SitesBLAST
Comparing WP_012675637.1 NCBI__GCF_000021565.1:WP_012675637.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 15 hits to proteins with known functional sites (download)
5ygeA Arga complexed with acecoa and glutamate (see paper)
37% identity, 83% coverage: 4:132/155 of query aligns to 7:137/169 of 5ygeA
- binding acetyl coenzyme *a: Y25 (= Y22), I73 (= I68), V76 (≠ L71), A77 (= A72), V78 (= V73), T83 (≠ Q78), G84 (= G79), H85 (≠ R80), G86 (= G81), G88 (= G83), H89 (≠ K84), T111 (= T106), E113 (≠ V108), F117 (= F112)
- binding glutamic acid: K33 (≠ R31), E44 (≠ D42), H64 (= H59), R74 (≠ K69)
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, 83% coverage: 4:132/155 of query aligns to 6:136/168 of 6addA
- binding coenzyme a: Y24 (= Y22), I28 (= I27), V75 (≠ L71), A76 (= A72), V77 (= V73), T82 (≠ Q78), G83 (= G79), H84 (≠ R80), G85 (= G81), G87 (= G83), H88 (≠ K84), T110 (= T106), E112 (≠ V108), F115 (= F111)
- binding n~2~-acetyl-l-glutamine: K27 (= K25), I28 (= I27), L30 (= L29), T74 (≠ S70), L109 (= L105)
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, 83% coverage: 4:132/155 of query aligns to 6:136/168 of 5yo2A
- binding acetyl coenzyme *a: Y24 (= Y22), I28 (= I27), I72 (= I68), R73 (≠ K69), T74 (≠ S70), V75 (≠ L71), V77 (= V73), T82 (≠ Q78), G83 (= G79), H84 (≠ R80), G85 (= G81), G87 (= G83), H88 (≠ K84), T110 (= T106), E112 (≠ V108), F115 (= F111), F116 (= F112)
- binding arginine: G26 (≠ I24), L29 (= L28), L30 (= L29), R73 (≠ K69), L109 (= L105)
Sites not aligning to the query:
4i49A Structure of ngnags bound with bisubstrate analog coa-NAG (see paper)
37% identity, 80% coverage: 4:127/155 of query aligns to 277:402/424 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 (= I27), L301 (= L28), L302 (= L29), R304 (= R31), A343 (≠ K69), C344 (≠ S70), L345 (= L71), A346 (= A72), V347 (= V73), Q352 (= Q78), D353 (≠ G79), G355 (= G81), G357 (= G83), E358 (≠ K84), L379 (= L105), S380 (vs. gap), T383 (≠ V108), W386 (≠ F111), F387 (= F112)
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)
37% identity, 80% coverage: 4:127/155 of query aligns to 277:402/424 of 3d2mA
- binding coenzyme a: L345 (= L71), V347 (= V73), Q352 (= Q78), D353 (≠ G79), G355 (= G81), G357 (= G83), E358 (≠ K84), S380 (vs. gap), T383 (≠ V108), W386 (≠ F111)
- binding glutamic acid: L302 (= L29), R304 (= R31), A343 (≠ K69), C344 (≠ S70), L379 (= L105)
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)
37% identity, 80% coverage: 4:127/155 of query aligns to 277:402/424 of 3b8gA
- binding coenzyme a: I300 (= I27), L345 (= L71), V347 (= V73), Q352 (= Q78), D353 (≠ G79), G355 (= G81), Y356 (≠ I82), G357 (= G83), E358 (≠ K84), S380 (vs. gap), T383 (≠ V108), E385 (≠ Q110), W386 (≠ F111)
- binding n-acetyl-l-glutamate: L302 (= L29), R304 (= R31), A343 (≠ K69), C344 (≠ S70), L379 (= L105)
Sites not aligning to the query:
2r8vA Native structure of n-acetylglutamate synthase from neisseria gonorrhoeae (see paper)
37% identity, 80% coverage: 4:127/155 of query aligns to 277:402/424 of 2r8vA
- binding acetyl coenzyme *a: I300 (= I27), L301 (= L28), L345 (= L71), V347 (= V73), Q352 (= Q78), D353 (≠ G79), G355 (= G81), G357 (= G83), E358 (≠ K84), T383 (≠ V108), E385 (≠ Q110), W386 (≠ F111), F387 (= F112)
Sites not aligning to the query:
3d2pA Crystal structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and l-arginine (see paper)
36% identity, 80% coverage: 4:127/155 of query aligns to 285:406/424 of 3d2pA
Sites not aligning to the query:
- active site: 26
- binding arginine: 13, 197, 216, 253, 266, 267, 269, 270, 271, 274, 276
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: 4:127/155 of query aligns to 298:423/443 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.
3f8kA Crystal structure of protein acetyltransferase (pat) from sulfolobus solfataricus (see paper)
34% identity, 74% coverage: 4:118/155 of query aligns to 3:116/131 of 3f8kA
- binding coenzyme a: L28 (= L29), L64 (= L71), V65 (≠ A72), V66 (= V73), R71 (≠ Q78), T72 (≠ G79), G74 (= G81), G76 (= G83), T77 (≠ K84), F97 (≠ V102), N103 (vs. gap), P105 (≠ Y107), M106 (≠ V108), K108 (≠ Q110), I109 (≠ F111), K112 (= K114)
6wqbA Crystal structure of vipf from legionella hackeliae in complex with acetyl-coa
31% identity, 46% coverage: 55:125/155 of query aligns to 201:277/290 of 6wqbA
- binding acetyl coenzyme *a: I218 (≠ L71), A219 (= A72), I220 (≠ V73), Q225 (= Q78), G226 (= G79), G228 (= G81), G230 (= G83), G231 (≠ K84), D252 (vs. gap), N259 (≠ Y107), Y264 (≠ F112)
Sites not aligning to the query:
- binding acetyl coenzyme *a: 76, 77, 78, 83, 84, 86, 88, 89, 109, 112, 119, 125, 169, 170, 289
Q7X9V3 GCN5-related N-acetyltransferase 2, chloroplastic; Acetyltransferase NSI; AtNSI; Nuclear shuttle protein-interacting protein; Serotonin N-acetyl transferase 1; AtSNAT; AtSNAT1; EC 2.3.1.255; EC 2.3.1.48; EC 2.3.1.87 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
40% identity, 43% coverage: 52:117/155 of query aligns to 179:243/258 of Q7X9V3
- D194 (≠ S70) mutation to G: Complete loss of interaction with CaLCuV NSP protein.
Sites not aligning to the query:
- 107 I→T: Complete loss of interaction with CaLCuV NSP protein.
- 136 K→E: Complete loss of interaction with CaLCuV NSP protein.
6wqcA Crystal structure of vipf from legionella hackeliae in complex with coa
32% identity, 43% coverage: 59:125/155 of query aligns to 207:279/293 of 6wqcA
- binding coenzyme a: I220 (≠ L71), A221 (= A72), I222 (≠ V73), P224 (= P75), Q227 (= Q78), G230 (= G81), G232 (= G83), G233 (≠ K84), A262 (≠ V108), H264 (≠ Q110), L265 (≠ F111)
Sites not aligning to the query:
- binding coenzyme a: 77, 78, 79, 84, 85, 87, 89, 90, 110, 113, 120, 124, 169, 170, 291
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)
30% identity, 74% coverage: 4:118/155 of query aligns to 7:131/160 of Q97V23
- D29 (≠ G26) mutation to A: Modestly reduces acetylation activity.
- Y31 (≠ L28) 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 (≠ E38) mutation to N: Reduces acetylation activity.
- E68 (≠ V55) mutation to Q: No effect on acetylation activity.
- H72 (= H59) 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 (= E63) 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 (= S70) mutation to A: No effect on acetylation activity.; mutation to C: Modestly reduces acetylation activity.
- L79 (= L71) binding CoA
- V81 (= V73) binding CoA
- T87 (≠ G79) binding CoA
- G89 (= G81) binding CoA
- GIG 89:91 (= GIG 81:83) mutation to AAA: Reduces acetylation activity.
- G91 (= G83) binding CoA
- T92 (≠ K84) binding CoA
- Y113 (≠ F103) mutation to F: No effect on acetylation activity.
- N118 (vs. gap) binding CoA
- M121 (≠ V108) mutation M->H,Y: Reduces acetylation activity, affinity to albA1 11-mer peptide and has no effect on acetyl-CoA affinity.
- K123 (≠ Q110) binding CoA
- K127 (= K114) binding CoA
6ao7A Crystal structure of a gnat family acetyltransferase from elizabethkingia anophelis with acetyl-coa bound (see paper)
25% identity, 62% coverage: 42:137/155 of query aligns to 38:144/153 of 6ao7A
- binding acetyl coenzyme *a: K65 (= K69), N66 (≠ S70), I67 (≠ L71), A68 (= A72), V69 (= V73), Q74 (= Q78), N75 (≠ G79), G77 (= G81), G79 (= G83), G101 (vs. gap), G108 (≠ Y107), Q109 (≠ V108), Y111 (≠ Q110), L112 (≠ F111), K115 (= K114)
Sites not aligning to the query:
Query Sequence
>WP_012675637.1 NCBI__GCF_000021565.1:WP_012675637.1
MTGIRKANVKDAHQIFKILQSYAIKGILLPRSLNSIYEHIRDFFVYEIDGKIAGVCSLHI
FWEDLAEIKSLAVLPEYQGRGIGKKLVERCIEDARSLGVKKVFALTYVPQFFEKLGFRTV
EKSEFPQKVWTECIHCVKFNECSEVPVLLNLEDQS
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