SitesBLAST
Comparing WP_057687528.1 NCBI__GCF_001431535.1:WP_057687528.1 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)
59% identity, 99% coverage: 3:554/558 of query aligns to 1:551/561 of P69451
- Y213 (= Y214) mutation to A: Loss of activity.
- T214 (= T215) mutation to A: 10% of wild-type activity.
- G216 (= G217) mutation to A: Decreases activity.
- T217 (= T218) mutation to A: Decreases activity.
- G219 (= G220) mutation to A: Decreases activity.
- K222 (= K223) mutation to A: Decreases activity.
- E361 (= E363) mutation to A: Loss of 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)
32% identity, 90% coverage: 51:554/558 of query aligns to 30:495/503 of P9WQ37
- K172 (= K223) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ G251) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ K252) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I264) 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 (= A266) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ A269) 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 (≠ F302) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G360) 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 (= W436) 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 (= D441) 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 (= R456) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V463) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G465) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K546) 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.
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)
28% identity, 93% coverage: 34:552/558 of query aligns to 39:536/546 of Q84P21
- K530 (= K546) mutation to N: Lossed enzymatic activity.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
32% identity, 90% coverage: 51:554/558 of query aligns to 33:495/502 of 3r44A
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, 91% coverage: 48:553/558 of query aligns to 62:570/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
30% identity, 90% coverage: 51:553/558 of query aligns to 49:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H263), F245 (= F265), T249 (≠ A269), G314 (= G336), A315 (≠ M337), P316 (≠ A338), G337 (≠ A358), Y338 (= Y359), G339 (= G360), L340 (= L361), T341 (= T362), A346 (= A367), D420 (= D441), I432 (= I453), K527 (= K546)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
30% identity, 90% coverage: 51:553/558 of query aligns to 49:534/539 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 (= H263), F245 (= F265), T249 (≠ A269), G314 (= G336), A315 (≠ M337), P316 (≠ A338), G337 (≠ A358), Y338 (= Y359), G339 (= G360), L340 (= L361), T341 (= T362), S345 (≠ P366), A346 (= A367), D420 (= D441), I432 (= I453), K527 (= K546)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F265), R335 (≠ V356), G337 (≠ A358), G339 (= G360), L340 (= L361), A346 (= A367)
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)
29% identity, 91% coverage: 48:553/558 of query aligns to 57:542/559 of Q67W82
- G395 (= G407) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
29% identity, 91% coverage: 45:554/558 of query aligns to 23:499/506 of 4gxqA
- active site: T163 (= T215), N183 (= N235), H207 (= H263), T303 (= T362), E304 (= E363), I403 (≠ L462), N408 (= N467), A491 (≠ K546)
- binding adenosine-5'-triphosphate: T163 (= T215), S164 (≠ G216), G165 (= G217), T166 (= T218), T167 (= T219), H207 (= H263), S277 (≠ G336), A278 (≠ M337), P279 (≠ A338), E298 (= E357), M302 (≠ L361), T303 (= T362), D382 (= D441), R397 (= R456)
- binding carbonate ion: H207 (= H263), S277 (≠ G336), R299 (≠ A358), G301 (= G360)
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)
28% identity, 93% coverage: 34:553/558 of query aligns to 34:533/542 of O24146
- S189 (≠ T215) binding
- S190 (≠ G216) binding
- G191 (= G217) binding
- T192 (= T218) binding
- T193 (= T219) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K223) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H263) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F265) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ A269) binding ; binding ; binding
- K260 (≠ P287) binding
- A309 (≠ G336) binding ; binding ; binding
- Q331 (≠ E357) binding
- G332 (≠ A358) binding ; binding ; binding ; binding ; binding
- T336 (= T362) 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 (≠ A368) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D441) binding ; binding ; binding ; binding ; binding
- R435 (= R456) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K458) binding ; binding ; binding ; binding
- K441 (≠ L462) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S464) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G465) binding
- Q446 (≠ N467) binding
- K526 (= K546) 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)
28% identity, 93% coverage: 34:553/558 of query aligns to 27:526/530 of 5bsmA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H263), T329 (= T362), E330 (= E363), K434 (≠ L462), Q439 (≠ N467), K519 (= K546)
- binding adenosine-5'-triphosphate: S182 (≠ T215), S183 (≠ G216), G184 (= G217), T185 (= T218), T186 (= T219), K190 (= K223), H230 (= H263), A302 (≠ G336), A303 (≠ M337), P304 (≠ A338), Y326 (= Y359), G327 (= G360), M328 (≠ L361), T329 (= T362), D413 (= D441), I425 (= I453), R428 (= R456), K519 (= K546)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
28% identity, 93% coverage: 34:553/558 of query aligns to 26:525/528 of 5bsrA
- active site: S181 (≠ T215), S201 (≠ N235), H229 (= H263), T328 (= T362), E329 (= E363), K433 (≠ L462), Q438 (≠ N467), K518 (= K546)
- binding adenosine monophosphate: A301 (≠ G336), G326 (= G360), T328 (= T362), D412 (= D441), K429 (= K458), K433 (≠ L462), Q438 (≠ N467)
- binding coenzyme a: L102 (= L109), P226 (= P260), H229 (= H263), Y231 (≠ F265), F253 (≠ R288), K435 (≠ S464), G436 (= G465), F437 (= F466), F498 (≠ G526)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
28% identity, 93% coverage: 34:553/558 of query aligns to 27:526/529 of 5bsvA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H263), T329 (= T362), E330 (= E363), K434 (≠ L462), Q439 (≠ N467), K519 (= K546)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H263), Y232 (≠ F265), S236 (≠ A269), A302 (≠ G336), A303 (≠ M337), P304 (≠ A338), G325 (≠ A358), G327 (= G360), M328 (≠ L361), T329 (= T362), P333 (= P366), V334 (vs. gap), D413 (= D441), K430 (= K458), K434 (≠ L462), Q439 (≠ N467)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
28% identity, 93% coverage: 34:553/558 of query aligns to 27:526/529 of 5bsuA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H263), T329 (= T362), E330 (= E363), K434 (≠ L462), Q439 (≠ N467), K519 (= K546)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H263), Y232 (≠ F265), S236 (≠ A269), M299 (≠ L333), A302 (≠ G336), A303 (≠ M337), P304 (≠ A338), G325 (≠ A358), G327 (= G360), M328 (≠ L361), T329 (= T362), P333 (= P366), D413 (= D441), K430 (= K458), K434 (≠ L462), Q439 (≠ N467)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
28% identity, 93% coverage: 34:553/558 of query aligns to 27:526/529 of 5bstA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H263), T329 (= T362), E330 (= E363), K434 (≠ L462), Q439 (≠ N467), K519 (= K546)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H263), Y232 (≠ F265), S236 (≠ A269), A302 (≠ G336), A303 (≠ M337), P304 (≠ A338), G325 (≠ A358), Y326 (= Y359), G327 (= G360), M328 (≠ L361), T329 (= T362), P333 (= P366), V334 (vs. gap), D413 (= D441), K430 (= K458), K434 (≠ L462), Q439 (≠ N467)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
27% identity, 91% coverage: 48:554/558 of query aligns to 43:527/528 of 3ni2A
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H263), T329 (= T362), E330 (= E363), K434 (≠ L462), Q439 (≠ N467), K519 (= K546)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F265), S236 (≠ A269), G302 (= G336), A303 (≠ M337), P304 (≠ A338), G325 (≠ A358), G327 (= G360), T329 (= T362), P333 (= P366), V334 (vs. gap), D413 (= D441), K430 (= K458), K434 (≠ L462), Q439 (≠ N467)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
27% identity, 91% coverage: 48:554/558 of query aligns to 43:527/528 of 3a9vA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H263), T329 (= T362), E330 (= E363), K434 (≠ L462), Q439 (≠ N467), K519 (= K546)
- binding adenosine monophosphate: H230 (= H263), G302 (= G336), A303 (≠ M337), P304 (≠ A338), Y326 (= Y359), G327 (= G360), M328 (≠ L361), T329 (= T362), D413 (= D441), K430 (= K458), K434 (≠ L462), Q439 (≠ N467)
Q17577 Acyl-CoA synthetase 7; EC 6.2.1.- from Caenorhabditis elegans (see paper)
29% identity, 86% coverage: 74:555/558 of query aligns to 68:531/540 of Q17577
- SS 186:187 (≠ TG 215:216) mutation to AA: Loss of catalytic activity; when associated with A-339.
- E339 (= E363) mutation to A: Severe loss of catalytic activity. Loss of catalytic activity; when associated with 186-A-A-187.
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)
27% identity, 91% coverage: 48:553/558 of query aligns to 61:547/556 of Q9S725
- K211 (= K223) mutation to S: Drastically reduces the activity.
- M293 (≠ T306) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ L333) mutation K->L,A: Affects the substrate specificity.
- E401 (= E408) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C410) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R456) mutation to Q: Drastically reduces the activity.
- K457 (≠ S464) mutation to S: Drastically reduces the activity.
- K540 (= K546) mutation to N: Abolishes the activity.
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
30% identity, 93% coverage: 37:554/558 of query aligns to 25:533/539 of 2d1sA
- active site: S194 (≠ T215), R214 (≠ N235), H241 (= H263), T339 (= T362), E340 (= E363), K439 (≠ L462), Q444 (≠ N467), K525 (= K546)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S194 (≠ T215), S195 (≠ G216), H241 (= H263), F243 (= F265), T247 (= T268), I282 (≠ T306), G312 (= G336), A313 (≠ M337), P314 (≠ A338), Q334 (≠ E357), G335 (≠ A358), Y336 (= Y359), G337 (= G360), L338 (= L361), T339 (= T362), S343 (≠ P366), A344 (= A367), D418 (= D441), R433 (= R456), K525 (= K546)
Query Sequence
>WP_057687528.1 NCBI__GCF_001431535.1:WP_057687528.1
MSLERPWLQSYPQGVPAEIDINEFHSVSSVFDASVAKYRDRPAYSSFGKVLTYGETDALV
EQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTARELKHQLV
DAGVTALVVVDNFGDTVQAVIADTQVKHVITTGLGDLLGAKGVVVNFVLKYIKKMVPNYT
LKGAVRFTQALKLGRRHDLPKVEIDHDDIAFLQYTGGTTGVAKGAMLTNRNLVANMQQAS
AWIGASGIEPGKEWIITALPLYHIFALTANGLVFMKFGGCNHLITNPRDMKGFVKELKGV
RFTAITGVNTLFNGLLNTPGFDEVDFSTLKVTLGGGMAVQRSVAERWKKTTGVTLVEAYG
LTETSPAACINPLTLAEYNGSIGLPIPSTDACIKDDSGKVLGLDEVGELCIKGPQVMKGY
WQRPEDTAAAIDADGWLHTGDMAKMDAQGFCYIVDRKKDMILVSGFNVYPNEVEDVIAMM
PGVLEVAAVGVPDEKSGEIVKVVIVKKDPNLTAEQVKEHARANLTGYKHPKIVEFRKELP
KTNVGKILRRELRDAPPA
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