SitesBLAST
Comparing WP_084055698.1 NCBI__GCF_900176285.1:WP_084055698.1 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: 3:554/557 of query aligns to 4:541/541 of Q5SKN9
- T184 (= T194) binding Mg(2+)
- G302 (≠ A313) binding tetradecanoyl-AMP
- Q322 (≠ H334) binding tetradecanoyl-AMP
- G323 (≠ A335) binding tetradecanoyl-AMP
- T327 (= T339) binding tetradecanoyl-AMP
- E328 (= E340) binding Mg(2+)
- D418 (= D429) binding tetradecanoyl-AMP
- K435 (= K446) binding tetradecanoyl-AMP
- K439 (= K450) binding tetradecanoyl-AMP
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
41% identity, 98% coverage: 8:554/557 of query aligns to 2:510/510 of 1v26B
- active site: T177 (= T194), H197 (= H214), H223 (= H238), T320 (= T339), E321 (= E340), K432 (= K450), W437 (= W455)
- binding adenosine monophosphate: G295 (≠ A313), S296 (≠ T314), A297 (≠ E315), G316 (≠ A335), Y317 (= Y336), G318 (= G337), L319 (≠ A338), T320 (= T339), D411 (= D429), K428 (= K446), K432 (= K450), W437 (= W455)
- binding magnesium ion: T177 (= T194), E321 (= E340)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
40% identity, 98% coverage: 8:554/557 of query aligns to 2:491/491 of 1v25A
- active site: T177 (= T194), H197 (= H214), H223 (= H238), T320 (= T339), E321 (= E340), K432 (= K450), W437 (= W455)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H238), V224 (≠ A239), G295 (≠ A313), S296 (≠ T314), A297 (≠ E315), Y317 (= Y336), G318 (= G337), L319 (≠ A338), T320 (= T339), D411 (= D429), I423 (= I441), K432 (= K450), W437 (= W455)
- binding magnesium ion: T177 (= T194), E321 (= E340)
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)
38% identity, 95% coverage: 17:547/557 of query aligns to 9:533/539 of P0DX84
- H231 (= H238) mutation to A: Retains 74% of wild-type activity.
- W235 (= W242) mutation to A: Almost completely abolishes the activity.
- G302 (≠ S311) mutation to P: Almost completely abolishes the activity.
- G303 (= G312) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y336) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P343) mutation to A: Retains 69% of wild-type activity.
- R432 (= R444) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K446) mutation to A: Retains 36% of wild-type activity.
- D435 (= D447) mutation to A: Retains 76% of wild-type activity.
- K438 (= K450) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G452) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G453) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E454) mutation to A: Retains 27% of wild-type activity.
- W443 (= W455) mutation to A: Retains 60% of wild-type activity.
- E474 (= E486) mutation to A: Retains 33% of wild-type activity.
- K523 (= K537) 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 (= K540) 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)
38% identity, 95% coverage: 17:547/557 of query aligns to 9:533/538 of 6ijbB
- active site: T185 (= T194), H205 (= H214), H231 (= H238), S329 (≠ T339), E330 (= E340), K438 (= K450), W443 (= W455), A523 (≠ K537)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W242), G303 (= G312), A325 (= A335), W326 (≠ Y336), G327 (= G337), M328 (≠ A338)
- binding adenosine monophosphate: G303 (= G312), A304 (= A313), A305 (≠ T314), H324 (= H334), W326 (≠ Y336), G327 (= G337), M328 (≠ A338), S329 (≠ T339), Q359 (= Q369), D417 (= D429)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
38% identity, 95% coverage: 17:547/557 of query aligns to 9:530/533 of 6ihkB
- active site: T185 (= T194), H202 (= H214), H228 (= H238), S326 (≠ T339), E327 (= E340), K435 (= K450), W440 (= W455), K520 (= K537)
- binding adenosine-5'-diphosphate: H228 (= H238), G300 (= G312), A301 (= A313), A302 (≠ T314), H321 (= H334), A322 (= A335), W323 (≠ Y336), G324 (= G337), M325 (≠ A338), S326 (≠ T339), Q356 (= Q369), D414 (= D429), R429 (= R444), K520 (= K537)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp (see paper)
36% identity, 92% coverage: 32:545/557 of query aligns to 24:527/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G312), G293 (≠ A313), A294 (≠ T314), A295 (≠ E315), G314 (≠ A335), Y315 (= Y336), M317 (≠ A338), S318 (≠ T339), D408 (= D429), R423 (= R444)
- binding 4'-phosphopantetheine: R93 (= R105), P220 (= P235), H223 (= H238)
8i49A Acyl-acp synthetase structure bound to atp (see paper)
36% identity, 92% coverage: 32:545/557 of query aligns to 24:527/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
36% identity, 92% coverage: 32:545/557 of query aligns to 24:527/530 of 8i22A
8i8dA Acyl-acp synthetase structure bound to mc7-acp (see paper)
36% identity, 92% coverage: 32:545/557 of query aligns to 24:527/529 of 8i8dA
- binding adenosine monophosphate: G292 (= G312), G293 (≠ A313), A295 (≠ E315), G314 (≠ A335), Y315 (= Y336), G316 (= G337), M317 (≠ A338), S318 (≠ T339), D408 (= D429), K429 (= K450)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H238), W227 (= W242), G292 (= G312), G316 (= G337), P322 (= P343)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R105), P220 (= P235), H223 (= H238), I269 (= I287), G432 (= G453)
8jylA Acyl-acp synthetase structure bound to c10-ams (see paper)
36% identity, 92% coverage: 32:545/557 of query aligns to 22:525/527 of 8jylA
- binding magnesium ion: S316 (≠ T339), E317 (= E340)
- binding [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl N-decanoylsulfamate: W225 (= W242), G290 (= G312), G291 (≠ A313), A292 (≠ T314), A293 (≠ E315), G312 (≠ A335), Y313 (= Y336), G314 (= G337), M315 (≠ A338), S316 (≠ T339), I321 (≠ L344), D406 (= D429), R421 (= R444), K427 (= K450), W432 (= W455)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1 (see paper)
36% identity, 92% coverage: 32:545/557 of query aligns to 22:525/528 of 8i6mA
- binding adenosine monophosphate: G291 (≠ A313), A293 (≠ E315), G312 (≠ A335), Y313 (= Y336), G314 (= G337), M315 (≠ A338), S316 (≠ T339), D406 (= D429), R421 (= R444)
- binding magnesium ion: M315 (≠ A338), S316 (≠ T339), E317 (= E340)
8i51A Acyl-acp synthetase structure bound to amp-mc7 (see paper)
36% identity, 92% coverage: 32:545/557 of query aligns to 22:525/528 of 8i51A
- binding adenosine monophosphate: G291 (≠ A313), A293 (≠ E315), Y313 (= Y336), M315 (≠ A338), S316 (≠ T339), D406 (= D429), R421 (= R444)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W242), G290 (= G312), G312 (≠ A335), G314 (= G337), M315 (≠ A338), P320 (= P343), I321 (≠ L344)
8i3iA Acyl-acp synthetase structure bound to amp-pnp in the presence of mgcl2 (see paper)
36% identity, 92% coverage: 32:545/557 of query aligns to 24:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T194), G174 (= G196), T175 (= T197), T176 (= T198), K180 (= K202), G293 (≠ A313), A294 (≠ T314), A295 (≠ E315), Y315 (= Y336), M317 (≠ A338), S318 (≠ T339), D408 (= D429), R423 (= R444)
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, 90% coverage: 49:549/557 of query aligns to 31:499/503 of P9WQ37
- K172 (= K202) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T225) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ D227) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ A239) 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 (≠ G241) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ M244) 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 (≠ K277) 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 (≠ Y424) 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 (= D429) 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 (= R444) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S451) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G453) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K537) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
Sites not aligning to the query:
- 9 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- 17 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
29% identity, 90% coverage: 49:549/557 of query aligns to 34:499/502 of 3r44A
Sites not aligning to the query:
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
32% identity, 89% coverage: 49:546/557 of query aligns to 31:486/486 of 8wevA
Sites not aligning to the query:
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
29% identity, 90% coverage: 49:551/557 of query aligns to 30:505/506 of 4gxqA
- active site: T163 (= T194), N183 (≠ H214), H207 (= H238), T303 (= T339), E304 (= E340), I403 (≠ K450), N408 (≠ W455), A491 (≠ K537)
- binding adenosine-5'-triphosphate: T163 (= T194), S164 (= S195), G165 (= G196), T166 (= T197), T167 (= T198), H207 (= H238), S277 (≠ T314), A278 (≠ E315), P279 (= P316), E298 (≠ H334), M302 (≠ A338), T303 (= T339), D382 (= D429), R397 (= R444)
- binding carbonate ion: H207 (= H238), S277 (≠ T314), R299 (≠ A335), G301 (= G337)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
27% identity, 90% coverage: 49:549/557 of query aligns to 29:482/484 of 5gtdA
- active site: T151 (= T194), S171 (≠ H214), H195 (= H238), T288 (= T339), E289 (= E340)
- binding adenosine-5'-monophosphate: G263 (= G312), G264 (≠ A313), Y285 (= Y336), G286 (= G337), M287 (≠ A338), T288 (= T339), D366 (= D429), V378 (≠ I441)
- binding magnesium ion: F314 (≠ P374), S315 (≠ G375)
- binding 2-succinylbenzoate: H195 (= H238), S197 (≠ Q240), A237 (≠ G283), L260 (≠ M309), G262 (≠ S311), G263 (= G312), G286 (= G337), M287 (≠ A338), S292 (≠ P343), Q293 (≠ L344)
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)
27% identity, 90% coverage: 49:549/557 of query aligns to 29:482/485 of 5x8fB
- active site: T151 (= T194), S171 (≠ H214), H195 (= H238), T288 (= T339), E289 (= E340), I387 (≠ K450), N392 (≠ W455), K470 (= K537)
- binding magnesium ion: H70 (≠ S93), N178 (≠ A221), L202 (≠ F245), L214 (≠ F257), T296 (≠ V347), L297 (≠ N348), S298 (≠ H349)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R105), L191 (≠ V234), P192 (= P235), H195 (= H238), I196 (≠ A239), S197 (≠ Q240), A237 (≠ G283), V238 (≠ A284), L260 (≠ M309), G262 (≠ S311), G286 (= G337), M287 (≠ A338), S292 (≠ P343), Q293 (≠ L344), S388 (= S451), G389 (= G452), G390 (= G453), E391 (= E454), K420 (= K483), W421 (= W484), K450 (= K517), Y451 (≠ W518)
Sites not aligning to the query:
Query Sequence
>WP_084055698.1 NCBI__GCF_900176285.1:WP_084055698.1
MKEIVQGFPATSNDDYPLNMIAFMKHAAQNYPETEVVSRNLDGSLRGSTYGEIWSRVKRL
AKALEGIGVRAGDRVGALDWNTHRFMELYFAVSGIGAVLLELNPRISAAERAYVLNHSEA
RFVAVSASLLPVMEPLAAECPTVQALIVLDDLGKGLPRTAFSRAHDYEGLIKETDDDFQF
PWVDERSACTACYTSGTTGKPKGVYNSHRAMYLHTLAIAQALNITQDDVILQIVPMFHAQ
GWGMFFCGPMLGAKLVFPGRYTMEDPSPLVDLLVDQKVTVTCGAPAIFLPMLHHIKKMDP
KPDLTGLRMISGATEPPLALMKGYHELGGARVIHAYGATETAPLVTVNHLKPSLKDLAEA
ERWELRKKQGFPVPGLDVKVVGPDGAELPRDGAKVGEVHIRGPWITRSYYKDSRSAESFT
EDGYWRSGDAGTIDPNGYLKITDRFKDLIKSGGEWISSIDLENAIMAHPDVLEAAVIGIP
HPKWEERPLALVVLHESARGTLTQEAILDFIRPHFAKWQLPDEVLFVDAIPKTSVGKFAK
RVAREQYAGYYGGARGE
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