SitesBLAST
Comparing WP_011384981.1 NCBI__GCF_000009985.1:WP_011384981.1 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)
33% identity, 94% coverage: 28:511/517 of query aligns to 14:503/506 of 4gxqA
- active site: T163 (= T171), N183 (≠ I191), H207 (= H215), T303 (= T314), E304 (= E315), I403 (= I414), N408 (= N419), A491 (≠ K499)
- binding adenosine-5'-triphosphate: T163 (= T171), S164 (= S172), G165 (= G173), T166 (= T174), T167 (= T175), H207 (= H215), S277 (≠ G288), A278 (≠ S289), P279 (= P290), E298 (≠ N309), M302 (≠ L313), T303 (= T314), D382 (= D393), R397 (= R408)
- binding carbonate ion: H207 (= H215), S277 (≠ G288), R299 (≠ G310), G301 (= G312)
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)
31% identity, 98% coverage: 5:510/517 of query aligns to 11:554/561 of P69451
- Y213 (= Y170) mutation to A: Loss of activity.
- T214 (= T171) mutation to A: 10% of wild-type activity.
- G216 (= G173) mutation to A: Decreases activity.
- T217 (= T174) mutation to A: Decreases activity.
- G219 (= G176) mutation to A: Decreases activity.
- K222 (= K179) mutation to A: Decreases activity.
- E361 (= E315) mutation to A: Loss of activity.
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, 92% coverage: 40:513/517 of query aligns to 59:544/546 of Q84P21
- K530 (= K499) mutation to N: Lossed enzymatic 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)
32% identity, 92% coverage: 30:505/517 of query aligns to 49:541/559 of Q67W82
- G395 (= G359) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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: 30:505/517 of query aligns to 53:546/556 of Q9S725
- K211 (= K179) mutation to S: Drastically reduces the activity.
- M293 (≠ N256) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ S285) mutation K->L,A: Affects the substrate specificity.
- E401 (= E360) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ W362) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R408) mutation to Q: Drastically reduces the activity.
- K457 (≠ S416) mutation to S: Drastically reduces the activity.
- K540 (= K499) 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, 95% coverage: 18:507/517 of query aligns to 7:495/503 of P9WQ37
- R9 (= R20) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D28) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K179) 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 (≠ G204) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V216) 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 (≠ G218) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ S221) 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 (≠ G251) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G312) 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 (= D393) 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 (= R408) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R415) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G417) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K499) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
37% identity, 66% coverage: 165:507/517 of query aligns to 176:527/528 of 3ni2A
- active site: S182 (≠ T171), S202 (≠ I191), H230 (= H215), T329 (= T314), E330 (= E315), K434 (≠ I414), Q439 (≠ N419), K519 (= K499)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F217), S236 (= S221), G302 (= G288), A303 (≠ S289), P304 (= P290), G325 (= G310), G327 (= G312), T329 (= T314), P333 (= P318), V334 (≠ T319), D413 (= D393), K430 (= K410), K434 (≠ I414), Q439 (≠ N419)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
37% identity, 66% coverage: 165:507/517 of query aligns to 176:527/528 of 3a9vA
- active site: S182 (≠ T171), S202 (≠ I191), H230 (= H215), T329 (= T314), E330 (= E315), K434 (≠ I414), Q439 (≠ N419), K519 (= K499)
- binding adenosine monophosphate: H230 (= H215), G302 (= G288), A303 (≠ S289), P304 (= P290), Y326 (= Y311), G327 (= G312), M328 (≠ L313), T329 (= T314), D413 (= D393), K430 (= K410), K434 (≠ I414), Q439 (≠ N419)
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)
28% identity, 92% coverage: 40:513/517 of query aligns to 29:508/512 of O74976
- S283 (≠ G288) modified: Phosphoserine
- S284 (= S289) modified: Phosphoserine
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
29% identity, 91% coverage: 36:507/517 of query aligns to 46:535/539 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 (= H215), F245 (= F217), T249 (≠ S221), G314 (= G288), A315 (≠ S289), P316 (= P290), G337 (= G310), Y338 (= Y311), G339 (= G312), L340 (= L313), T341 (= T314), S345 (≠ P318), A346 (≠ T319), D420 (= D393), I432 (= I405), K527 (= K499)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F217), R335 (≠ N308), G337 (= G310), G339 (= G312), L340 (= L313), A346 (≠ T319)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
29% identity, 91% coverage: 36:507/517 of query aligns to 46:535/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H215), F245 (= F217), T249 (≠ S221), G314 (= G288), A315 (≠ S289), P316 (= P290), G337 (= G310), Y338 (= Y311), G339 (= G312), L340 (= L313), T341 (= T314), A346 (≠ T319), D420 (= D393), I432 (= I405), K527 (= K499)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
30% identity, 96% coverage: 10:507/517 of query aligns to 2:495/502 of 3r44A
5ie2A Crystal structure of a plant enzyme (see paper)
30% identity, 95% coverage: 15:507/517 of query aligns to 6:503/506 of 5ie2A
- active site: T165 (= T171), S185 (≠ I191), H209 (= H215), T310 (= T314), E311 (= E315), N410 (≠ I414), K415 (≠ N419), K495 (= K499)
- binding adenosine-5'-triphosphate: T165 (= T171), S166 (= S172), G167 (= G173), T168 (= T174), T169 (= T175), S284 (≠ G288), A285 (≠ S289), S286 (≠ P290), Y307 (= Y311), A308 (≠ G312), M309 (≠ L313), T310 (= T314), D389 (= D393), L401 (≠ I405), R404 (= R408), K495 (= K499)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 92% coverage: 30:505/517 of query aligns to 34:524/528 of 5bsrA
- active site: S181 (≠ T171), S201 (≠ I191), H229 (= H215), T328 (= T314), E329 (= E315), K433 (≠ I414), Q438 (≠ N419), K518 (= K499)
- binding adenosine monophosphate: A301 (≠ G288), G326 (= G312), T328 (= T314), D412 (= D393), K429 (= K410), K433 (≠ I414), Q438 (≠ N419)
- binding coenzyme a: L102 (≠ R96), P226 (= P212), H229 (= H215), Y231 (≠ F217), F253 (= F239), K435 (≠ S416), G436 (= G417), F437 (= F418), F498 (≠ P479)
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, 92% coverage: 30:505/517 of query aligns to 42:532/542 of O24146
- S189 (≠ T171) binding
- S190 (= S172) binding
- G191 (= G173) binding
- T192 (= T174) binding
- T193 (= T175) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K179) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H215) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F217) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (= S221) binding ; binding ; binding
- K260 (≠ R238) binding
- A309 (≠ G288) binding ; binding ; binding
- Q331 (≠ N309) binding
- G332 (= G310) binding ; binding ; binding ; binding ; binding
- T336 (= T314) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ T319) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (vs. gap) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D393) binding ; binding ; binding ; binding ; binding
- R435 (= R408) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K410) binding ; binding ; binding ; binding
- K441 (≠ I414) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S416) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G417) binding
- Q446 (≠ N419) binding
- K526 (= K499) 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, 92% coverage: 30:505/517 of query aligns to 35:525/530 of 5bsmA
- active site: S182 (≠ T171), S202 (≠ I191), H230 (= H215), T329 (= T314), E330 (= E315), K434 (≠ I414), Q439 (≠ N419), K519 (= K499)
- binding adenosine-5'-triphosphate: S182 (≠ T171), S183 (= S172), G184 (= G173), T185 (= T174), T186 (= T175), K190 (= K179), H230 (= H215), A302 (≠ G288), A303 (≠ S289), P304 (= P290), Y326 (= Y311), G327 (= G312), M328 (≠ L313), T329 (= T314), D413 (= D393), I425 (= I405), R428 (= R408), K519 (= K499)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 92% coverage: 30:505/517 of query aligns to 35:525/529 of 5bsvA
- active site: S182 (≠ T171), S202 (≠ I191), H230 (= H215), T329 (= T314), E330 (= E315), K434 (≠ I414), Q439 (≠ N419), K519 (= K499)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H215), Y232 (≠ F217), S236 (= S221), A302 (≠ G288), A303 (≠ S289), P304 (= P290), G325 (= G310), G327 (= G312), M328 (≠ L313), T329 (= T314), P333 (= P318), V334 (≠ T319), D413 (= D393), K430 (= K410), K434 (≠ I414), Q439 (≠ N419)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 92% coverage: 30:505/517 of query aligns to 35:525/529 of 5bsuA
- active site: S182 (≠ T171), S202 (≠ I191), H230 (= H215), T329 (= T314), E330 (= E315), K434 (≠ I414), Q439 (≠ N419), K519 (= K499)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H215), Y232 (≠ F217), S236 (= S221), M299 (≠ S285), A302 (≠ G288), A303 (≠ S289), P304 (= P290), G325 (= G310), G327 (= G312), M328 (≠ L313), T329 (= T314), P333 (= P318), D413 (= D393), K430 (= K410), K434 (≠ I414), Q439 (≠ N419)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
30% identity, 92% coverage: 30:505/517 of query aligns to 35:525/529 of 5bstA
- active site: S182 (≠ T171), S202 (≠ I191), H230 (= H215), T329 (= T314), E330 (= E315), K434 (≠ I414), Q439 (≠ N419), K519 (= K499)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H215), Y232 (≠ F217), S236 (= S221), A302 (≠ G288), A303 (≠ S289), P304 (= P290), G325 (= G310), Y326 (= Y311), G327 (= G312), M328 (≠ L313), T329 (= T314), P333 (= P318), V334 (≠ T319), D413 (= D393), K430 (= K410), K434 (≠ I414), Q439 (≠ N419)
Q4G176 Malonate--CoA ligase ACSF3, mitochondrial; Acyl-CoA synthetase family member 3; EC 6.2.1.76 from Homo sapiens (Human) (see 2 papers)
34% identity, 66% coverage: 166:505/517 of query aligns to 197:569/576 of Q4G176
- R354 (≠ G310) mutation to A: Impairs malonyl-CoA synthase activity.; mutation to L: Impairs malonyl-CoA synthase activity.
- V372 (≠ P328) to M: in dbSNP:rs3743979
Sites not aligning to the query:
- 2 L → P: in dbSNP:rs7188200
- 17 A → P: in dbSNP:rs11547019
Query Sequence
>WP_011384981.1 NCBI__GCF_000009985.1:WP_011384981.1
MRPIADILADLPPRLAQLARQWQRRTPDAPAMIQGETRWSYARLGQAMDEAGALLRGLEV
RPGDRVMLVGENCLALVAMILAAGELDAWAAIINARLSEREIDTIRDHCGARRVIYTTDV
SAEATAHARRHGAELRASPLLGSFAVGPLNHQCGSEPVEPGNGQVAALIYTSGTTGTPKG
VMLPHRNIMFIGAVSGGLRDIGSGDVAYGVLPMSHVFGLASVLVGTLFGGACLHVAPRFA
PAQVLADLKAGLTMWNGVPAMFAKFLEHIRLTGAKVEAPALRFLSAGGSPLDPAIKAETE
ALFGQVLNNGYGLTESAPTICQTRLDAPRSDCSVGHALPGVEVRIVGEGGKDMPDGQVGE
LWSRGPGTMKGYYRAPDMTREVIDAEGWLNTGDFARRDPDGALFIVGRAKELIIRSGFNV
YPAEVEAVFNAHPLVTHSAVVGRPAADGNEEVVAFVQVAPGTELGSAELTEWAAARLAPY
KRPGEVVVVGHLPAGATGKILKNRLAEAARNHAYDTL
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