SitesBLAST
Comparing WP_028999882.1 NCBI__GCF_000430725.1:WP_028999882.1 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)
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)
40% identity, 95% coverage: 25:542/547 of query aligns to 22:536/541 of Q5SKN9
- T184 (= T193) binding Mg(2+)
- G302 (= G308) binding tetradecanoyl-AMP
- Q322 (≠ H328) binding tetradecanoyl-AMP
- G323 (≠ V329) binding tetradecanoyl-AMP
- T327 (= T333) binding tetradecanoyl-AMP
- E328 (= E334) binding Mg(2+)
- D418 (= D425) binding tetradecanoyl-AMP
- K435 (= K442) binding tetradecanoyl-AMP
- K439 (≠ I446) binding tetradecanoyl-AMP
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
38% identity, 94% coverage: 21:532/547 of query aligns to 11:502/510 of 1v26B
- active site: T177 (= T193), H197 (≠ N213), H223 (= H237), T320 (= T333), E321 (= E334), K432 (≠ I446), W437 (≠ N451)
- binding adenosine monophosphate: G295 (= G308), S296 (≠ A309), A297 (= A310), G316 (≠ V329), Y317 (= Y330), G318 (= G331), L319 (= L332), T320 (= T333), D411 (= D425), K428 (= K442), K432 (≠ I446), W437 (≠ N451)
- binding magnesium ion: T177 (= T193), E321 (= E334)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
40% identity, 86% coverage: 21:488/547 of query aligns to 11:464/491 of 1v25A
- active site: T177 (= T193), H197 (≠ N213), H223 (= H237), T320 (= T333), E321 (= E334), K432 (≠ I446), W437 (≠ N451)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H237), V224 (≠ C238), G295 (= G308), S296 (≠ A309), A297 (= A310), Y317 (= Y330), G318 (= G331), L319 (= L332), T320 (= T333), D411 (= D425), I423 (= I437), K432 (≠ I446), W437 (≠ N451)
- binding magnesium ion: T177 (= T193), E321 (= E334)
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)
35% identity, 91% coverage: 46:543/547 of query aligns to 39:536/539 of P0DX84
- H231 (= H237) mutation to A: Retains 74% of wild-type activity.
- W235 (= W241) mutation to A: Almost completely abolishes the activity.
- G302 (≠ A307) mutation to P: Almost completely abolishes the activity.
- G303 (= G308) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y330) mutation to A: Retains 7.7% of wild-type activity.
- P333 (≠ G337) mutation to A: Retains 69% of wild-type activity.
- R432 (= R440) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K442) mutation to A: Retains 36% of wild-type activity.
- D435 (= D443) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I446) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G448) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G449) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E450) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N451) mutation to A: Retains 60% of wild-type activity.
- E474 (= E482) mutation to A: Retains 33% of wild-type activity.
- K523 (= K530) 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 (= K533) 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)
35% identity, 91% coverage: 46:543/547 of query aligns to 39:536/538 of 6ijbB
- active site: T185 (= T193), H205 (≠ N213), H231 (= H237), S329 (≠ T333), E330 (= E334), K438 (≠ I446), W443 (≠ N451), A523 (≠ K530)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W241), G303 (= G308), A325 (≠ V329), W326 (≠ Y330), G327 (= G331), M328 (≠ L332)
- binding adenosine monophosphate: G303 (= G308), A304 (= A309), A305 (= A310), H324 (= H328), W326 (≠ Y330), G327 (= G331), M328 (≠ L332), S329 (≠ T333), Q359 (= Q363), D417 (= D425)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
35% identity, 91% coverage: 46:543/547 of query aligns to 39:533/533 of 6ihkB
- active site: T185 (= T193), H202 (≠ N213), H228 (= H237), S326 (≠ T333), E327 (= E334), K435 (≠ I446), W440 (≠ N451), K520 (= K530)
- binding adenosine-5'-diphosphate: H228 (= H237), G300 (= G308), A301 (= A309), A302 (= A310), H321 (= H328), A322 (≠ V329), W323 (≠ Y330), G324 (= G331), M325 (≠ L332), S326 (≠ T333), Q356 (= Q363), D414 (= D425), R429 (= R440), K520 (= K530)
8i3iA Acyl-acp synthetase structure bound to amp-pnp in the presence of mgcl2 (see paper)
32% identity, 93% coverage: 31:538/547 of query aligns to 20:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T193), G174 (= G195), T175 (= T196), T176 (= T197), K180 (= K201), G293 (= G308), A294 (= A309), A295 (= A310), Y315 (= Y330), M317 (≠ L332), S318 (≠ T333), D408 (= D425), R423 (= R440)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1 (see paper)
32% identity, 93% coverage: 31:538/547 of query aligns to 18:525/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G308), A293 (= A310), G312 (≠ V329), Y313 (= Y330), G314 (= G331), M315 (≠ L332), S316 (≠ T333), D406 (= D425), R421 (= R440)
- binding magnesium ion: M315 (≠ L332), S316 (≠ T333), E317 (= E334)
8i51A Acyl-acp synthetase structure bound to amp-mc7 (see paper)
32% identity, 93% coverage: 31:538/547 of query aligns to 18:525/528 of 8i51A
- binding adenosine monophosphate: G291 (= G308), A293 (= A310), Y313 (= Y330), M315 (≠ L332), S316 (≠ T333), D406 (= D425), R421 (= R440)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W241), G290 (≠ A307), G312 (≠ V329), G314 (= G331), M315 (≠ L332), P320 (= P338), I321 (≠ A339)
8jylA Acyl-acp synthetase structure bound to c10-ams (see paper)
32% identity, 93% coverage: 31:538/547 of query aligns to 18:525/527 of 8jylA
- binding magnesium ion: S316 (≠ T333), E317 (= E334)
- binding [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl N-decanoylsulfamate: W225 (= W241), G290 (≠ A307), G291 (= G308), A292 (= A309), A293 (= A310), G312 (≠ V329), Y313 (= Y330), G314 (= G331), M315 (≠ L332), S316 (≠ T333), I321 (≠ P338), D406 (= D425), R421 (= R440), K427 (≠ I446), W432 (≠ N451)
8i8dA Acyl-acp synthetase structure bound to mc7-acp (see paper)
32% identity, 93% coverage: 31:538/547 of query aligns to 20:527/529 of 8i8dA
- binding adenosine monophosphate: G292 (≠ A307), G293 (= G308), A295 (= A310), G314 (≠ V329), Y315 (= Y330), G316 (= G331), M317 (≠ L332), S318 (≠ T333), D408 (= D425), K429 (≠ I446)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H237), W227 (= W241), G292 (≠ A307), G316 (= G331), P322 (= P338)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R104), P220 (= P234), H223 (= H237), I269 (≠ V283), G432 (= G449)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp (see paper)
32% identity, 93% coverage: 31:538/547 of query aligns to 20:527/530 of 8i8eA
- binding adenosine monophosphate: G292 (≠ A307), G293 (= G308), A294 (= A309), A295 (= A310), G314 (≠ V329), Y315 (= Y330), M317 (≠ L332), S318 (≠ T333), D408 (= D425), R423 (= R440)
- binding 4'-phosphopantetheine: R93 (= R104), P220 (= P234), H223 (= H237)
8i49A Acyl-acp synthetase structure bound to atp (see paper)
32% identity, 93% coverage: 31:538/547 of query aligns to 20:527/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
32% identity, 93% coverage: 31:538/547 of query aligns to 20:527/530 of 8i22A
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
34% identity, 94% coverage: 25:538/547 of query aligns to 8:485/486 of 8wevA
5ie2A Crystal structure of a plant enzyme (see paper)
31% identity, 94% coverage: 27:538/547 of query aligns to 10:503/506 of 5ie2A
- active site: T165 (= T193), S185 (≠ N217), H209 (= H237), T310 (= T333), E311 (= E334), N410 (≠ I446), K415 (≠ N451), K495 (= K530)
- binding adenosine-5'-triphosphate: T165 (= T193), S166 (= S194), G167 (= G195), T168 (= T196), T169 (= T197), S284 (≠ A309), A285 (= A310), S286 (≠ P311), Y307 (= Y330), A308 (≠ G331), M309 (≠ L332), T310 (= T333), D389 (= D425), L401 (≠ I437), R404 (= R440), K495 (= K530)
5ie3A Crystal structure of a plant enzyme (see paper)
31% identity, 94% coverage: 27:538/547 of query aligns to 10:501/504 of 5ie3A
- active site: T163 (= T193), S183 (≠ N217), H207 (= H237), T308 (= T333), E309 (= E334), N408 (≠ I446), K413 (≠ N451), K493 (= K530)
- binding adenosine monophosphate: S164 (= S194), S282 (≠ A309), A283 (= A310), S284 (≠ P311), Y305 (= Y330), A306 (≠ G331), M307 (≠ L332), T308 (= T333), D387 (= D425), L399 (≠ I437), R402 (= R440), K493 (= K530)
- binding oxalic acid: V208 (≠ C238), S282 (≠ A309), A306 (≠ G331), M307 (≠ L332), H312 (≠ E346), K493 (= K530)
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, 94% coverage: 27:538/547 of query aligns to 10:508/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 193:197) binding ATP
- H214 (= H237) binding ATP; mutation to A: Abolished activity.
- S289 (≠ A309) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ AAP 309:311) binding ATP
- EA 310:311 (≠ HV 328:329) binding ATP
- M314 (≠ L332) binding oxalate
- T315 (= T333) binding ATP
- H319 (≠ E346) binding oxalate; mutation to A: Abolished activity.
- D394 (= D425) binding ATP
- R409 (= R440) binding ATP; mutation to A: Abolished activity.
- K500 (= K530) binding ATP; binding oxalate; 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)
28% identity, 97% coverage: 11:538/547 of query aligns to 35:571/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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, 90% coverage: 48:540/547 of query aligns to 61:545/559 of Q67W82
- G395 (vs. gap) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
Query Sequence
>WP_028999882.1 NCBI__GCF_000430725.1:WP_028999882.1
MTRTNPYEIGLDKNAANYVPLSPLSYLERAAAVYPQRLALVHGALRQTWRETFERCRRLA
SALQRRGVGRGDTVAAMLPNVPAMFEAHFGVPAAGAVLNTLNTRLDAESIAFMLQHGEAK
VLLTDREFAGVVSKALALLGEQRPLVVEVEDELAPPGPRLGEMSYEELLAGGDPAAPWTL
PGDEWDAIALNYTSGTTGNPKGVVTHHRGAYLNAASNAIGWSLPQHPTYLWTLPMFHCNG
WCFPWTLALVAGTSVCLRKVDPALIYPLIREHHVTHMCGAPIVYGLLIHAPAALREGIGH
EIKGLIAGAAPPAAVIEGCERIGIAITHVYGLTEVYGPAALCAQQEEWASLPLPERARLN
ARQGVPYPLQQAVTVLDTATMQPVPADGQTLGEVCFRGNAVMKGYLKNPAATQEAFEGGW
FRTGDLAVLHPDGYVKITDRSKDVIISGGENISSLEVEDVLHRHPDVMLAAVVAQPDPKW
GEVPCAFVEVKLGSTVTEDELIEFCRGHLARFKAPKRIVFGELPKTSTGKIQKFVLRQAL
KSASAIG
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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