SitesBLAST
Comparing GFF3443 FitnessBrowser__Phaeo:GFF3443 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)
7z79B Crystal structure of aminotransferase-like protein from variovorax paradoxus
50% identity, 97% coverage: 6:299/302 of query aligns to 3:297/306 of 7z79B
- binding pyridoxal-5'-phosphate: W46 (= W49), R65 (= R68), N166 (= N166), S202 (≠ A202), T203 (≠ C203), F222 (≠ M222), G224 (= G224), I225 (= I225), T226 (= T226), G261 (= G261), T262 (= T262)
5e25A Crystal structure of branched-chain aminotransferase from thermophilic archaea geoglobus acetivorans complexed with alpha-ketoglutarate (see paper)
39% identity, 94% coverage: 18:300/302 of query aligns to 2:285/290 of 5e25A
- active site: F33 (≠ W49), G35 (= G51), K151 (≠ N166), E184 (≠ T199), L207 (≠ M222)
- binding 2-oxoglutaric acid: Y88 (≠ H105), K151 (≠ N166), T247 (= T262), A248 (≠ F263)
- binding pyridoxal-5'-phosphate: R52 (= R68), K151 (≠ N166), Y155 (≠ K170), E184 (≠ T199), G187 (≠ A202), D188 (≠ C203), L207 (≠ M222), G209 (= G224), I210 (= I225), T211 (= T226), G246 (= G261), T247 (= T262)
5mr0D Thermophilic archaeal branched-chain amino acid transaminases from geoglobus acetivorans and archaeoglobus fulgidus: biochemical and structural characterisation (see paper)
38% identity, 93% coverage: 19:300/302 of query aligns to 2:284/290 of 5mr0D
- active site: F32 (≠ W49), G34 (= G51), K150 (≠ N166), E183 (≠ T199), L206 (≠ M222)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: R51 (= R68), G100 (vs. gap), L101 (vs. gap), K150 (≠ N166), Y154 (≠ K170), E183 (≠ T199), G186 (≠ A202), D187 (≠ C203), L206 (≠ M222), I209 (= I225), T210 (= T226), G245 (= G261), T246 (= T262)
7p3tB Transaminase of gamma-proteobacterium (see paper)
35% identity, 92% coverage: 16:293/302 of query aligns to 1:279/299 of 7p3tB
- binding pyridoxal-5'-phosphate: R53 (= R68), K153 (≠ N166), R157 (≠ K170), E186 (≠ T199), S187 (≠ T200), A188 (≠ N201), A189 (= A202), S190 (≠ C203), G210 (= G224), I211 (= I225), T212 (= T226), T248 (= T262)
4whxA X-ray crystal structure of an amino acid aminotransferase from burkholderia pseudomallei bound to the co-factor pyridoxal phosphate
31% identity, 93% coverage: 21:302/302 of query aligns to 9:297/306 of 4whxA
3lqsA Complex structure of d-amino acid aminotransferase and 4-amino-4,5- dihydro-thiophenecarboxylic acid (adta) (see paper)
30% identity, 91% coverage: 24:299/302 of query aligns to 6:278/280 of 3lqsA
- active site: Y31 (≠ W49), V33 (≠ G51), K145 (≠ N166), E177 (≠ T199), L201 (≠ M222)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]thiophene-2-carboxylic acid: V33 (≠ G51), R50 (= R68), E177 (≠ T199), S180 (≠ A202), S181 (≠ C203), N182 (= N204), L201 (≠ M222), G203 (= G224), I204 (= I225), T205 (= T226), S240 (≠ G261), T241 (= T262), T242 (≠ F263)
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)
30% identity, 91% coverage: 24:299/302 of query aligns to 7:279/283 of P19938
- Y32 (≠ W49) binding
- R51 (= R68) binding
- R99 (= R117) binding
- H101 (≠ F119) binding
- K146 (≠ N166) active site, Proton acceptor; modified: N6-(pyridoxal phosphate)lysine
- E178 (≠ T199) binding ; mutation to K: Loss of transaminase activity and small gain in racemase activity.
- L202 (≠ M222) 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)
30% identity, 91% coverage: 24:297/302 of query aligns to 6:276/277 of 3daaA
- active site: Y31 (≠ W49), V33 (≠ G51), K145 (≠ N166), E177 (≠ T199), L201 (≠ M222)
- binding n-(5'-phosphopyridoxyl)-d-alanine: Y31 (≠ W49), R50 (= R68), K145 (≠ N166), E177 (≠ T199), S180 (≠ A202), S181 (≠ C203), L201 (≠ M222), G203 (= G224), I204 (= I225), T205 (= T226), S240 (≠ G261), T241 (= T262)
2daaA Crystallographic structure of d-amino acid aminotransferase inactivated by d-cycloserine
30% identity, 91% coverage: 24:297/302 of query aligns to 6:276/277 of 2daaA
- active site: Y31 (≠ W49), V33 (≠ G51), K145 (≠ N166), E177 (≠ T199), L201 (≠ M222)
- binding d-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-n,o-cycloserylamide: Y31 (≠ W49), V33 (≠ G51), R50 (= R68), R98 (= R117), H100 (≠ F119), K145 (≠ N166), E177 (≠ T199), S180 (≠ A202), S181 (≠ C203), N182 (= N204), L201 (≠ M222), G203 (= G224), I204 (= I225), T205 (= T226), T241 (= T262)
1daaA Crystallographic structure of d-amino acid aminotransferase complexed with pyridoxal-5'-phosphate (see paper)
30% identity, 91% coverage: 24:297/302 of query aligns to 6:276/277 of 1daaA
- active site: Y31 (≠ W49), V33 (≠ G51), K145 (≠ N166), E177 (≠ T199), L201 (≠ M222)
- binding pyridoxal-5'-phosphate: R50 (= R68), K145 (≠ N166), E177 (≠ T199), S180 (≠ A202), S181 (≠ C203), L201 (≠ M222), G203 (= G224), I204 (= I225), T205 (= T226), S240 (≠ G261), T241 (= T262)
1a0gB L201a mutant of d-amino acid aminotransferase complexed with pyridoxamine-5'-phosphate (see paper)
30% identity, 91% coverage: 24:299/302 of query aligns to 6:278/282 of 1a0gB
- active site: Y31 (≠ W49), V33 (≠ G51), K145 (≠ N166), E177 (≠ T199), A201 (vs. gap)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: R50 (= R68), K145 (≠ N166), E177 (≠ T199), S180 (≠ A202), S181 (≠ C203), G203 (= G224), I204 (= I225), T205 (= T226), S240 (≠ G261), T241 (= T262)
6thqB Crystal structure of branched-chain aminotransferase from thermophilic archaea thermoproteus uzoniensis with norvaline
31% identity, 92% coverage: 21:297/302 of query aligns to 9:286/301 of 6thqB
- active site: F37 (≠ W49), K156 (≠ S167), E190 (≠ T199), L214 (≠ M222)
- binding pyridoxal-5'-phosphate: R60 (= R68), K156 (≠ S167), Y161 (≠ K170), E190 (≠ T199), N195 (= N204), L214 (≠ M222), G216 (= G224), I217 (= I225), T218 (= T226), T254 (= T262)
- binding 2-[o-phosphonopyridoxyl]-amino-pentanoic acid: R60 (= R68), Y97 (≠ H105), K156 (≠ S167), Y161 (≠ K170), E190 (≠ T199), G193 (≠ A202), E194 (≠ C203), N195 (= N204), G216 (= G224), I217 (= I225), T218 (= T226), G253 (= G261), T254 (= T262), A255 (≠ F263)
2ej3A Crystal structure of t.Th.Hb8 branched-chain amino acid aminotransferase complexed with gabapentin
32% identity, 92% coverage: 20:297/302 of query aligns to 6:282/297 of 2ej3A
- active site: F35 (≠ W49), G37 (= G51), K150 (= K164), E184 (≠ T199), L207 (≠ M222)
- binding [1-(aminomethyl)cyclohexyl]acetic acid: G187 (≠ A202), G246 (= G261), T247 (= T262), A248 (≠ F263)
- binding pyridoxal-5'-phosphate: R58 (= R68), K150 (= K164), Y155 (≠ S169), E184 (≠ T199), G187 (≠ A202), L207 (≠ M222), G209 (= G224), I210 (= I225), T211 (= T226), G246 (= G261), T247 (= T262)
2ej0B Crystal structure of t.Th.Hb8 branched-chain amino acid aminotransferase with pyridoxamine 5'-phosphate
31% identity, 92% coverage: 20:297/302 of query aligns to 6:290/305 of 2ej0B
- active site: F35 (≠ W49), G37 (= G51), K158 (= K164), E192 (≠ T199), L215 (≠ M222)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: R58 (= R68), Y163 (≠ S169), E192 (≠ T199), G195 (≠ A202), E196 (≠ C203), L215 (≠ M222), G217 (= G224), I218 (= I225), T219 (= T226), G254 (= G261), T255 (= T262)
2ej2A Crystal structure of t.Th.Hb8 branched-chain amino acid aminotransferase complexed with n-(5'-phosphopyridoxyl)-l-glutamate
32% identity, 92% coverage: 20:297/302 of query aligns to 6:279/294 of 2ej2A
- active site: F35 (≠ W49), G37 (= G51), K147 (= K164), E181 (≠ T199), L204 (≠ M222)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: R58 (= R68), Y94 (≠ H105), Y152 (≠ S169), E181 (≠ T199), G184 (≠ A202), E185 (≠ C203), L204 (≠ M222), G206 (= G224), I207 (= I225), T208 (= T226), T244 (= T262), A245 (≠ F263)
1iyeA Crystal structure of eschelichia coli branched-chain amino acid aminotransferase (see paper)
30% identity, 93% coverage: 21:300/302 of query aligns to 5:292/304 of 1iyeA
- active site: F33 (≠ W49), G35 (= G51), K156 (≠ N166), A157 (≠ S167), E190 (≠ T199), L214 (≠ M222)
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: R56 (= R68), Y92 (≠ H105), Y126 (vs. gap), K156 (≠ N166), Y161 (vs. gap), E190 (≠ T199), G193 (≠ A202), E194 (≠ C203), N195 (= N204), L214 (≠ M222), G216 (= G224), I217 (= I225), T218 (= T226), G253 (= G261), T254 (= T262), A255 (≠ F263)
1iydA Crystal structure of eschelichia coli branched-chain amino acid aminotransferase (see paper)
30% identity, 93% coverage: 21:300/302 of query aligns to 5:292/304 of 1iydA
- active site: F33 (≠ W49), G35 (= G51), K156 (≠ N166), A157 (≠ S167), E190 (≠ T199), L214 (≠ M222)
- binding glutaric acid: Y92 (≠ H105), Y126 (vs. gap), A255 (≠ F263)
- binding pyridoxal-5'-phosphate: R56 (= R68), K156 (≠ N166), Y161 (vs. gap), E190 (≠ T199), G193 (≠ A202), E194 (≠ C203), L214 (≠ M222), G216 (= G224), I217 (= I225), T218 (= T226), T254 (= T262)
1i1mA Crystal structure of escherichia coli branched-chain amino acid aminotransferase. (see paper)
30% identity, 93% coverage: 21:300/302 of query aligns to 5:292/304 of 1i1mA
- active site: K156 (≠ N166)
- binding 4-methyl valeric acid: Y92 (≠ H105), K156 (≠ N166), T254 (= T262), A255 (≠ F263)
- binding pyridoxal-5'-phosphate: R56 (= R68), K156 (≠ N166), Y161 (vs. gap), E190 (≠ T199), G193 (≠ A202), E194 (≠ C203), L214 (≠ M222), G216 (= G224), I217 (= I225), T218 (= T226), G253 (= G261), T254 (= T262)
1i1lA Crystal structure of eschelichia coli branched-chain amino acid aminotransferase. (see paper)
30% identity, 93% coverage: 21:300/302 of query aligns to 5:292/304 of 1i1lA
- active site: K156 (≠ N166)
- binding 2-methylleucine: Y92 (≠ H105), K156 (≠ N166), T254 (= T262), A255 (≠ F263)
- binding pyridoxal-5'-phosphate: R56 (= R68), K156 (≠ N166), Y161 (vs. gap), E190 (≠ T199), G193 (≠ A202), G216 (= G224), I217 (= I225), T218 (= T226), T254 (= T262)
6h65C Crystal structure of the branched-chain-amino-acid aminotransferase from haliangium ochraceum
29% identity, 90% coverage: 22:293/302 of query aligns to 8:288/308 of 6h65C
- active site: F35 (≠ W49), K158 (≠ N166), E192 (≠ T199), L216 (≠ M222)
- binding pyridoxal-5'-phosphate: R60 (= R68), K158 (≠ N166), Y163 (≠ L171), E192 (≠ T199), A196 (≠ C203), L216 (≠ M222), S218 (≠ G224), V219 (≠ I225), T220 (= T226), G256 (= G261), T257 (= T262)
Query Sequence
>GFF3443 FitnessBrowser__Phaeo:GFF3443
MTEKMSTHQAQEDQRNEEILIYLNGEIVPKAEAKVSVYDSGFMLGDGVWEGLRLYNGTWA
FIDEHLDRLFEAAKTIDLDIGMDRDQVKQAVLDTQDANDMTSDAHARLMVTRGVKSRPFQ
HPSLSQQGPTFTIIMEHSRPNLPRPIRLATVPHLRGLPMTQDPKLNSHSKLNCILACIAA
EKAGADEGLMLDVNGFVNTTNACNFFIVRKGAVWTSTGDYCMNGITRQKVIDLCRANDIP
VFERNYSLVDTYGADEAFLTGTFGAQTPVGDIDGRQIGDGEMGPVTKRLRALYKDLIAQE
CA
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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