SitesBLAST
Comparing WP_015949835.1 NCBI__GCF_000429905.1:WP_015949835.1 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)
43% identity, 99% coverage: 2:553/555 of query aligns to 4:538/541 of Q5SKN9
- T184 (= T195) binding Mg(2+)
- G302 (≠ A314) binding tetradecanoyl-AMP
- Q322 (≠ H335) binding tetradecanoyl-AMP
- G323 (≠ A336) binding tetradecanoyl-AMP
- T327 (= T340) binding tetradecanoyl-AMP
- E328 (= E341) binding Mg(2+)
- D418 (= D431) binding tetradecanoyl-AMP
- K435 (= K448) binding tetradecanoyl-AMP
- K439 (= K452) binding tetradecanoyl-AMP
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
41% identity, 99% coverage: 6:553/555 of query aligns to 1:507/510 of 1v26B
- active site: T177 (= T195), H197 (= H215), H223 (= H239), T320 (= T340), E321 (= E341), K432 (= K452), W437 (= W457)
- binding adenosine monophosphate: G295 (≠ A314), S296 (≠ T315), A297 (≠ E316), G316 (≠ A336), Y317 (= Y337), G318 (= G338), L319 (≠ A339), T320 (= T340), D411 (= D431), K428 (= K448), K432 (= K452), W437 (= W457)
- binding magnesium ion: T177 (= T195), E321 (= E341)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
40% identity, 99% coverage: 7:553/555 of query aligns to 2:488/491 of 1v25A
- active site: T177 (= T195), H197 (= H215), H223 (= H239), T320 (= T340), E321 (= E341), K432 (= K452), W437 (= W457)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H239), V224 (≠ A240), G295 (≠ A314), S296 (≠ T315), A297 (≠ E316), Y317 (= Y337), G318 (= G338), L319 (≠ A339), T320 (= T340), D411 (= D431), I423 (= I443), K432 (= K452), W437 (= W457)
- binding magnesium ion: T177 (= T195), E321 (= E341)
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)
37% identity, 97% coverage: 16:551/555 of query aligns to 9:535/539 of P0DX84
- H231 (= H239) mutation to A: Retains 74% of wild-type activity.
- W235 (= W243) mutation to A: Almost completely abolishes the activity.
- G302 (≠ S312) mutation to P: Almost completely abolishes the activity.
- G303 (= G313) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y337) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P344) mutation to A: Retains 69% of wild-type activity.
- R432 (= R446) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K448) mutation to A: Retains 36% of wild-type activity.
- D435 (= D449) mutation to A: Retains 76% of wild-type activity.
- K438 (= K452) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G454) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G455) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E456) mutation to A: Retains 27% of wild-type activity.
- W443 (= W457) mutation to A: Retains 60% of wild-type activity.
- E474 (= E488) mutation to A: Retains 33% of wild-type activity.
- K523 (= K539) 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 (= K542) 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)
36% identity, 97% coverage: 16:551/555 of query aligns to 9:535/538 of 6ijbB
- active site: T185 (= T195), H205 (= H215), H231 (= H239), S329 (≠ T340), E330 (= E341), K438 (= K452), W443 (= W457), A523 (≠ K539)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W243), G303 (= G313), A325 (= A336), W326 (≠ Y337), G327 (= G338), M328 (≠ A339)
- binding adenosine monophosphate: G303 (= G313), A304 (= A314), A305 (≠ T315), H324 (= H335), W326 (≠ Y337), G327 (= G338), M328 (≠ A339), S329 (≠ T340), Q359 (= Q371), D417 (= D431)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
36% identity, 97% coverage: 16:551/555 of query aligns to 9:532/533 of 6ihkB
- active site: T185 (= T198), H202 (= H215), H228 (= H239), S326 (≠ T340), E327 (= E341), K435 (= K452), W440 (= W457), K520 (= K539)
- binding adenosine-5'-diphosphate: H228 (= H239), G300 (= G313), A301 (= A314), A302 (≠ T315), H321 (= H335), A322 (= A336), W323 (≠ Y337), G324 (= G338), M325 (≠ A339), S326 (≠ T340), Q356 (= Q371), D414 (= D431), R429 (= R446), K520 (= K539)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
35% identity, 96% coverage: 15:549/555 of query aligns to 8:529/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G313), G293 (≠ A314), A294 (≠ T315), A295 (≠ E316), G314 (≠ A336), Y315 (= Y337), M317 (≠ A339), S318 (≠ T340), D408 (= D431), R423 (= R446)
- binding 4'-phosphopantetheine: R93 (= R104), P220 (= P236), H223 (= H239)
8i49A Acyl-acp synthetase structure bound to atp
35% identity, 96% coverage: 15:549/555 of query aligns to 8:529/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
35% identity, 96% coverage: 15:549/555 of query aligns to 8:529/530 of 8i22A
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
35% identity, 96% coverage: 15:549/555 of query aligns to 6:527/528 of 8i6mA
- binding adenosine monophosphate: G291 (≠ A314), A293 (≠ E316), G312 (≠ A336), Y313 (= Y337), G314 (= G338), M315 (≠ A339), S316 (≠ T340), D406 (= D431), R421 (= R446)
- binding magnesium ion: M315 (≠ A339), S316 (≠ T340), E317 (= E341)
8i51A Acyl-acp synthetase structure bound to amp-mc7
35% identity, 96% coverage: 15:549/555 of query aligns to 6:527/528 of 8i51A
- binding adenosine monophosphate: G291 (≠ A314), A293 (≠ E316), Y313 (= Y337), M315 (≠ A339), S316 (≠ T340), D406 (= D431), R421 (= R446)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W243), G290 (= G313), G312 (≠ A336), G314 (= G338), M315 (≠ A339), P320 (= P344), I321 (≠ L345)
8jylA Acyl-acp synthetase structure bound to c10-ams
35% identity, 96% coverage: 15:549/555 of query aligns to 6:527/527 of 8jylA
- binding magnesium ion: S316 (≠ T340), E317 (= E341)
- binding [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl N-decanoylsulfamate: W225 (= W243), G290 (= G313), G291 (≠ A314), A292 (≠ T315), A293 (≠ E316), G312 (≠ A336), Y313 (= Y337), G314 (= G338), M315 (≠ A339), S316 (≠ T340), I321 (≠ L345), D406 (= D431), R421 (= R446), K427 (= K452), W432 (= W457)
8i8dA Acyl-acp synthetase structure bound to mc7-acp
35% identity, 96% coverage: 15:549/555 of query aligns to 8:529/529 of 8i8dA
- binding adenosine monophosphate: G292 (= G313), G293 (≠ A314), A295 (≠ E316), G314 (≠ A336), Y315 (= Y337), G316 (= G338), M317 (≠ A339), S318 (≠ T340), D408 (= D431), K429 (= K452)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H239), W227 (= W243), G292 (= G313), G316 (= G338), P322 (= P344)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R104), P220 (= P236), H223 (= H239), I269 (= I288), G432 (= G455)
8i3iA Acyl-acp synthetase structure bound to amp-pnp in the presence of mgcl2
35% identity, 96% coverage: 15:549/555 of query aligns to 8:521/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T195), G174 (= G197), T175 (= T198), T176 (= T199), K180 (= K203), G293 (≠ A314), A294 (≠ T315), A295 (≠ E316), Y315 (= Y337), M317 (≠ A339), S318 (≠ T340), D408 (= D431), R423 (= R446)
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
29% identity, 90% coverage: 48:546/555 of query aligns to 31:484/486 of 8wevA
Sites not aligning to the query:
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)
27% identity, 90% coverage: 46:546/555 of query aligns to 64:570/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
27% identity, 92% coverage: 46:553/555 of query aligns to 28:505/506 of 4gxqA
- active site: T163 (= T195), N183 (≠ H215), H207 (= H239), T303 (= T340), E304 (= E341), I403 (≠ K452), N408 (≠ W457), A491 (≠ K539)
- binding adenosine-5'-triphosphate: T163 (= T195), S164 (≠ T196), G165 (= G197), T166 (= T198), T167 (= T199), H207 (= H239), S277 (≠ T315), A278 (≠ E316), P279 (= P317), E298 (≠ H335), M302 (≠ A339), T303 (= T340), D382 (= D431), R397 (= R446)
- binding carbonate ion: H207 (= H239), S277 (≠ T315), R299 (≠ A336), G301 (= G338)
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, 90% coverage: 47:547/555 of query aligns to 64:548/556 of Q9S725
- K211 (= K203) mutation to S: Drastically reduces the activity.
- M293 (≠ A283) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ S312) mutation K->L,A: Affects the substrate specificity.
- E401 (= E399) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ L401) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R446) mutation to Q: Drastically reduces the activity.
- K457 (≠ G454) mutation to S: Drastically reduces the activity.
- K540 (= K539) mutation to N: Abolishes the activity.
5wm6A Crystal structure of cahj in complex with benzoyl adenylate (see paper)
29% identity, 91% coverage: 40:543/555 of query aligns to 47:528/535 of 5wm6A
- active site: S193 (≠ T195), N213 (≠ H215), H237 (= H239), A336 (≠ T340), E337 (= E341), N437 (≠ K452), K442 (≠ W457), K524 (= K539)
- binding magnesium ion: S301 (≠ T306), L303 (≠ V308), G326 (= G330)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: F239 (≠ L241), G310 (≠ A314), S311 (≠ T315), K312 (≠ E316), V332 (≠ A336), F333 (≠ Y337), G334 (= G338), M335 (≠ A339), A336 (≠ T340), D416 (= D431), K433 (= K448), K442 (≠ W457)
5wm2A Crystal structure of cahj in complex with salicylic acid and amp (see paper)
29% identity, 91% coverage: 40:543/555 of query aligns to 47:528/536 of 5wm2A
- active site: S193 (≠ T195), N213 (≠ H215), H237 (= H239), A336 (≠ T340), E337 (= E341), N437 (≠ K452), K442 (≠ W457), K524 (= K539)
- binding adenosine monophosphate: G310 (≠ A314), S311 (≠ T315), K312 (≠ E316), V332 (≠ A336), F333 (≠ Y337), G334 (= G338), M335 (≠ A339), A336 (≠ T340), E337 (= E341), D416 (= D431), V428 (≠ I443), K433 (= K448), K442 (≠ W457)
Query Sequence
>WP_015949835.1 NCBI__GCF_000429905.1:WP_015949835.1
MELIKGFPATSQDRYPLNVTNIIKHSVRNYGPQEIASRRLDGSMFRYTYSDAYERMQRLA
NGLTKLGVKVGDRVGVLAWNSNENYEVYFGVPGMGAVMLLLNLRLTPQDLAYVVEHSGCE
YIIVDETLLPIAHALAPLCPQIKGYVVITMPGKKMSDVETPLENTHSYEELLAESDPVFD
WPMMEETSAYAACYTTGTTGKPKGVYYSHRDVYLHSMCIGMNTGMNVKDTCCQIVPMFHA
LGWGLPQAATLVGSRIILPGMYTLETLDSLSKLIVDEGVTMSAGAPAIFMPLLEYIRNLE
ERPDLTGVRLLSGATEPPVSMMKGFWDMTGAEIIHAYGATETTPLVTINRLMPWLETSLS
EDERWNLKKKQGFAVGGLDVKVVDATLKDVAHDGKTPGEILIRGPWITGAYHNAPGSEAS
FTEDGFWRSGDVGTMDENGYLKITDRVKDVIKSGGEWISSVDMENEIISHNDVLDAAVVG
VEHPKWQERPLALVVLRDDAKGKVNADDIRAHLSNVFAKWQLPDEVLFVDEIPKTSVGKT
DKKVIRAEHKDMYSE
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