SitesBLAST
Comparing WP_086508794.1 NCBI__GCF_002151265.1:WP_086508794.1 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)
5vwrA E.Coli aspartate aminotransferase-(1r,3s,4s)-3-amino-4- fluorocyclopentane-1-carboxylic acid (fcp)-alpha-ketoglutarate (see paper)
49% identity, 100% coverage: 1:394/395 of query aligns to 1:395/396 of 5vwrA
- active site: W130 (= W130), D211 (= D210), A213 (= A212), K246 (= K245)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-glutamic acid: I13 (= I13), G34 (= G34), G102 (= G102), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N182), D211 (= D210), Y214 (= Y213), S243 (= S242), S245 (= S244), K246 (= K245), R254 (= R253), R374 (= R373)
5t4lA Plp and gaba trigger gabr-mediated transcription regulation in bacillus subsidies via external aldimine formation (see paper)
49% identity, 100% coverage: 1:394/395 of query aligns to 1:395/396 of 5t4lA
- active site: W130 (= W130), D211 (= D210), A213 (= A212), K246 (= K245)
- binding (4R)-4-amino-6-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}hexanoic acid: G102 (= G102), G103 (= G103), T104 (= T104), W130 (= W130), D211 (= D210), Y214 (= Y213), S243 (= S242), S245 (= S244), K246 (= K245), R254 (= R253)
3qpgA Crystal structures of escherichia coli aspartate aminotransferase reconstituted with 1-deaza-pyridoxal 5'-phosphate: internal aldimine and stable l-aspartate external aldimine (see paper)
49% identity, 100% coverage: 1:394/395 of query aligns to 1:395/396 of 3qpgA
- active site: W130 (= W130), D211 (= D210), A213 (= A212), K246 (= K245)
- binding (E)-N-{2-hydroxy-3-methyl-6-[(phosphonooxy)methyl]benzylidene}-L-aspartic acid: I13 (= I13), G34 (= G34), G102 (= G102), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N182), D211 (= D210), Y214 (= Y213), S243 (= S242), S245 (= S244), K246 (= K245), R254 (= R253), R374 (= R373)
3pa9A Mechanism of inactivation of e. Coli aspartate aminotransferase by (s)-4-amino-4,5-dihydro-2-furancarboxylic acid (s-adfa) ph 7.5 (see paper)
49% identity, 100% coverage: 1:394/395 of query aligns to 1:395/396 of 3pa9A
- active site: W130 (= W130), D211 (= D210), A213 (= A212), K246 (= K245)
- binding 4-aminofuran-2-carboxylic acid: G34 (= G34), W130 (= W130), K246 (= K245), F348 (= F347), R374 (= R373)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G103 (= G103), T104 (= T104), W130 (= W130), D211 (= D210), A213 (= A212), Y214 (= Y213), S243 (= S242), S245 (= S244), K246 (= K245), R254 (= R253)
1x2aA Crystal structure of e.Coli aspat complexed with n-phosphopyridoxyl-d- glutamic acid (see paper)
49% identity, 100% coverage: 1:394/395 of query aligns to 1:395/396 of 1x2aA
- active site: W130 (= W130), D211 (= D210), A213 (= A212), K246 (= K245)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-d-glutamic acid: I33 (≠ V33), G34 (= G34), Y65 (= Y65), G102 (= G102), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N182), D211 (= D210), Y214 (= Y213), S243 (= S242), S245 (= S244), K246 (= K245), R254 (= R253), R280 (= R279), F348 (= F347), R374 (= R373)
1x29A Crystal structure of e.Coli aspat complexed with n-phosphopyridoxyl-2- methyl-l-glutamic acid (see paper)
49% identity, 100% coverage: 1:394/395 of query aligns to 1:395/396 of 1x29A
- active site: W130 (= W130), D211 (= D210), A213 (= A212), K246 (= K245)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-2-methyl-l-glutamic acid: I13 (= I13), G34 (= G34), Y65 (= Y65), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N182), D211 (= D210), Y214 (= Y213), S243 (= S242), S245 (= S244), K246 (= K245), R254 (= R253), R280 (= R279), F348 (= F347), R374 (= R373)
1x28A Crystal structure of e.Coli aspat complexed with n-phosphopyridoxyl-l- glutamic acid (see paper)
49% identity, 100% coverage: 1:394/395 of query aligns to 1:395/396 of 1x28A
- active site: W130 (= W130), D211 (= D210), A213 (= A212), K246 (= K245)
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I13 (= I13), Y65 (= Y65), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N182), D211 (= D210), Y214 (= Y213), S243 (= S242), S245 (= S244), K246 (= K245), R254 (= R253), R280 (= R279), F348 (= F347), R374 (= R373)
1cq8A Aspartate aminotransferase (E.C. 2.6.1.1) complexed with c6-pyridoxal- 5p-phosphate (see paper)
49% identity, 100% coverage: 1:394/395 of query aligns to 1:395/396 of 1cq8A
- active site: W130 (= W130), D211 (= D210), A213 (= A212), K246 (= K245)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: I33 (≠ V33), G34 (= G34), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N182), D211 (= D210), A213 (= A212), Y214 (= Y213), S243 (= S242), S245 (= S244), K246 (= K245), R254 (= R253), R374 (= R373)
1cq7A Aspartate aminotransferase (E.C. 2.6.1.1) complexed with c5-pyridoxal- 5p-phosphate (see paper)
49% identity, 100% coverage: 1:394/395 of query aligns to 1:395/396 of 1cq7A
- active site: W130 (= W130), D211 (= D210), A213 (= A212), K246 (= K245)
- binding 2-[o-phosphonopyridoxyl]-amino-pentanoic acid: I13 (= I13), I33 (≠ V33), G34 (= G34), G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N182), D211 (= D210), Y214 (= Y213), S243 (= S242), S245 (= S244), K246 (= K245), R254 (= R253), R374 (= R373)
1cq6A Aspartate aminotransferase complex with c4-pyridoxal-5p-phosphate (see paper)
49% identity, 100% coverage: 1:394/395 of query aligns to 1:395/396 of 1cq6A
- active site: W130 (= W130), D211 (= D210), A213 (= A212), K246 (= K245)
- binding 2-[o-phosphonopyridoxyl]-amino- butyric acid: G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N182), D211 (= D210), Y214 (= Y213), S243 (= S242), S245 (= S244), R254 (= R253)
1c9cA Aspartate aminotransferase complexed with c3-pyridoxal-5'-phosphate (see paper)
49% identity, 100% coverage: 1:394/395 of query aligns to 1:395/396 of 1c9cA
- active site: W130 (= W130), D211 (= D210), A213 (= A212), K246 (= K245)
- binding alanyl-pyridoxal-5'-phosphate: G103 (= G103), T104 (= T104), W130 (= W130), N183 (= N182), D211 (= D210), A213 (= A212), Y214 (= Y213), S243 (= S242), S245 (= S244), K246 (= K245), R254 (= R253)
1aslA Crystal structures of escherichia coli aspartate aminotransferase in two conformations: comparison of an unliganded open and two liganded closed forms (see paper)
49% identity, 100% coverage: 1:394/395 of query aligns to 1:395/396 of 1aslA