299 (≠ N321), A302 (≠ F324), A303 (= A325), P304 (≠ F326), G325 (≠ T347), G327 (= G349), M328 (= M350), T329 (= T351), P333 (= P362), D413 (= D433), K430 (= K450), K434 (= K454), Q439 (≠ N459)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
29% identity, 91% coverage: 43:548/556 of query aligns to 47:529/529 of 5bstA
- active site: S182 (≠ T207), S202 (≠ N230), H230 (= H252), T329 (= T351), E330 (= E352), K434 (= K454), Q439 (≠ N459), K519 (= K538)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H252), Y232 (≠ A254), S236 (≠ L257), A302 (≠ F324), A303 (= A325), P304 (≠ F326), G325 (≠ T347), Y326 (≠ M348), G327 (= G349), M328 (= M350), T329 (= T351), P333 (= P362), V334 (≠ A363), D413 (= D433), K430 (= K450), K434 (= K454), Q439 (≠ N459)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
29% identity, 91% coverage: 43:548/556 of query aligns to 46:528/528 of 5bsrA
- active site: S181 (≠ T207), S201 (≠ N230), H229 (= H252), T328 (= T351), E329 (= E352), K433 (= K454), Q438 (≠ N459), K518 (= K538)
- binding adenosine monophosphate: A301 (≠ F324), G326 (= G349), T328 (= T351), D412 (= D433), K429 (= K450), K433 (= K454), Q438 (≠ N459)
- binding coenzyme a: L102 (≠ R99), P226 (= P249), H229 (= H252), Y231 (≠ A254), F253 (= F275), K435 (≠ G456), G436 (= G457), F437 (≠ E458), F498 (≠ S519)
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, 90% coverage: 43:541/556 of query aligns to 29:497/512 of O74976
- S283 (≠ F324) modified: Phosphoserine
- S284 (≠ A325) modified: Phosphoserine
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
28% identity, 92% coverage: 39:550/556 of query aligns to 26:503/506 of 4gxqA
- active site: T163 (= T207), N183 (≠ E227), H207 (= H252), T303 (= T351), E304 (= E352), I403 (≠ K454), N408 (= N459), A491 (≠ K538)
- binding adenosine-5'-triphosphate: T163 (= T207), S164 (= S208), G165 (= G209), T166 (= T210), T167 (≠ S211), H207 (= H252), S277 (≠ F324), A278 (= A325), P279 (≠ F326), E298 (≠ G346), M302 (= M350), T303 (= T351), D382 (= D433), R397 (= R448)
- binding carbonate ion: H207 (= H252), S277 (≠ F324), R299 (≠ T347), G301 (= G349)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
29% identity, 91% coverage: 43:548/556 of query aligns to 46:525/527 of 5u95B
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
28% identity, 92% coverage: 40:548/556 of query aligns to 47:537/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H252), F245 (≠ A254), T249 (≠ C258), G314 (≠ F324), A315 (= A325), P316 (≠ F326), G337 (≠ T347), Y338 (≠ M348), G339 (= G349), L340 (≠ M350), T341 (= T351), A346 (vs. gap), D420 (= D433), I432 (≠ F445), K527 (= K538)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
28% identity, 92% coverage: 40:548/556 of query aligns to 47:537/539 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 (= H252), F245 (≠ A254), T249 (≠ C258), G314 (≠ F324), A315 (= A325), P316 (≠ F326), G337 (≠ T347), Y338 (≠ M348), G339 (= G349), L340 (≠ M350), T341 (= T351), S345 (≠ G355), A346 (vs. gap), D420 (= D433), I432 (≠ F445), K527 (= K538)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ A254), R335 (≠ L343), G337 (≠ T347), G339 (= G349), L340 (≠ M350), A346 (vs. gap)
5wm4A Crystal structure of cahj in complex with 6-methylsalicyl adenylate (see paper)
29% identity, 92% coverage: 39:547/556 of query aligns to 51:532/534 of 5wm4A
- active site: S193 (≠ T207), N213 (≠ E227), H237 (= H252), A336 (≠ T351), E337 (= E352), N437 (≠ K454), K442 (≠ N459), K521 (≠ A536)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxy-6-methylbenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: N238 (≠ I253), F239 (≠ A254), C243 (= C258), G309 (≠ S322), G310 (≠ C323), S311 (≠ F324), K312 (≠ A325), V332 (= V345), F333 (≠ M348), G334 (= G349), M335 (= M350), A336 (≠ T351), L340 (≠ V357), D416 (= D433), K433 (= K450), K442 (≠ N459)
- binding magnesium ion: M453 (≠ A470), H455 (= H472), V458 (= V475)
Query Sequence
>WP_066607782.1 NCBI__GCF_001046645.1:WP_066607782.1
MGIKGEDSAAIRITATTLGDLLLAGWDKGRGKDALVFPGERKSYDDLVASVLRRARGLKA
LGIGRGDHVGILLPSSIEFVETLFANAMCGAVSVLMNARYKAPEMAYVAQNADLRAIVTN
DLISEHVDFGARLTEAFPDLSSAVDPAALTLAETPLLRQIIMLGGRSAPGFIDQAMFDAA
ADGVSEMDIHDARLTVRVRDTAMILYTSGTSANPKGCLLSHEAVTREANNLARYRWGFQP
DERAWSPLPLFHIAAMLCMLGAMDVGGTFIGQPHFDAGESLRQIEAERVTMMFLPFVTFH
QAMIAHPDWDKTDMSSVRLQNSCFAFMPDRVGRAYRDKAPNMLQVGTMGMTEATGIVTTG
GPAMDPEMGFRKLGYPLAGIEMKIIDPDTGVERGVDERGEILIRGYNLFDGYYRDPEKTA
EAIDPDGWYHSADIGSIDAEGHVMFHGRFKDMLKVGGENVAAAEVEAVLASHPAVRLAQV
VGLPDDRLAEIPAAYIECDGDVSVEPDELIAYTKARLASFKVPRHIRFVDEWPMSASKIQ
KFKLRAALMDELGLND
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