SitesBLAST
Comparing 7026634 Shewana3_3767 N-acetylglutamate synthase (RefSeq) 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)
P0A6C5 Amino-acid acetyltransferase; N-acetylglutamate synthase; AGS; NAGS; EC 2.3.1.1 from Escherichia coli (strain K12) (see paper)
65% identity, 98% coverage: 8:445/445 of query aligns to 5:442/443 of P0A6C5
- H15 (= H18) mutation to Y: In EE17.
- Y19 (= Y22) mutation to C: In EE51.
- S54 (= S57) mutation to N: In PT2M217.
- R58 (≠ K61) mutation to H: In EE11.
- G287 (= G290) mutation to S: In PT2M216.
- Q432 (= Q435) mutation to R: In PT2M217.
4i49A Structure of ngnags bound with bisubstrate analog coa-NAG (see paper)
40% identity, 97% coverage: 12:441/445 of query aligns to 3:418/424 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 (= L319), I300 (= I324), L301 (= L325), L302 (≠ V326), R304 (= R328), A343 (= A367), C344 (= C368), L345 (= L369), A346 (≠ V370), V347 (= V371), Q352 (≠ R376), D353 (= D377), G354 (≠ A378), G355 (≠ D379), Y356 (≠ R380), G357 (= G381), E358 (≠ S382), L379 (= L403), S380 (≠ T404), N382 (≠ R406), T383 (≠ S407), E385 (≠ H409), W386 (= W410), F387 (= F411), R390 (≠ H414), R404 (≠ K428), R413 (= R436), S415 (= S438)
3d2mA Crystal structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and l-glutamate (see paper)
40% identity, 97% coverage: 12:441/445 of query aligns to 3:418/424 of 3d2mA
- active site: I26 (≠ L35)
- binding coenzyme a: L295 (= L319), I300 (= I324), L345 (= L369), A346 (≠ V370), V347 (= V371), Q352 (≠ R376), D353 (= D377), G354 (≠ A378), G355 (≠ D379), Y356 (≠ R380), G357 (= G381), E358 (≠ S382), S380 (≠ T404), T383 (≠ S407), E385 (≠ H409), W386 (= W410), F387 (= F411), R390 (≠ H414)
- binding glutamic acid: I300 (= I324), L301 (= L325), L302 (≠ V326), R304 (= R328), A343 (= A367), C344 (= C368), L379 (= L403), R404 (≠ K428), R413 (= R436), S415 (= S438)
3b8gA Crysta structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and n-acetyl-glutamate (see paper)
40% identity, 97% coverage: 12:441/445 of query aligns to 3:418/424 of 3b8gA
- active site: I26 (≠ L35)
- binding coenzyme a: L295 (= L319), I300 (= I324), L301 (= L325), L345 (= L369), V347 (= V371), Q352 (≠ R376), D353 (= D377), G354 (≠ A378), G355 (≠ D379), Y356 (≠ R380), G357 (= G381), E358 (≠ S382), S380 (≠ T404), T383 (≠ S407), E385 (≠ H409), W386 (= W410), R390 (≠ H414)
- binding n-acetyl-l-glutamate: I300 (= I324), L301 (= L325), L302 (≠ V326), R304 (= R328), A343 (= A367), C344 (= C368), L345 (= L369), L379 (= L403), S380 (≠ T404), R413 (= R436), S415 (= S438)
2r8vA Native structure of n-acetylglutamate synthase from neisseria gonorrhoeae (see paper)
40% identity, 97% coverage: 12:441/445 of query aligns to 3:418/424 of 2r8vA
- active site: I26 (≠ L35)
- binding acetyl coenzyme *a: L295 (= L319), I300 (= I324), L301 (= L325), A343 (= A367), C344 (= C368), L345 (= L369), A346 (≠ V370), V347 (= V371), Q352 (≠ R376), D353 (= D377), G354 (≠ A378), G355 (≠ D379), Y356 (≠ R380), G357 (= G381), E358 (≠ S382), L379 (= L403), S380 (≠ T404), T383 (≠ S407), E385 (≠ H409), W386 (= W410), F387 (= F411)
3d2pA Crystal structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and l-arginine (see paper)
39% identity, 97% coverage: 12:441/445 of query aligns to 3:418/424 of 3d2pA
- active site: I26 (≠ L35)
- binding arginine: Y13 (= Y22), K197 (= K207), E216 (≠ A226), Q253 (≠ H269), E266 (= E282), L267 (= L283), T269 (≠ S285), R270 (= R286), N271 (≠ E287), G272 (= G288), I273 (= I289), G274 (= G290), T275 (= T291), S276 (≠ Q292), D326 (= D346)
- binding coenzyme a: L303 (= L319), L349 (= L369), A350 (≠ V370), V351 (= V371), Q356 (≠ R376), D357 (= D377), G358 (≠ A378), G359 (≠ D379), Y360 (≠ R380), G361 (= G381), E362 (≠ S382), N386 (≠ R406), T387 (≠ S407), E389 (≠ H409), W390 (= W410), R394 (≠ H414)
2btyA Acetylglutamate kinase from thermotoga maritima complexed with its inhibitor arginine (see paper)
30% identity, 61% coverage: 21:293/445 of query aligns to 14:277/282 of 2btyA
- active site: K27 (≠ M34), G30 (= G37), G63 (≠ R69), D182 (≠ E193), K237 (≠ F253)
- binding arginine: Y15 (= Y22), F19 (≠ H26), K196 (= K207), S214 (≠ A226), H253 (= H269), E266 (= E282), I267 (≠ L283), S269 (= S285), R270 (= R286), K271 (≠ E287), G272 (= G288), G274 (= G290), T275 (= T291), M276 (≠ Q292)
- binding n-acetyl-l-glutamate: K27 (≠ M34), G29 (= G36), G30 (= G37), G61 (= G67), G62 (≠ A68), G63 (≠ R69), N180 (≠ T191), 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)
30% identity, 61% coverage: 21:293/445 of query aligns to 14:277/282 of Q9X2A4
2v5hB Controlling the storage of nitrogen as arginine: the complex of pii and acetylglutamate kinase from synechococcus elongatus pcc 7942 (see paper)
31% identity, 62% coverage: 21:294/445 of query aligns to 15:282/289 of 2v5hB
- active site: K28 (≠ M34), G31 (= G37), G64 (≠ R69), D182 (≠ E193), K241 (≠ F253)
- binding n-acetyl-l-glutamate: G62 (= G67), G63 (≠ A68), G64 (≠ R69), I67 (= I72), L84 (≠ V89), R85 (= R90), N178 (= N189), I179 (≠ L190), N180 (≠ T191), A181 (= A192)
2bufA Arginine feed-back inhibitable acetylglutamate kinase (see paper)
28% identity, 61% coverage: 21:293/445 of query aligns to 19:286/292 of 2bufA
- active site: K32 (≠ M34), G35 (= G37), G68 (≠ R69), D190 (≠ E193), K246 (≠ F253)
- binding n-acetyl-l-glutamate: G66 (= G67), G67 (≠ A68), I71 (= I72), M88 (≠ V89), R89 (= R90), N186 (= N189), A189 (= A192)
2bufC Arginine feed-back inhibitable acetylglutamate kinase (see paper)
27% identity, 62% coverage: 16:293/445 of query aligns to 14:294/298 of 2bufC
- active site: K32 (≠ M34), G35 (= G37), G68 (≠ R69), D198 (≠ E193), K254 (≠ F253)
- binding adenosine-5'-diphosphate: N36 (≠ E38), T217 (≠ S212), N218 (≠ S213), I219 (≠ Q214), L222 (≠ I217), M223 (≠ L218), T246 (≠ S245), I247 (≠ A246), Y248 (≠ C247), G250 (= G249), M251 (≠ T250), K254 (≠ F253)
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)
27% identity, 62% coverage: 16:293/445 of query aligns to 15:295/301 of Q9HTN2
- R90 (= R90) binding
- N195 (= N189) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4usjB N-acetylglutamate kinase from arabidopsis thaliana in complex with pii from chlamydomonas reinhardtii (see paper)
27% identity, 63% coverage: 13:293/445 of query aligns to 4:279/281 of 4usjB