SitesBLAST
Comparing WP_111608988.1 NCBI__GCF_003259225.1:WP_111608988.1 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)
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)
43% identity, 99% coverage: 3:324/326 of query aligns to 6:324/338 of P0A962
- T14 (= T11) active site, O-isoaspartyl threonine intermediate; mutation T->A,V: Loss of enzyme activity.
- T91 (= T87) mutation T->A,V: Loss of enzyme activity.
- Q118 (= Q114) mutation to D: Loss of enzyme activity.
- T162 (≠ H162) mutation to A: No effect on activity at saturating substrate concentration. Abolishes cooperativity.
- R240 (≠ L239) 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)
42% identity, 99% coverage: 3:324/326 of query aligns to 13:323/336 of 6nxcB
2himA Crystal structure and allosteric regulation of the cytoplasmic escherichia coli l-asparaginase i (see paper)
42% identity, 99% coverage: 3:324/326 of query aligns to 4:312/324 of 2himA
- active site: T12 (= T11), T84 (= T87), D85 (= D88), K156 (= K163), G274 (= G286)
- binding asparagine: T12 (= T11), D52 (= D55), S53 (= S56), S54 (= S57), G83 (= G86), D85 (= D88), R233 (≠ L239), C266 (= C273), T289 (= T301), V290 (≠ Y302), E291 (= E303)
- binding aspartic acid: T12 (= T11), D52 (= D55), S53 (= S56), G83 (= G86), T84 (= T87), D85 (= D88)
7r6bB Crystal structure of mutant r43d/l124d/r125a/c273s of l-asparaginase i from yersinia pestis (see paper)
40% identity, 99% coverage: 3:326/326 of query aligns to 4:291/301 of 7r6bB
4r8lA Crystal structure of the asp-bound guinea pig l-asparaginase 1 catalytic domain (see paper)
36% identity, 99% coverage: 3:326/326 of query aligns to 4:343/354 of 4r8lA
5dndD Crystal structure of the asn-bound guinea pig l-asparaginase 1 catalytic domain active site mutant t116a (see paper)
36% identity, 99% coverage: 3:326/326 of query aligns to 4:343/357 of 5dndD
- active site: T12 (= T11), V21 (≠ G20), A109 (≠ T87), D110 (= D88), K181 (= K163)
- binding asparagine: T12 (= T11), D77 (= D55), S78 (= S56), G108 (= G86), A109 (≠ T87), D110 (= D88), A135 (≠ S113)
1zq1A Structure of gatde tRNA-dependent amidotransferase from pyrococcus abyssi (see paper)
30% identity, 98% coverage: 8:326/326 of query aligns to 98:418/437 of 1zq1A
5ot0A The thermostable l-asparaginase from thermococcus kodakarensis (see paper)
30% identity, 100% coverage: 1:326/326 of query aligns to 1:317/328 of 5ot0A
- active site: T11 (= T11), Y21 (≠ L21), T85 (= T87), D86 (= D88), K156 (= K163), G277 (= G286)
- binding phosphate ion: G10 (= G10), T11 (= T11), S54 (= S56), G84 (= G86), T85 (= T87), D86 (= D88)
4q0mA Crystal structure of pyrococcus furiosus l-asparaginase (see paper)
29% identity, 100% coverage: 1:326/326 of query aligns to 2:317/327 of 4q0mA
- active site: T12 (= T11), Y22 (≠ L21), T84 (= T87), D85 (= D88), K155 (= K163), G277 (= G286)
- binding (4s)-2-methyl-1,4,5,6-tetrahydropyrimidine-4-carboxylic acid: Y69 (≠ E72), V193 (= V211), T194 (= T212), L195 (vs. gap)
Q8TZE8 L-asparaginase; EC 3.5.1.1 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see 2 papers)
29% identity, 100% coverage: 1:326/326 of query aligns to 1:316/326 of Q8TZE8
- T11 (= T11) binding L-aspartate
- D51 (= D55) binding L-aspartate
- S52 (= S56) binding L-aspartate
- T53 (≠ S57) 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 (= T87) binding L-aspartate
- D84 (= D88) binding L-aspartate
- Y273 (= Y283) mutation to A: 95% reduction in activity compared to wild type.
- K274 (≠ A284) 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.
5b5uA Crystal structure of truncated pyrococcus furiosus l-asparaginase with peptide (see paper)
32% identity, 55% coverage: 1:178/326 of query aligns to 1:169/175 of 5b5uA
- active site: T11 (= T11), Y21 (≠ L21), T83 (= T87), D84 (= D88), K154 (= K163)
- binding aspartic acid: T11 (= T11), D51 (= D55), S52 (= S56), G82 (= G86), T83 (= T87), D84 (= D88), S109 (= S113), M110 (≠ Q114)
- binding : D43 (= D39), F44 (≠ E40)
Sites not aligning to the query:
4njeA Crystal structure of pyrococcus furiosus l-asparaginase with ligand (see paper)
32% identity, 55% coverage: 1:178/326 of query aligns to 1:169/182 of 4njeA
8h4aB Blasnase-t13a/m57p
25% identity, 96% coverage: 2:315/326 of query aligns to 3:310/328 of 8h4aB
7c8qA Blasnase-t13a with d-asn (see paper)
25% identity, 96% coverage: 2:315/326 of query aligns to 3:310/321 of 7c8qA
- active site: A12 (≠ T11), L23 (≠ I22), E35 (= E37), T88 (= T87), D89 (= D88), N155 (≠ E157), K161 (= K163), T273 (≠ A280), A278 (= A285), G279 (= G286), S281 (≠ A288)
- binding d-asparagine: A12 (≠ T11), S55 (= S56), G87 (= G86), T88 (= T87), D89 (= D88), Y275 (≠ A282), Y277 (≠ A284)
- binding magnesium ion: N245 (≠ T252), D249 (≠ L256)
7cbuA Blasnase-t13a with l-asp (see paper)
26% identity, 94% coverage: 11:315/326 of query aligns to 9:307/318 of 7cbuA