SitesBLAST
Comparing GFF3324 PS417_17010 AMP-binding protein 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)
40% identity, 99% coverage: 7:544/544 of query aligns to 24:581/590 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)
32% identity, 94% coverage: 26:534/544 of query aligns to 29:551/561 of P69451
- Y213 (= Y194) mutation to A: Loss of activity.
- T214 (= T195) mutation to A: 10% of wild-type activity.
- G216 (= G197) mutation to A: Decreases activity.
- T217 (= T198) mutation to A: Decreases activity.
- G219 (= G200) mutation to A: Decreases activity.
- K222 (= K203) mutation to A: Decreases activity.
- E361 (= E340) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 90% coverage: 47:534/544 of query aligns to 28:499/506 of 4gxqA
- active site: T163 (= T195), N183 (= N215), H207 (= H239), T303 (= T339), E304 (= E340), I403 (= I441), N408 (= N446), A491 (≠ K526)
- binding adenosine-5'-triphosphate: T163 (= T195), S164 (= S196), G165 (= G197), T166 (= T198), T167 (= T199), H207 (= H239), S277 (≠ G312), A278 (= A313), P279 (≠ T314), E298 (≠ Q333), M302 (= M338), T303 (= T339), D382 (= D420), R397 (= R435)
- binding carbonate ion: H207 (= H239), S277 (≠ G312), R299 (≠ A335), G301 (= G337)
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)
30% identity, 94% coverage: 22:534/544 of query aligns to 4:495/503 of P9WQ37
- R9 (≠ D27) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D35) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K203) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T226) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ Q228) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C240) 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 (≠ G242) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ M245) 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 (≠ H277) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G337) 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 (= W415) 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 (= D420) 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 (= R435) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R442) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G444) 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.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
29% identity, 92% coverage: 34:534/544 of query aligns to 19:495/502 of 3r44A
Sites not aligning to the query:
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
29% identity, 93% coverage: 28:535/544 of query aligns to 29:536/539 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 (= H239), F245 (= F241), T249 (≠ G246), G314 (= G312), A315 (= A313), P316 (≠ T314), G337 (≠ A335), Y338 (= Y336), G339 (= G337), L340 (≠ M338), T341 (= T339), S345 (≠ P343), A346 (≠ V344), D420 (= D420), I432 (= I432), K527 (= K526)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F241), R335 (≠ Q333), G337 (≠ A335), G339 (= G337), L340 (≠ M338), A346 (≠ V344)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
29% identity, 93% coverage: 28:535/544 of query aligns to 29:536/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H239), F245 (= F241), T249 (≠ G246), G314 (= G312), A315 (= A313), P316 (≠ T314), G337 (≠ A335), Y338 (= Y336), G339 (= G337), L340 (≠ M338), T341 (= T339), A346 (≠ V344), D420 (= D420), I432 (= I432), K527 (= K526)
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)
26% identity, 91% coverage: 49:541/544 of query aligns to 59:545/546 of Q84P21
- K530 (= K526) mutation to N: Lossed enzymatic activity.
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
29% identity, 90% coverage: 48:535/544 of query aligns to 47:534/539 of 2d1sA
- active site: S194 (≠ T195), R214 (≠ N215), H241 (= H239), T339 (= T339), E340 (= E340), K439 (≠ I441), Q444 (≠ N446), K525 (= K526)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S194 (≠ T195), S195 (= S196), H241 (= H239), F243 (= F241), T247 (≠ M245), I282 (≠ Y282), G312 (= G312), A313 (= A313), P314 (≠ T314), Q334 (≠ I334), G335 (≠ A335), Y336 (= Y336), G337 (= G337), L338 (≠ M338), T339 (= T339), S343 (≠ P343), A344 (≠ V344), D418 (= D420), R433 (= R435), K525 (= K526)
2d1rA Crystal structure of the thermostable japanese firefly luciferase complexed with oxyluciferin and amp (see paper)
29% identity, 90% coverage: 48:535/544 of query aligns to 47:534/539 of 2d1rA
- active site: S194 (≠ T195), R214 (≠ N215), H241 (= H239), T339 (= T339), E340 (= E340), K439 (≠ I441), Q444 (≠ N446), K525 (= K526)
- binding adenosine monophosphate: S194 (≠ T195), S195 (= S196), H241 (= H239), G312 (= G312), A313 (= A313), P314 (≠ T314), G335 (≠ A335), Y336 (= Y336), G337 (= G337), L338 (≠ M338), T339 (= T339), D418 (= D420), K525 (= K526)
- binding 2-(6-hydroxy-1,3-benzothiazol-2-yl)-1,3-thiazol-4(5h)-one: H241 (= H239), F243 (= F241), T247 (≠ M245), G335 (≠ A335), G337 (= G337), L338 (≠ M338), A344 (≠ V344)
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)
29% identity, 93% coverage: 28:533/544 of query aligns to 33:533/542 of O24146
- S189 (≠ T195) binding
- S190 (= S196) binding
- G191 (= G197) binding
- T192 (= T198) binding
- T193 (= T199) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K203) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H239) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F241) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ G246) binding ; binding ; binding
- K260 (≠ G263) binding
- A309 (≠ G312) binding ; binding ; binding
- Q331 (≠ I334) binding
- G332 (≠ A335) binding ; binding ; binding ; binding ; binding
- T336 (= T339) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V344) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ Q347) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D420) binding ; binding ; binding ; binding ; binding
- R435 (= R435) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K437) binding ; binding ; binding ; binding
- K441 (≠ I441) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G443) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G444) binding
- Q446 (≠ N446) binding
- K526 (= K526) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
29% identity, 93% coverage: 28:533/544 of query aligns to 25:525/528 of 5bsrA
- active site: S181 (≠ T195), S201 (≠ N215), H229 (= H239), T328 (= T339), E329 (= E340), K433 (≠ I441), Q438 (≠ N446), K518 (= K526)
- binding adenosine monophosphate: A301 (≠ G312), G326 (= G337), T328 (= T339), D412 (= D420), K429 (= K437), K433 (≠ I441), Q438 (≠ N446)
- binding coenzyme a: L102 (≠ A105), P226 (= P236), H229 (= H239), Y231 (≠ F241), F253 (= F264), K435 (≠ G443), G436 (= G444), F437 (≠ E445), F498 (≠ H506)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
29% identity, 93% coverage: 28:533/544 of query aligns to 26:526/530 of 5bsmA
- active site: S182 (≠ T195), S202 (≠ N215), H230 (= H239), T329 (= T339), E330 (= E340), K434 (≠ I441), Q439 (≠ N446), K519 (= K526)
- binding adenosine-5'-triphosphate: S182 (≠ T195), S183 (= S196), G184 (= G197), T185 (= T198), T186 (= T199), K190 (= K203), H230 (= H239), A302 (≠ G312), A303 (= A313), P304 (≠ T314), Y326 (= Y336), G327 (= G337), M328 (= M338), T329 (= T339), D413 (= D420), I425 (= I432), R428 (= R435), K519 (= K526)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
29% identity, 93% coverage: 28:533/544 of query aligns to 26:526/529 of 5bsvA
- active site: S182 (≠ T195), S202 (≠ N215), H230 (= H239), T329 (= T339), E330 (= E340), K434 (≠ I441), Q439 (≠ N446), 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 (= H239), Y232 (≠ F241), S236 (≠ G246), A302 (≠ G312), A303 (= A313), P304 (≠ T314), G325 (≠ A335), G327 (= G337), M328 (= M338), T329 (= T339), P333 (= P343), V334 (= V344), D413 (= D420), K430 (= K437), K434 (≠ I441), Q439 (≠ N446)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
29% identity, 93% coverage: 28:533/544 of query aligns to 26:526/529 of 5bsuA
- active site: S182 (≠ T195), S202 (≠ N215), H230 (= H239), T329 (= T339), E330 (= E340), K434 (≠ I441), Q439 (≠ N446), K519 (= K526)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H239), Y232 (≠ F241), S236 (≠ G246), M299 (≠ I309), A302 (≠ G312), A303 (= A313), P304 (≠ T314), G325 (≠ A335), G327 (= G337), M328 (= M338), T329 (= T339), P333 (= P343), D413 (= D420), K430 (= K437), K434 (≠ I441), Q439 (≠ N446)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
29% identity, 93% coverage: 28:533/544 of query aligns to 26:526/529 of 5bstA
- active site: S182 (≠ T195), S202 (≠ N215), H230 (= H239), T329 (= T339), E330 (= E340), K434 (≠ I441), Q439 (≠ N446), K519 (= K526)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H239), Y232 (≠ F241), S236 (≠ G246), A302 (≠ G312), A303 (= A313), P304 (≠ T314), G325 (≠ A335), Y326 (= Y336), G327 (= G337), M328 (= M338), T329 (= T339), P333 (= P343), V334 (= V344), D413 (= D420), K430 (= K437), K434 (≠ I441), Q439 (≠ N446)
5ie3A Crystal structure of a plant enzyme (see paper)
28% identity, 94% coverage: 21:529/544 of query aligns to 5:496/504 of 5ie3A
- active site: T163 (= T195), S183 (≠ N215), H207 (= H239), T308 (= T339), E309 (= E340), N408 (≠ I441), K413 (≠ N446), K493 (= K526)
- binding adenosine monophosphate: S164 (= S196), S282 (≠ A311), A283 (≠ G312), S284 (≠ A313), Y305 (= Y336), A306 (≠ G337), M307 (= M338), T308 (= T339), D387 (= D420), L399 (≠ I432), R402 (= R435), K493 (= K526)
- binding oxalic acid: V208 (≠ C240), S282 (≠ A311), A306 (≠ G337), M307 (= M338), H312 (≠ P343), K493 (= K526)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
28% identity, 90% coverage: 48:534/544 of query aligns to 46:527/528 of 3ni2A
- active site: S182 (≠ T195), S202 (≠ N215), H230 (= H239), T329 (= T339), E330 (= E340), K434 (≠ I441), Q439 (≠ N446), K519 (= K526)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F241), S236 (≠ M245), G302 (= G312), A303 (= A313), P304 (≠ T314), G325 (≠ A335), G327 (= G337), T329 (= T339), P333 (= P343), V334 (= V344), D413 (= D420), K430 (= K437), K434 (≠ I441), Q439 (≠ N446)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
28% identity, 90% coverage: 48:534/544 of query aligns to 46:527/528 of 3a9vA
- active site: S182 (≠ T195), S202 (≠ N215), H230 (= H239), T329 (= T339), E330 (= E340), K434 (≠ I441), Q439 (≠ N446), K519 (= K526)
- binding adenosine monophosphate: H230 (= H239), G302 (= G312), A303 (= A313), P304 (≠ T314), Y326 (= Y336), G327 (= G337), M328 (= M338), T329 (= T339), D413 (= D420), K430 (= K437), K434 (≠ I441), Q439 (≠ N446)
5ie2A Crystal structure of a plant enzyme (see paper)
28% identity, 94% coverage: 21:529/544 of query aligns to 5:498/506 of 5ie2A
- active site: T165 (= T195), S185 (≠ N215), H209 (= H239), T310 (= T339), E311 (= E340), N410 (≠ I441), K415 (≠ N446), K495 (= K526)
- binding adenosine-5'-triphosphate: T165 (= T195), S166 (= S196), G167 (= G197), T168 (= T198), T169 (= T199), S284 (≠ A311), A285 (≠ G312), S286 (≠ A313), Y307 (= Y336), A308 (≠ G337), M309 (= M338), T310 (= T339), D389 (= D420), L401 (≠ I432), R404 (= R435), K495 (= K526)
Query Sequence
>GFF3324 PS417_17010 AMP-binding protein
MDQPNQSYSRGSQDKTLLAMTIGQAFDRTVAQFPDGEALVVRHQQRRYTWRQLAETVDLH
ARAFLALGMQTGDRLGIWAPNCAEWCISQIASAKLGVILVNINPAYRSSELEYVLKQSGC
QWLVCAGSFKTSDYHAMLQALNPDLRGMISLDPSPPPGFLPWAQLAALGTGIPLEQLHSR
QTSLHFDQAVNIQYTSGTTGFPKGATLSHHNILNNGYMVGESLGLTAQDRLVIPVPLYHC
FGMVMGNLGCITHGTTMIYPNDGFDPLLTLTAVAEEHATGLYGVPTMFIAMLDHPQLGGF
DLSSLRTGIMAGATCPIEVMRRVISEMHMSEVQIAYGMTETSPVSLQTGADDDLERRVTT
VGRTQPQLENKIIDADGNTVARGEIGELCTRGYSVMLGYWNNPDATREAIDDAGWMHTGD
LASMDAHGYVCIAGRNKDMIIRGGENVYPRELEEFFFTHPAVADVQVIGIPDERYGEAIV
AWVKFHPGHVANELELQTWCKGRIAHFKTPKHFKFVEEFPMTVTGKIQKFRMREISIQEL
KNAL
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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