SitesBLAST
Comparing 208718 DVU3197 branched-chain amino acid aminotransferase 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)
4whxA X-ray crystal structure of an amino acid aminotransferase from burkholderia pseudomallei bound to the co-factor pyridoxal phosphate
55% identity, 99% coverage: 2:306/309 of query aligns to 1:305/306 of 4whxA
2ej0B Crystal structure of t.Th.Hb8 branched-chain amino acid aminotransferase with pyridoxamine 5'-phosphate
55% identity, 97% coverage: 6:304/309 of query aligns to 3:301/305 of 2ej0B
- active site: F35 (= F38), G37 (= G40), K158 (= K161), E192 (= E195), L215 (= L218)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: R58 (= R62), Y163 (= Y166), E192 (= E195), G195 (= G198), E196 (= E199), L215 (= L218), G217 (= G220), I218 (= I221), T219 (= T222), G254 (= G257), T255 (= T258)
2ej3A Crystal structure of t.Th.Hb8 branched-chain amino acid aminotransferase complexed with gabapentin
53% identity, 97% coverage: 6:304/309 of query aligns to 3:293/297 of 2ej3A
- active site: F35 (= F38), G37 (= G40), K150 (= K161), E184 (= E195), L207 (= L218)
- binding [1-(aminomethyl)cyclohexyl]acetic acid: G187 (= G198), G246 (= G257), T247 (= T258), A248 (= A259)
- binding pyridoxal-5'-phosphate: R58 (= R62), K150 (= K161), Y155 (= Y166), E184 (= E195), G187 (= G198), L207 (= L218), G209 (= G220), I210 (= I221), T211 (= T222), G246 (= G257), T247 (= T258)
2eiyA Crystal structure of t.Th.Hb8 branched-chain amino acid aminotransferase complexed with 4-methylvaleric acid
53% identity, 97% coverage: 6:304/309 of query aligns to 3:293/297 of 2eiyA
- active site: F35 (= F38), G37 (= G40), K150 (= K161), E184 (= E195), L207 (= L218)
- binding 4-methyl valeric acid: F35 (= F38), Y94 (= Y98), T247 (= T258), A248 (= A259)
- binding pyridoxal-5'-phosphate: R58 (= R62), K150 (= K161), Y155 (= Y166), E184 (= E195), G187 (= G198), E188 (= E199), L207 (= L218), G209 (= G220), I210 (= I221), T211 (= T222), G246 (= G257), T247 (= T258)
1wrvA Crystal structure of t.Th.Hb8 branched-chain amino acid aminotransferase
53% identity, 97% coverage: 6:304/309 of query aligns to 3:293/297 of 1wrvA
- active site: F35 (= F38), G37 (= G40), K150 (= K161), E184 (= E195), L207 (= L218)
- binding pyridoxal-5'-phosphate: R58 (= R62), K150 (= K161), Y155 (= Y166), E184 (= E195), G187 (= G198), L207 (= L218), G209 (= G220), I210 (= I221), T211 (= T222), T247 (= T258)
2ej2A Crystal structure of t.Th.Hb8 branched-chain amino acid aminotransferase complexed with n-(5'-phosphopyridoxyl)-l-glutamate
53% identity, 97% coverage: 6:304/309 of query aligns to 3:290/294 of 2ej2A
- active site: F35 (= F38), G37 (= G40), K147 (= K161), E181 (= E195), L204 (= L218)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: R58 (= R62), Y94 (= Y98), Y152 (= Y166), E181 (= E195), G184 (= G198), E185 (= E199), L204 (= L218), G206 (= G220), I207 (= I221), T208 (= T222), T244 (= T258), A245 (= A259)
1iyeA Crystal structure of eschelichia coli branched-chain amino acid aminotransferase (see paper)
50% identity, 97% coverage: 6:306/309 of query aligns to 1:302/304 of 1iyeA
- active site: F33 (= F38), G35 (= G40), K156 (= K161), A157 (= A162), E190 (= E195), L214 (= L218)
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: R56 (= R62), Y92 (= Y98), Y126 (= Y131), K156 (= K161), Y161 (= Y166), E190 (= E195), G193 (= G198), E194 (= E199), N195 (= N200), L214 (= L218), G216 (= G220), I217 (= I221), T218 (= T222), G253 (= G257), T254 (= T258), A255 (= A259)
1iydA Crystal structure of eschelichia coli branched-chain amino acid aminotransferase (see paper)
50% identity, 97% coverage: 6:306/309 of query aligns to 1:302/304 of 1iydA
- active site: F33 (= F38), G35 (= G40), K156 (= K161), A157 (= A162), E190 (= E195), L214 (= L218)
- binding glutaric acid: Y92 (= Y98), Y126 (= Y131), A255 (= A259)
- binding pyridoxal-5'-phosphate: R56 (= R62), K156 (= K161), Y161 (= Y166), E190 (= E195), G193 (= G198), E194 (= E199), L214 (= L218), G216 (= G220), I217 (= I221), T218 (= T222), T254 (= T258)
1i1mA Crystal structure of escherichia coli branched-chain amino acid aminotransferase. (see paper)
50% identity, 97% coverage: 6:306/309 of query aligns to 1:302/304 of 1i1mA
- active site: K156 (= K161)
- binding 4-methyl valeric acid: Y92 (= Y98), K156 (= K161), T254 (= T258), A255 (= A259)
- binding pyridoxal-5'-phosphate: R56 (= R62), K156 (= K161), Y161 (= Y166), E190 (= E195), G193 (= G198), E194 (= E199), L214 (= L218), G216 (= G220), I217 (= I221), T218 (= T222), G253 (= G257), T254 (= T258)
1i1lA Crystal structure of eschelichia coli branched-chain amino acid aminotransferase. (see paper)
50% identity, 97% coverage: 6:306/309 of query aligns to 1:302/304 of 1i1lA
- active site: K156 (= K161)
- binding 2-methylleucine: Y92 (= Y98), K156 (= K161), T254 (= T258), A255 (= A259)
- binding pyridoxal-5'-phosphate: R56 (= R62), K156 (= K161), Y161 (= Y166), E190 (= E195), G193 (= G198), G216 (= G220), I217 (= I221), T218 (= T222), T254 (= T258)
6thqB Crystal structure of branched-chain aminotransferase from thermophilic archaea thermoproteus uzoniensis with norvaline
45% identity, 96% coverage: 7:304/309 of query aligns to 6:297/301 of 6thqB
- active site: F37 (= F38), K156 (= K161), E190 (= E195), L214 (= L218)
- binding pyridoxal-5'-phosphate: R60 (= R62), K156 (= K161), Y161 (= Y166), E190 (= E195), N195 (= N200), L214 (= L218), G216 (= G220), I217 (= I221), T218 (= T222), T254 (= T258)
- binding 2-[o-phosphonopyridoxyl]-amino-pentanoic acid: R60 (= R62), Y97 (= Y98), K156 (= K161), Y161 (= Y166), E190 (= E195), G193 (= G198), E194 (= E199), N195 (= N200), G216 (= G220), I217 (= I221), T218 (= T222), G253 (= G257), T254 (= T258), A255 (= A259)
5mr0D Thermophilic archaeal branched-chain amino acid transaminases from geoglobus acetivorans and archaeoglobus fulgidus: biochemical and structural characterisation (see paper)
42% identity, 94% coverage: 10:301/309 of query aligns to 4:290/290 of 5mr0D
- active site: F32 (= F38), G34 (= G40), K150 (= K161), E183 (= E195), L206 (= L218)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: R51 (= R62), G100 (= G111), L101 (≠ V112), K150 (= K161), Y154 (= Y166), E183 (= E195), G186 (= G198), D187 (≠ E199), L206 (= L218), I209 (= I221), T210 (= T222), G245 (= G257), T246 (= T258)
5e25A Crystal structure of branched-chain aminotransferase from thermophilic archaea geoglobus acetivorans complexed with alpha-ketoglutarate (see paper)
41% identity, 91% coverage: 10:289/309 of query aligns to 5:278/290 of 5e25A
- active site: F33 (= F38), G35 (= G40), K151 (= K161), E184 (= E195), L207 (= L218)
- binding 2-oxoglutaric acid: Y88 (= Y98), K151 (= K161), T247 (= T258), A248 (= A259)
- binding pyridoxal-5'-phosphate: R52 (= R62), K151 (= K161), Y155 (= Y166), E184 (= E195), G187 (= G198), D188 (≠ E199), L207 (= L218), G209 (= G220), I210 (= I221), T211 (= T222), G246 (= G257), T247 (= T258)
6h65C Crystal structure of the branched-chain-amino-acid aminotransferase from haliangium ochraceum
36% identity, 95% coverage: 11:304/309 of query aligns to 8:303/308 of 6h65C
- active site: F35 (= F38), K158 (= K161), E192 (= E195), L216 (= L218)
- binding pyridoxal-5'-phosphate: R60 (= R62), K158 (= K161), Y163 (= Y166), E192 (= E195), A196 (≠ E199), L216 (= L218), S218 (≠ G220), V219 (≠ I221), T220 (= T222), G256 (= G257), T257 (= T258)
6q8eA Crystal structure of branched-chain amino acid aminotransferase from thermobaculum terrenum in pmp-form (see paper)
38% identity, 97% coverage: 5:304/309 of query aligns to 1:301/307 of 6q8eA
- active site: F34 (= F38), K156 (= K161), E190 (= E195), L214 (= L218)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: R59 (= R62), K156 (= K161), Y161 (= Y166), E190 (= E195), G193 (= G198), S194 (≠ E199), C195 (≠ N200), L214 (= L218), S216 (≠ G220), I217 (= I221), T218 (= T222), G254 (= G257), T255 (= T258)
7neaA Crystal structure of branched-chain amino acid aminotransferase from thermobaculum terrenum (m3 mutant). (see paper)
37% identity, 97% coverage: 5:304/309 of query aligns to 1:301/309 of 7neaA
- active site: F34 (= F38), K156 (= K161), E190 (= E195), L214 (= L218)
- binding pyridoxal-5'-phosphate: R59 (= R62), K156 (= K161), Y161 (= Y166), E190 (= E195), G193 (= G198), S194 (≠ E199), L214 (= L218), S216 (≠ G220), I217 (= I221), T218 (= T222), T255 (= T258)
7p3tB Transaminase of gamma-proteobacterium (see paper)
33% identity, 93% coverage: 10:296/309 of query aligns to 6:286/299 of 7p3tB
- binding pyridoxal-5'-phosphate: R53 (= R62), K153 (= K161), R157 (≠ Y166), E186 (= E195), S187 (≠ A196), A188 (≠ T197), A189 (≠ G198), S190 (≠ E199), G210 (= G220), I211 (= I221), T212 (= T222), T248 (= T258)
P19938 D-alanine aminotransferase; D-amino acid aminotransferase; D-amino acid transaminase; DAAT; D-aspartate aminotransferase; EC 2.6.1.21 from Bacillus sp. (strain YM-1) (see 5 papers)
29% identity, 91% coverage: 9:289/309 of query aligns to 4:273/283 of P19938
- Y32 (≠ F38) binding
- R51 (= R62) binding
- R99 (≠ M110) binding
- H101 (≠ V112) binding
- K146 (≠ N154) active site, Proton acceptor; modified: N6-(pyridoxal phosphate)lysine
- E178 (= E195) binding ; mutation to K: Loss of transaminase activity and small gain in racemase activity.
- L202 (= L218) mutation to A: Inactivates enzyme.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3daaA Crystallographic structure of d-amino acid aminotransferase inactivated by pyridoxyl-d-alanine (see paper)
29% identity, 91% coverage: 9:289/309 of query aligns to 3:272/277 of 3daaA
- active site: Y31 (≠ F38), V33 (≠ G40), K145 (≠ N154), E177 (= E195), L201 (= L218)
- binding n-(5'-phosphopyridoxyl)-d-alanine: Y31 (≠ F38), R50 (= R62), K145 (≠ N154), E177 (= E195), S180 (≠ G198), S181 (≠ E199), L201 (= L218), G203 (= G220), I204 (= I221), T205 (= T222), S240 (≠ G257), T241 (= T258)
2daaA Crystallographic structure of d-amino acid aminotransferase inactivated by d-cycloserine
29% identity, 91% coverage: 9:289/309 of query aligns to 3:272/277 of 2daaA
- active site: Y31 (≠ F38), V33 (≠ G40), K145 (≠ N154), E177 (= E195), L201 (= L218)
- binding d-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-n,o-cycloserylamide: Y31 (≠ F38), V33 (≠ G40), R50 (= R62), R98 (≠ M110), H100 (≠ V112), K145 (≠ N154), E177 (= E195), S180 (≠ G198), S181 (≠ E199), N182 (= N200), L201 (= L218), G203 (= G220), I204 (= I221), T205 (= T222), T241 (= T258)
Query Sequence
>208718 DVU3197 branched-chain amino acid aminotransferase
MSMVQKSETIWFDGKQVPWDEANVHVLTHALHYGVGVFEGIRAYRCADGSSAVFRLREHV
QRLFSSAKILRMEIPFTEDAIFDAIVETLQRNRLAEGYIRPLSFVGAGAMGVYPGDNPVQ
TIIAVWPWGAYLGAEALEKGIRVKTSSFARHHVNAMMTKAKASGNYVNSVLAKMEAKADG
YDEALMLDVSGFVSEATGENIFMVRNGVIKTTPLTSILDGITRNSLMTLARDLGYEVVEQ
QFTRDELYVADEAFFCGTAAEVTPIREVDRRVIGKGSAGPVTKHLQQEYFKAVKGDNPSY
DHWLHRYAL
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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