SitesBLAST
Comparing WP_011021336.1 NCBI__GCF_000007345.1:WP_011021336.1 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)
1zq1A Structure of gatde tRNA-dependent amidotransferase from pyrococcus abyssi (see paper)
46% identity, 99% coverage: 6:423/424 of query aligns to 14:431/437 of 1zq1A
5ot0A The thermostable l-asparaginase from thermococcus kodakarensis (see paper)
33% identity, 79% coverage: 85:419/424 of query aligns to 2:326/328 of 5ot0A
- active site: T11 (= T94), Y21 (= Y101), T85 (= T170), D86 (= D171), K156 (= K247), G277 (= G370)
- binding phosphate ion: G10 (= G93), T11 (= T94), S54 (= S138), G84 (= G169), T85 (= T170), D86 (= D171)
Q8TZE8 L-asparaginase; EC 3.5.1.1 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see 2 papers)
31% identity, 79% coverage: 85:418/424 of query aligns to 2:324/326 of Q8TZE8
- T11 (= T94) binding L-aspartate
- D51 (≠ L137) binding L-aspartate
- S52 (= S138) binding L-aspartate
- T53 (≠ E139) 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 (= T170) binding L-aspartate
- D84 (= D171) binding L-aspartate
- Y273 (= Y367) mutation to A: 95% reduction in activity compared to wild type.
- K274 (≠ D368) 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.
4q0mA Crystal structure of pyrococcus furiosus l-asparaginase (see paper)
31% identity, 79% coverage: 85:418/424 of query aligns to 3:325/327 of 4q0mA
- active site: T12 (= T94), Y22 (≠ A105), T84 (= T170), D85 (= D171), K155 (= K247), G277 (= G370)
- binding (4s)-2-methyl-1,4,5,6-tetrahydropyrimidine-4-carboxylic acid: Y69 (≠ V154), V193 (≠ K286), T194 (≠ A287), L195 (= L288)
2wltA The crystal structure of helicobacter pylori l-asparaginase at 1.4 a resolution (see paper)
30% identity, 78% coverage: 83:412/424 of query aligns to 1:325/326 of 2wltA
- active site: T12 (= T94), Y23 (= Y101), T89 (= T170), D90 (= D171), K162 (= K247), E283 (≠ R361)
- binding aspartic acid: T12 (= T94), S25 (≠ T103), G55 (≠ L137), S56 (= S138), Q57 (≠ E139), G88 (= G169), T89 (= T170), D90 (= D171)
5k45A Wolinella succinogenes l-asparaginase p121 + l-glutamic acid (see paper)
33% identity, 76% coverage: 84:404/424 of query aligns to 2:319/328 of 5k45A
- active site: T12 (= T94), Y25 (= Y101), T91 (= T170), D92 (= D171), K164 (= K247), E285 (≠ G370)
- binding glutamic acid: G57 (≠ L137), S58 (= S138), Q59 (≠ E139), G90 (= G169), T91 (= T170), D92 (= D171), A116 (≠ S195)
5k3oA Wolinella succinogenes l-asparaginase p121 and l-aspartic acid (see paper)
33% identity, 76% coverage: 84:404/424 of query aligns to 2:319/328 of 5k3oA
- active site: T12 (= T94), Y25 (= Y101), T91 (= T170), D92 (= D171), K164 (= K247), E285 (≠ G370)
- binding aspartic acid: T12 (= T94), G57 (≠ L137), S58 (= S138), Q59 (≠ E139), G90 (= G169), T91 (= T170), D92 (= D171)
6nxcB Ecai(t162a) mutant in complex with citrate at ph 4 (see paper)
29% identity, 79% coverage: 86:419/424 of query aligns to 13:334/336 of 6nxcB
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)
29% identity, 79% coverage: 86:419/424 of query aligns to 6:335/338 of P0A962
- T14 (= T94) active site, O-isoaspartyl threonine intermediate; mutation T->A,V: Loss of enzyme activity.
- T91 (= T170) mutation T->A,V: Loss of enzyme activity.
- Q118 (= Q196) mutation to D: Loss of enzyme activity.
- T162 (≠ R246) mutation to A: No effect on activity at saturating substrate concentration. Abolishes cooperativity.
- R240 (≠ E326) mutation to A: No effect on activity at saturating substrate concentration. Reduced activity at lower substrate concentrations.
2himA Crystal structure and allosteric regulation of the cytoplasmic escherichia coli l-asparaginase i (see paper)
28% identity, 79% coverage: 86:419/424 of query aligns to 4:323/324 of 2himA
- active site: T12 (= T94), T84 (= T170), D85 (= D171), K156 (= K247), G274 (= G370)
- binding asparagine: T12 (= T94), D52 (vs. gap), S53 (= S138), S54 (≠ E139), G83 (= G169), D85 (= D171), R233 (≠ E326), C266 (= C357), T289 (≠ L385), V290 (≠ P386), E291 (= E387)
- binding aspartic acid: T12 (= T94), D52 (vs. gap), S53 (= S138), G83 (= G169), T84 (= T170), D85 (= D171)
P06608 L-asparaginase; L-ASNase; L-asparagine amidohydrolase; EC 3.5.1.1 from Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi) (see 2 papers)
33% identity, 66% coverage: 82:360/424 of query aligns to 24:303/348 of P06608
- T36 (= T94) active site, O-isoaspartyl threonine intermediate
7u6mC Albumin binding domain fused to a mutant of the erwinia asparaginase (see paper)
33% identity, 67% coverage: 76:360/424 of query aligns to 12:297/342 of 7u6mC
1hg0A X-ray structure of the complex between erwinia chrysanthemi l- asparaginase and succinic acid (see paper)
33% identity, 66% coverage: 82:360/424 of query aligns to 3:282/327 of 1hg0A
7r5qA Escherichia coli type ii asparaginase n24s mutant in complex with glu (see paper)
29% identity, 78% coverage: 83:412/424 of query aligns to 1:305/306 of 7r5qA