SitesBLAST
Comparing GFF5498 FitnessBrowser__WCS417:GFF5498 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)
P0A962 L-asparaginase 1; L-asparaginase I; L-ASNase I; L-asparagine amidohydrolase I; EC 3.5.1.1 from Escherichia coli (strain K12) (see paper)
37% identity, 99% coverage: 4:324/325 of query aligns to 3:334/338 of P0A962
- T14 (= T15) active site, O-isoaspartyl threonine intermediate; mutation T->A,V: Loss of enzyme activity.
- T91 (= T90) mutation T->A,V: Loss of enzyme activity.
- Q118 (≠ M117) mutation to D: Loss of enzyme activity.
- T162 (≠ A161) mutation to A: No effect on activity at saturating substrate concentration. Abolishes cooperativity.
- R240 (≠ E229) mutation to A: No effect on activity at saturating substrate concentration. Reduced activity at lower substrate concentrations.
6nxcB Ecai(t162a) mutant in complex with citrate at ph 4 (see paper)
36% identity, 99% coverage: 4:324/325 of query aligns to 10:333/336 of 6nxcB
- active site: T21 (= T15), T90 (= T90), D91 (= D91), K162 (= K162), G285 (= G276)
- binding asparagine: R239 (≠ E229), T270 (= T261), Q271 (= Q262), C272 (= C263), M273 (≠ H264), T300 (= T291), V301 (≠ R292), E302 (= E293)
2himA Crystal structure and allosteric regulation of the cytoplasmic escherichia coli l-asparaginase i (see paper)
36% identity, 99% coverage: 4:324/325 of query aligns to 1:322/324 of 2himA
- active site: T12 (= T15), T84 (= T90), D85 (= D91), K156 (= K162), G274 (= G276)
- binding asparagine: G11 (= G14), T12 (= T15), D52 (= D57), S53 (= S58), S54 (≠ A59), G83 (= G89), T84 (= T90), D85 (= D91), R233 (≠ E229), T264 (= T261), Q265 (= Q262), C266 (= C263), T289 (= T291), V290 (≠ R292), E291 (= E293)
- binding aspartic acid: G11 (= G14), T12 (= T15), D52 (= D57), S53 (= S58), G83 (= G89), T84 (= T90), D85 (= D91), S110 (= S116)
7r6bB Crystal structure of mutant r43d/l124d/r125a/c273s of l-asparaginase i from yersinia pestis (see paper)
35% identity, 99% coverage: 4:324/325 of query aligns to 1:299/301 of 7r6bB
5ot0A The thermostable l-asparaginase from thermococcus kodakarensis (see paper)
33% identity, 98% coverage: 6:324/325 of query aligns to 2:325/328 of 5ot0A
- active site: T11 (= T15), Y21 (≠ L25), T85 (= T90), D86 (= D91), K156 (= K162), G277 (= G276)
- binding phosphate ion: G10 (= G14), T11 (= T15), D53 (= D57), S54 (= S58), G84 (= G89), T85 (= T90), D86 (= D91)
4r8lA Crystal structure of the asp-bound guinea pig l-asparaginase 1 catalytic domain (see paper)
31% identity, 98% coverage: 6:324/325 of query aligns to 3:351/354 of 4r8lA
- active site: T12 (= T15), V21 (≠ G24), T109 (= T90), D110 (= D91), K181 (= K162)
- binding aspartic acid: G11 (= G14), T12 (= T15), D77 (= D57), S78 (= S58), G108 (= G89), T109 (= T90), D110 (= D91), A135 (≠ S116)
4q0mA Crystal structure of pyrococcus furiosus l-asparaginase (see paper)
32% identity, 83% coverage: 56:325/325 of query aligns to 51:326/327 of 4q0mA
Sites not aligning to the query:
Q8TZE8 L-asparaginase; EC 3.5.1.1 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see 2 papers)
32% identity, 83% coverage: 56:325/325 of query aligns to 50:325/326 of Q8TZE8
- DS 51:52 (= DS 57:58) binding
- T53 (≠ A59) mutation to Q: Shows improved enzymatic properties at physiological conditions (pH 7.4 and 37 degrees Celsius) as compared to the wild type with a 2-fold increase in catalytic efficiency. Shows higher and significant killing of human leukemic and breast carcinoma cell lines as compared to the E.coli L-asparaginase.
- TD 83:84 (= TD 90:91) binding
- Y273 (= Y273) mutation to A: 95% reduction in activity compared to wild type.
- K274 (≠ E274) mutation to E: Shows improved enzymatic properties at physiological conditions (pH 7.4 and 37 degrees Celsius) as compared to the wild type with a 2.6-fold increase in catalytic efficiency. Shows higher and significant killing of human leukemic and breast carcinoma cell lines as compared to the E.coli L-asparaginase.
Sites not aligning to the query:
5dndD Crystal structure of the asn-bound guinea pig l-asparaginase 1 catalytic domain active site mutant t116a (see paper)
31% identity, 98% coverage: 6:324/325 of query aligns to 3:351/357 of 5dndD
- active site: T12 (= T15), V21 (≠ G24), A109 (≠ T90), D110 (= D91), K181 (= K162)
- binding asparagine: G11 (= G14), T12 (= T15), D77 (= D57), S78 (= S58), G108 (= G89), A109 (≠ T90), D110 (= D91), A135 (≠ S116), Q136 (≠ M117)
1zq1A Structure of gatde tRNA-dependent amidotransferase from pyrococcus abyssi (see paper)
28% identity, 98% coverage: 7:324/325 of query aligns to 93:426/437 of 1zq1A
- active site: T101 (= T15), A112 (= A26), T177 (= T90), D178 (= D91), K255 (= K162), G378 (= G276)
- binding aspartic acid: F144 (≠ D57), S145 (= S58), E146 (≠ A59), G176 (= G89), T177 (= T90), D178 (= D91), A203 (≠ S116)
4njeA Crystal structure of pyrococcus furiosus l-asparaginase with ligand (see paper)
38% identity, 37% coverage: 56:175/325 of query aligns to 50:167/182 of 4njeA
Sites not aligning to the query:
5b5uA Crystal structure of truncated pyrococcus furiosus l-asparaginase with peptide (see paper)
38% identity, 37% coverage: 56:175/325 of query aligns to 50:167/175 of 5b5uA
Sites not aligning to the query:
1hg1A X-ray structure of the complex between erwinia chrysanthemi l-asparaginase and d-aspartate (see paper)
26% identity, 82% coverage: 6:271/325 of query aligns to 3:266/306 of 1hg1A
- active site: T12 (= T15), T74 (= T90), D75 (= D91), K147 (≠ P157)
- binding d-aspartic acid: G11 (= G14), T12 (= T15), A40 (= A53), S41 (= S58), E42 (≠ A59), G73 (= G89), T74 (= T90), D75 (= D91)
2wltA The crystal structure of helicobacter pylori l-asparaginase at 1.4 a resolution (see paper)
27% identity, 82% coverage: 7:271/325 of query aligns to 4:285/326 of 2wltA
- active site: T12 (= T15), Y23 (≠ P27), T89 (= T90), D90 (= D91), K162 (= K162), E283 (= E269)
- binding aspartic acid: G11 (= G14), T12 (= T15), S25 (= S29), G55 (≠ D57), S56 (= S58), Q57 (≠ A59), G88 (= G89), T89 (= T90), D90 (= D91), A114 (≠ S116), M115 (= M117)
1hfwA X-ray structure of the complex between erwinia chrysanthemi l-asparaginase and l-glutamate (see paper)
26% identity, 82% coverage: 6:271/325 of query aligns to 4:267/307 of 1hfwA
- active site: T13 (= T15), T75 (= T90), D76 (= D91), K148 (≠ P157)
- binding glutamic acid: G12 (= G14), T13 (= T15), A41 (= A53), S42 (= S58), E43 (≠ A59), G74 (= G89), T75 (= T90), D76 (= D91), A100 (≠ S116)
P06608 L-asparaginase; L-ASNase; L-asparagine amidohydrolase; EC 3.5.1.1 from Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi) (see 2 papers)
27% identity, 82% coverage: 6:271/325 of query aligns to 27:308/348 of P06608