SitesBLAST
Comparing GFF3354 FitnessBrowser__Phaeo:GFF3354 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)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
60% identity, 97% coverage: 15:499/500 of query aligns to 12:505/506 of 4gxqA
- active site: T163 (= T163), N183 (= N183), H207 (= H207), T303 (= T303), E304 (= E304), I403 (= I401), N408 (= N406), A491 (≠ K485)
- binding adenosine-5'-triphosphate: T163 (= T163), S164 (= S164), G165 (= G165), T166 (= T166), T167 (= T167), H207 (= H207), S277 (= S277), A278 (= A278), P279 (= P279), E298 (= E298), M302 (= M302), T303 (= T303), D382 (= D380), R397 (= R395)
- binding carbonate ion: H207 (= H207), S277 (= S277), R299 (= R299), G301 (= G301)
3nyrA Malonyl-coa ligase ternary product complex with malonyl-coa and amp bound (see paper)
40% identity, 79% coverage: 85:480/500 of query aligns to 71:460/460 of 3nyrA
- active site: T137 (= T163), T157 (≠ N183), H181 (= H207), T281 (= T303), E282 (= E304), K379 (≠ I401), K384 (≠ N406)
- binding adenosine monophosphate: S255 (= S277), A256 (= A278), A257 (≠ P279), R277 (= R299), Y278 (= Y300), G279 (= G301), M280 (= M302), T281 (= T303), D357 (= D380), K379 (≠ I401), K384 (≠ N406)
- binding malonyl-coenzyme a: P178 (= P204), H181 (= H207), T226 (= T251), R230 (= R255), S255 (= S277), R277 (= R299), G279 (= G301), G381 (= G403), G382 (= G404), Y383 (≠ F405)
3nyqA Malonyl-coa ligase ternary product complex with methylmalonyl-coa and amp bound (see paper)
40% identity, 79% coverage: 85:480/500 of query aligns to 71:460/460 of 3nyqA
- active site: T137 (= T163), T157 (≠ N183), H181 (= H207), T281 (= T303), E282 (= E304), K379 (≠ I401), K384 (≠ N406)
- binding adenosine monophosphate: S255 (= S277), A256 (= A278), A257 (≠ P279), R277 (= R299), Y278 (= Y300), G279 (= G301), M280 (= M302), T281 (= T303), D357 (= D380), K379 (≠ I401), K384 (≠ N406)
- binding methylmalonyl-coenzyme a: P178 (= P204), H181 (= H207), H183 (= H209), T226 (= T251), R230 (= R255), S255 (= S277), R277 (= R299), G279 (= G301), M280 (= M302), M285 (= M307), G381 (= G403), G382 (= G404), Y383 (≠ F405)
Q4G176 Malonate--CoA ligase ACSF3, mitochondrial; Acyl-CoA synthetase family member 3; EC 6.2.1.76 from Homo sapiens (Human) (see 2 papers)
32% identity, 92% coverage: 34:495/500 of query aligns to 68:573/576 of Q4G176
- R354 (= R299) mutation to A: Impairs malonyl-CoA synthase activity.; mutation to L: Impairs malonyl-CoA synthase activity.
- V372 (= V316) to M: in dbSNP:rs3743979
Sites not aligning to the query:
- 2 L → P: in dbSNP:rs7188200
- 17 A → P: in dbSNP:rs11547019
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)
33% identity, 88% coverage: 52:493/500 of query aligns to 70:551/561 of P69451
- Y213 (= Y162) mutation to A: Loss of activity.
- T214 (= T163) mutation to A: 10% of wild-type activity.
- G216 (= G165) mutation to A: Decreases activity.
- T217 (= T166) mutation to A: Decreases activity.
- G219 (= G168) mutation to A: Decreases activity.
- K222 (= K171) mutation to A: Decreases activity.
- E361 (= E304) 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, 93% coverage: 34:496/500 of query aligns to 32:498/503 of P9WQ37
- K172 (= K171) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T194) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ E196) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ T208) 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 (≠ G210) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V213) 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 (≠ T244) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G301) 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 (= W375) 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 (= D380) 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 (= R395) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S402) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G404) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K485) 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, 93% coverage: 34:496/500 of query aligns to 35:498/502 of 3r44A
Sites not aligning to the query:
5ie3A Crystal structure of a plant enzyme (see paper)
33% identity, 91% coverage: 42:495/500 of query aligns to 41:503/504 of 5ie3A
- active site: T163 (= T163), S183 (≠ N183), H207 (= H207), T308 (= T303), E309 (= E304), N408 (≠ I401), K413 (≠ N406), K493 (= K485)
- binding adenosine monophosphate: S164 (= S164), S282 (= S277), A283 (= A278), S284 (≠ P279), Y305 (= Y300), A306 (≠ G301), M307 (= M302), T308 (= T303), D387 (= D380), L399 (≠ I392), R402 (= R395), K493 (= K485)
- binding oxalic acid: V208 (≠ T208), S282 (= S277), A306 (≠ G301), M307 (= M302), H312 (≠ N306), K493 (= K485)
5ie2A Crystal structure of a plant enzyme (see paper)
33% identity, 91% coverage: 42:495/500 of query aligns to 41:505/506 of 5ie2A
- active site: T165 (= T163), S185 (≠ N183), H209 (= H207), T310 (= T303), E311 (= E304), N410 (≠ I401), K415 (≠ N406), K495 (= K485)
- binding adenosine-5'-triphosphate: T165 (= T163), S166 (= S164), G167 (= G165), T168 (= T166), T169 (= T167), S284 (= S277), A285 (= A278), S286 (≠ P279), Y307 (= Y300), A308 (≠ G301), M309 (= M302), T310 (= T303), D389 (= D380), L401 (≠ I392), R404 (= R395), K495 (= K485)
Q9SMT7 Oxalate--CoA ligase; 4-coumarate--CoA ligase isoform 8; At4CL8; 4-coumarate--CoA ligase-like 10; Acyl-activating enzyme 3; Adenosine monophosphate binding protein 3; AtMPBP3; Oxalyl-CoA synthetase; EC 6.2.1.8 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 91% coverage: 42:497/500 of query aligns to 41:512/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 163:167) binding
- H214 (= H207) binding ; mutation to A: Abolished activity.
- S289 (= S277) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ SAP 277:279) binding
- EA 310:311 (≠ ER 298:299) binding
- M314 (= M302) binding
- T315 (= T303) binding
- H319 (≠ N306) binding ; mutation to A: Abolished activity.
- D394 (= D380) binding
- R409 (= R395) binding ; mutation to A: Abolished activity.
- K500 (= K485) binding ; binding ; mutation to A: Abolished activity.
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, 93% coverage: 34:499/500 of query aligns to 67:577/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
32% identity, 88% coverage: 42:480/500 of query aligns to 41:494/504 of 6qjzA
- active site: T169 (= T163), S189 (≠ N183), H213 (= H207), T314 (= T303), E315 (= E304), N414 (≠ I401), K419 (≠ N406)
- binding adenosine monophosphate: H213 (= H207), S288 (= S277), A289 (= A278), S290 (≠ P279), A312 (≠ G301), M313 (= M302), T314 (= T303), D393 (= D380), L405 (≠ I392), K410 (= K397), K419 (≠ N406)
P0DX84 3-methylmercaptopropionyl-CoA ligase; MMPA-CoA ligase; EC 6.2.1.44 from Ruegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157) (Silicibacter lacuscaerulensis) (see paper)
30% identity, 93% coverage: 34:500/500 of query aligns to 42:538/539 of P0DX84
- H231 (= H207) mutation to A: Retains 74% of wild-type activity.
- W235 (≠ L211) mutation to A: Almost completely abolishes the activity.
- G302 (≠ S275) mutation to P: Almost completely abolishes the activity.
- G303 (= G276) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y300) mutation to A: Retains 7.7% of wild-type activity.
- P333 (vs. gap) mutation to A: Retains 69% of wild-type activity.
- R432 (= R395) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K397) mutation to A: Retains 36% of wild-type activity.
- D435 (= D398) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I401) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G403) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G404) mutation to P: Retains 2.7% of wild-type activity.
- E442 (≠ F405) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N406) mutation to A: Retains 60% of wild-type activity.
- E474 (= E437) mutation to A: Retains 33% of wild-type activity.
- K523 (= K485) Plays an important role in catalysis; mutation to A: Retains 1.6% of wild-type activity.; mutation to E: Retains 1.4% of wild-type activity.; mutation to R: Retains 57% of wild-type activity.
- K526 (= K488) mutation to A: Retains 48% of wild-type activity.
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
30% identity, 93% coverage: 34:500/500 of query aligns to 42:538/538 of 6ijbB
- active site: T185 (= T163), H205 (≠ Y181), H231 (= H207), S329 (≠ T303), E330 (= E304), K438 (≠ I401), W443 (≠ N406), A523 (≠ K485)
- binding 3-(methylsulfanyl)propanoic acid: W235 (≠ L211), G303 (= G276), A325 (≠ R299), W326 (≠ Y300), G327 (= G301), M328 (= M302)
- binding adenosine monophosphate: G303 (= G276), A304 (≠ S277), A305 (= A278), H324 (≠ E298), W326 (≠ Y300), G327 (= G301), M328 (= M302), S329 (≠ T303), Q359 (≠ V322), D417 (= D380)
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)
29% identity, 93% coverage: 34:499/500 of query aligns to 50:538/541 of Q5SKN9
- T184 (= T163) binding
- G302 (≠ S277) binding
- Q322 (≠ E298) binding
- G323 (≠ R299) binding
- T327 (= T303) binding
- E328 (= E304) binding
- D418 (= D380) binding
- K435 (= K397) binding
- K439 (≠ I401) binding
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)
29% identity, 93% coverage: 32:495/500 of query aligns to 28:504/512 of O74976
- S283 (= S277) modified: Phosphoserine
- S284 (≠ A278) modified: Phosphoserine
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, 93% coverage: 34:496/500 of query aligns to 62:546/559 of Q67W82
- G395 (= G346) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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, 92% coverage: 34:491/500 of query aligns to 60:536/546 of Q84P21
- K530 (= K485) mutation to N: Lossed enzymatic activity.
5x8fB Ternary complex structure of a double mutant i454ra456k of o- succinylbenzoate coa synthetase (mene) from bacillus subtilis bound with amp and its product analogue osb-ncoa at 1.76 angstrom (see paper)
29% identity, 92% coverage: 32:493/500 of query aligns to 28:478/485 of 5x8fB
- active site: T151 (= T163), S171 (≠ N183), H195 (= H207), T288 (= T303), E289 (= E304), I387 (= I401), N392 (= N406), K470 (= K485)
- binding magnesium ion: H70 (≠ L74), N178 (≠ Y190), L202 (≠ T215), L214 (= L227), T296 (= T309), L297 (≠ S310), S298 (≠ N311)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ A89), L191 (= L203), P192 (= P204), H195 (= H207), I196 (≠ T208), S197 (≠ H209), A237 (≠ G248), V238 (= V249), L260 (≠ I274), G262 (= G276), G286 (= G301), M287 (= M302), S292 (vs. gap), Q293 (≠ N306), S388 (= S402), G389 (= G403), G390 (= G404), E391 (≠ F405), K420 (≠ D434), W421 (≠ F435), K450 (= K465), Y451 (≠ F466)
Sites not aligning to the query:
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
30% identity, 92% coverage: 34:495/500 of query aligns to 42:530/533 of 6ihkB
- active site: T185 (= T163), H202 (≠ Y181), H228 (= H207), S326 (≠ T303), E327 (= E304), K435 (≠ I401), W440 (≠ N406), K520 (= K485)
- binding adenosine-5'-diphosphate: H228 (= H207), G300 (= G276), A301 (≠ S277), A302 (= A278), H321 (≠ E298), A322 (≠ R299), W323 (≠ Y300), G324 (= G301), M325 (= M302), S326 (≠ T303), Q356 (≠ V322), D414 (= D380), R429 (= R395), K520 (= K485)
Query Sequence
>GFF3354 FitnessBrowser__Phaeo:GFF3354
MYDANPLIRHLRAASLDREGALFATRPGADPVGYGELFAGAERMAAALVSRGVAPGDRVA
AQVDKSLAAIQLYLGTVMAGAIFLPLNPAYTEAEVAYFIGDATPRVFVCNPVRHESLRAV
AGEATVLTLDGEGQGSLADLAAGHAGFEPIERKPSDLAAILYTSGTTGRSKGAMLSHENL
YSNSLTLRDYWQFTAEDVLIHALPIFHTHGLFVATNVALLAGAQVVLLPGFDAEAILAAM
PNATALMGVPTFYTRLLVDARLTPDLAANMRLFISGSAPLLVETHEQWEARTGHRILERY
GMTETNMSTSNPYDGVRVAGTVGPPLPGVEARVTLDNAEIPLGEIGVLEVRGPNVFQGYW
QMPEKTAEELRPDGWFITGDLAKIDSNGYVTIVGREKDLVISGGFNVYPKEVETLIDDLP
GVLESAVIGVPHPDFGEAVVAVVVPTEEGTDAASIQAALSEHLAKFKQPKHIALMDELPR
NTMGKVQKKALRETFAQLFT
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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