SitesBLAST
Comparing GFF5312 FitnessBrowser__WCS417:GFF5312 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)
51% identity, 99% coverage: 3:429/433 of query aligns to 8:438/443 of P0A6C5
- H15 (= H10) mutation to Y: In EE17.
- Y19 (= Y14) mutation to C: In EE51.
- S54 (= S49) mutation to N: In PT2M217.
- R58 (= R53) mutation to H: In EE11.
- G287 (= G278) mutation to S: In PT2M216.
- Q432 (= Q423) mutation to R: In PT2M217.
4i49A Structure of ngnags bound with bisubstrate analog coa-NAG (see paper)
39% identity, 99% coverage: 4:433/433 of query aligns to 3:422/424 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 (= I312), L301 (= L313), L302 (≠ V314), R304 (= R316), A343 (= A355), C344 (= C356), L345 (= L357), A346 (= A358), V347 (= V359), Q352 (≠ R364), D353 (≠ H365), G355 (≠ A367), G357 (= G369), E358 (≠ D370), L379 (= L391), S380 (≠ T392), T383 (= T395), W386 (= W398), F387 (= F399), R413 (= R424), S415 (= S426)
3d2mA Crystal structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and l-glutamate (see paper)
39% identity, 99% coverage: 4:433/433 of query aligns to 3:422/424 of 3d2mA
- active site: I26 (≠ L27)
- binding coenzyme a: L345 (= L357), V347 (= V359), Q352 (≠ R364), D353 (≠ H365), G355 (≠ A367), G357 (= G369), E358 (≠ D370), S380 (≠ T392), T383 (= T395), W386 (= W398)
- binding glutamic acid: L302 (≠ V314), R304 (= R316), A343 (= A355), C344 (= C356), L379 (= L391), R413 (= R424), S415 (= S426)
3b8gA Crysta structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and n-acetyl-glutamate (see paper)
39% identity, 99% coverage: 4:433/433 of query aligns to 3:422/424 of 3b8gA
- active site: I26 (≠ L27)
- binding coenzyme a: I300 (= I312), L345 (= L357), V347 (= V359), Q352 (≠ R364), D353 (≠ H365), G355 (≠ A367), Y356 (≠ R368), G357 (= G369), E358 (≠ D370), S380 (≠ T392), T383 (= T395), E385 (≠ H397), W386 (= W398)
- binding n-acetyl-l-glutamate: L302 (≠ V314), R304 (= R316), A343 (= A355), C344 (= C356), L379 (= L391), R413 (= R424), S415 (= S426)
2r8vA Native structure of n-acetylglutamate synthase from neisseria gonorrhoeae (see paper)
39% identity, 99% coverage: 4:433/433 of query aligns to 3:422/424 of 2r8vA
- active site: I26 (≠ L27)
- binding acetyl coenzyme *a: I300 (= I312), L301 (= L313), L345 (= L357), V347 (= V359), Q352 (≠ R364), D353 (≠ H365), G355 (≠ A367), G357 (= G369), E358 (≠ D370), T383 (= T395), E385 (≠ H397), W386 (= W398), F387 (= F399)
3d2pA Crystal structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and l-arginine (see paper)
38% identity, 99% coverage: 4:433/433 of query aligns to 3:422/424 of 3d2pA
- active site: I26 (≠ L27)
- binding arginine: Y13 (= Y14), K197 (= K199), E216 (≠ R218), Q253 (≠ H257), E266 (= E270), L267 (= L271), T269 (= T273), R270 (= R274), N271 (≠ D275), G274 (= G278), S276 (≠ L280)
- binding coenzyme a: L303 (= L307), L349 (= L357), V351 (= V359), Q356 (≠ R364), D357 (≠ H365), G359 (≠ A367), G361 (= G369), E362 (≠ D370), E389 (≠ H397), W390 (= W398)
2btyA Acetylglutamate kinase from thermotoga maritima complexed with its inhibitor arginine (see paper)
27% identity, 65% coverage: 3:283/433 of query aligns to 4:279/282 of 2btyA
- active site: K27 (≠ M26), G30 (= G29), G63 (≠ R61), D182 (≠ E185), K237 (≠ L241)
- binding arginine: Y15 (= Y14), F19 (≠ H18), K196 (= K199), S214 (≠ R218), E266 (= E270), I267 (≠ L271), R270 (= R274), K271 (≠ D275), G274 (= G278), M276 (≠ L280)
- binding n-acetyl-l-glutamate: G29 (≠ P28), G30 (= G29), G61 (= G59), G62 (≠ S60), N180 (≠ A183), D182 (≠ E185)
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)
27% identity, 65% coverage: 3:283/433 of query aligns to 4:279/282 of Q9X2A4
- N178 (= N181) binding substrate
- K196 (= K199) binding L-arginine
- S214 (≠ R218) binding L-arginine
- EIFS 266:269 (≠ ELFT 270:273) binding L-arginine
2bufA Arginine feed-back inhibitable acetylglutamate kinase (see paper)
29% identity, 64% coverage: 8:285/433 of query aligns to 14:290/292 of 2bufA
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)
29% identity, 64% coverage: 8:285/433 of query aligns to 15:299/301 of Q9HTN2
- R90 (= R82) binding substrate
- N195 (= N181) binding substrate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2bufC Arginine feed-back inhibitable acetylglutamate kinase (see paper)
29% identity, 64% coverage: 8:285/433 of query aligns to 14:298/298 of 2bufC
- active site: K32 (≠ M26), G35 (= G29), G68 (≠ R61), D198 (≠ E185), K254 (vs. gap)
- binding adenosine-5'-diphosphate: N36 (≠ D30), N218 (≠ A205), L222 (= L209), M223 (≠ I210), T246 (≠ S235), I247 (≠ N236), Y248 (= Y237), G250 (≠ A239), M251 (≠ E240)
2v5hB Controlling the storage of nitrogen as arginine: the complex of pii and acetylglutamate kinase from synechococcus elongatus pcc 7942 (see paper)
29% identity, 66% coverage: 3:286/433 of query aligns to 5:286/289 of 2v5hB
2bufK Arginine feed-back inhibitable acetylglutamate kinase (see paper)
29% identity, 64% coverage: 8:283/433 of query aligns to 14:273/273 of 2bufK