SitesBLAST
Comparing GFF4155 FitnessBrowser__psRCH2:GFF4155 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)
46% identity, 98% coverage: 9:538/541 of query aligns to 13:555/561 of P69451
- Y213 (= Y193) mutation to A: Loss of activity.
- T214 (= T194) mutation to A: 10% of wild-type activity.
- G216 (= G196) mutation to A: Decreases activity.
- T217 (= T197) mutation to A: Decreases activity.
- G219 (= G199) mutation to A: Decreases activity.
- K222 (= K202) mutation to A: Decreases activity.
- E361 (= E343) mutation to A: Loss of activity.
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)
28% identity, 95% coverage: 18:533/541 of query aligns to 43:547/556 of Q9S725
- K211 (= K202) mutation to S: Drastically reduces the activity.
- M293 (≠ S286) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ T313) mutation K->L,A: Affects the substrate specificity.
- E401 (= E388) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ W390) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R436) mutation to Q: Drastically reduces the activity.
- K457 (≠ S444) mutation to S: Drastically reduces the activity.
- K540 (= K526) mutation to N: Abolishes the 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)
30% identity, 95% coverage: 18:533/541 of query aligns to 39:542/559 of Q67W82
- G395 (= G387) 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, 98% coverage: 8:535/541 of query aligns to 13:528/528 of 3ni2A
- active site: S182 (≠ T194), S202 (≠ N214), H230 (= H243), T329 (= T342), E330 (= E343), K434 (≠ L442), Q439 (≠ N447), K519 (= K526)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ M245), S236 (≠ T249), G302 (= G316), A303 (= A317), P304 (= P318), G325 (= G338), G327 (= G340), T329 (= T342), P333 (= P346), V334 (= V347), D413 (= D421), K430 (= K438), K434 (≠ L442), Q439 (≠ N447)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
29% identity, 98% coverage: 8:535/541 of query aligns to 13:528/528 of 3a9vA
- active site: S182 (≠ T194), S202 (≠ N214), H230 (= H243), T329 (= T342), E330 (= E343), K434 (≠ L442), Q439 (≠ N447), K519 (= K526)
- binding adenosine monophosphate: H230 (= H243), G302 (= G316), A303 (= A317), P304 (= P318), Y326 (≠ F339), G327 (= G340), M328 (≠ L341), T329 (= T342), D413 (= D421), K430 (= K438), K434 (≠ L442), Q439 (≠ N447)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 97% coverage: 8:533/541 of query aligns to 12:525/528 of 5bsrA
- active site: S181 (≠ T194), S201 (≠ N214), H229 (= H243), T328 (= T342), E329 (= E343), K433 (≠ L442), Q438 (≠ N447), K518 (= K526)
- binding adenosine monophosphate: A301 (≠ G316), G326 (= G340), T328 (= T342), D412 (= D421), K429 (= K438), K433 (≠ L442), Q438 (≠ N447)
- binding coenzyme a: L102 (≠ Q103), P226 (= P240), H229 (= H243), Y231 (≠ M245), F253 (≠ R268), K435 (≠ S444), G436 (= G445), F437 (= F446), F498 (≠ G506)
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, 99% coverage: 8:540/541 of query aligns to 20:538/542 of O24146
- S189 (≠ T194) binding
- S190 (≠ G195) binding
- G191 (= G196) binding
- T192 (= T197) binding
- T193 (= T198) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K202) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H243) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ M245) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ T249) binding ; binding ; binding
- K260 (≠ G267) binding
- A309 (≠ G316) binding ; binding ; binding
- Q331 (≠ E337) binding
- G332 (= G338) binding ; binding ; binding ; binding ; binding
- T336 (= T342) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V347) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ T350) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D421) binding ; binding ; binding ; binding ; binding
- R435 (= R436) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K438) binding ; binding ; binding ; binding
- K441 (≠ L442) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S444) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G445) binding
- Q446 (≠ N447) binding
- K526 (= K526) 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, 97% coverage: 8:533/541 of query aligns to 13:526/530 of 5bsmA
- active site: S182 (≠ T194), S202 (≠ N214), H230 (= H243), T329 (= T342), E330 (= E343), K434 (≠ L442), Q439 (≠ N447), K519 (= K526)
- binding adenosine-5'-triphosphate: S182 (≠ T194), S183 (≠ G195), G184 (= G196), T185 (= T197), T186 (= T198), K190 (= K202), H230 (= H243), A302 (≠ G316), A303 (= A317), P304 (= P318), Y326 (≠ F339), G327 (= G340), M328 (≠ L341), T329 (= T342), D413 (= D421), I425 (= I433), R428 (= R436), K519 (= K526)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 97% coverage: 8:533/541 of query aligns to 13:526/529 of 5bsvA
- active site: S182 (≠ T194), S202 (≠ N214), H230 (= H243), T329 (= T342), E330 (= E343), K434 (≠ L442), Q439 (≠ N447), K519 (= K526)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H243), Y232 (≠ M245), S236 (≠ T249), A302 (≠ G316), A303 (= A317), P304 (= P318), G325 (= G338), G327 (= G340), M328 (≠ L341), T329 (= T342), P333 (= P346), V334 (= V347), D413 (= D421), K430 (= K438), K434 (≠ L442), Q439 (≠ N447)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 97% coverage: 8:533/541 of query aligns to 13:526/529 of 5bsuA
- active site: S182 (≠ T194), S202 (≠ N214), H230 (= H243), T329 (= T342), E330 (= E343), K434 (≠ L442), Q439 (≠ N447), K519 (= K526)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H243), Y232 (≠ M245), S236 (≠ T249), M299 (≠ T313), A302 (≠ G316), A303 (= A317), P304 (= P318), G325 (= G338), G327 (= G340), M328 (≠ L341), T329 (= T342), P333 (= P346), D413 (= D421), K430 (= K438), K434 (≠ L442), Q439 (≠ N447)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
30% identity, 97% coverage: 8:533/541 of query aligns to 13:526/529 of 5bstA
- active site: S182 (≠ T194), S202 (≠ N214), H230 (= H243), T329 (= T342), E330 (= E343), K434 (≠ L442), Q439 (≠ N447), K519 (= K526)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H243), Y232 (≠ M245), S236 (≠ T249), A302 (≠ G316), A303 (= A317), P304 (= P318), G325 (= G338), Y326 (≠ F339), G327 (= G340), M328 (≠ L341), T329 (= T342), P333 (= P346), V334 (= V347), D413 (= D421), K430 (= K438), K434 (≠ L442), Q439 (≠ N447)
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: 32:532/541 of query aligns to 43:536/546 of Q84P21
- K530 (= K526) mutation to N: Lossed enzymatic activity.
Q17577 Acyl-CoA synthetase 7; EC 6.2.1.- from Caenorhabditis elegans (see paper)
29% identity, 95% coverage: 21:533/541 of query aligns to 15:529/540 of Q17577
- SS 186:187 (≠ TG 194:195) mutation to AA: Loss of catalytic activity; when associated with A-339.
- E339 (= E343) mutation to A: Severe loss of catalytic activity. Loss of catalytic activity; when associated with 186-A-A-187.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 93% coverage: 33:534/541 of query aligns to 16:499/506 of 4gxqA
- active site: T163 (= T194), N183 (= N214), H207 (= H243), T303 (= T342), E304 (= E343), I403 (≠ L442), N408 (= N447), A491 (≠ K526)
- binding adenosine-5'-triphosphate: T163 (= T194), S164 (≠ G195), G165 (= G196), T166 (= T197), T167 (= T198), H207 (= H243), S277 (≠ G316), A278 (= A317), P279 (= P318), E298 (= E337), M302 (≠ L341), T303 (= T342), D382 (= D421), R397 (= R436)
- binding carbonate ion: H207 (= H243), S277 (≠ G316), R299 (≠ G338), G301 (= G340)
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, 91% coverage: 46:536/541 of query aligns to 66:573/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
29% identity, 98% coverage: 8:538/541 of query aligns to 12:527/527 of 5u95B
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)
27% identity, 96% coverage: 19:538/541 of query aligns to 2:499/503 of P9WQ37
- R9 (≠ S26) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ Q34) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K202) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ P225) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ K232) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I244) 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 (= A246) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (= T249) 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 (≠ F282) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G340) 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 (= W416) 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 (= D421) 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 (= R436) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V443) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G445) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K526) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
27% identity, 97% coverage: 18:541/541 of query aligns to 9:517/518 of 4wv3B
- active site: S175 (≠ T194), T320 (= T342), E321 (= E343), K418 (≠ L442), W423 (≠ N447), K502 (= K526)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H243), T221 (≠ I244), F222 (≠ M245), A293 (≠ G315), S294 (≠ G316), E295 (≠ A317), A296 (≠ P318), G316 (= G338), I317 (≠ F339), G318 (= G340), C319 (≠ L341), T320 (= T342), D397 (= D421), H409 (≠ I433), R412 (= R436), K502 (= K526)
Q5SKN9 Long-chain-fatty-acid--CoA ligase; Long-chain fatty acyl-CoA synthetase; LC-FACS; EC 6.2.1.3 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
30% identity, 96% coverage: 20:537/541 of query aligns to 19:535/541 of Q5SKN9
- T184 (= T194) binding
- G302 (= G316) binding
- Q322 (≠ E337) binding
- G323 (= G338) binding
- T327 (= T342) binding
- E328 (= E343) binding
- D418 (= D421) binding
- K435 (= K438) binding
- K439 (≠ L442) binding
5ie3A Crystal structure of a plant enzyme (see paper)
29% identity, 94% coverage: 24:530/541 of query aligns to 9:497/504 of 5ie3A
- active site: T163 (= T194), S183 (≠ N214), H207 (= H243), T308 (= T342), E309 (= E343), N408 (≠ L442), K413 (≠ N447), K493 (= K526)
- binding adenosine monophosphate: S164 (≠ G195), S282 (≠ G316), A283 (= A317), S284 (≠ P318), Y305 (≠ F339), A306 (≠ G340), M307 (≠ L341), T308 (= T342), D387 (= D421), L399 (≠ I433), R402 (= R436), K493 (= K526)
- binding oxalic acid: V208 (≠ I244), S282 (≠ G316), A306 (≠ G340), M307 (≠ L341), H312 (≠ P346), K493 (= K526)
Query Sequence
>GFF4155 FitnessBrowser__psRCH2:GFF4155
MSASVQGYVAAELARGSYQNVHDLLSRACATHPQRTAFSCGDDHLTYAELGSRADAFARY
LRYHAGLQPGDRLALQLPNCLQYPIAVFGALKAGLVIVNTNPQYTAAEARHQFHDSGAKA
ILVLDRLLPQVRAVQADTALRQIILTSVDDLQQPIYESQEDGTLRFMQALRLGEQRSPVQ
REAGLDRLALLQYTGGTTGVSKGAMLTHRNLLANVLQTIELFDQPGLLEPEKDVRIAPLP
LYHIMAFATNCLSSVGMGLHTVFIRDGRNLDETIGAMQRHPFSLLSGINTLFVGLMNHPE
FRSIDFSHLKWATSGGAPLNSEVGRRWQALTGAPIREGFGLTEASPVVATGTQLSPYREG
YIGQALIETELRTVDDEGNDVPPETPGELWLRGPQVMQGYWQRPDETAKVLTPDGWLKTG
DIALLDVDGFVKIVDRKKDMILVSGFNVFPNEIEDVLMQHPSVRECVAVGVPDARKGEAV
KVFVSLKDDTVDERALLEHCRQYLTGYKMPSFLELRDELPKTAVGKLLRRQLRDEARAAA
S
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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