SitesBLAST
Comparing WP_089323136.1 NCBI__GCF_900188395.1:WP_089323136.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 11 hits to proteins with known functional sites (download)
5ygeA Arga complexed with acecoa and glutamate (see paper)
37% identity, 80% coverage: 5:131/158 of query aligns to 7:135/169 of 5ygeA
- binding acetyl coenzyme *a: Y25 (= Y23), I73 (= I69), V76 (≠ L72), A77 (= A73), V78 (= V74), T83 (≠ R79), G84 (≠ K80), H85 (≠ Q81), G86 (= G82), G88 (= G84), H89 (≠ R85), T111 (= T107), E113 (≠ Q109), F117 (= F113)
- binding glutamic acid: K33 (≠ R32), E44 (≠ D43), H64 (≠ T60), R74 (= R70)
Sites not aligning to the query:
6addA The crystal structure of rv2747 from mycobacterium tuberculosis in complex with coa and nlq (see paper)
37% identity, 80% coverage: 5:131/158 of query aligns to 6:134/168 of 6addA
- binding coenzyme a: Y24 (= Y23), I28 (≠ L28), V75 (≠ L72), A76 (= A73), V77 (= V74), T82 (≠ R79), G83 (≠ K80), H84 (≠ Q81), G85 (= G82), G87 (= G84), H88 (≠ R85), T110 (= T107), E112 (≠ Q109), F115 (= F112)
- binding n~2~-acetyl-l-glutamine: K27 (≠ Q26), I28 (≠ L28), L30 (= L30), T74 (≠ S71), L109 (= L106)
Sites not aligning to the query:
5yo2A The crystal structure of rv2747 from mycobacterium tuberculosis in complex with acetyl coa and l-arginine (see paper)
37% identity, 80% coverage: 5:131/158 of query aligns to 6:134/168 of 5yo2A
- binding acetyl coenzyme *a: Y24 (= Y23), I28 (≠ L28), I72 (= I69), R73 (= R70), T74 (≠ S71), V75 (≠ L72), V77 (= V74), T82 (≠ R79), G83 (≠ K80), H84 (≠ Q81), G85 (= G82), G87 (= G84), H88 (≠ R85), T110 (= T107), E112 (≠ Q109), F115 (= F112), F116 (= F113)
- binding arginine: G26 (≠ K25), L29 (≠ M29), L30 (= L30), R73 (= R70), L109 (= L106)
Sites not aligning to the query:
4i49A Structure of ngnags bound with bisubstrate analog coa-NAG (see paper)
32% identity, 82% coverage: 4:133/158 of query aligns to 276:407/424 of 4i49A
- binding (2S)-2-({(3S,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14,20-trioxo-2,4,6-trioxa-18-thia-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaicosan-20-yl}amino)pentanedioic acid (non-preferred name): I300 (≠ L28), L301 (≠ M29), L302 (= L30), R304 (= R32), A343 (≠ R70), C344 (≠ S71), L345 (= L72), A346 (= A73), V347 (= V74), Q352 (≠ R79), D353 (≠ K80), G355 (= G82), G357 (= G84), E358 (≠ R85), L379 (= L106), S380 (vs. gap), T383 (≠ Q109), W386 (≠ F112), F387 (= F113)
Sites not aligning to the query:
- binding (2S)-2-({(3S,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14,20-trioxo-2,4,6-trioxa-18-thia-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaicosan-20-yl}amino)pentanedioic acid (non-preferred name): 413, 415
3d2mA Crystal structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and l-glutamate (see paper)
32% identity, 82% coverage: 4:133/158 of query aligns to 276:407/424 of 3d2mA
- binding coenzyme a: L345 (= L72), V347 (= V74), Q352 (≠ R79), D353 (≠ K80), G355 (= G82), G357 (= G84), E358 (≠ R85), S380 (vs. gap), T383 (≠ Q109), W386 (≠ F112)
- binding glutamic acid: L302 (= L30), R304 (= R32), A343 (≠ R70), C344 (≠ S71), L379 (= L106)
Sites not aligning to the query:
3b8gA Crysta structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and n-acetyl-glutamate (see paper)
32% identity, 82% coverage: 4:133/158 of query aligns to 276:407/424 of 3b8gA
- binding coenzyme a: I300 (≠ L28), L345 (= L72), V347 (= V74), Q352 (≠ R79), D353 (≠ K80), G355 (= G82), Y356 (≠ I83), G357 (= G84), E358 (≠ R85), S380 (vs. gap), T383 (≠ Q109), E385 (= E111), W386 (≠ F112)
- binding n-acetyl-l-glutamate: L302 (= L30), R304 (= R32), A343 (≠ R70), C344 (≠ S71), L379 (= L106)
Sites not aligning to the query:
2r8vA Native structure of n-acetylglutamate synthase from neisseria gonorrhoeae (see paper)
32% identity, 82% coverage: 4:133/158 of query aligns to 276:407/424 of 2r8vA
- binding acetyl coenzyme *a: I300 (≠ L28), L301 (≠ M29), L345 (= L72), V347 (= V74), Q352 (≠ R79), D353 (≠ K80), G355 (= G82), G357 (= G84), E358 (≠ R85), T383 (≠ Q109), E385 (= E111), W386 (≠ F112), F387 (= F113)
Sites not aligning to the query:
P0A6C5 Amino-acid acetyltransferase; N-acetylglutamate synthase; AGS; NAGS; EC 2.3.1.1 from Escherichia coli (strain K12) (see paper)
29% identity, 80% coverage: 4:129/158 of query aligns to 297:424/443 of P0A6C5
Sites not aligning to the query:
- 15 H→Y: In EE17.
- 19 Y→C: In EE51.
- 54 S→N: In PT2M217.
- 58 R→H: In EE11.
- 287 G→S: In PT2M216.
- 432 Q→R: In PT2M217.
3d2pA Crystal structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and l-arginine (see paper)
30% identity, 85% coverage: 4:137/158 of query aligns to 284:415/424 of 3d2pA
Sites not aligning to the query:
- active site: 26
- binding arginine: 13, 197, 216, 253, 266, 267, 269, 270, 271, 274, 276
3f8kA Crystal structure of protein acetyltransferase (pat) from sulfolobus solfataricus (see paper)
36% identity, 73% coverage: 4:119/158 of query aligns to 2:116/131 of 3f8kA
- binding coenzyme a: L28 (= L30), L64 (= L72), V65 (≠ A73), V66 (= V74), R71 (= R79), T72 (≠ K80), G74 (= G82), G76 (= G84), T77 (≠ R85), F97 (≠ I103), N103 (≠ Q109), P105 (≠ E111), M106 (≠ F112), K108 (= K114), I109 (vs. gap), K112 (= K115)
Q97V23 N-acetyltransferase Pat; ssPat; EC 2.3.1.- from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see 2 papers)
32% identity, 73% coverage: 4:119/158 of query aligns to 6:131/160 of Q97V23
- D29 (≠ G27) mutation to A: Modestly reduces acetylation activity.
- Y31 (≠ M29) mutation to S: No effect on acetylation activity.
- R33 (vs. gap) mutation to A: Reduces acetylation activity, affinity to albA1 11-mer peptide and has no effect on acetyl-CoA affinity.
- H36 (vs. gap) mutation to A: No effect on acetylation activity.
- Y38 (vs. gap) mutation to S: Reduces acetylation activity.
- E42 (vs. gap) mutation to Q: Modestly reduces acetylation activity.
- E43 (vs. gap) mutation to Q: Modestly reduces acetylation activity.
- D53 (≠ E39) mutation to N: Reduces acetylation activity.
- E68 (≠ V56) mutation to Q: No effect on acetylation activity.
- H72 (≠ T60) mutation to A: Modestly reduces acetylation activity. Modestly reduces acetylation activity, reduces affinity to albA1 11-mer peptide and has no effect on acetyl-CoA affinity; when associated with Q-76. Reduces acetylation activity; when associated with A-76.
- E76 (≠ D64) mutation to A: Reduces acetylation activity, affinity to albA1 11-mer peptide and has no effect on acetyl-CoA affinity. Reduces acetylation activity; when associated with A-72.; mutation to Q: No effect on acetylation activity. Modestly reduces acetylation activity, reduces affinity to albA1 11-mer peptide and has no effect on acetyl-CoA affinity; when associated with A-72.
- S78 (= S71) mutation to A: No effect on acetylation activity.; mutation to C: Modestly reduces acetylation activity.
- L79 (= L72) binding CoA
- V81 (= V74) binding CoA
- T87 (≠ K80) binding CoA
- G89 (= G82) binding CoA
- GIG 89:91 (= GIG 82:84) mutation to AAA: Reduces acetylation activity.
- G91 (= G84) binding CoA
- T92 (≠ R85) binding CoA
- Y113 (≠ F104) mutation to F: No effect on acetylation activity.
- N118 (≠ Q109) binding CoA
- M121 (≠ F112) mutation M->H,Y: Reduces acetylation activity, affinity to albA1 11-mer peptide and has no effect on acetyl-CoA affinity.
- K123 (= K114) binding CoA
- K127 (= K115) binding CoA
Query Sequence
>WP_089323136.1 NCBI__GCF_900188395.1:WP_089323136.1
MKGKVRKATIKDAEAIQFLINEYAKQGLMLPRSLNSIYENIRDFFVYEEDGKILGVCALT
VVWDNLAEIRSLAVHPEKRKQGIGRTLIKACLEDAKHLQITRIFTLTYQSEFFKKLGFKE
IDKNTLPQKIWRDCINCVKFPNCDETAMEIETGGNNDT
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