SitesBLAST
Comparing WP_111607229.1 NCBI__GCF_003259225.1:WP_111607229.1 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)
42% identity, 98% coverage: 5:342/345 of query aligns to 6:336/338 of P0A962
- T14 (= T13) active site, O-isoaspartyl threonine intermediate; mutation T->A,V: Loss of enzyme activity.
- T91 (= T89) mutation T->A,V: Loss of enzyme activity.
- Q118 (= Q116) mutation to D: Loss of enzyme activity.
- T162 (≠ Q160) mutation to A: No effect on activity at saturating substrate concentration. Abolishes cooperativity.
- R240 (≠ L245) 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)
40% identity, 98% coverage: 5:342/345 of query aligns to 13:335/336 of 6nxcB
2himA Crystal structure and allosteric regulation of the cytoplasmic escherichia coli l-asparaginase i (see paper)
40% identity, 98% coverage: 5:342/345 of query aligns to 4:324/324 of 2himA
- active site: T12 (= T13), T84 (= T89), D85 (= D90), K156 (= K161), G274 (= G292)
- binding asparagine: T12 (= T13), D52 (= D57), S53 (= S58), S54 (≠ A59), G83 (= G88), D85 (= D90), R233 (≠ L245), C266 (= C279), T289 (= T307), V290 (≠ L308), E291 (= E309)
- binding aspartic acid: T12 (= T13), D52 (= D57), S53 (= S58), G83 (= G88), T84 (= T89), D85 (= D90)
7r6bB Crystal structure of mutant r43d/l124d/r125a/c273s of l-asparaginase i from yersinia pestis (see paper)
38% identity, 98% coverage: 5:341/345 of query aligns to 4:300/301 of 7r6bB
4r8lA Crystal structure of the asp-bound guinea pig l-asparaginase 1 catalytic domain (see paper)
36% identity, 93% coverage: 4:323/345 of query aligns to 3:333/354 of 4r8lA
5dndD Crystal structure of the asn-bound guinea pig l-asparaginase 1 catalytic domain active site mutant t116a (see paper)
36% identity, 93% coverage: 4:323/345 of query aligns to 3:333/357 of 5dndD
- active site: T12 (= T13), V21 (≠ G22), A109 (≠ T89), D110 (= D90), K181 (= K161)
- binding asparagine: T12 (= T13), D77 (= D57), S78 (= S58), G108 (= G88), A109 (≠ T89), D110 (= D90), A135 (≠ S115)
4q0mA Crystal structure of pyrococcus furiosus l-asparaginase (see paper)
30% identity, 98% coverage: 4:340/345 of query aligns to 3:325/327 of 4q0mA
- active site: T12 (= T13), Y22 (≠ L23), T84 (= T89), D85 (= D90), K155 (= K161), G277 (= G292)
- binding (4s)-2-methyl-1,4,5,6-tetrahydropyrimidine-4-carboxylic acid: Y69 (≠ A74), V193 (≠ D198), T194 (= T199), L195 (≠ S200)
Q8TZE8 L-asparaginase; EC 3.5.1.1 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see 2 papers)
30% identity, 98% coverage: 4:340/345 of query aligns to 2:324/326 of Q8TZE8
- T11 (= T13) binding L-aspartate
- D51 (= D57) binding L-aspartate
- S52 (= S58) binding L-aspartate
- 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.
- T83 (= T89) binding L-aspartate
- D84 (= D90) binding L-aspartate
- Y273 (= Y289) mutation to A: 95% reduction in activity compared to wild type.
- K274 (≠ A290) 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.
1zq1A Structure of gatde tRNA-dependent amidotransferase from pyrococcus abyssi (see paper)
30% identity, 98% coverage: 4:342/345 of query aligns to 92:428/437 of 1zq1A
5ot0A The thermostable l-asparaginase from thermococcus kodakarensis (see paper)
31% identity, 98% coverage: 4:341/345 of query aligns to 2:326/328 of 5ot0A
- active site: T11 (= T13), Y21 (≠ L23), T85 (= T89), D86 (= D90), K156 (= K161), G277 (= G292)
- binding phosphate ion: G10 (= G12), T11 (= T13), S54 (= S58), G84 (= G88), T85 (= T89), D86 (= D90)
4njeA Crystal structure of pyrococcus furiosus l-asparaginase with ligand (see paper)
35% identity, 52% coverage: 4:181/345 of query aligns to 2:174/182 of 4njeA
5b5uA Crystal structure of truncated pyrococcus furiosus l-asparaginase with peptide (see paper)
35% identity, 52% coverage: 4:181/345 of query aligns to 2:174/175 of 5b5uA
- active site: T11 (= T13), Y21 (≠ L23), T83 (= T89), D84 (= D90), K154 (= K161)
- binding aspartic acid: T11 (= T13), D51 (= D57), S52 (= S58), G82 (= G88), T83 (= T89), D84 (= D90), S109 (= S115), M110 (≠ Q116)
- binding : D43 (≠ E48), F44 (≠ V49), I171 (≠ L178), A172 (≠ G179), E173 (= E180), L174 (= L181)
Sites not aligning to the query:
8h4aB Blasnase-t13a/m57p
25% identity, 95% coverage: 4:332/345 of query aligns to 3:319/328 of 8h4aB
7c8qA Blasnase-t13a with d-asn (see paper)
25% identity, 95% coverage: 4:332/345 of query aligns to 3:319/321 of 7c8qA
- active site: A12 (≠ T13), L23 (≠ A24), E35 (= E31), T88 (= T89), D89 (= D90), N155 (≠ R155), K161 (= K161), T273 (≠ S285), A278 (= A290), G279 (≠ T291), S281 (= S293)
- binding d-asparagine: A12 (≠ T13), S55 (= S58), G87 (= G88), T88 (= T89), D89 (= D90), Y275 (≠ G287), Y277 (= Y289)
- binding magnesium ion: N245 (≠ A258), D249 (≠ F262)
7c8xA Blasnase-t13a with l-asn (see paper)
26% identity, 95% coverage: 4:332/345 of query aligns to 3:318/319 of 7c8xA