SitesBLAST
Comparing Echvi_0009 FitnessBrowser__Cola:Echvi_0009 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)
7p7xA Crystal structure of d-amino acid transaminase from haliscomenobacter hydrossis (holo form). (see paper)
36% identity, 93% coverage: 12:264/273 of query aligns to 13:271/282 of 7p7xA
- binding pyridoxal-5'-phosphate: R53 (= R52), R138 (= R137), K144 (= K143), Y148 (= Y147), E177 (= E175), A179 (≠ S177), R180 (= R178), S181 (= S179), L200 (= L197), G202 (= G199), I203 (= I200), T204 (= T201), T240 (= T233)
- binding phosphate ion: L47 (= L46), D48 (≠ E47), R73 (≠ K72)
Sites not aligning to the query:
8ahuA Crystal structure of d-amino acid aminotrensferase from haliscomenobacter hydrossis complexed with d-cycloserine
36% identity, 93% coverage: 12:264/273 of query aligns to 14:272/283 of 8ahuA
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: F35 (= F33), R54 (= R52), R139 (= R137), K145 (= K143), Y149 (= Y147), E178 (= E175), A180 (≠ S177), R181 (= R178), S182 (= S179), L201 (= L197), G203 (= G199), I204 (= I200), T205 (= T201), S240 (= S232), T241 (= T233)
8raiA Crystal structure of d-amino acid transaminase from haliscomenobacter hydrossis point mutant r90i complexed with phenylhydrazine
36% identity, 93% coverage: 12:264/273 of query aligns to 13:271/282 of 8raiA
- binding [6-methyl-5-oxidanyl-4-[(2-phenylhydrazinyl)methyl]pyridin-3-yl]methyl dihydrogen phosphate: F34 (= F33), R53 (= R52), R138 (= R137), K144 (= K143), Y148 (= Y147), E177 (= E175), A179 (≠ S177), R180 (= R178), S181 (= S179), N182 (= N180), L200 (= L197), G202 (= G199), I203 (= I200), T204 (= T201), T240 (= T233)
5e25A Crystal structure of branched-chain aminotransferase from thermophilic archaea geoglobus acetivorans complexed with alpha-ketoglutarate (see paper)
32% identity, 96% coverage: 12:272/273 of query aligns to 12:287/290 of 5e25A
- active site: F33 (= F33), G35 (≠ F35), K151 (= K143), E184 (= E175), L207 (= L197)
- binding 2-oxoglutaric acid: Y88 (≠ G88), K151 (= K143), T247 (= T233), A248 (≠ T234)
- binding pyridoxal-5'-phosphate: R52 (= R52), K151 (= K143), Y155 (= Y147), E184 (= E175), G187 (≠ R178), D188 (≠ S179), L207 (= L197), G209 (= G199), I210 (= I200), T211 (= T201), G246 (≠ S232), T247 (= T233)
5mr0D Thermophilic archaeal branched-chain amino acid transaminases from geoglobus acetivorans and archaeoglobus fulgidus: biochemical and structural characterisation (see paper)
30% identity, 97% coverage: 4:269/273 of query aligns to 3:282/290 of 5mr0D
- active site: F32 (= F33), G34 (≠ F35), K150 (= K143), E183 (= E175), L206 (= L197)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: R51 (= R52), G100 (≠ H101), L101 (≠ F102), K150 (= K143), Y154 (= Y147), E183 (= E175), G186 (≠ R178), D187 (≠ S179), L206 (= L197), I209 (= I200), T210 (= T201), G245 (≠ S232), T246 (= T233)
8aieB Crystal structure of d-amino acid aminotransferase from aminobacterium colombiense complexed with d-cycloserine
31% identity, 95% coverage: 5:264/273 of query aligns to 4:266/275 of 8aieB
- binding 3-azanyloxy-2-[(~{E})-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]propanoic acid: T34 (≠ F35), R51 (= R52), K142 (= K143), Y146 (= Y147), E172 (= E175), H175 (≠ R178), S176 (= S179), T198 (≠ I200), T199 (= T201), G234 (≠ S232), T235 (= T233), V236 (≠ T234), K237 (= K235)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: R51 (= R52), Y146 (= Y147), E172 (= E175), S174 (= S177), H175 (≠ R178), S176 (= S179), L195 (= L197), T198 (≠ I200), T199 (= T201), G234 (≠ S232), T235 (= T233)
8aykA Crystal structure of d-amino acid aminotrensferase from aminobacterium colombiense complexed with d-glutamate (see paper)
31% identity, 95% coverage: 5:264/273 of query aligns to 5:267/276 of 8aykA
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: R52 (= R52), R137 (= R137), K143 (= K143), E173 (= E175), S175 (= S177), H176 (≠ R178), S177 (= S179), L196 (= L197), T199 (≠ I200), T200 (= T201), G235 (≠ S232), T236 (= T233)
- binding (~{Z})-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pent-2-enedioic acid: T35 (≠ F35), R52 (= R52), R137 (= R137), K143 (= K143), E173 (= E175), H176 (≠ R178), S177 (= S179), L196 (= L197), G198 (= G199), T199 (≠ I200), T200 (= T201), G235 (≠ S232), T236 (= T233), V237 (≠ T234), K238 (= K235)
8ayjA Crystal structure of d-amino acid aminotransferase from aminobacterium colombiens complexed with 3-aminooxypropionic acid (see paper)
31% identity, 95% coverage: 5:264/273 of query aligns to 5:267/276 of 8ayjA
- binding 3-[(~{E})-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxypropanoic acid: T35 (≠ F35), T35 (≠ F35), R52 (= R52), M87 (≠ G88), R89 (= R90), R137 (= R137), K143 (= K143), Y147 (= Y147), Y147 (= Y147), E173 (= E175), H176 (≠ R178), H176 (≠ R178), S177 (= S179), L196 (= L197), G198 (= G199), T199 (≠ I200), T200 (= T201), G235 (≠ S232), T236 (= T233), T236 (= T233), V237 (≠ T234), K238 (= K235)
- binding pyridoxal-5'-phosphate: R52 (= R52), R137 (= R137), Y147 (= Y147), E173 (= E175), S175 (= S177), H176 (≠ R178), S177 (= S179), L196 (= L197), G198 (= G199), T199 (≠ I200), T200 (= T201), T236 (= T233)
8aieA Crystal structure of d-amino acid aminotransferase from aminobacterium colombiense complexed with d-cycloserine
31% identity, 95% coverage: 5:264/273 of query aligns to 5:267/276 of 8aieA
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: T35 (≠ F35), R52 (= R52), K143 (= K143), Y147 (= Y147), S175 (= S177), H176 (≠ R178), S177 (= S179), T199 (≠ I200), T200 (= T201), G235 (≠ S232), T236 (= T233), V237 (≠ T234), K238 (= K235)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: R52 (= R52), R137 (= R137), K143 (= K143), Y147 (= Y147), E173 (= E175), S177 (= S179), L196 (= L197), G198 (= G199), T199 (≠ I200), T200 (= T201), G235 (≠ S232), T236 (= T233)
8onjA Crystal structure of d-amino acid aminotransferase from aminobacterium colombiense point mutant r88l (see paper)
32% identity, 95% coverage: 5:264/273 of query aligns to 6:268/277 of 8onjA
- binding pyridoxal-5'-phosphate: R53 (= R52), R138 (= R137), K144 (= K143), E174 (= E175), H177 (≠ R178), S178 (= S179), L197 (= L197), T200 (≠ I200), T201 (= T201), G236 (≠ S232), T237 (= T233)
5fr9A Structure of transaminase ata-117 arrmut11 from arthrobacter sp. Knk168 inhibited with 1-(4-bromophenyl)-2-fluoroethylamine (see paper)
26% identity, 96% coverage: 12:273/273 of query aligns to 35:312/319 of 5fr9A
- active site: Y56 (≠ F33), K177 (= K143), E210 (= E175), L232 (= L197)
- binding [4-[3-(4-bromophenyl)-3-oxidanylidene-propyl]-6-methyl-5-oxidanyl-pyridin-3-yl]methyl phosphate: R75 (= R52), K177 (= K143), E210 (= E175), G213 (≠ R178), F214 (≠ S179), L232 (= L197), G234 (= G199), I235 (= I200), T236 (= T201), T272 (= T233)
3lqsA Complex structure of d-amino acid aminotransferase and 4-amino-4,5- dihydro-thiophenecarboxylic acid (adta) (see paper)
28% identity, 96% coverage: 4:265/273 of query aligns to 2:273/280 of 3lqsA
- active site: Y31 (≠ F33), V33 (≠ F35), K145 (= K143), E177 (= E175), L201 (= L197)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]thiophene-2-carboxylic acid: V33 (≠ F35), R50 (= R52), E177 (= E175), S180 (≠ R178), S181 (= S179), N182 (= N180), L201 (= L197), G203 (= G199), I204 (= I200), T205 (= T201), S240 (= S232), T241 (= T233), T242 (= T234)
3daaA Crystallographic structure of d-amino acid aminotransferase inactivated by pyridoxyl-d-alanine (see paper)
28% identity, 96% coverage: 4:265/273 of query aligns to 2:273/277 of 3daaA
- active site: Y31 (≠ F33), V33 (≠ F35), K145 (= K143), E177 (= E175), L201 (= L197)
- binding n-(5'-phosphopyridoxyl)-d-alanine: Y31 (≠ F33), R50 (= R52), K145 (= K143), E177 (= E175), S180 (≠ R178), S181 (= S179), L201 (= L197), G203 (= G199), I204 (= I200), T205 (= T201), S240 (= S232), T241 (= T233)
2daaA Crystallographic structure of d-amino acid aminotransferase inactivated by d-cycloserine
28% identity, 96% coverage: 4:265/273 of query aligns to 2:273/277 of 2daaA
- active site: Y31 (≠ F33), V33 (≠ F35), K145 (= K143), E177 (= E175), L201 (= L197)
- binding d-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-n,o-cycloserylamide: Y31 (≠ F33), V33 (≠ F35), R50 (= R52), R98 (vs. gap), H100 (≠ N100), K145 (= K143), E177 (= E175), S180 (≠ R178), S181 (= S179), N182 (= N180), L201 (= L197), G203 (= G199), I204 (= I200), T205 (= T201), T241 (= T233)
1daaA Crystallographic structure of d-amino acid aminotransferase complexed with pyridoxal-5'-phosphate (see paper)
28% identity, 96% coverage: 4:265/273 of query aligns to 2:273/277 of 1daaA
- active site: Y31 (≠ F33), V33 (≠ F35), K145 (= K143), E177 (= E175), L201 (= L197)
- binding pyridoxal-5'-phosphate: R50 (= R52), K145 (= K143), E177 (= E175), S180 (≠ R178), S181 (= S179), L201 (= L197), G203 (= G199), I204 (= I200), T205 (= T201), S240 (= S232), T241 (= T233)
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)
28% identity, 96% coverage: 4:265/273 of query aligns to 3:274/283 of P19938
- Y32 (≠ F33) binding
- R51 (= R52) binding
- R99 (vs. gap) binding
- H101 (≠ N100) binding
- K146 (= K143) active site, Proton acceptor; modified: N6-(pyridoxal phosphate)lysine
- E178 (= E175) binding ; mutation to K: Loss of transaminase activity and small gain in racemase activity.
- L202 (= L197) mutation to A: Inactivates enzyme.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7p3tB Transaminase of gamma-proteobacterium (see paper)
29% identity, 95% coverage: 12:269/273 of query aligns to 13:284/299 of 7p3tB
- binding pyridoxal-5'-phosphate: R53 (= R52), K153 (= K143), R157 (≠ Y147), E186 (= E175), S187 (= S176), A188 (≠ S177), A189 (≠ R178), S190 (= S179), G210 (= G199), I211 (= I200), T212 (= T201), T248 (= T233)
6xu3B (R)-selective amine transaminase from shinella sp. (see paper)
25% identity, 93% coverage: 12:264/273 of query aligns to 36:303/321 of 6xu3B
- active site: Y57 (≠ F33), K177 (vs. gap), E210 (= E175), L232 (= L197)
- binding 3-aminobenzoic acid: P169 (vs. gap), D173 (vs. gap), K229 (≠ T194)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: R76 (= R52), Y112 (≠ G88), K177 (vs. gap), F184 (≠ Y147), E210 (= E175), G213 (≠ R178), F214 (≠ S179), N215 (= N180), L232 (= L197), G234 (= G199), V235 (≠ I200), T236 (= T201), T272 (= T233)
6xu3A (R)-selective amine transaminase from shinella sp. (see paper)
25% identity, 93% coverage: 12:264/273 of query aligns to 35:302/320 of 6xu3A
- active site: Y56 (≠ F33), K176 (vs. gap), E209 (= E175), L231 (= L197)
- binding pyridoxal-5'-phosphate: R75 (= R52), K176 (vs. gap), F183 (≠ Y147), E209 (= E175), G212 (≠ R178), F213 (≠ S179), L231 (= L197), G233 (= G199), V234 (≠ I200), T235 (= T201), T271 (= T233)
6xu3C (R)-selective amine transaminase from shinella sp. (see paper)
25% identity, 93% coverage: 12:264/273 of query aligns to 37:304/322 of 6xu3C
- active site: Y58 (≠ F33), K178 (vs. gap), E211 (= E175), L233 (= L197)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: V60 (≠ F35), R77 (= R52), K178 (vs. gap), F185 (≠ Y147), E211 (= E175), G214 (≠ R178), N216 (= N180), L233 (= L197), G235 (= G199), V236 (≠ I200), T237 (= T201), T272 (≠ S232), T273 (= T233), A274 (≠ T234)
Query Sequence
>Echvi_0009 FitnessBrowser__Cola:Echvi_0009
MKPYCFAIDRIIPSEDASLHPLDIGLIRGYAVFDFFRTVDYHPLFLEDYLDRFIASAAKA
HLVLDQGHEELKSIVLELIQKNDLKQGGIRMVLSGGNSDNHFSPTKGSLFIFCEALQMPS
DDKYRNGVHLLTTEYIRPVPEIKTTNYALPVYLSKDWKANNAEDVLYHADGIISESSRSN
IFIVKDGTISTPKTNILKGITRKNILALVPDAQIRDITLEEVMAADEVFMSSTTKRILPI
TKIDHQPISNGAVGTRTTALMEQFKRMEEETVS
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