SitesBLAST
Comparing WP_012471443.1 NCBI__GCF_000020385.1:WP_012471443.1 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)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp (see paper)
64% identity, 98% coverage: 10:545/545 of query aligns to 5:530/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G307), G293 (= G308), A294 (= A309), A295 (= A310), G314 (= G329), Y315 (= Y330), M317 (= M332), S318 (= S333), D408 (= D423), R423 (= R438)
- binding 4'-phosphopantetheine: R93 (= R99), P220 (= P235), H223 (= H238)
8i49A Acyl-acp synthetase structure bound to atp (see paper)
64% identity, 98% coverage: 10:545/545 of query aligns to 5:530/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
64% identity, 98% coverage: 10:545/545 of query aligns to 5:530/530 of 8i22A
8i6mA Acyl-acp synthetase structure bound to amp-c18:1 (see paper)
64% identity, 98% coverage: 10:545/545 of query aligns to 3:528/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G308), A293 (= A310), G312 (= G329), Y313 (= Y330), G314 (= G331), M315 (= M332), S316 (= S333), D406 (= D423), R421 (= R438)
- binding magnesium ion: M315 (= M332), S316 (= S333), E317 (= E334)
8i51A Acyl-acp synthetase structure bound to amp-mc7 (see paper)
64% identity, 98% coverage: 10:545/545 of query aligns to 3:528/528 of 8i51A
- binding adenosine monophosphate: G291 (= G308), A293 (= A310), Y313 (= Y330), M315 (= M332), S316 (= S333), D406 (= D423), R421 (= R438)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W242), G290 (= G307), G312 (= G329), G314 (= G331), M315 (= M332), P320 (= P337), I321 (= I338)
8i8dA Acyl-acp synthetase structure bound to mc7-acp (see paper)
64% identity, 98% coverage: 10:542/545 of query aligns to 5:527/529 of 8i8dA
- binding adenosine monophosphate: G292 (= G307), G293 (= G308), A295 (= A310), G314 (= G329), Y315 (= Y330), G316 (= G331), M317 (= M332), S318 (= S333), D408 (= D423), K429 (= K444)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H238), W227 (= W242), G292 (= G307), G316 (= G331), P322 (= P337)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R99), P220 (= P235), H223 (= H238), I269 (= I284), G432 (= G447)
8jylA Acyl-acp synthetase structure bound to c10-ams (see paper)
64% identity, 98% coverage: 10:542/545 of query aligns to 3:525/527 of 8jylA
- binding magnesium ion: S316 (= S333), E317 (= E334)
- binding [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl N-decanoylsulfamate: W225 (= W242), G290 (= G307), G291 (= G308), A292 (= A309), A293 (= A310), G312 (= G329), Y313 (= Y330), G314 (= G331), M315 (= M332), S316 (= S333), I321 (= I338), D406 (= D423), R421 (= R438), K427 (= K444), W432 (= W449)
8i3iA Acyl-acp synthetase structure bound to amp-pnp in the presence of mgcl2 (see paper)
63% identity, 98% coverage: 10:545/545 of query aligns to 5:522/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T187), G174 (= G189), T175 (= T190), T176 (= T191), K180 (= K195), G293 (= G308), A294 (= A309), A295 (= A310), Y315 (= Y330), M317 (= M332), S318 (= S333), D408 (= D423), R423 (= R438)
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)
42% identity, 93% coverage: 40:544/545 of query aligns to 46:534/541 of Q5SKN9
- T184 (= T187) binding Mg(2+)
- G302 (= G308) binding tetradecanoyl-AMP
- Q322 (≠ T328) binding tetradecanoyl-AMP
- G323 (= G329) binding tetradecanoyl-AMP
- T327 (≠ S333) binding tetradecanoyl-AMP
- E328 (= E334) binding Mg(2+)
- D418 (= D423) binding tetradecanoyl-AMP
- K435 (= K440) binding tetradecanoyl-AMP
- K439 (= K444) binding tetradecanoyl-AMP
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
42% identity, 82% coverage: 40:486/545 of query aligns to 39:464/491 of 1v25A
- active site: T177 (= T187), H197 (= H207), H223 (= H238), T320 (≠ S333), E321 (= E334), K432 (= K444), W437 (= W449)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H238), V224 (= V239), G295 (= G308), S296 (≠ A309), A297 (= A310), Y317 (= Y330), G318 (= G331), L319 (≠ M332), T320 (≠ S333), D411 (= D423), I423 (= I435), K432 (= K444), W437 (= W449)
- binding magnesium ion: T177 (= T187), E321 (= E334)
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
42% identity, 82% coverage: 40:485/545 of query aligns to 39:464/510 of 1v26B
- active site: T177 (= T187), H197 (= H207), H223 (= H238), T320 (≠ S333), E321 (= E334), K432 (= K444), W437 (= W449)
- binding adenosine monophosphate: G295 (= G308), S296 (≠ A309), A297 (= A310), G316 (= G329), Y317 (= Y330), G318 (= G331), L319 (≠ M332), T320 (≠ S333), D411 (= D423), K428 (= K440), K432 (= K444), W437 (= W449)
- binding magnesium ion: T177 (= T187), 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)
38% identity, 97% coverage: 16:544/545 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 (= G307) 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 (= P337) mutation to A: Retains 69% of wild-type activity.
- R432 (= R438) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K440) mutation to A: Retains 36% of wild-type activity.
- D435 (= D441) mutation to A: Retains 76% of wild-type activity.
- K438 (= K444) mutation to A: Retains 5.6% of wild-type activity.
- G440 (≠ S446) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G447) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E448) mutation to A: Retains 27% of wild-type activity.
- W443 (= W449) mutation to A: Retains 60% of wild-type activity.
- E474 (= E480) mutation to A: Retains 33% of wild-type activity.
- K523 (= K534) 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 (= K537) 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, 97% coverage: 16:544/545 of query aligns to 9:533/538 of 6ijbB
- active site: T185 (= T187), H205 (= H207), H231 (= H238), S329 (= S333), E330 (= E334), K438 (= K444), W443 (= W449), A523 (≠ K534)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W242), G303 (= G308), A325 (≠ G329), W326 (≠ Y330), G327 (= G331), M328 (= M332)
- binding adenosine monophosphate: G303 (= G308), A304 (= A309), A305 (= A310), H324 (≠ T328), W326 (≠ Y330), G327 (= G331), M328 (= M332), S329 (= S333), Q359 (≠ T363), D417 (= D423)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
37% identity, 97% coverage: 16:544/545 of query aligns to 9:530/533 of 6ihkB
- active site: T185 (= T190), H202 (= H207), H228 (= H238), S326 (= S333), E327 (= E334), K435 (= K444), W440 (= W449), K520 (= K534)
- binding adenosine-5'-diphosphate: H228 (= H238), G300 (= G308), A301 (= A309), A302 (= A310), H321 (≠ T328), A322 (≠ G329), W323 (≠ Y330), G324 (= G331), M325 (= M332), S326 (= S333), Q356 (≠ T363), D414 (= D423), R429 (= R438), K520 (= K534)
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)
29% identity, 93% coverage: 39:544/545 of query aligns to 27:497/503 of P9WQ37
- K172 (= K195) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ S220) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R226) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V239) 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 (= A241) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ L244) 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 (≠ K274) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G331) 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 (≠ Y418) 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 (= D423) 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 (= R438) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V445) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G447) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K534) 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)
28% identity, 93% coverage: 39:544/545 of query aligns to 30:497/502 of 3r44A
Sites not aligning to the query:
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, 92% coverage: 42:543/545 of query aligns to 64:549/556 of Q9S725
- K211 (= K195) mutation to S: Drastically reduces the activity.
- M293 (≠ H279) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I306) mutation K->L,A: Affects the substrate specificity.
- E401 (= E391) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ V393) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R438) mutation to Q: Drastically reduces the activity.
- K457 (≠ S446) mutation to S: Drastically reduces the activity.
- K540 (= K534) mutation to N: Abolishes the activity.
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
27% identity, 93% coverage: 37:542/545 of query aligns to 44:535/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H240), F245 (≠ W242), T249 (≠ Y246), G314 (= G308), A315 (= A309), P316 (≠ A310), G337 (= G329), Y338 (= Y330), G339 (= G331), L340 (≠ M332), T341 (≠ S333), A346 (≠ I338), D420 (= D423), I432 (= I435), K527 (= K534)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
27% identity, 93% coverage: 37:542/545 of query aligns to 44:535/539 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 (= H240), F245 (≠ W242), T249 (≠ Y246), G314 (= G308), A315 (= A309), P316 (≠ A310), G337 (= G329), Y338 (= Y330), G339 (= G331), L340 (≠ M332), T341 (≠ S333), S345 (≠ P337), A346 (≠ I338), D420 (= D423), I432 (= I435), K527 (= K534)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ W242), R335 (≠ D325), G337 (= G329), G339 (= G331), L340 (≠ M332), A346 (≠ I338)
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, 92% coverage: 41:542/545 of query aligns to 64:571/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
Query Sequence
>WP_012471443.1 NCBI__GCF_000020385.1:WP_012471443.1
MPDALITRTPSAYEYPLLIKNLLFCPVVDTPDQEIVYRDHRFSYRDLRQRVARLANALTD
LGVKRGDTVAVMDWDSNRYLECFFAVPMIGAVLHTINVRLSPEQILYTIDHAEDDVLLVN
SEFLPILEQIRGRMDTVKSFVLLNDEPTVPESHIPFSGEYEALLAAASDQFNFADFDENT
RATTFYTTGTTGMPKGVYFSHRQLVLHTLGVLAVLGSSVSHGGFNRQDVYMPITPMFHVH
AWGLPYVATMLGVKQVYPGRYLPDHLLELIDREKVTFSHCVPTILHMLLKHPHAGRMDLS
GWKVIIGGAAMSRALCLDALQRGIDLFTGYGMSETCPILTISHLTPEMLELSPEEQAVIR
CKTGRSLPLVDLKIVDSARQEQPRDGKSTGEIVVRAPWLTQGYLKDHKASERLWEGGYLH
TGDVAVRDEQGYVKITDRTKDVLKVSGEWVSSLELEDIIAHHPGVAEVAVIGQPDEKWGE
RPLALVVAKPDNPVTEKELTHLVREYADKGVVTKQVVLLKVKLVEAIDKTSVGKVNKVAL
REKYL
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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