SitesBLAST
Comparing Dsui_2808 FitnessBrowser__PS:Dsui_2808 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
8i3iA Acyl-acp synthetase structure bound to amp-pnp
32% identity, 91% coverage: 40:544/552 of query aligns to 24:520/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T198), G174 (= G200), T175 (= T201), T176 (= T202), K180 (= K206), G293 (≠ A313), A294 (= A314), A295 (≠ P315), Y315 (= Y335), M317 (≠ L337), S318 (≠ T338), D408 (= D430), R423 (= R445)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
32% identity, 91% coverage: 40:544/552 of query aligns to 24:528/530 of 8i8eA
- binding adenosine monophosphate: G292 (≠ A312), G293 (≠ A313), A294 (= A314), A295 (≠ P315), G314 (≠ V334), Y315 (= Y335), M317 (≠ L337), S318 (≠ T338), D408 (= D430), R423 (= R445)
- binding 4'-phosphopantetheine: R93 (= R109), P220 (= P239), H223 (= H242)
8i49A Acyl-acp synthetase structure bound to atp
32% identity, 91% coverage: 40:544/552 of query aligns to 24:528/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
32% identity, 91% coverage: 40:544/552 of query aligns to 24:528/530 of 8i22A
8i8dA Acyl-acp synthetase structure bound to mc7-acp
32% identity, 91% coverage: 40:544/552 of query aligns to 24:528/529 of 8i8dA
- binding adenosine monophosphate: G292 (≠ A312), G293 (≠ A313), A295 (≠ P315), G314 (≠ V334), Y315 (= Y335), G316 (= G336), M317 (≠ L337), S318 (≠ T338), D408 (= D430), K429 (≠ I451)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H242), W227 (= W246), G292 (≠ A312), G316 (= G336), P322 (≠ G342)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R109), P220 (= P239), H223 (= H242), I269 (= I287), G432 (= G454)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
32% identity, 91% coverage: 40:544/552 of query aligns to 22:526/528 of 8i6mA
- binding adenosine monophosphate: G291 (≠ A313), A293 (≠ P315), G312 (≠ V334), Y313 (= Y335), G314 (= G336), M315 (≠ L337), S316 (≠ T338), D406 (= D430), R421 (= R445)
- binding magnesium ion: M315 (≠ L337), S316 (≠ T338), E317 (= E339)
8i51A Acyl-acp synthetase structure bound to amp-mc7
32% identity, 91% coverage: 40:544/552 of query aligns to 22:526/528 of 8i51A
- binding adenosine monophosphate: G291 (≠ A313), A293 (≠ P315), Y313 (= Y335), M315 (≠ L337), S316 (≠ T338), D406 (= D430), R421 (= R445)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W246), G290 (≠ A312), G312 (≠ V334), G314 (= G336), M315 (≠ L337), P320 (≠ G342), I321 (≠ P343)
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)
35% identity, 94% coverage: 31:547/552 of query aligns to 23:536/541 of Q5SKN9
- T184 (= T198) binding
- G302 (≠ A313) binding
- Q322 (≠ H333) binding
- G323 (≠ V334) binding
- T327 (= T338) binding
- E328 (= E339) binding
- D418 (= D430) binding
- K435 (= K447) binding
- K439 (≠ I451) binding
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)
32% identity, 90% coverage: 51:547/552 of query aligns to 39:535/539 of P0DX84
- H231 (= H242) mutation to A: Retains 74% of wild-type activity.
- W235 (= W246) mutation to A: Almost completely abolishes the activity.
- G302 (= G309) mutation to P: Almost completely abolishes the activity.
- G303 (≠ A312) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y335) mutation to A: Retains 7.7% of wild-type activity.
- P333 (≠ G342) mutation to A: Retains 69% of wild-type activity.
- R432 (= R445) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K447) mutation to A: Retains 36% of wild-type activity.
- D435 (= D448) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I451) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G453) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G454) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E455) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N456) mutation to A: Retains 60% of wild-type activity.
- E474 (= E487) mutation to A: Retains 33% of wild-type activity.
- K523 (= K535) 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 (= K538) 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)
32% identity, 90% coverage: 51:547/552 of query aligns to 39:535/538 of 6ijbB
- active site: T185 (= T198), H205 (≠ N218), H231 (= H242), S329 (≠ T338), E330 (= E339), K438 (≠ I451), W443 (≠ N456), A523 (≠ K535)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W246), G303 (≠ A312), A325 (≠ V334), W326 (≠ Y335), G327 (= G336), M328 (≠ L337)
- binding adenosine monophosphate: G303 (≠ A312), A304 (= A313), A305 (= A314), H324 (= H333), W326 (≠ Y335), G327 (= G336), M328 (≠ L337), S329 (≠ T338), Q359 (= Q368), D417 (= D430)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
31% identity, 90% coverage: 51:547/552 of query aligns to 39:532/533 of 6ihkB
- active site: T185 (= T198), H202 (≠ N218), H228 (= H242), S326 (≠ T338), E327 (= E339), K435 (≠ I451), W440 (≠ N456), K520 (= K535)
- binding adenosine-5'-diphosphate: H228 (= H242), G300 (≠ A312), A301 (= A313), A302 (= A314), H321 (= H333), A322 (≠ V334), W323 (≠ Y335), G324 (= G336), M325 (≠ L337), S326 (≠ T338), Q356 (= Q368), D414 (= D430), R429 (= R445), K520 (= K535)
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: 32:546/552 of query aligns to 8:481/485 of 5x8fB
- active site: T151 (= T198), S171 (≠ N218), H195 (= H242), T288 (= T338), E289 (= E339), I387 (= I451), N392 (= N456), K470 (= K535)
- binding magnesium ion: Y23 (≠ H47), E24 (≠ G48), H70 (≠ F94), N178 (≠ S225), L202 (≠ P249), L214 (≠ C261), T296 (≠ A348), L297 (≠ Q349), S298 (≠ Q350)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R109), L191 (= L238), P192 (= P239), H195 (= H242), I196 (≠ C243), S197 (≠ N244), A237 (≠ G284), V238 (= V288), L260 (= L310), G262 (≠ A312), G286 (= G336), M287 (≠ L337), S292 (≠ A344), Q293 (≠ S345), S388 (= S452), G389 (= G453), G390 (= G454), E391 (= E455), K420 (= K484), W421 (= W485), K450 (≠ R516), Y451 (≠ F517)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
30% identity, 93% coverage: 32:546/552 of query aligns to 8:481/484 of 5gtdA
- active site: T151 (= T198), S171 (≠ N218), H195 (= H242), T288 (= T338), E289 (= E339)
- binding adenosine-5'-monophosphate: G263 (≠ A313), G264 (≠ A314), Y285 (= Y335), G286 (= G336), M287 (≠ L337), T288 (= T338), D366 (= D430), V378 (≠ I442)
- binding magnesium ion: F314 (≠ H373), S315 (≠ A374)
- binding 2-succinylbenzoate: H195 (= H242), S197 (≠ N244), A237 (≠ G284), L260 (= L310), G262 (≠ A312), G263 (≠ A313), G286 (= G336), M287 (≠ L337), S292 (≠ A344), Q293 (≠ S345)
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
34% identity, 92% coverage: 31:537/552 of query aligns to 16:502/510 of 1v26B
- active site: T177 (= T198), H197 (≠ N218), H223 (= H242), T320 (= T338), E321 (= E339), K432 (≠ I451), W437 (≠ N456)
- binding adenosine monophosphate: G295 (≠ A313), S296 (≠ A314), A297 (≠ P315), G316 (≠ V334), Y317 (= Y335), G318 (= G336), L319 (= L337), T320 (= T338), D411 (= D430), K428 (= K447), K432 (≠ I451), W437 (≠ N456)
- binding magnesium ion: T177 (= T198), E321 (= E339)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
35% identity, 84% coverage: 31:493/552 of query aligns to 16:464/491 of 1v25A
- active site: T177 (= T198), H197 (≠ N218), H223 (= H242), T320 (= T338), E321 (= E339), K432 (≠ I451), W437 (≠ N456)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H242), V224 (≠ C243), G295 (≠ A313), S296 (≠ A314), A297 (≠ P315), Y317 (= Y335), G318 (= G336), L319 (= L337), T320 (= T338), D411 (= D430), I423 (= I442), K432 (≠ I451), W437 (≠ N456)
- binding magnesium ion: T177 (= T198), E321 (= E339)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
30% identity, 93% coverage: 32:546/552 of query aligns to 7:478/481 of 5busA
- active site: T150 (= T198), S170 (≠ N218), H194 (= H242), T287 (= T338), E288 (= E339)
- binding adenosine monophosphate: H194 (= H242), G262 (≠ A313), G263 (≠ A314), S283 (≠ V334), M286 (≠ L337), T287 (= T338), D365 (= D430), V377 (≠ I442), R380 (= R445), K467 (= K535)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
30% identity, 93% coverage: 32:543/552 of query aligns to 7:475/475 of 5burA
- active site: T150 (= T198), S170 (≠ N218), H194 (= H242), T287 (= T338), E288 (= E339)
- binding adenosine-5'-triphosphate: T150 (= T198), S151 (= S199), T153 (= T201), T154 (= T202), K158 (= K206), G263 (≠ A314), S283 (≠ V334), T287 (= T338), D365 (= D430), V377 (≠ I442), R380 (= R445)
5buqB Unliganded form of o-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, solved at 1.98 angstroms (see paper)
29% identity, 93% coverage: 32:546/552 of query aligns to 7:469/473 of 5buqB
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, 90% coverage: 51:547/552 of query aligns to 64:575/590 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)
30% identity, 90% coverage: 51:547/552 of query aligns to 28:503/506 of 4gxqA
- active site: T163 (= T198), N183 (= N218), H207 (= H242), T303 (= T338), E304 (= E339), I403 (= I451), N408 (= N456), A491 (≠ K535)
- binding adenosine-5'-triphosphate: T163 (= T198), S164 (= S199), G165 (= G200), T166 (= T201), T167 (= T202), H207 (= H242), S277 (≠ A313), A278 (= A314), P279 (= P315), E298 (≠ H333), M302 (≠ L337), T303 (= T338), D382 (= D430), R397 (= R445)
- binding carbonate ion: H207 (= H242), S277 (≠ A313), R299 (≠ V334), G301 (= G336)
Query Sequence
>Dsui_2808 FitnessBrowser__PS:Dsui_2808
MAGHNDNSSNIYKQGLEKNAANYVPLSPLTFIARSAYIYPERVSVIHGQRRYTWLETFNR
ARRLASALEARGIKEGDTVAVMLNNTPEMYECHFGVPVTGAVLNTLNTRLDPEAVAFMLN
HGEAKILITDKEYSHIVGPALEKLGRSIVVIDVNDSEYTGPGDLLGEKDYEALLAEGTPD
YEWKGPQDEWDAISLNYTSGTTGNPKGVVYHHRGAYLNAMSNIVSWGMPPHSVYLWTLPM
FHCNGWCFPWTMAANAGTNVCLRRVDPKLILQSIRENKVTHYCGAPIVHSMLANAPAEWR
EGINHGVSGLIAAAPPPAAVIEGMAKIGFKITHVYGLTETYGPASVCAQQPEWFDLPVGE
QVNLNGRQGVRYHAQEAITVLDPATMEAVPWDNETMGEIMFRGNLVMKGYLKNPKATEES
FAGGYYHTGDLAVMQADGYVKIKDRSKDVIISGGENISSIEVEDTLYRHPAVMAAAVVAT
PDPKWGEVPAAFIELKDGVSITEVEIIEFCREHMARFKVPKKVIFGPLPKTSTGKIQKYV
LREMAKSTAAIE
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