SitesBLAST
Comparing WP_013533413.1 NCBI__GCF_000185905.1:WP_013533413.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 4 hits to proteins with known functional sites (download)
Q05514 Methylaspartate ammonia-lyase; MAL; 3-methylaspartase ammonia-lyase; Beta-methylaspartase; EC 4.3.1.2 from Clostridium tetanomorphum (see 3 papers)
43% identity, 98% coverage: 1:410/417 of query aligns to 1:413/413 of Q05514
- Q73 (= Q73) mutation to A: It has very broad nucleophile scope and excellent regio- and diastereoselectivity in the amination reaction. This mutation strongly moves the specificity of MAL away from ammonia and towards methylamine. It is highly enantioselective.
- H194 (= H193) mutation to A: Strong (160-fold) decrease of the catalytic efficiency for deamination and slight (1.8-fold) decrease of affinity binding for L-threo-beta-methylaspartate. 7-fold decrease of the catalytic efficiency for amination and 20-fold decrease of affinity binding for mesaconate. It does not show any major conformational changes.; mutation to R: It abolishes deaminase and aminase activities and does not show any major conformational changes.
- D238 (= D235) binding Mg(2+)
- E273 (= E270) binding Mg(2+)
- D307 (= D304) binding Mg(2+)
- Q329 (= Q326) mutation to A: Very strong decrease of the catalytic efficiency for deamination, whereas the affinity binding for L-threo-beta-methylaspartate is not affected. Strong (240-fold) decrease of the catalytic efficiency for amination and slight (2.4-fold) decrease of affinity binding for mesaconate. It does not show any major conformational changes.; mutation to R: It abolishes deaminase and aminase activities and does not show any major conformational changes.
- K331 (= K328) active site, Proton acceptor; mutation to A: It abolishes deaminase and aminase activities and does not show any major conformational changes.; mutation to G: It abolishes deaminase and aminase activities and does not show any major conformational changes.; mutation to H: It abolishes deaminase and aminase activities and does not show any major conformational changes.; mutation to Q: It abolishes deaminase and aminase activities and does not show any major conformational changes.; mutation to R: It abolishes deaminase and aminase activities and does not show any major conformational changes.
- L384 (= L381) mutation to A: It has very broad electrophile scope and excellent regio- and enantioselectivity in the amination reaction.
3zvhA Methylaspartate ammonia lyase from clostridium tetanomorphum mutant q73a (see paper)
43% identity, 98% coverage: 1:410/417 of query aligns to 1:413/415 of 3zvhA
O66145 Methylaspartate ammonia-lyase; MAL; 3-methylaspartate ammonia-lyase; Beta-methylaspartase; EC 4.3.1.2 from Citrobacter amalonaticus (see paper)
44% identity, 98% coverage: 1:409/417 of query aligns to 1:412/413 of O66145
- Q172 (= Q171) binding (2S,3S)-3-methyl-L-aspartate
- D238 (= D235) binding Mg(2+)
- E273 (= E270) binding Mg(2+)
- D307 (= D304) binding Mg(2+)
- Q329 (= Q326) binding (2S,3S)-3-methyl-L-aspartate
- K331 (= K328) active site, Proton acceptor
1kkrA Crystal structure of citrobacter amalonaticus methylaspartate ammonia lyase containing (2s,3s)-3-methylaspartic acid (see paper)
44% identity, 98% coverage: 1:407/417 of query aligns to 1:410/411 of 1kkrA
- active site: Q172 (= Q171), H194 (= H193), D238 (= D235), E273 (= E270), D307 (= D304), Q329 (= Q326), K331 (= K328)
- binding (2S,3S)-3-methyl-aspartic acid: Q172 (= Q171), H194 (= H193), D238 (= D235), T360 (≠ S357), C361 (= C358)
- binding magnesium ion: D238 (= D235), E273 (= E270), D307 (= D304)
Query Sequence
>WP_013533413.1 NCBI__GCF_000185905.1:WP_013533413.1
MQIKDVLLAPGNGAFFYDDQEAIRSGAIQDGFMYVGAPTTPGFKSIRIPASSLSIGLVLA
DETVVWGDMMNVQYAGAGGRDPLFDTNQISDLTSCVVAPRLFDVDASRFIDSCTRVFESV
EHLRIPLAIEYGVSQALLRAAAHLQRKTMAEIVCAEFDLPLPTCRVPIYCQSGDAREINV
DRMILKGVDILPHGLINSRQKFGTDGQTFMDFVKWVATRTRQIGLPGYHPVLHFDVYGWI
GLEIGLEPQRIADFICRVAESVPGFALNVESPADFGSTQAQIENYAEIVSILDNRGSRAR
IVVDERCNTLEDIRLFAEAKATHLVQIKTPDVGSIADTARAVLICKENRVGAYVGGSCTE
TDLSAQASVHISVATQADMMLAKPGMGVDEGFSIVGNEQNRLLAILNRRRVQADNVG
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory