SitesBLAST
Comparing BPHYT_RS15945 FitnessBrowser__BFirm:BPHYT_RS15945 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)
34% identity, 93% coverage: 35:518/520 of query aligns to 15:499/506 of 4gxqA
- active site: T163 (= T182), N183 (≠ I202), H207 (= H226), T303 (= T326), E304 (= E327), I403 (= I426), N408 (= N431), A491 (≠ K510)
- binding adenosine-5'-triphosphate: T163 (= T182), S164 (≠ T183), G165 (= G184), T166 (= T185), T167 (= T186), H207 (= H226), S277 (≠ G300), A278 (≠ S301), P279 (= P302), E298 (≠ N321), M302 (= M325), T303 (= T326), D382 (= D405), R397 (= R420)
- binding carbonate ion: H207 (= H226), S277 (≠ G300), R299 (≠ G322), G301 (= G324)
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, 91% coverage: 47:518/520 of query aligns to 29:495/503 of P9WQ37
- K172 (= K190) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ G213) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ D215) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V227) 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 (≠ G229) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ S232) 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 (= R263) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G324) 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 (= W400) 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 (= D405) 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 (= R420) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R427) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G429) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K510) 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)
29% identity, 92% coverage: 38:516/520 of query aligns to 46:536/546 of Q84P21
- K530 (= K510) mutation to N: Lossed enzymatic activity.
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)
29% identity, 98% coverage: 7:518/520 of query aligns to 7:551/561 of P69451
- Y213 (= Y181) mutation to A: Loss of activity.
- T214 (= T182) mutation to A: 10% of wild-type activity.
- G216 (= G184) mutation to A: Decreases activity.
- T217 (= T185) mutation to A: Decreases activity.
- G219 (= G187) mutation to A: Decreases activity.
- K222 (= K190) mutation to A: Decreases activity.
- E361 (= E327) mutation to A: Loss of activity.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
32% identity, 91% coverage: 47:518/520 of query aligns to 32:495/502 of 3r44A
Sites not aligning to the query:
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)
29% identity, 87% coverage: 64:517/520 of query aligns to 80:547/556 of Q9S725
- K211 (= K190) mutation to S: Drastically reduces the activity.
- M293 (≠ Q268) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ Y297) mutation K->L,A: Affects the substrate specificity.
- E401 (= E372) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ W374) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R420) mutation to Q: Drastically reduces the activity.
- K457 (≠ S428) mutation to S: Drastically reduces the activity.
- K540 (= K510) mutation to N: Abolishes the activity.
Q4G176 Malonate--CoA ligase ACSF3, mitochondrial; Acyl-CoA synthetase family member 3; EC 6.2.1.76 from Homo sapiens (Human) (see 2 papers)
31% identity, 93% coverage: 39:519/520 of query aligns to 57:573/576 of Q4G176
- R354 (≠ G322) mutation to A: Impairs malonyl-CoA synthase activity.; mutation to L: Impairs malonyl-CoA synthase activity.
- V372 (≠ P340) to M: in dbSNP:rs3743979
Sites not aligning to the query:
- 2 L → P: in dbSNP:rs7188200
- 17 A → P: in dbSNP:rs11547019
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
30% identity, 93% coverage: 36:518/520 of query aligns to 15:475/475 of 5burA
- active site: T150 (= T182), S170 (≠ I202), H194 (= H226), T287 (= T326), E288 (= E327)
- binding adenosine-5'-triphosphate: T150 (= T182), S151 (≠ T183), T153 (= T185), T154 (= T186), K158 (= K190), G263 (≠ S301), S283 (≠ G322), T287 (= T326), D365 (= D405), V377 (≠ I417), R380 (= R420)
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)
30% identity, 93% coverage: 36:518/520 of query aligns to 16:478/485 of 5x8fB
- active site: T151 (= T182), S171 (≠ I202), H195 (= H226), T288 (= T326), E289 (= E327), I387 (= I426), N392 (= N431), K470 (= K510)
- binding magnesium ion: Y23 (≠ E43), E24 (≠ D44), H70 (≠ F90), N178 (≠ L209), L202 (≠ V233), L214 (= L246), T296 (≠ L337), L297 (≠ D338), S298 (≠ A339)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R105), L191 (= L222), P192 (= P223), H195 (= H226), I196 (≠ V227), S197 (≠ Y228), A237 (≠ G269), V238 (= V270), L260 (≠ Y297), G262 (= G299), G286 (= G324), M287 (= M325), S292 (= S333), Q293 (≠ H334), S388 (≠ R427), G389 (≠ S428), G390 (= G429), E391 (≠ F430), K420 (≠ N460), W421 (≠ E461), K450 (≠ P490), Y451 (= Y491)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
30% identity, 93% coverage: 36:518/520 of query aligns to 15:475/481 of 5busA
- active site: T150 (= T182), S170 (≠ I202), H194 (= H226), T287 (= T326), E288 (= E327)
- binding adenosine monophosphate: H194 (= H226), G262 (= G300), G263 (≠ S301), S283 (≠ G322), M286 (= M325), T287 (= T326), D365 (= D405), V377 (≠ I417), R380 (= R420), K467 (= K510)
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, 88% coverage: 60:517/520 of query aligns to 72:542/559 of Q67W82
- G395 (= G371) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
30% identity, 93% coverage: 36:518/520 of query aligns to 16:478/484 of 5gtdA
- active site: T151 (= T182), S171 (≠ I202), H195 (= H226), T288 (= T326), E289 (= E327)
- binding adenosine-5'-monophosphate: G263 (= G300), G264 (≠ S301), Y285 (= Y323), G286 (= G324), M287 (= M325), T288 (= T326), D366 (= D405), V378 (≠ I417)
- binding magnesium ion: F314 (≠ P351), S315 (≠ G352)
- binding 2-succinylbenzoate: H195 (= H226), S197 (≠ Y228), A237 (≠ G269), L260 (≠ Y297), G262 (= G299), G263 (= G300), G286 (= G324), M287 (= M325), S292 (= S333), Q293 (≠ H334)
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)
31% identity, 89% coverage: 47:511/520 of query aligns to 30:501/514 of Q9SMT7
- TSGTT 170:174 (≠ TTGTT 182:186) binding
- H214 (= H226) binding ; mutation to A: Abolished activity.
- S289 (≠ G300) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ GSP 300:302) binding
- EA 310:311 (≠ NG 321:322) binding
- M314 (= M325) binding
- T315 (= T326) binding
- H319 (≠ P330) binding ; mutation to A: Abolished activity.
- D394 (= D405) binding
- R409 (= R420) binding ; mutation to A: Abolished activity.
- K500 (= K510) binding ; binding ; mutation to A: Abolished activity.
5ie2A Crystal structure of a plant enzyme (see paper)
32% identity, 89% coverage: 47:511/520 of query aligns to 30:496/506 of 5ie2A
- active site: T165 (= T182), S185 (≠ I202), H209 (= H226), T310 (= T326), E311 (= E327), N410 (≠ I426), K415 (≠ N431), K495 (= K510)
- binding adenosine-5'-triphosphate: T165 (= T182), S166 (≠ T183), G167 (= G184), T168 (= T185), T169 (= T186), S284 (≠ G300), A285 (≠ S301), S286 (≠ P302), Y307 (= Y323), A308 (≠ G324), M309 (= M325), T310 (= T326), D389 (= D405), L401 (≠ I417), R404 (= R420), K495 (= K510)
5ie3A Crystal structure of a plant enzyme (see paper)
31% identity, 89% coverage: 47:511/520 of query aligns to 30:494/504 of 5ie3A
- active site: T163 (= T182), S183 (≠ I202), H207 (= H226), T308 (= T326), E309 (= E327), N408 (≠ I426), K413 (≠ N431), K493 (= K510)
- binding adenosine monophosphate: S164 (≠ T183), S282 (≠ G300), A283 (≠ S301), S284 (≠ P302), Y305 (= Y323), A306 (≠ G324), M307 (= M325), T308 (= T326), D387 (= D405), L399 (≠ I417), R402 (= R420), K493 (= K510)
- binding oxalic acid: V208 (= V227), S282 (≠ G300), A306 (≠ G324), M307 (= M325), H312 (≠ P330), K493 (= K510)
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
30% identity, 88% coverage: 48:504/520 of query aligns to 31:493/504 of 6qjzA
- active site: T169 (= T182), S189 (≠ I202), H213 (= H226), T314 (= T326), E315 (= E327), N414 (≠ I426), K419 (≠ N431)
- binding adenosine monophosphate: H213 (= H226), S288 (≠ G300), A289 (≠ S301), S290 (≠ P302), A312 (≠ G324), M313 (= M325), T314 (= T326), D393 (= D405), L405 (≠ I417), K410 (= K422), K419 (≠ N431)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
35% identity, 66% coverage: 178:518/520 of query aligns to 178:527/528 of 3ni2A
- active site: S182 (≠ T182), S202 (≠ A204), H230 (= H226), T329 (= T326), E330 (= E327), K434 (≠ I426), Q439 (≠ N431), K519 (= K510)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (= Y228), S236 (= S232), G302 (= G300), A303 (≠ S301), P304 (= P302), G325 (= G322), G327 (= G324), T329 (= T326), P333 (= P330), V334 (≠ T331), D413 (= D405), K430 (= K422), K434 (≠ I426), Q439 (≠ N431)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
35% identity, 66% coverage: 178:518/520 of query aligns to 178:527/528 of 3a9vA
- active site: S182 (≠ T182), S202 (≠ A204), H230 (= H226), T329 (= T326), E330 (= E327), K434 (≠ I426), Q439 (≠ N431), K519 (= K510)
- binding adenosine monophosphate: H230 (= H226), G302 (= G300), A303 (≠ S301), P304 (= P302), Y326 (= Y323), G327 (= G324), M328 (= M325), T329 (= T326), D413 (= D405), K430 (= K422), K434 (≠ I426), Q439 (≠ N431)
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, 85% coverage: 68:511/520 of query aligns to 48:495/512 of O74976
- S283 (≠ G300) modified: Phosphoserine
- S284 (= S301) modified: Phosphoserine
7tz4A Salicylate adenylate pchd from pseudomonas aeruginosa containing 4- cyanosalicyl-ams (see paper)
31% identity, 96% coverage: 22:520/520 of query aligns to 22:527/530 of 7tz4A
- binding 5'-O-[(4-cyano-2-hydroxybenzoyl)sulfamoyl]adenosine: H232 (= H226), N233 (≠ G229), F234 (= F230), C238 (= C234), G305 (= G300), S306 (= S301), R307 (≠ P302), V327 (≠ G322), L328 (≠ Y323), G329 (= G324), M330 (= M325), A331 (≠ T326), I335 (≠ V332), D411 (= D405), V423 (≠ I417), K517 (= K510)
Query Sequence
>BPHYT_RS15945 FitnessBrowser__BFirm:BPHYT_RS15945
MSFDSPTRSTIDIPALLAALPERIADIPALAAARDPQHIAVIEDARRLTSAQLLEAVDAA
TALLREWGVRGGDRVMIVAENSIVQIVLLFATARLDAWALVSNARLSAAELDSIRAHAQP
RIVAYATESSADAKLHAERHHAAKAPAFTPDIGAWSYTVDSAAVAEPVEAASERQCAALI
YTTGTTGAPKGVMLSHRNLLFIAAISSRLRKVGPDDVVYAVLPISHVYGFASVCLGSLHA
GATLRLVPRFAPEAVRRALADERVSIFQGVPAMHAKLLEHLQTHGHAWSAPHLRFAYSGG
SPLDAALKAQVESVCGLPLHNGYGMTESSPTVSHTMLDAPRSDCSVGEVIPGVEVRFVGL
DGIDAAQGDIGELWVRGPNVMLGYYRSLEQTRAAVTEDGWLKTGDLARQDADGALHIVGR
SKELIIRSGFNVYPAEVEHVLNAHPQVVQSAVIGRAVEGNEEVVAFVELLTGATVTPAEL
IDCCGERLAPYKRPAEVKVLAALPAASTGKILKHRLREFL
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