SitesBLAST
Comparing Ac3H11_3009 FitnessBrowser__acidovorax_3H11:Ac3H11_3009 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)
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)
41% identity, 98% coverage: 11:578/578 of query aligns to 19:585/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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, 94% coverage: 29:570/578 of query aligns to 23:557/561 of P69451
- Y213 (≠ F223) mutation to A: Loss of activity.
- T214 (= T224) mutation to A: 10% of wild-type activity.
- G216 (= G226) mutation to A: Decreases activity.
- T217 (= T227) mutation to A: Decreases activity.
- G219 (= G229) mutation to A: Decreases activity.
- K222 (= K232) mutation to A: Decreases activity.
- E361 (= E369) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 90% coverage: 49:568/578 of query aligns to 21:503/506 of 4gxqA
- active site: T163 (= T193), N183 (= N244), H207 (= H268), T303 (= T368), E304 (= E369), I403 (= I471), N408 (= N476), A491 (≠ K556)
- binding adenosine-5'-triphosphate: T163 (= T193), S164 (= S225), G165 (= G226), T166 (= T227), T167 (= T228), H207 (= H268), S277 (≠ G341), A278 (≠ S342), P279 (= P343), E298 (≠ I363), M302 (= M367), T303 (= T368), D382 (= D450), R397 (= R465)
- binding carbonate ion: H207 (= H268), S277 (≠ G341), R299 (≠ A364), G301 (= G366)
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, 91% coverage: 45:570/578 of query aligns to 52:554/556 of Q9S725
- K211 (= K232) mutation to S: Drastically reduces the activity.
- M293 (≠ H311) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I338) mutation K->L,A: Affects the substrate specificity.
- E401 (= E417) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C419) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R465) mutation to Q: Drastically reduces the activity.
- K457 (≠ G473) mutation to S: Drastically reduces the activity.
- K540 (= K556) mutation to N: Abolishes the activity.
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
28% identity, 91% coverage: 40:563/578 of query aligns to 32:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H268), F245 (= F270), T249 (≠ G275), G314 (= G341), A315 (≠ S342), P316 (= P343), G337 (≠ A364), Y338 (= Y365), G339 (= G366), L340 (≠ M367), T341 (= T368), A346 (≠ P372), D420 (= D450), I432 (= I462), K527 (= K556)
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)
29% identity, 93% coverage: 29:565/578 of query aligns to 2:496/503 of P9WQ37
- R9 (≠ A36) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ E44) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K232) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T255) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ A257) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C269) 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 (≠ G271) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ L274) 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 (= R306) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G366) 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 (= W445) 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 (= D450) 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 (= R465) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R472) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G474) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K556) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
28% identity, 91% coverage: 40:563/578 of query aligns to 32:534/539 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 (= H268), F245 (= F270), T249 (≠ G275), G314 (= G341), A315 (≠ S342), P316 (= P343), G337 (≠ A364), Y338 (= Y365), G339 (= G366), L340 (≠ M367), T341 (= T368), S345 (= S371), A346 (≠ P372), D420 (= D450), I432 (= I462), K527 (= K556)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F270), R335 (≠ T362), G337 (≠ A364), G339 (= G366), L340 (≠ M367), A346 (≠ P372)
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)
27% identity, 89% coverage: 45:559/578 of query aligns to 46:533/546 of Q84P21
- K530 (= K556) mutation to N: Lossed enzymatic activity.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
27% identity, 92% coverage: 33:565/578 of query aligns to 22:528/528 of 3ni2A
- active site: S182 (≠ T224), S202 (vs. gap), H230 (= H268), T329 (= T368), E330 (= E369), K434 (≠ I471), Q439 (≠ N476), K519 (= K556)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F270), S236 (≠ L274), G302 (= G341), A303 (≠ S342), P304 (= P343), G325 (≠ A364), G327 (= G366), T329 (= T368), P333 (= P372), V334 (= V373), D413 (= D450), K430 (= K467), K434 (≠ I471), Q439 (≠ N476)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
27% identity, 92% coverage: 33:565/578 of query aligns to 22:528/528 of 3a9vA
- active site: S182 (≠ T224), S202 (vs. gap), H230 (= H268), T329 (= T368), E330 (= E369), K434 (≠ I471), Q439 (≠ N476), K519 (= K556)
- binding adenosine monophosphate: H230 (= H268), G302 (= G341), A303 (≠ S342), P304 (= P343), Y326 (= Y365), G327 (= G366), M328 (= M367), T329 (= T368), D413 (= D450), K430 (= K467), K434 (≠ I471), Q439 (≠ N476)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
28% identity, 93% coverage: 29:565/578 of query aligns to 5:496/502 of 3r44A
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
27% identity, 90% coverage: 45:566/578 of query aligns to 34:529/530 of 5bsmA
- active site: S182 (≠ T224), S202 (vs. gap), H230 (= H268), T329 (= T368), E330 (= E369), K434 (≠ I471), Q439 (≠ N476), K519 (= K556)
- binding adenosine-5'-triphosphate: S182 (≠ T224), S183 (= S225), G184 (= G226), T185 (= T227), T186 (= T228), K190 (= K232), H230 (= H268), A302 (≠ G341), A303 (≠ S342), P304 (= P343), Y326 (= Y365), G327 (= G366), M328 (= M367), T329 (= T368), D413 (= D450), I425 (= I462), R428 (= R465), K519 (= K556)
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)
27% identity, 90% coverage: 45:566/578 of query aligns to 41:536/542 of O24146
- S189 (≠ T224) binding
- S190 (= S225) binding
- G191 (= G226) binding
- T192 (= T227) binding
- T193 (= T228) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K232) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H268) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F270) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ L274) binding ; binding ; binding
- K260 (≠ G292) binding
- A309 (≠ G341) binding ; binding ; binding
- Q331 (≠ I363) binding
- G332 (≠ A364) binding ; binding ; binding ; binding ; binding
- T336 (= T368) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V373) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ S374) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D450) binding ; binding ; binding ; binding ; binding
- R435 (= R465) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K467) binding ; binding ; binding ; binding
- K441 (≠ I471) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G473) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G474) binding
- Q446 (≠ N476) binding
- K526 (= K556) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
27% identity, 90% coverage: 45:566/578 of query aligns to 34:529/529 of 5bsvA
- active site: S182 (≠ T224), S202 (vs. gap), H230 (= H268), T329 (= T368), E330 (= E369), K434 (≠ I471), Q439 (≠ N476), K519 (= K556)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H268), Y232 (≠ F270), S236 (≠ L274), A302 (≠ G341), A303 (≠ S342), P304 (= P343), G325 (≠ A364), G327 (= G366), M328 (= M367), T329 (= T368), P333 (= P372), V334 (= V373), D413 (= D450), K430 (= K467), K434 (≠ I471), Q439 (≠ N476)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
27% identity, 90% coverage: 45:566/578 of query aligns to 34:529/529 of 5bsuA
- active site: S182 (≠ T224), S202 (vs. gap), H230 (= H268), T329 (= T368), E330 (= E369), K434 (≠ I471), Q439 (≠ N476), K519 (= K556)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H268), Y232 (≠ F270), S236 (≠ L274), M299 (≠ I338), A302 (≠ G341), A303 (≠ S342), P304 (= P343), G325 (≠ A364), G327 (= G366), M328 (= M367), T329 (= T368), P333 (= P372), D413 (= D450), K430 (= K467), K434 (≠ I471), Q439 (≠ N476)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
27% identity, 90% coverage: 45:566/578 of query aligns to 34:529/529 of 5bstA
- active site: S182 (≠ T224), S202 (vs. gap), H230 (= H268), T329 (= T368), E330 (= E369), K434 (≠ I471), Q439 (≠ N476), K519 (= K556)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H268), Y232 (≠ F270), S236 (≠ L274), A302 (≠ G341), A303 (≠ S342), P304 (= P343), G325 (≠ A364), Y326 (= Y365), G327 (= G366), M328 (= M367), T329 (= T368), P333 (= P372), V334 (= V373), D413 (= D450), K430 (= K467), K434 (≠ I471), Q439 (≠ N476)
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)
30% identity, 92% coverage: 29:559/578 of query aligns to 4:503/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 224:228) binding
- H214 (= H268) binding ; mutation to A: Abolished activity.
- S289 (≠ I338) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ IMA 338:340) binding
- EA 310:311 (≠ IA 363:364) binding
- M314 (= M367) binding
- T315 (= T368) binding
- H319 (≠ P372) binding ; mutation to A: Abolished activity.
- D394 (= D450) binding
- R409 (= R465) binding ; mutation to A: Abolished activity.
- K500 (= K556) binding ; binding ; mutation to A: Abolished activity.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
27% identity, 90% coverage: 45:566/578 of query aligns to 33:528/528 of 5bsrA
- active site: S181 (≠ T224), S201 (vs. gap), H229 (= H268), T328 (= T368), E329 (= E369), K433 (≠ I471), Q438 (≠ N476), K518 (= K556)
- binding adenosine monophosphate: A301 (≠ G341), G326 (= G366), T328 (= T368), D412 (= D450), K429 (= K467), K433 (≠ I471), Q438 (≠ N476)
- binding coenzyme a: L102 (≠ A114), P226 (= P265), H229 (= H268), Y231 (≠ F270), F253 (= F293), K435 (≠ G473), G436 (= G474), F437 (≠ E475), F498 (≠ H536)
5ie2A Crystal structure of a plant enzyme (see paper)
30% identity, 92% coverage: 29:559/578 of query aligns to 4:498/506 of 5ie2A
- active site: T165 (= T224), S185 (≠ N244), H209 (= H268), T310 (= T368), E311 (= E369), N410 (≠ I471), K415 (≠ N476), K495 (= K556)
- binding adenosine-5'-triphosphate: T165 (= T224), S166 (= S225), G167 (= G226), T168 (= T227), T169 (= T228), S284 (≠ I338), A285 (≠ M339), S286 (≠ A340), Y307 (= Y365), A308 (≠ G366), M309 (= M367), T310 (= T368), D389 (= D450), L401 (≠ I462), R404 (= R465), K495 (= K556)
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
29% identity, 90% coverage: 47:567/578 of query aligns to 37:536/539 of 2d1sA
- active site: S194 (≠ T224), R214 (≠ N244), H241 (= H268), T339 (= T368), E340 (= E369), K439 (≠ I471), Q444 (≠ N476), K525 (= K556)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S194 (≠ T224), S195 (= S225), H241 (= H268), F243 (= F270), T247 (vs. gap), I282 (≠ H311), G312 (= G341), A313 (≠ S342), P314 (= P343), Q334 (≠ I363), G335 (≠ A364), Y336 (= Y365), G337 (= G366), L338 (≠ M367), T339 (= T368), S343 (≠ P372), A344 (vs. gap), D418 (= D450), R433 (= R465), K525 (= K556)
Query Sequence
>Ac3H11_3009 FitnessBrowser__acidovorax_3H11:Ac3H11_3009
VTSSAAATNSAPLVDSHARGATDVPLIEQTIGAFFADMVARQPEREALVSVHQGRRYTYA
QLQTEAHRLASALLGMGLTPGDRVGIWSHNNAEWVLMQLATAQVGLVLVNINPAYRTAEV
EYALNKVGCKLLVSMARFKTSDYLGMLRELAPEWQGQQPGHLQAAKLPQLKTVVWIDDEA
GQGADEPGLLRFTELIARGNAADPRLAQVAAGLQATDPINIQFTSGTTGFPKGATLTHRN
ILNNGFFIGECMKLTPADRLCIPVPLYHCFGMVLGNLACFTHGATIVYPNDGFDPLTVLQ
TVQDERCTGLHGVPTMFIAELDHPRFAEFNLSTLRTGIMAGSPCPTEVMKRVVEQMNLRE
ITIAYGMTETSPVSCQSSTDTPLSKRVSTVGQVQPHLEVKIVDPDTGAVVPIGQRGEFCT
KGYSVMHGYWGDEAKTREAIDEGGWMHTGDLATMDAEGYVNIVGRIKDMVIRGGENIYPR
EIEEFLYRHPQVQDVQVVGVPDQKYGEELCAWIIAKPGTQPTEDDIRAFCKGQIAHYKVP
RYIRFVTSFPMTVTGKIQKFKIRDEMKDQLGLEEQKTA
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