SitesBLAST
Comparing WP_245566311.1 NCBI__GCF_000483485.1:WP_245566311.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
5mr0D Thermophilic archaeal branched-chain amino acid transaminases from geoglobus acetivorans and archaeoglobus fulgidus: biochemical and structural characterisation (see paper)
35% identity, 92% coverage: 13:285/296 of query aligns to 4:278/290 of 5mr0D
- active site: F32 (≠ Y41), G34 (≠ V43), K150 (= K156), E183 (= E189), L206 (= L213)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: R51 (= R60), G100 (≠ Q108), L101 (≠ R109), K150 (= K156), Y154 (≠ L160), E183 (= E189), G186 (≠ A192), D187 (≠ S193), L206 (= L213), I209 (≠ V216), T210 (= T217), G245 (≠ S252), T246 (≠ S253)
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)
39% identity, 91% coverage: 16:285/296 of query aligns to 7:274/283 of P19938
- Y32 (= Y41) binding substrate
- R51 (= R60) binding pyridoxal 5'-phosphate
- R99 (≠ Q108) binding substrate
- H101 (≠ D110) binding substrate
- K146 (= K156) active site, Proton acceptor; modified: N6-(pyridoxal phosphate)lysine
- E178 (= E189) binding pyridoxal 5'-phosphate; mutation to K: Loss of transaminase activity and small gain in racemase activity.
- L202 (= L213) 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)
39% identity, 91% coverage: 16:285/296 of query aligns to 6:273/277 of 3daaA
- active site: Y31 (= Y41), V33 (= V43), K145 (= K156), E177 (= E189), L201 (= L213)
- binding n-(5'-phosphopyridoxyl)-d-alanine: Y31 (= Y41), R50 (= R60), K145 (= K156), E177 (= E189), S180 (≠ A192), S181 (= S193), L201 (= L213), G203 (= G215), I204 (≠ V216), T205 (= T217), S240 (= S252), T241 (≠ S253)
2daaA Crystallographic structure of d-amino acid aminotransferase inactivated by d-cycloserine
39% identity, 91% coverage: 16:285/296 of query aligns to 6:273/277 of 2daaA
- active site: Y31 (= Y41), V33 (= V43), K145 (= K156), E177 (= E189), L201 (= L213)
- binding d-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-n,o-cycloserylamide: Y31 (= Y41), V33 (= V43), R50 (= R60), R98 (≠ Q108), H100 (≠ D110), K145 (= K156), E177 (= E189), S180 (≠ A192), S181 (= S193), N182 (= N194), L201 (= L213), G203 (= G215), I204 (≠ V216), T205 (= T217), T241 (≠ S253)
1daaA Crystallographic structure of d-amino acid aminotransferase complexed with pyridoxal-5'-phosphate (see paper)
39% identity, 91% coverage: 16:285/296 of query aligns to 6:273/277 of 1daaA
- active site: Y31 (= Y41), V33 (= V43), K145 (= K156), E177 (= E189), L201 (= L213)
- binding pyridoxal-5'-phosphate: R50 (= R60), K145 (= K156), E177 (= E189), S180 (≠ A192), S181 (= S193), L201 (= L213), G203 (= G215), I204 (≠ V216), T205 (= T217), S240 (= S252), T241 (≠ S253)
3lqsA Complex structure of d-amino acid aminotransferase and 4-amino-4,5- dihydro-thiophenecarboxylic acid (adta) (see paper)
39% identity, 91% coverage: 16:285/296 of query aligns to 6:273/280 of 3lqsA
- active site: Y31 (= Y41), V33 (= V43), K145 (= K156), E177 (= E189), L201 (= L213)
- binding 4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]thiophene-2-carboxylic acid: V33 (= V43), R50 (= R60), E177 (= E189), S180 (≠ A192), S181 (= S193), N182 (= N194), L201 (= L213), G203 (= G215), I204 (≠ V216), T205 (= T217), S240 (= S252), T241 (≠ S253), T242 (= T254)
1a0gB L201a mutant of d-amino acid aminotransferase complexed with pyridoxamine-5'-phosphate (see paper)
39% identity, 91% coverage: 16:285/296 of query aligns to 6:273/282 of 1a0gB
- active site: Y31 (= Y41), V33 (= V43), K145 (= K156), E177 (= E189), A201 (≠ L213)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: R50 (= R60), K145 (= K156), E177 (= E189), S180 (≠ A192), S181 (= S193), G203 (= G215), I204 (≠ V216), T205 (= T217), S240 (= S252), T241 (≠ S253)
5e25A Crystal structure of branched-chain aminotransferase from thermophilic archaea geoglobus acetivorans complexed with alpha-ketoglutarate (see paper)
34% identity, 94% coverage: 10:286/296 of query aligns to 2:280/290 of 5e25A
- active site: F33 (≠ Y41), G35 (≠ V43), K151 (= K156), E184 (= E189), L207 (= L213)
- binding 2-oxoglutaric acid: Y88 (≠ F96), K151 (= K156), T247 (≠ S253), A248 (≠ T254)
- binding pyridoxal-5'-phosphate: R52 (= R60), K151 (= K156), Y155 (≠ L160), E184 (= E189), G187 (≠ A192), D188 (≠ S193), L207 (= L213), G209 (= G215), I210 (≠ V216), T211 (= T217), G246 (≠ S252), T247 (≠ S253)
7p3tB Transaminase of gamma-proteobacterium (see paper)
32% identity, 93% coverage: 10:284/296 of query aligns to 3:279/299 of 7p3tB
- binding pyridoxal-5'-phosphate: R53 (= R60), K153 (= K156), R157 (≠ L160), E186 (= E189), S187 (≠ G190), A188 (≠ S191), A189 (= A192), S190 (= S193), G210 (= G215), I211 (≠ V216), T212 (= T217), T248 (≠ S253)
6xu3B (R)-selective amine transaminase from shinella sp. (see paper)
30% identity, 98% coverage: 1:290/296 of query aligns to 17:309/321 of 6xu3B
- active site: Y57 (= Y41), K177 (≠ P162), E210 (= E189), L232 (= L213)
- binding 3-aminobenzoic acid: P169 (≠ T155), D173 (≠ T159), K229 (≠ Q210)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: R76 (= R60), Y112 (≠ F96), K177 (≠ P162), F184 (vs. gap), E210 (= E189), G213 (≠ A192), F214 (≠ S193), N215 (= N194), L232 (= L213), G234 (= G215), V235 (= V216), T236 (= T217), T272 (≠ S253)
6xu3A (R)-selective amine transaminase from shinella sp. (see paper)
30% identity, 98% coverage: 1:290/296 of query aligns to 16:308/320 of 6xu3A
- active site: Y56 (= Y41), K176 (≠ P162), E209 (= E189), L231 (= L213)
- binding pyridoxal-5'-phosphate: R75 (= R60), K176 (≠ P162), F183 (vs. gap), E209 (= E189), G212 (≠ A192), F213 (≠ S193), L231 (= L213), G233 (= G215), V234 (= V216), T235 (= T217), T271 (≠ S253)
6xu3C (R)-selective amine transaminase from shinella sp. (see paper)
30% identity, 98% coverage: 1:290/296 of query aligns to 18:310/322 of 6xu3C
- active site: Y58 (= Y41), K178 (≠ P162), E211 (= E189), L233 (= L213)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: V60 (= V43), R77 (= R60), K178 (≠ P162), F185 (vs. gap), E211 (= E189), G214 (≠ A192), N216 (= N194), L233 (= L213), G235 (= G215), V236 (= V216), T237 (= T217), T272 (≠ S252), T273 (≠ S253), A274 (≠ T254)
7dbeB Structure of a novel transaminase
29% identity, 94% coverage: 6:284/296 of query aligns to 34:316/332 of 7dbeB
- binding pyridoxal-5'-phosphate: R88 (= R60), K190 (= K156), E223 (= E189), G226 (≠ A192), F227 (≠ S193), N228 (= N194), L245 (= L213), G247 (= G215), I248 (≠ V216), T249 (= T217), T285 (≠ S253)
8ivpB Crystal structure of mv in complex with llp and fru from mycobacterium vanbaalenii
31% identity, 94% coverage: 6:284/296 of query aligns to 24:306/322 of 8ivpB
6snlD (R)-selective amine transaminase from exophiala sideris (see paper)
28% identity, 96% coverage: 1:284/296 of query aligns to 17:304/320 of 6snlD
- active site: Y57 (= Y41), K178 (≠ I158), E211 (= E189), L233 (= L213)
- binding pyridoxal-5'-phosphate: R76 (= R60), K178 (≠ I158), E211 (= E189), G214 (≠ A192), F215 (≠ S193), L233 (= L213), G235 (= G215), V236 (= V216), T237 (= T217), T273 (≠ S253)
4cmfA The (r)-selective transaminase from nectria haematococca with inhibitor bound (see paper)
27% identity, 96% coverage: 1:284/296 of query aligns to 18:305/322 of 4cmfA
- active site: Y58 (= Y41), V60 (= V43), K179 (≠ I158), E212 (= E189), L234 (= L213)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: V60 (= V43), R77 (= R60), F113 (= F96), K179 (≠ I158), E212 (= E189), G215 (≠ A192), F216 (≠ S193), N217 (= N194), L234 (= L213), G236 (= G215), I237 (≠ V216), T238 (= T217), T273 (≠ S252), T274 (≠ S253), A275 (≠ T254)
4cmdA The (r)-selective transaminase from nectria haematococca (see paper)
27% identity, 96% coverage: 1:284/296 of query aligns to 18:305/322 of 4cmdA
- active site: Y58 (= Y41), V60 (= V43), K179 (≠ I158), E212 (= E189), L234 (= L213)
- binding pyridoxal-5'-phosphate: R77 (= R60), K179 (≠ I158), E212 (= E189), G215 (≠ A192), F216 (≠ S193), L234 (= L213), G236 (= G215), I237 (≠ V216), T238 (= T217), T274 (≠ S253)
6xwbA Crystal structure of an r-selective transaminase from thermomyces stellatus. (see paper)
27% identity, 96% coverage: 1:284/296 of query aligns to 18:304/319 of 6xwbA
- binding pyridoxal-5'-phosphate: R77 (= R60), K178 (= K156), F185 (≠ N163), E211 (= E189), G214 (≠ A192), F215 (≠ S193), N216 (= N194), L233 (= L213), G235 (= G215), V236 (= V216), T237 (= T217), T273 (≠ S253)
8onjA Crystal structure of d-amino acid aminotransferase from aminobacterium colombiense point mutant r88l (see paper)
29% identity, 93% coverage: 11:284/296 of query aligns to 4:268/277 of 8onjA
- binding pyridoxal-5'-phosphate: R53 (= R60), R138 (= R149), K144 (= K156), E174 (= E189), H177 (≠ A192), S178 (= S193), L197 (= L213), T200 (≠ V216), T201 (= T217), G236 (≠ S252), T237 (≠ S253)
8aieB Crystal structure of d-amino acid aminotransferase from aminobacterium colombiense complexed with d-cycloserine
29% identity, 93% coverage: 11:284/296 of query aligns to 2:266/275 of 8aieB
- binding 3-azanyloxy-2-[(~{E})-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]propanoic acid: T34 (≠ V43), R51 (= R60), K142 (= K156), Y146 (≠ V164), E172 (= E189), H175 (≠ A192), S176 (= S193), T198 (≠ V216), T199 (= T217), G234 (≠ S252), T235 (≠ S253), V236 (≠ T254), K237 (= K255)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: R51 (= R60), Y146 (≠ V164), E172 (= E189), S174 (= S191), H175 (≠ A192), S176 (= S193), L195 (= L213), T198 (≠ V216), T199 (= T217), G234 (≠ S252), T235 (≠ S253)
Query Sequence
>WP_245566311.1 NCBI__GCF_000483485.1:WP_245566311.1
MSQNESPVMQQIVYLNGEYLPMADSKISTQDRGFLFGDGIYEVIPVYQRKLFAWPEHLQR
LKNSLQAVSIPNPLTDEEWLDLLTGLVKKHPWENQFIYLQVTRGIQMQRDHMPADCLHPT
IYAYTNPLKPLDAKILSHGIKVVSLEDIRWLRCDTKAITLLPNVMMKLAAKQQGADDAIL
ISRDGKVTEGSASNVVIVKEGKLLTPPNSQHILPGVTRLVIEKVANQHHIPFIERELSLA
DLQTADEIWLTSSTKEAVPVTQLDGKEVGDGRPGPVWQKLHQHYQDYKAEFIAQYT
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