SitesBLAST
Comparing WP_010443284.1 NCBI__GCF_000192475.1:WP_010443284.1 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)
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)
31% identity, 97% coverage: 6:523/534 of query aligns to 23:570/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
35% identity, 89% coverage: 51:525/534 of query aligns to 27:486/486 of 8wevA
Sites not aligning to the query:
P69451 Long-chain-fatty-acid--CoA ligase; Long-chain acyl-CoA synthetase; Acyl-CoA synthetase; EC 6.2.1.3 from Escherichia coli (strain K12) (see paper)
29% identity, 97% coverage: 9:524/534 of query aligns to 7:551/561 of P69451
- Y213 (= Y187) mutation to A: Loss of activity.
- T214 (= T188) mutation to A: 10% of wild-type activity.
- G216 (= G190) mutation to A: Decreases activity.
- T217 (= T191) mutation to A: Decreases activity.
- G219 (= G193) mutation to A: Decreases activity.
- K222 (= K196) mutation to A: Decreases activity.
- E361 (= E331) mutation to A: Loss of activity.
5wm3A Crystal structure of cahj in complex with salicyl adenylate (see paper)
32% identity, 94% coverage: 27:529/534 of query aligns to 32:536/537 of 5wm3A
- active site: S193 (≠ T188), N213 (= N208), H237 (= H232), A336 (≠ T330), E337 (= E331), N437 (≠ I433), K442 (≠ N438), K524 (= K516)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxybenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: N238 (≠ T233), F239 (≠ S234), G310 (= G304), S311 (= S305), K312 (≠ M306), V332 (≠ L326), F333 (≠ Y327), G334 (= G328), M335 (≠ Q329), A336 (≠ T330), D416 (= D412), K433 (= K429), K442 (≠ N438)
- binding magnesium ion: S301 (= S295), L303 (= L297), G326 (= G320)
5wm2A Crystal structure of cahj in complex with salicylic acid and amp (see paper)
32% identity, 94% coverage: 27:529/534 of query aligns to 32:536/536 of 5wm2A
- active site: S193 (≠ T188), N213 (= N208), H237 (= H232), A336 (≠ T330), E337 (= E331), N437 (≠ I433), K442 (≠ N438), K524 (= K516)
- binding adenosine monophosphate: G310 (= G304), S311 (= S305), K312 (≠ M306), V332 (≠ L326), F333 (≠ Y327), G334 (= G328), M335 (≠ Q329), A336 (≠ T330), E337 (= E331), D416 (= D412), V428 (= V424), K433 (= K429), K442 (≠ N438)
5wm6A Crystal structure of cahj in complex with benzoyl adenylate (see paper)
32% identity, 92% coverage: 27:519/534 of query aligns to 32:527/535 of 5wm6A
- active site: S193 (≠ T188), N213 (= N208), H237 (= H232), A336 (≠ T330), E337 (= E331), N437 (≠ I433), K442 (≠ N438), K524 (= K516)
- binding magnesium ion: S301 (= S295), L303 (= L297), G326 (= G320)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: F239 (≠ S234), G310 (= G304), S311 (= S305), K312 (≠ M306), V332 (≠ L326), F333 (≠ Y327), G334 (= G328), M335 (≠ Q329), A336 (≠ T330), D416 (= D412), K433 (= K429), K442 (≠ N438)
6e97B Crystal structure of the aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with dhb-adenylate
32% identity, 89% coverage: 51:523/534 of query aligns to 45:529/537 of 6e97B
- active site: S190 (≠ T188), S210 (≠ N208), H234 (= H232), A336 (≠ T330), E337 (= E331), N437 (≠ I433), K442 (≠ N438), K522 (= K516)
- binding 5'-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine: H234 (= H232), N235 (≠ T233), F236 (vs. gap), S240 (≠ G235), G310 (= G304), A311 (≠ S305), K312 (≠ M306), V332 (≠ L326), F333 (≠ Y327), G334 (= G328), M335 (≠ Q329), A336 (≠ T330), D416 (= D412), K433 (= K429), K442 (≠ N438)
5wm5A Crystal structure of cahj in complex with 5-methylsalicyl adenylate (see paper)
33% identity, 83% coverage: 27:469/534 of query aligns to 32:473/533 of 5wm5A
- active site: S193 (≠ T188), N213 (= N208), H237 (= H232), A336 (≠ T330), E337 (= E331), N437 (≠ I433), K442 (≠ N438)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxy-5-methylbenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: H237 (= H232), N238 (≠ T233), F239 (≠ S234), G309 (= G303), G310 (= G304), S311 (= S305), K312 (≠ M306), V332 (≠ L326), F333 (≠ Y327), G334 (= G328), M335 (≠ Q329), A336 (≠ T330), L340 (≠ I336), D416 (= D412), K433 (= K429), K442 (≠ N438)
Sites not aligning to the query:
5wm4A Crystal structure of cahj in complex with 6-methylsalicyl adenylate (see paper)
33% identity, 83% coverage: 27:469/534 of query aligns to 32:473/534 of 5wm4A
- active site: S193 (≠ T188), N213 (= N208), H237 (= H232), A336 (≠ T330), E337 (= E331), N437 (≠ I433), K442 (≠ N438)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxy-6-methylbenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: N238 (≠ T233), F239 (≠ S234), C243 (≠ M238), G309 (= G303), G310 (= G304), S311 (= S305), K312 (≠ M306), V332 (≠ L326), F333 (≠ Y327), G334 (= G328), M335 (≠ Q329), A336 (≠ T330), L340 (≠ I336), D416 (= D412), K433 (= K429), K442 (≠ N438)
- binding magnesium ion: M453 (≠ L449), H455 (= H451), V458 (= V454)
Sites not aligning to the query:
1md9A Crystal structure of dhbe in complex with dhb and amp (see paper)
29% identity, 94% coverage: 23:524/534 of query aligns to 26:527/536 of 1md9A
- active site: S190 (≠ T188), S210 (≠ N208), H234 (= H232), A333 (≠ T330), E334 (= E331), N434 (≠ I433), K439 (≠ N438), K519 (= K516)
- binding adenosine monophosphate: G191 (≠ S189), G307 (= G304), A308 (≠ S305), K309 (≠ M306), V329 (≠ L326), F330 (≠ Y327), G331 (= G328), M332 (≠ Q329), D413 (= D412), V425 (= V424), R428 (= R427), K519 (= K516)
- binding 2,3-dihydroxy-benzoic acid: H234 (= H232), N235 (≠ T233), Y236 (vs. gap), S240 (≠ G235), G307 (= G304), V329 (≠ L326), G331 (= G328), M332 (≠ Q329), K519 (= K516)
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, 95% coverage: 23:528/534 of query aligns to 3:499/503 of P9WQ37
- R9 (= R29) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D37) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K196) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T219) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ T221) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ T233) 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 (≠ G235) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ M238) 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 (≠ G269) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G328) 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 (= W407) 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 (= D412) 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 (= R427) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R434) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G436) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K516) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
P40871 2,3-dihydroxybenzoate-AMP ligase; Dihydroxybenzoic acid-activating enzyme; EC 6.2.1.71 from Bacillus subtilis (strain 168) (see paper)
29% identity, 94% coverage: 23:524/534 of query aligns to 26:527/539 of P40871
- G191 (≠ S189) binding ATP
- HN 234:235 (≠ HT 232:233) binding substrate
- S240 (≠ G235) binding substrate
- G307 (= G304) binding ATP
- V329 (≠ L326) binding ATP
- D413 (= D412) binding ATP
- R428 (= R427) binding ATP
- K519 (= K516) binding ATP; binding substrate
6e8oA Crystal structure of aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with amp
32% identity, 89% coverage: 51:523/534 of query aligns to 45:528/536 of 6e8oA
- active site: S190 (≠ T188), S210 (≠ N208), H234 (= H232), A336 (≠ T330), E337 (= E331), N437 (≠ I433), K442 (≠ N438), K521 (= K516)
- binding adenosine monophosphate: H234 (= H232), G310 (= G304), A311 (≠ S305), K312 (≠ M306), V332 (≠ L326), F333 (≠ Y327), G334 (= G328), M335 (≠ Q329), A336 (≠ T330), D416 (= D412), V428 (= V424), K442 (≠ N438)
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: 47:529/534 of query aligns to 57:553/556 of Q9S725
- K211 (= K196) mutation to S: Drastically reduces the activity.
- M293 (≠ L274) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ S301) mutation K->L,A: Affects the substrate specificity.
- E401 (= E379) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C381) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R427) mutation to Q: Drastically reduces the activity.
- K457 (≠ G435) mutation to S: Drastically reduces the activity.
- K540 (= K516) mutation to N: Abolishes the activity.
7tz4A Salicylate adenylate pchd from pseudomonas aeruginosa containing 4- cyanosalicyl-ams (see paper)
32% identity, 90% coverage: 49:526/534 of query aligns to 43:527/530 of 7tz4A
- binding 5'-O-[(4-cyano-2-hydroxybenzoyl)sulfamoyl]adenosine: H232 (= H232), N233 (≠ T233), F234 (vs. gap), C238 (≠ G237), G305 (= G304), S306 (= S305), R307 (≠ M306), V327 (≠ L326), L328 (≠ Y327), G329 (= G328), M330 (≠ Q329), A331 (≠ T330), I335 (= I336), D411 (= D412), V423 (= V424), K517 (= K516)
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)
31% identity, 89% coverage: 50:524/534 of query aligns to 24:478/485 of 5x8fB
- active site: T151 (= T188), S171 (≠ N208), H195 (= H232), T288 (= T330), E289 (= E331), I387 (= I433), N392 (= N438), K470 (= K516)
- binding magnesium ion: E24 (= E50), H70 (≠ Y95), N178 (≠ R215), L202 (≠ V239), L214 (= L252), T296 (≠ Q338), L297 (≠ H339), S298 (≠ H340)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ A110), L191 (≠ M228), P192 (= P229), H195 (= H232), I196 (≠ T233), S197 (= S234), A237 (≠ G275), V238 (= V276), L260 (≠ K298), G262 (= G303), G286 (= G328), M287 (≠ Q329), S292 (≠ P334), Q293 (≠ V335), S388 (≠ R434), G389 (= G435), G390 (= G436), E391 (= E437), K420 (= K466), W421 (= W467), K450 (≠ P496), Y451 (≠ Q497)
Sites not aligning to the query:
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)
31% identity, 96% coverage: 15:526/534 of query aligns to 11:534/541 of Q5SKN9
- T184 (= T188) binding Mg(2+)
- G302 (= G304) binding tetradecanoyl-AMP
- Q322 (≠ T325) binding tetradecanoyl-AMP
- G323 (≠ L326) binding tetradecanoyl-AMP
- T327 (= T330) binding tetradecanoyl-AMP
- E328 (= E331) binding Mg(2+)
- D418 (= D412) binding tetradecanoyl-AMP
- K435 (= K429) binding tetradecanoyl-AMP
- K439 (≠ I433) binding tetradecanoyl-AMP
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
31% identity, 89% coverage: 50:524/534 of query aligns to 24:478/484 of 5gtdA
- active site: T151 (= T188), S171 (≠ N208), H195 (= H232), T288 (= T330), E289 (= E331)
- binding adenosine-5'-monophosphate: G263 (= G304), G264 (≠ A308), Y285 (= Y327), G286 (= G328), M287 (≠ Q329), T288 (= T330), D366 (= D412), V378 (= V424)
- binding magnesium ion: F314 (≠ A357), S315 (≠ Q358)
- binding 2-succinylbenzoate: H195 (= H232), S197 (= S234), A237 (≠ G275), L260 (≠ K298), G262 (= G303), G263 (= G304), G286 (= G328), M287 (≠ Q329), S292 (≠ P334), Q293 (≠ V335)
5ie2A Crystal structure of a plant enzyme (see paper)
29% identity, 95% coverage: 23:527/534 of query aligns to 5:506/506 of 5ie2A
- active site: T165 (= T188), S185 (≠ N208), H209 (= H232), T310 (= T330), E311 (= E331), N410 (≠ I433), K415 (≠ N438), K495 (= K516)
- binding adenosine-5'-triphosphate: T165 (= T188), S166 (= S189), G167 (= G190), T168 (= T191), T169 (= T192), S284 (≠ G304), A285 (≠ S305), S286 (≠ M306), Y307 (= Y327), A308 (≠ G328), M309 (≠ Q329), T310 (= T330), D389 (= D412), L401 (≠ V424), R404 (= R427), K495 (= K516)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
30% identity, 95% coverage: 23:528/534 of query aligns to 6:499/502 of 3r44A
Sites not aligning to the query:
Query Sequence
>WP_010443284.1 NCBI__GCF_000192475.1:WP_010443284.1
MYDLTLTTSRAPAQSDMETREITIGALLREVAAARPDAEALVEVMQDGSEGQRWTYAELL
AEAERLALALSSRFAPGERVVIWSPNSPEWVLMEYACSLSGLVLVTANPAFQARELAYVL
EQSGAVALFLVEEFRGNPMGRIGAEVVTDIAAIREVTDMESDAFFAQGTRPPALPEVAPG
DAAMIQYTSGTTGFPKGAVLSHRGLVNNARFYASRCGATETTTWVNIMPMFHTSGCGMVT
LGCLQAGCKMVLVSLFDPNIVLDQLEASGADIILGVPTMVVALLDAQEARPRNLSALKLV
SCGGSMVAPELVRRVEALMGAGFSTLYGQTEHCPVITQHHLSDSIDDICNTAGQPVAQTE
VSIRSVDDNSVVAVGEVGEICARGPCVMLEYNDNPKATSETVDAMGWLHTGDLGRMDARG
YVTVTGRVKEMIIRGGENHFPAEIENCLLEHASVAEVAVVGLPDPKWGEVIGAFLRGTEP
LDKTALHAHCRANMSPQKTPNIWVQVEVFPLTGSGKIQKFILRDRFVAGDFTEL
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