SitesBLAST
Comparing WP_084516686.1 NCBI__GCF_000422285.1:WP_084516686.1 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)
5e25A Crystal structure of branched-chain aminotransferase from thermophilic archaea geoglobus acetivorans complexed with alpha-ketoglutarate (see paper)
35% identity, 70% coverage: 100:369/383 of query aligns to 19:284/290 of 5e25A
- active site: F33 (= F114), G35 (≠ V116), K151 (= K230), E184 (= E263), L207 (= L287)
- binding 2-oxoglutaric acid: Y88 (≠ L169), K151 (= K230), T247 (= T332), A248 (≠ S333)
- binding pyridoxal-5'-phosphate: R52 (= R133), K151 (= K230), Y155 (= Y234), E184 (= E263), G187 (≠ T266), D188 (≠ E267), L207 (= L287), G209 (= G289), I210 (= I290), T211 (= T291), G246 (= G331), T247 (= T332)
5mr0D Thermophilic archaeal branched-chain amino acid transaminases from geoglobus acetivorans and archaeoglobus fulgidus: biochemical and structural characterisation (see paper)
35% identity, 66% coverage: 100:353/383 of query aligns to 18:267/290 of 5mr0D
- active site: F32 (= F114), G34 (≠ V116), K150 (= K230), E183 (= E263), L206 (= L287)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: R51 (= R133), G100 (≠ T182), L101 (≠ A183), K150 (= K230), Y154 (= Y234), E183 (= E263), G186 (≠ T266), D187 (≠ E267), L206 (= L287), I209 (= I290), T210 (= T291), G245 (= G331), T246 (= T332)
2ej0B Crystal structure of t.Th.Hb8 branched-chain amino acid aminotransferase with pyridoxamine 5'-phosphate
32% identity, 68% coverage: 102:362/383 of query aligns to 23:285/305 of 2ej0B
- active site: F35 (= F114), G37 (≠ V116), K158 (≠ I229), E192 (= E263), L215 (= L287)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: R58 (= R133), Y163 (= Y234), E192 (= E263), G195 (≠ T266), E196 (= E267), L215 (= L287), G217 (= G289), I218 (= I290), T219 (= T291), G254 (= G331), T255 (= T332)
2ej3A Crystal structure of t.Th.Hb8 branched-chain amino acid aminotransferase complexed with gabapentin
32% identity, 68% coverage: 102:362/383 of query aligns to 23:277/297 of 2ej3A
- active site: F35 (= F114), G37 (≠ V116), K150 (≠ I229), E184 (= E263), L207 (= L287)
- binding [1-(aminomethyl)cyclohexyl]acetic acid: G187 (≠ T266), G246 (= G331), T247 (= T332), A248 (≠ S333)
- binding pyridoxal-5'-phosphate: R58 (= R133), K150 (≠ I229), Y155 (= Y234), E184 (= E263), G187 (≠ T266), L207 (= L287), G209 (= G289), I210 (= I290), T211 (= T291), G246 (= G331), T247 (= T332)
2eiyA Crystal structure of t.Th.Hb8 branched-chain amino acid aminotransferase complexed with 4-methylvaleric acid
32% identity, 68% coverage: 102:362/383 of query aligns to 23:277/297 of 2eiyA
- active site: F35 (= F114), G37 (≠ V116), K150 (≠ I229), E184 (= E263), L207 (= L287)
- binding 4-methyl valeric acid: F35 (= F114), Y94 (≠ L169), T247 (= T332), A248 (≠ S333)
- binding pyridoxal-5'-phosphate: R58 (= R133), K150 (≠ I229), Y155 (= Y234), E184 (= E263), G187 (≠ T266), E188 (= E267), L207 (= L287), G209 (= G289), I210 (= I290), T211 (= T291), G246 (= G331), T247 (= T332)
1wrvA Crystal structure of t.Th.Hb8 branched-chain amino acid aminotransferase
32% identity, 68% coverage: 102:362/383 of query aligns to 23:277/297 of 1wrvA
- active site: F35 (= F114), G37 (≠ V116), K150 (≠ I229), E184 (= E263), L207 (= L287)
- binding pyridoxal-5'-phosphate: R58 (= R133), K150 (≠ I229), Y155 (= Y234), E184 (= E263), G187 (≠ T266), L207 (= L287), G209 (= G289), I210 (= I290), T211 (= T291), T247 (= T332)
2ej2A Crystal structure of t.Th.Hb8 branched-chain amino acid aminotransferase complexed with n-(5'-phosphopyridoxyl)-l-glutamate
32% identity, 68% coverage: 102:362/383 of query aligns to 23:274/294 of 2ej2A
- active site: F35 (= F114), G37 (≠ V116), K147 (≠ I229), E181 (= E263), L204 (= L287)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: R58 (= R133), Y94 (≠ L169), Y152 (= Y234), E181 (= E263), G184 (≠ T266), E185 (= E267), L204 (= L287), G206 (= G289), I207 (= I290), T208 (= T291), T244 (= T332), A245 (≠ S333)
4uugA The (r)-selective amine transaminase from aspergillus fumigatus with inhibitor bound (see paper)
28% identity, 68% coverage: 100:360/383 of query aligns to 43:308/320 of 4uugA
- active site: Y57 (≠ F114), K178 (= K230), E211 (= E263), L233 (= L287)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: R76 (= R133), K178 (= K230), E211 (= E263), G214 (≠ T266), F215 (≠ E267), N216 (= N268), L233 (= L287), G235 (= G289), I236 (= I290), T237 (= T291), T272 (≠ G331), T273 (= T332), A274 (≠ S333)
4chiA (R)-selective amine transaminase from aspergillus fumigatus at 1.27 a resolution (see paper)
28% identity, 68% coverage: 100:360/383 of query aligns to 43:308/320 of 4chiA
- active site: Y57 (≠ F114), K178 (= K230), E211 (= E263), L233 (= L287)
- binding pyridoxal-5'-phosphate: R76 (= R133), K178 (= K230), E211 (= E263), F215 (≠ E267), L233 (= L287), G235 (= G289), I236 (= I290), T237 (= T291), T272 (≠ G331), T273 (= T332)
- binding phosphate ion: R76 (= R133), G235 (= G289), I236 (= I290), T237 (= T291), T273 (= T332)
5fr9A Structure of transaminase ata-117 arrmut11 from arthrobacter sp. Knk168 inhibited with 1-(4-bromophenyl)-2-fluoroethylamine (see paper)
27% identity, 74% coverage: 95:377/383 of query aligns to 37:317/319 of 5fr9A
- active site: Y56 (≠ F114), K177 (= K230), E210 (= E263), L232 (= L287)
- binding [4-[3-(4-bromophenyl)-3-oxidanylidene-propyl]-6-methyl-5-oxidanyl-pyridin-3-yl]methyl phosphate: R75 (= R133), K177 (= K230), E210 (= E263), G213 (≠ T266), F214 (≠ E267), L232 (= L287), G234 (= G289), I235 (= I290), T236 (= T291), T272 (= T332)
7p3tB Transaminase of gamma-proteobacterium (see paper)
32% identity, 72% coverage: 101:377/383 of query aligns to 22:292/299 of 7p3tB
- binding pyridoxal-5'-phosphate: R53 (= R133), K153 (= K230), R157 (≠ Y234), E186 (= E263), S187 (≠ G264), A188 (≠ S265), A189 (≠ T266), S190 (≠ E267), G210 (= G289), I211 (= I290), T212 (= T291), T248 (= T332)
4whxA X-ray crystal structure of an amino acid aminotransferase from burkholderia pseudomallei bound to the co-factor pyridoxal phosphate
30% identity, 67% coverage: 100:354/383 of query aligns to 23:279/306 of 4whxA
4cmfA The (r)-selective transaminase from nectria haematococca with inhibitor bound (see paper)
29% identity, 67% coverage: 100:354/383 of query aligns to 44:296/322 of 4cmfA
- active site: Y58 (≠ F114), V60 (= V116), K179 (= K230), E212 (= E263), L234 (= L287)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: V60 (= V116), R77 (= R133), F113 (≠ L169), K179 (= K230), E212 (= E263), G215 (≠ T266), F216 (≠ E267), N217 (= N268), L234 (= L287), G236 (= G289), I237 (= I290), T238 (= T291), T273 (≠ G331), T274 (= T332), A275 (≠ S333)
4cmdA The (r)-selective transaminase from nectria haematococca (see paper)
29% identity, 67% coverage: 100:354/383 of query aligns to 44:296/322 of 4cmdA
- active site: Y58 (≠ F114), V60 (= V116), K179 (= K230), E212 (= E263), L234 (= L287)
- binding pyridoxal-5'-phosphate: R77 (= R133), K179 (= K230), E212 (= E263), G215 (≠ T266), F216 (≠ E267), L234 (= L287), G236 (= G289), I237 (= I290), T238 (= T291), T274 (= T332)
7dbeB Structure of a novel transaminase
28% identity, 73% coverage: 100:377/383 of query aligns to 55:330/332 of 7dbeB
- binding pyridoxal-5'-phosphate: R88 (= R133), K190 (= K230), E223 (= E263), G226 (≠ T266), F227 (≠ E267), N228 (= N268), L245 (= L287), G247 (= G289), I248 (= I290), T249 (= T291), T285 (= T332)
1iyeA Crystal structure of eschelichia coli branched-chain amino acid aminotransferase (see paper)
27% identity, 68% coverage: 100:361/383 of query aligns to 19:283/304 of 1iyeA
- active site: F33 (= F114), G35 (≠ V116), K156 (≠ I229), A157 (≠ K230), E190 (= E263), L214 (= L287)
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: R56 (= R133), Y92 (≠ L169), Y126 (vs. gap), K156 (≠ I229), Y161 (= Y234), E190 (= E263), G193 (≠ T266), E194 (= E267), N195 (= N268), L214 (= L287), G216 (= G289), I217 (= I290), T218 (= T291), G253 (= G331), T254 (= T332), A255 (≠ S333)
1iydA Crystal structure of eschelichia coli branched-chain amino acid aminotransferase (see paper)
27% identity, 68% coverage: 100:361/383 of query aligns to 19:283/304 of 1iydA
- active site: F33 (= F114), G35 (≠ V116), K156 (≠ I229), A157 (≠ K230), E190 (= E263), L214 (= L287)
- binding glutaric acid: Y92 (≠ L169), Y126 (vs. gap), A255 (≠ S333)
- binding pyridoxal-5'-phosphate: R56 (= R133), K156 (≠ I229), Y161 (= Y234), E190 (= E263), G193 (≠ T266), E194 (= E267), L214 (= L287), G216 (= G289), I217 (= I290), T218 (= T291), T254 (= T332)
1i1mA Crystal structure of escherichia coli branched-chain amino acid aminotransferase. (see paper)
27% identity, 68% coverage: 100:361/383 of query aligns to 19:283/304 of 1i1mA
- active site: K156 (≠ I229)
- binding 4-methyl valeric acid: Y92 (≠ L169), K156 (≠ I229), T254 (= T332), A255 (≠ S333)
- binding pyridoxal-5'-phosphate: R56 (= R133), K156 (≠ I229), Y161 (= Y234), E190 (= E263), G193 (≠ T266), E194 (= E267), L214 (= L287), G216 (= G289), I217 (= I290), T218 (= T291), G253 (= G331), T254 (= T332)
1i1lA Crystal structure of eschelichia coli branched-chain amino acid aminotransferase. (see paper)
27% identity, 68% coverage: 100:361/383 of query aligns to 19:283/304 of 1i1lA
- active site: K156 (≠ I229)
- binding 2-methylleucine: Y92 (≠ L169), K156 (≠ I229), T254 (= T332), A255 (≠ S333)
- binding pyridoxal-5'-phosphate: R56 (= R133), K156 (≠ I229), Y161 (= Y234), E190 (= E263), G193 (≠ T266), G216 (= G289), I217 (= I290), T218 (= T291), T254 (= T332)
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, 73% coverage: 83:361/383 of query aligns to 1:271/283 of P19938
- M1 (= M83) modified: Initiator methionine, Removed
- Y32 (≠ F114) binding
- R51 (= R133) binding
- R99 (≠ T182) binding
- H101 (≠ N184) binding
- K146 (= K230) active site, Proton acceptor; modified: N6-(pyridoxal phosphate)lysine
- E178 (= E263) binding ; mutation to K: Loss of transaminase activity and small gain in racemase activity.
- L202 (= L287) mutation to A: Inactivates enzyme.
Query Sequence
>WP_084516686.1 NCBI__GCF_000422285.1:WP_084516686.1
MVVFGYNGVKHLSRLIRIKPFPYRPFEWQASNLIQRSGGRDLYTVDHGVFPSSMMKLPEI
TRTDFFDRISAREKPWQHNYLTMYSTQWGGFTTDPDLMLIPVDDHLVHRGDGVFDVMRCV
DGKIYQMEEHLKRLNRSARAISLSPPEVYADIRDLIRFLVRKGGQRDCLIRLMVSRGPGS
FTANPFDCPESQLYVNVIRFKGLPEAHYREGISIITSRIPIKKSFFATIKSCDYLPNVLM
KMEAVEAGCGYSVGLDEKGFLAEGSTENLGIVTAEGILKFPGLDTTLSGITEQRVFELAR
QLVQEGHLKDAVFGEIPPEEAYQAREVFLTGTSLDILPVVRFDGRTIGDGTPGPGYARLH
RLLRQDMRNNERLLTPVIWEDAQ
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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