SitesBLAST
Comparing 6939205 FitnessBrowser__SB2B:6939205 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)
3ht5A Crystal structure of ilve a branched chain amino acid transaminase from mycobacterium tuberculosis (see paper)
41% identity, 91% coverage: 31:357/361 of query aligns to 3:334/335 of 3ht5A
- active site: K171 (= K197)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: R68 (= R95), K171 (= K197), Y176 (= Y202), E207 (= E232), G210 (≠ A235), M211 (= M236), N212 (= N237), L235 (= L257), G237 (≠ S259), I238 (= I260), T239 (= T261), T281 (= T303)
3dtgA Structural analysis of mycobacterial branched chain aminotransferase- implications for inhibitor design
40% identity, 98% coverage: 3:357/361 of query aligns to 5:362/363 of 3dtgA
- active site: K199 (= K197)
- binding O-benzylhydroxylamine: F72 (= F71), Y171 (= Y169), Y204 (= Y202)
- binding pyridoxal-5'-phosphate: R96 (= R95), R189 (= R187), K199 (= K197), Y204 (= Y202), E235 (= E232), G238 (≠ A235), L263 (= L257), I266 (= I260), T267 (= T261), T309 (= T303)
3dtfA Structural analysis of mycobacterial branched chain aminotransferase- implications for inhibitor design (see paper)
40% identity, 98% coverage: 3:357/361 of query aligns to 5:362/363 of 3dtfA
A0R066 Branched-chain-amino-acid aminotransferase; BCAT; EC 2.6.1.42 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see 2 papers)
40% identity, 98% coverage: 3:357/361 of query aligns to 10:367/368 of A0R066
- R101 (= R95) binding
- Y209 (= Y202) binding
- K299 (≠ A288) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- T314 (= T303) binding
5u3fA Structure of mycobacterium tuberculosis ilve, a branched-chain amino acid transaminase, in complex with d-cycloserine derivative (see paper)
41% identity, 91% coverage: 31:357/361 of query aligns to 2:325/326 of 5u3fA
- active site: K162 (= K197)
- binding (5-hydroxy-6-methyl-4-{[(3-oxo-2,3-dihydro-1,2-oxazol-4-yl)amino]methyl}pyridin-3-yl)methyl dihydrogen phosphate: G45 (= G73), R67 (= R95), Y110 (= Y137), K162 (= K197), Y167 (= Y202), E198 (= E232), G201 (≠ A235), M202 (= M236), N203 (= N237), L226 (= L257), G228 (≠ S259), I229 (= I260), T230 (= T261), T272 (= T303)
3uyyB Crystal structures of branched-chain aminotransferase from deinococcus radiodurans complexes with alpha-ketoisocaproate and l-glutamate suggest its radio-resistance for catalysis (see paper)
36% identity, 93% coverage: 24:357/361 of query aligns to 8:337/337 of 3uyyB
- active site: K181 (= K197)
- binding pyridoxal-5'-phosphate: R79 (= R95), R171 (= R187), K181 (= K197), Y186 (= Y202), E217 (= E232), G219 (= G234), A220 (= A235), A221 (≠ M236), S244 (= S259), I245 (= I260), T246 (= T261), G282 (= G302), T283 (= T303)
3uzoA Crystal structures of branched-chain aminotransferase from deinococcus radiodurans complexes with alpha-ketoisocaproate and l-glutamate suggest its radio-resistance for catalysis (see paper)
36% identity, 93% coverage: 24:357/361 of query aligns to 6:335/335 of 3uzoA
- active site: K179 (= K197)
- binding glutamic acid: Y48 (= Y66), F53 (= F71), R122 (= R139), V134 (= V151), Y152 (= Y169), T281 (= T303), A282 (= A304)
- binding pyridoxal-5'-phosphate: R77 (= R95), K179 (= K197), Y184 (= Y202), E215 (= E232), G217 (= G234), A218 (= A235), A219 (≠ M236), N220 (= N237), L240 (= L257), S242 (= S259), I243 (= I260), T244 (= T261), G280 (= G302), T281 (= T303)
3uzbA Crystal structures of branched-chain aminotransferase from deinococcus radiodurans complexes with alpha-ketoisocaproate and l-glutamate suggest its radio-resistance for catalysis (see paper)
36% identity, 93% coverage: 24:357/361 of query aligns to 6:335/335 of 3uzbA
- active site: K179 (= K197)
- binding 2-oxo-4-methylpentanoic acid: Y120 (= Y137), K179 (= K197), T281 (= T303), A282 (= A304)
- binding pyridoxal-5'-phosphate: R77 (= R95), K179 (= K197), Y184 (= Y202), E215 (= E232), G217 (= G234), A218 (= A235), A219 (≠ M236), N220 (= N237), S242 (= S259), I243 (= I260), T244 (= T261), G280 (= G302), T281 (= T303)
2hdkB Crystal structure of cys315ala-cys318ala mutant of human mitochondrial branched chain aminotransferase (see paper)
34% identity, 96% coverage: 2:347/361 of query aligns to 7:355/363 of 2hdkB
- active site: K200 (= K197)
- binding 2-oxo-4-methylpentanoic acid: G310 (= G302), T311 (= T303), A312 (= A304)
- binding pyridoxal-5'-phosphate: R97 (= R95), K200 (= K197), Y205 (= Y202), E235 (= E232), T238 (≠ A235), L264 (= L257), G266 (≠ S259), V267 (≠ I260), V268 (≠ T261), G310 (= G302), T311 (= T303)
5i5xA X-ray crystal structure at 1.65a resolution of human mitochondrial branched chain aminotransferase (bcatm) complexed with a thiazole compound and pmp cofactor. (see paper)
34% identity, 93% coverage: 12:347/361 of query aligns to 11:350/358 of 5i5xA
- active site: K195 (= K197)
- binding 5-methyl-4-oxo-N-(1,3,4-thiadiazol-2-yl)-3,4-dihydrothieno[2,3-d]pyrimidine-6-carboxamide: F25 (= F26), F70 (= F71), K74 (= K75), Y136 (= Y137), V165 (≠ S166), Y168 (= Y169), A307 (= A304)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: R94 (= R95), R185 (= R187), K195 (= K197), Y200 (= Y202), E230 (= E232), T233 (≠ A235), M234 (= M236), N235 (= N237), L259 (= L257), G261 (≠ S259), V262 (≠ I260), V263 (≠ T261), T306 (= T303)
5i5vA X-ray crystal structure at 1.94a resolution of human mitochondrial branched chain aminotransferase (bcatm) complexed with a thienopyrimidine compound and an internal aldimine linked plp cofactor. (see paper)
34% identity, 93% coverage: 12:347/361 of query aligns to 11:352/360 of 5i5vA
- active site: K197 (= K197)
- binding 3,5-dimethyl-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-6-carboxylic acid: F25 (= F26), K74 (= K75), Y136 (= Y137), Y168 (= Y169), A309 (= A304)
- binding pyridoxal-5'-phosphate: R94 (= R95), R187 (= R187), K197 (= K197), Y202 (= Y202), E232 (= E232), T235 (≠ A235), M236 (= M236), L261 (= L257), G263 (≠ S259), V264 (≠ I260), V265 (≠ T261), G307 (= G302), T308 (= T303)
O15382 Branched-chain-amino-acid aminotransferase, mitochondrial; BCAT(m); Placental protein 18; PP18; EC 2.6.1.42 from Homo sapiens (Human) (see 6 papers)
33% identity, 96% coverage: 2:347/361 of query aligns to 36:384/392 of O15382
- Y168 (= Y137) binding
- R170 (= R139) to Q: in HVLI; reduced catalytic activity; dbSNP:rs749866079
- T186 (≠ N155) to R: in dbSNP:rs11548193
- K229 (= K197) modified: N6-(pyridoxal phosphate)lysine
- E264 (= E232) to K: in HVLI; reduced catalytic activity; dbSNP:rs767653663
- C342 (≠ A305) mutation to A: Reduces activity about 6-fold.
- C345 (≠ S308) mutation to A: Slight reduction of activity.
6jifB Crystal structures of branched-chain aminotransferase from pseudomonas sp. Uw4 (see paper)
36% identity, 93% coverage: 24:357/361 of query aligns to 6:334/334 of 6jifB
- binding pyridoxal-5'-phosphate: R77 (= R95), R169 (= R187), K179 (= K197), Y184 (= Y202), E215 (= E232), S218 (≠ A235), A219 (≠ M236), N220 (= N237), L239 (= L257), G241 (≠ S259), I242 (= I260), T243 (= T261), G279 (= G302), T280 (= T303)
5i5yA X-ray crystal structure at 1.81a resolution of human mitochondrial branched chain aminotransferase (bcatm) complexed with an aryl acetate compound and an internal aldimine linked plp cofactor. (see paper)
33% identity, 96% coverage: 2:347/361 of query aligns to 7:355/363 of 5i5yA
- active site: K200 (= K197)
- binding {2-[(5-methyl-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-6-carbonyl)amino]phenyl}acetic acid: F28 (= F26), Y68 (= Y66), F73 (= F71), K77 (= K75), Y139 (= Y137), V153 (= V151), Y171 (= Y169), T238 (≠ A235), T311 (= T303), A312 (= A304)
- binding pyridoxal-5'-phosphate: R97 (= R95), R190 (= R187), K200 (= K197), Y205 (= Y202), E235 (= E232), T238 (≠ A235), L264 (= L257), G266 (≠ S259), V267 (≠ I260), V268 (≠ T261), T311 (= T303)
5i5uA X-ray crystal structure at 2.40a resolution of human mitochondrial branched chain aminotransferase (bcatm) complexed with a tetrahydronaphthalenyl compound and an internal aldimine linked plp cofactor. (see paper)
33% identity, 96% coverage: 2:347/361 of query aligns to 7:355/363 of 5i5uA
- active site: K200 (= K197)
- binding 2-hydroxy-N-[(1R)-1,2,3,4-tetrahydronaphthalen-1-yl]acetamide: F28 (= F26), Y68 (= Y66), F73 (= F71), V153 (= V151), K200 (= K197), Y205 (= Y202), T238 (≠ A235), G310 (= G302), T311 (= T303), A312 (= A304)
- binding pyridoxal-5'-phosphate: R97 (= R95), R190 (= R187), K200 (= K197), Y205 (= Y202), E235 (= E232), T238 (≠ A235), M239 (= M236), L264 (= L257), G266 (≠ S259), V267 (≠ I260), V268 (≠ T261), G310 (= G302), T311 (= T303)
2a1hA X-ray crystal structure of human mitochondrial branched chain aminotransferase (bcatm) complexed with gabapentin (see paper)
33% identity, 96% coverage: 2:347/361 of query aligns to 7:355/363 of 2a1hA
- active site: K200 (= K197)
- binding [1-(aminomethyl)cyclohexyl]acetic acid: Y68 (= Y66), R141 (= R139), V153 (= V151), T238 (≠ A235), G310 (= G302), T311 (= T303), A312 (= A304)
- binding pyridoxal-5'-phosphate: R97 (= R95), R190 (= R187), K200 (= K197), Y205 (= Y202), E235 (= E232), T238 (≠ A235), M239 (= M236), N240 (= N237), L264 (= L257), G266 (≠ S259), V267 (≠ I260), V268 (≠ T261), T311 (= T303)
1ktaA Human branched chain amino acid aminotransferase : three dimensional structure of the enzyme in its pyridoxamine phosphate form. (see paper)
33% identity, 96% coverage: 2:347/361 of query aligns to 9:357/365 of 1ktaA
- binding 3-methyl-2-oxobutanoic acid: F75 (= F71), K202 (= K197), Y207 (= Y202)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: R99 (= R95), R192 (= R187), K202 (= K197), Y207 (= Y202), E237 (= E232), T240 (≠ A235), M241 (= M236), N242 (= N237), L266 (= L257), G268 (≠ S259), V269 (≠ I260), V270 (≠ T261), G312 (= G302), T313 (= T303)
1ekfA Crystallographic structure of human branched chain amino acid aminotransferase (mitochondrial) complexed with pyridoxal-5'- phosphate at 1.95 angstroms (orthorhombic form) (see paper)
33% identity, 96% coverage: 2:347/361 of query aligns to 9:357/365 of 1ekfA
- active site: K202 (= K197)
- binding pyridoxal-5'-phosphate: R99 (= R95), R192 (= R187), K202 (= K197), Y207 (= Y202), E237 (= E232), T240 (≠ A235), M241 (= M236), N242 (= N237), L266 (= L257), G268 (≠ S259), V269 (≠ I260), V270 (≠ T261), T313 (= T303)
5i5tA X-ray crystal structure at 2.31a resolution of human mitochondrial branched chain aminotransferase (bcatm) complexed with a tetrahydroquinoline compound and an internal aldimine linked plp cofactor. (see paper)
34% identity, 91% coverage: 19:347/361 of query aligns to 19:353/361 of 5i5tA
- active site: K198 (= K197)
- binding (3R)-3-methyl-1,2,3,4-tetrahydroquinoline-8-sulfonamide: F26 (= F26), F71 (= F71), Y169 (= Y169), K198 (= K197), T236 (≠ A235), A310 (= A304)
- binding pyridoxal-5'-phosphate: R95 (= R95), R188 (= R187), K198 (= K197), Y203 (= Y202), E233 (= E232), T236 (≠ A235), M237 (= M236), N238 (= N237), L262 (= L257), G264 (≠ S259), V265 (≠ I260), V266 (≠ T261), G308 (= G302), T309 (= T303)
5bwtA X-ray crystal structure at 2.20a resolution of human mitochondrial branched chain aminotransferase (bcatm) complexed with a pyrazolopyrimidinone fragment and an internal aldimine linked plp. (see paper)
33% identity, 96% coverage: 2:347/361 of query aligns to 7:352/360 of 5bwtA
- active site: K197 (= K197)
- binding 5-ethyl-2-methyl-7-oxo-4,7-dihydropyrazolo[1,5-a]pyrimidine-3-carbonitrile: Y171 (= Y169), T235 (≠ A235), M236 (= M236), A309 (= A304), C310 (≠ A305)
- binding pyridoxal-5'-phosphate: R97 (= R95), K197 (= K197), Y202 (= Y202), E232 (= E232), T235 (≠ A235), M236 (= M236), N237 (= N237), L261 (= L257), G263 (≠ S259), V264 (≠ I260), V265 (≠ T261), G307 (= G302), T308 (= T303)
Query Sequence
>6939205 FitnessBrowser__SB2B:6939205
MDIKYNLKPASERRTEPFEPQGDVGFGKLRTDHMFMMDYKDGQWQNARILPYGPFEMMPG
AMALHYGQSIFEGAKAFMHDDGEIYTFRLDKNAQRLNRSADIVCIPNIPEAVQLEAINAL
IDVDRLWFPRQEGACLYIRPFVFATEDRLSVSPANQYTFCVVLSPSGAYYGKNLNAIRLL
ITTQFHRAVSGGTGASKAAGNYAASLRAGKAAAEHGAAQVLYLDSTNQYIEEVGAMNHFH
IRKDGTLIIPEFTDTILRSITSESILALGEELGCEVRQETVKLSDFIADIEAGEIVEAGG
FGTAAVVSPVGSYIFEDGRIVTVGDGKVGERISHIYKVYTEMQKGLRPAPEGWVRKVERR
S
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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