SitesBLAST
Comparing N515DRAFT_3488 FitnessBrowser__Dyella79:N515DRAFT_3488 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)
1ahxA Aspartate aminotransferase hexamutant (see paper)
49% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 1ahxA
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding hydrocinnamic acid: I13 (= I15), L14 (= L16), G34 (= G36), W130 (= W132), K246 (= K249), R374 (= R376)
- binding pyridoxal-5'-phosphate: G102 (= G104), G103 (= G105), S104 (= S106), W130 (= W132), N183 (= N185), D211 (= D213), A213 (= A215), Y214 (= Y216), S243 (= S246), S245 (≠ A248), K246 (= K249), R254 (= R257)
1ahgA Aspartate aminotransferase hexamutant (see paper)
49% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 1ahgA
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding pyridoxal-5'-phosphate: G103 (= G105), S104 (= S106), W130 (= W132), N183 (= N185), D211 (= D213), S243 (= S246), S245 (≠ A248), R254 (= R257)
- binding tyrosine: D11 (= D13), I13 (= I15), L14 (= L16), W130 (= W132), R374 (= R376)
1ahfA Aspartate aminotransferase hexamutant (see paper)
49% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 1ahfA
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding indolylpropionic acid: I13 (= I15), L14 (= L16), I33 (≠ V35), G34 (= G36), W130 (= W132), R374 (= R376)
- binding pyridoxal-5'-phosphate: G102 (= G104), G103 (= G105), S104 (= S106), W130 (= W132), N183 (= N185), D211 (= D213), A213 (= A215), S243 (= S246), S245 (≠ A248), K246 (= K249), R254 (= R257)
3fslA Crystal structure of tyrosine aminotransferase tripple mutant (p181q, r183g,a321k) from escherichia coli at 2.35 a resolution
50% identity, 99% coverage: 4:397/400 of query aligns to 2:396/397 of 3fslA
- active site: W131 (= W132), D212 (= D213), A214 (= A215), K247 (= K249)
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: G103 (= G104), G104 (= G105), S105 (= S106), W131 (= W132), N184 (= N185), D212 (= D213), A214 (= A215), Y215 (= Y216), S244 (= S246), S246 (≠ A248), K247 (= K249), R255 (= R257)
5vwrA E.Coli aspartate aminotransferase-(1r,3s,4s)-3-amino-4- fluorocyclopentane-1-carboxylic acid (fcp)-alpha-ketoglutarate (see paper)
48% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 5vwrA
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-glutamic acid: I13 (= I15), G34 (= G36), G102 (= G104), G103 (= G105), T104 (≠ S106), W130 (= W132), N183 (= N185), D211 (= D213), Y214 (= Y216), S243 (= S246), S245 (≠ A248), K246 (= K249), R254 (= R257), R374 (= R376)
5t4lA Plp and gaba trigger gabr-mediated transcription regulation in bacillus subsidies via external aldimine formation (see paper)
48% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 5t4lA
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding (4R)-4-amino-6-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}hexanoic acid: G102 (= G104), G103 (= G105), T104 (≠ S106), W130 (= W132), D211 (= D213), Y214 (= Y216), S243 (= S246), S245 (≠ A248), K246 (= K249), R254 (= R257)
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)
48% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 3qpgA
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding (E)-N-{2-hydroxy-3-methyl-6-[(phosphonooxy)methyl]benzylidene}-L-aspartic acid: I13 (= I15), G34 (= G36), G102 (= G104), G103 (= G105), T104 (≠ S106), W130 (= W132), N183 (= N185), D211 (= D213), Y214 (= Y216), S243 (= S246), S245 (≠ A248), K246 (= K249), R254 (= R257), R374 (= R376)
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)
48% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 3pa9A
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding 4-aminofuran-2-carboxylic acid: G34 (= G36), W130 (= W132), K246 (= K249), F348 (= F350), R374 (= R376)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G103 (= G105), T104 (≠ S106), W130 (= W132), D211 (= D213), A213 (= A215), Y214 (= Y216), S243 (= S246), S245 (≠ A248), K246 (= K249), R254 (= R257)
1x2aA Crystal structure of e.Coli aspat complexed with n-phosphopyridoxyl-d- glutamic acid (see paper)
48% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 1x2aA
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-d-glutamic acid: I33 (≠ V35), G34 (= G36), Y65 (= Y67), G102 (= G104), G103 (= G105), T104 (≠ S106), W130 (= W132), N183 (= N185), D211 (= D213), Y214 (= Y216), S243 (= S246), S245 (≠ A248), K246 (= K249), R254 (= R257), R280 (= R283), F348 (= F350), R374 (= R376)
1x29A Crystal structure of e.Coli aspat complexed with n-phosphopyridoxyl-2- methyl-l-glutamic acid (see paper)
48% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 1x29A
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-2-methyl-l-glutamic acid: I13 (= I15), G34 (= G36), Y65 (= Y67), G103 (= G105), T104 (≠ S106), W130 (= W132), N183 (= N185), D211 (= D213), Y214 (= Y216), S243 (= S246), S245 (≠ A248), K246 (= K249), R254 (= R257), R280 (= R283), F348 (= F350), R374 (= R376)
1x28A Crystal structure of e.Coli aspat complexed with n-phosphopyridoxyl-l- glutamic acid (see paper)
48% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 1x28A
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I13 (= I15), Y65 (= Y67), G103 (= G105), T104 (≠ S106), W130 (= W132), N183 (= N185), D211 (= D213), Y214 (= Y216), S243 (= S246), S245 (≠ A248), K246 (= K249), R254 (= R257), R280 (= R283), F348 (= F350), R374 (= R376)
1cq8A Aspartate aminotransferase (E.C. 2.6.1.1) complexed with c6-pyridoxal- 5p-phosphate (see paper)
48% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 1cq8A
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: I33 (≠ V35), G34 (= G36), G103 (= G105), T104 (≠ S106), W130 (= W132), N183 (= N185), D211 (= D213), A213 (= A215), Y214 (= Y216), S243 (= S246), S245 (≠ A248), K246 (= K249), R254 (= R257), R374 (= R376)
1cq7A Aspartate aminotransferase (E.C. 2.6.1.1) complexed with c5-pyridoxal- 5p-phosphate (see paper)
48% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 1cq7A
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding 2-[o-phosphonopyridoxyl]-amino-pentanoic acid: I13 (= I15), I33 (≠ V35), G34 (= G36), G103 (= G105), T104 (≠ S106), W130 (= W132), N183 (= N185), D211 (= D213), Y214 (= Y216), S243 (= S246), S245 (≠ A248), K246 (= K249), R254 (= R257), R374 (= R376)
1cq6A Aspartate aminotransferase complex with c4-pyridoxal-5p-phosphate (see paper)
48% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 1cq6A
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding 2-[o-phosphonopyridoxyl]-amino- butyric acid: G103 (= G105), T104 (≠ S106), W130 (= W132), N183 (= N185), D211 (= D213), Y214 (= Y216), S243 (= S246), S245 (≠ A248), R254 (= R257)
1c9cA Aspartate aminotransferase complexed with c3-pyridoxal-5'-phosphate (see paper)
48% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 1c9cA
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding alanyl-pyridoxal-5'-phosphate: G103 (= G105), T104 (≠ S106), W130 (= W132), N183 (= N185), D211 (= D213), A213 (= A215), Y214 (= Y216), S243 (= S246), S245 (≠ A248), K246 (= K249), R254 (= R257)
1aslA Crystal structures of escherichia coli aspartate aminotransferase in two conformations: comparison of an unliganded open and two liganded closed forms (see paper)
48% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 1aslA
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-2-methyl-succinic acid: I13 (= I15), G34 (= G36), Y65 (= Y67), G102 (= G104), G103 (= G105), T104 (≠ S106), W130 (= W132), N183 (= N185), D211 (= D213), Y214 (= Y216), S243 (= S246), K246 (= K249), R254 (= R257), R280 (= R283), R374 (= R376)
1aseA The structure of wild type e. Coli aspartate aminotransferase reconstituted with plp-n-oxide
48% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 1aseA
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding pyridoxal-5'-phosphate-n-oxide: G102 (= G104), G103 (= G105), T104 (≠ S106), W130 (= W132), N183 (= N185), D211 (= D213), A213 (= A215), Y214 (= Y216), S243 (= S246), S245 (≠ A248), K246 (= K249), R254 (= R257)
1asdA The structure of wild type e. Coli aspartate aminotransferase reconstituted with n-meplp
48% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 1asdA
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding n-methyl-pyridoxal-5'-phosphate: G102 (= G104), G103 (= G105), T104 (≠ S106), W130 (= W132), N183 (= N185), D211 (= D213), A213 (= A215), Y214 (= Y216), S243 (= S246), S245 (≠ A248), K246 (= K249), R254 (= R257)
1artA X-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from escherichia coli in open and closed form (see paper)
48% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 1artA
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding 2-methyl-L-aspartic acid: I33 (≠ V35), G34 (= G36), W130 (= W132), Y214 (= Y216), R374 (= R376)
- binding pyridoxal-5'-phosphate: G102 (= G104), G103 (= G105), T104 (≠ S106), W130 (= W132), N183 (= N185), D211 (= D213), Y214 (= Y216), S243 (= S246), S245 (≠ A248), K246 (= K249), R254 (= R257)
1argA Aspartate aminotransferase, phospho-5'-pyridoxyl aspartate complex (see paper)
48% identity, 99% coverage: 4:397/400 of query aligns to 2:395/396 of 1argA
- active site: W130 (= W132), D211 (= D213), A213 (= A215), K246 (= K249)
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethylene)-amino]-succinic acid: I13 (= I15), G34 (= G36), Y65 (= Y67), G103 (= G105), T104 (≠ S106), W130 (= W132), N183 (= N185), D211 (= D213), Y214 (= Y216), S243 (= S246), S245 (≠ A248), K246 (= K249), R254 (= R257), R280 (= R283), R374 (= R376)
Query Sequence
>N515DRAFT_3488 FitnessBrowser__Dyella79:N515DRAFT_3488
MSHFASVEMTPGDPILGLTEAYLADARPGKVNLGVGIYYDEQGRIPLLRAVHEVEQRLAQ
EAKPRGYLPIDGLPAYTQGTQKLVFGAESPLLAAGRVATSQTIGGSGALRVGADVLKKAL
PKAKIAISNPSWENHRVVFIAAGFEVVEYTYYDPQTHGLDFAGMLADLGKLEPGTVVLLH
ACCHNPTGVDLNAAQWQQVVEVVKERQLLPFIDMAYQGFDQGIDADATAVRLFAASGIES
FVVTSSYAKSFSLYGERAGALTFVAADRDEALRVQSLVKRTIRSIYSSPSTHGGALVAGV
LNSPELRAMWEQELGEMRERIHAMRAGMVEKLAAHGAPQFAFIQQQAGMFSYSGLSKAQV
DRLRDEYAIYAIGTGRICVAALNRSNLDTVAAAVAAVSKA
Or try a new SitesBLAST search
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