SitesBLAST
Comparing Dsui_1570 Dsui_1570 amino-acid N-acetyltransferase 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)
P0A6C5 Amino-acid acetyltransferase; N-acetylglutamate synthase; AGS; NAGS; EC 2.3.1.1 from Escherichia coli (strain K12) (see paper)
45% identity, 98% coverage: 10:447/448 of query aligns to 7:443/443 of P0A6C5
- H15 (≠ S18) mutation to Y: In EE17.
- Y19 (= Y22) mutation to C: In EE51.
- S54 (≠ N57) mutation to N: In PT2M217.
- R58 (= R61) mutation to H: In EE11.
- G287 (= G287) mutation to S: In PT2M216.
- Q432 (= Q436) mutation to R: In PT2M217.
4i49A Structure of ngnags bound with bisubstrate analog coa-NAG (see paper)
42% identity, 98% coverage: 12:448/448 of query aligns to 3:424/424 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): L295 (= L316), I300 (≠ T321), L301 (= L322), L302 (≠ V323), R304 (= R325), A343 (= A368), C344 (= C369), L345 (= L370), A346 (= A371), V347 (= V372), Q352 (≠ R377), D353 (≠ R378), G354 (≠ W379), G355 (= G380), Y356 (= Y381), G357 (= G382), E358 (= E383), L379 (= L404), S380 (≠ T405), N382 (≠ R407), T383 (= T408), E385 (≠ H410), W386 (= W411), F387 (= F412), R390 (= R415), R404 (≠ K429), R413 (= R437), S415 (= S439)
3d2mA Crystal structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and l-glutamate (see paper)
42% identity, 98% coverage: 12:448/448 of query aligns to 3:424/424 of 3d2mA
- active site: I26 (≠ F35)
- binding coenzyme a: L295 (= L316), I300 (≠ T321), L345 (= L370), A346 (= A371), V347 (= V372), Q352 (≠ R377), D353 (≠ R378), G354 (≠ W379), G355 (= G380), Y356 (= Y381), G357 (= G382), E358 (= E383), S380 (≠ T405), T383 (= T408), E385 (≠ H410), W386 (= W411), F387 (= F412), R390 (= R415)
- binding glutamic acid: I300 (≠ T321), L301 (= L322), L302 (≠ V323), R304 (= R325), A343 (= A368), C344 (= C369), L379 (= L404), R404 (≠ K429), R413 (= R437), S415 (= S439)
3b8gA Crysta structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and n-acetyl-glutamate (see paper)
42% identity, 98% coverage: 12:448/448 of query aligns to 3:424/424 of 3b8gA
- active site: I26 (≠ F35)
- binding coenzyme a: L295 (= L316), I300 (≠ T321), L301 (= L322), L345 (= L370), V347 (= V372), Q352 (≠ R377), D353 (≠ R378), G354 (≠ W379), G355 (= G380), Y356 (= Y381), G357 (= G382), E358 (= E383), S380 (≠ T405), T383 (= T408), E385 (≠ H410), W386 (= W411), R390 (= R415)
- binding n-acetyl-l-glutamate: I300 (≠ T321), L301 (= L322), L302 (≠ V323), R304 (= R325), A343 (= A368), C344 (= C369), L345 (= L370), L379 (= L404), S380 (≠ T405), R413 (= R437), S415 (= S439)
2r8vA Native structure of n-acetylglutamate synthase from neisseria gonorrhoeae (see paper)
42% identity, 98% coverage: 12:448/448 of query aligns to 3:424/424 of 2r8vA
- active site: I26 (≠ F35)
- binding acetyl coenzyme *a: L295 (= L316), I300 (≠ T321), L301 (= L322), A343 (= A368), C344 (= C369), L345 (= L370), A346 (= A371), V347 (= V372), Q352 (≠ R377), D353 (≠ R378), G354 (≠ W379), G355 (= G380), Y356 (= Y381), G357 (= G382), E358 (= E383), L379 (= L404), S380 (≠ T405), T383 (= T408), E385 (≠ H410), W386 (= W411), F387 (= F412)
3d2pA Crystal structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and l-arginine (see paper)
42% identity, 98% coverage: 12:448/448 of query aligns to 3:424/424 of 3d2pA
- active site: I26 (≠ F35)
- binding arginine: Y13 (= Y22), K197 (= K207), E216 (≠ D226), Q253 (≠ H266), E266 (= E279), L267 (= L280), T269 (= T282), R270 (≠ H283), N271 (≠ D284), G272 (= G285), I273 (≠ V286), G274 (= G287), T275 (= T288), S276 (≠ V289), D326 (= D343)
- binding coenzyme a: L303 (= L316), L349 (= L370), A350 (= A371), V351 (= V372), Q356 (≠ R377), D357 (≠ R378), G358 (≠ W379), G359 (= G380), Y360 (= Y381), G361 (= G382), E362 (= E383), N386 (≠ R407), T387 (= T408), E389 (≠ H410), W390 (= W411), R394 (= R415)
2btyA Acetylglutamate kinase from thermotoga maritima complexed with its inhibitor arginine (see paper)
34% identity, 60% coverage: 21:290/448 of query aligns to 14:277/282 of 2btyA
- active site: K27 (≠ A34), G30 (= G37), G63 (≠ R69), D182 (≠ E193), K237 (≠ Y250)
- binding arginine: Y15 (= Y22), F19 (= F26), K196 (= K207), S214 (≠ D226), H253 (= H266), E266 (= E279), I267 (≠ L280), S269 (≠ T282), R270 (≠ H283), K271 (≠ D284), G272 (= G285), G274 (= G287), T275 (= T288), M276 (≠ V289)
- binding n-acetyl-l-glutamate: K27 (≠ A34), G29 (= G36), G30 (= G37), G61 (= G67), G62 (≠ S68), G63 (≠ R69), N180 (≠ S191), D182 (≠ E193)
Q9X2A4 Acetylglutamate kinase; N-acetyl-L-glutamate 5-phosphotransferase; NAG kinase; NAGK; EC 2.7.2.8 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
34% identity, 60% coverage: 21:290/448 of query aligns to 14:277/282 of Q9X2A4
2bufA Arginine feed-back inhibitable acetylglutamate kinase (see paper)
33% identity, 64% coverage: 8:292/448 of query aligns to 6:288/292 of 2bufA
- active site: K32 (≠ A34), G35 (= G37), G68 (≠ R69), D190 (≠ E193), K246 (≠ R249)
- binding n-acetyl-l-glutamate: G66 (= G67), G67 (≠ S68), I71 (= I72), M88 (≠ Q89), R89 (= R90), N186 (= N189), A189 (≠ M192)
2bufC Arginine feed-back inhibitable acetylglutamate kinase (see paper)
32% identity, 64% coverage: 8:292/448 of query aligns to 6:296/298 of 2bufC
- active site: K32 (≠ A34), G35 (= G37), G68 (≠ R69), D198 (≠ E193), K254 (≠ R249)
- binding adenosine-5'-diphosphate: N36 (≠ K38), T217 (= T212), N218 (≠ D213), I219 (≠ S214), L222 (≠ A217), M223 (≠ T218), T246 (≠ E241), I247 (≠ W242), Y248 (≠ L243), G250 (≠ P245), M251 (≠ D246), K254 (≠ R249)
Q9HTN2 Acetylglutamate kinase; N-acetyl-L-glutamate 5-phosphotransferase; NAG kinase; NAGK; EC 2.7.2.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
32% identity, 64% coverage: 8:292/448 of query aligns to 7:297/301 of Q9HTN2
- R90 (= R90) binding
- N195 (= N189) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2v5hB Controlling the storage of nitrogen as arginine: the complex of pii and acetylglutamate kinase from synechococcus elongatus pcc 7942 (see paper)
32% identity, 63% coverage: 9:291/448 of query aligns to 3:282/289 of 2v5hB