SitesBLAST
Comparing PfGW456L13_3544 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3544 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)
6jifB Crystal structures of branched-chain aminotransferase from pseudomonas sp. Uw4 (see paper)
96% identity, 99% coverage: 6:339/339 of query aligns to 1:334/334 of 6jifB
- binding pyridoxal-5'-phosphate: R77 (= R82), R169 (= R174), K179 (= K184), Y184 (= Y189), E215 (= E220), S218 (= S223), A219 (= A224), N220 (= N225), L239 (= L244), G241 (= G246), I242 (= I247), T243 (= T248), G279 (= G284), T280 (= T285)
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)
74% identity, 99% coverage: 6:339/339 of query aligns to 1:335/335 of 3uzoA
- active site: K179 (= K184)
- binding glutamic acid: Y48 (= Y53), F53 (= F58), R122 (= R127), V134 (= V139), Y152 (= Y157), T281 (= T285), A282 (= A286)
- binding pyridoxal-5'-phosphate: R77 (= R82), K179 (= K184), Y184 (= Y189), E215 (= E220), G217 (= G222), A218 (≠ S223), A219 (= A224), N220 (= N225), L240 (= L244), S242 (≠ G246), I243 (= I247), T244 (= T248), G280 (= G284), T281 (= T285)
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)
74% identity, 99% coverage: 6:339/339 of query aligns to 1:335/335 of 3uzbA
- active site: K179 (= K184)
- binding 2-oxo-4-methylpentanoic acid: Y120 (= Y125), K179 (= K184), T281 (= T285), A282 (= A286)
- binding pyridoxal-5'-phosphate: R77 (= R82), K179 (= K184), Y184 (= Y189), E215 (= E220), G217 (= G222), A218 (≠ S223), A219 (= A224), N220 (= N225), S242 (≠ G246), I243 (= I247), T244 (= T248), G280 (= G284), T281 (= T285)
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)
74% identity, 99% coverage: 6:339/339 of query aligns to 3:337/337 of 3uyyB
- active site: K181 (= K184)
- binding pyridoxal-5'-phosphate: R79 (= R82), R171 (= R174), K181 (= K184), Y186 (= Y189), E217 (= E220), G219 (= G222), A220 (≠ S223), A221 (= A224), S244 (≠ G246), I245 (= I247), T246 (= T248), G282 (= G284), T283 (= T285)
3dtgA Structural analysis of mycobacterial branched chain aminotransferase- implications for inhibitor design
39% identity, 97% coverage: 12:339/339 of query aligns to 25:362/363 of 3dtgA
- active site: K199 (= K184)
- binding O-benzylhydroxylamine: F72 (= F58), Y171 (= Y157), Y204 (= Y189)
- binding pyridoxal-5'-phosphate: R96 (= R82), R189 (= R174), K199 (= K184), Y204 (= Y189), E235 (= E220), G238 (≠ S223), L263 (= L244), I266 (= I247), T267 (= T248), T309 (= T285)
3dtfA Structural analysis of mycobacterial branched chain aminotransferase- implications for inhibitor design (see paper)
39% identity, 97% coverage: 12:339/339 of query aligns to 25:362/363 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)
39% identity, 97% coverage: 12:339/339 of query aligns to 30:367/368 of A0R066
- R101 (= R82) binding
- Y209 (= Y189) binding
- K299 (vs. gap) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
- T314 (= T285) binding
3ht5A Crystal structure of ilve a branched chain amino acid transaminase from mycobacterium tuberculosis (see paper)
38% identity, 94% coverage: 23:339/339 of query aligns to 9:334/335 of 3ht5A
- active site: K171 (= K184)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: R68 (= R82), K171 (= K184), Y176 (= Y189), E207 (= E220), G210 (≠ S223), M211 (≠ A224), N212 (= N225), L235 (= L244), G237 (= G246), I238 (= I247), T239 (= T248), T281 (= T285)
5u3fA Structure of mycobacterium tuberculosis ilve, a branched-chain amino acid transaminase, in complex with d-cycloserine derivative (see paper)
35% identity, 94% coverage: 23:339/339 of query aligns to 8:325/326 of 5u3fA
- active site: K162 (= K184)
- 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 (= G60), R67 (= R82), Y110 (= Y125), K162 (= K184), Y167 (= Y189), E198 (= E220), G201 (≠ S223), M202 (≠ A224), N203 (= N225), L226 (= L244), G228 (= G246), I229 (= I247), T230 (= T248), T272 (= T285)
2hdkB Crystal structure of cys315ala-cys318ala mutant of human mitochondrial branched chain aminotransferase (see paper)
32% identity, 94% coverage: 9:327/339 of query aligns to 24:353/363 of 2hdkB
- active site: K200 (= K184)
- binding 2-oxo-4-methylpentanoic acid: G310 (= G284), T311 (= T285), A312 (= A286)
- binding pyridoxal-5'-phosphate: R97 (= R82), K200 (= K184), Y205 (= Y189), E235 (= E220), T238 (≠ S223), L264 (= L244), G266 (= G246), V267 (≠ I247), V268 (≠ T248), G310 (= G284), T311 (= T285)
5i5sA X-ray crystal structure at 2.06a resolution of human mitochondrial branched chain aminotransferase (bcatm) complexed with a benzisoxazole compound and an internal aldimine linked plp cofactor. (see paper)
32% identity, 94% coverage: 9:327/339 of query aligns to 22:351/361 of 5i5sA
- active site: K198 (= K184)
- binding 2-(1,2-benzoxazol-3-yl)ethanoic acid: F26 (= F13), F71 (= F58), K198 (= K184), T236 (≠ S223), T309 (= T285), A310 (= A286)
- binding pyridoxal-5'-phosphate: R95 (= R82), R188 (= R174), K198 (= K184), Y203 (= Y189), E233 (= E220), T236 (≠ S223), M237 (≠ A224), N238 (= N225), L262 (= L244), G264 (= G246), V265 (≠ I247), V266 (≠ T248), G308 (= G284), T309 (= T285)
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)
32% identity, 94% coverage: 9:327/339 of query aligns to 24:353/363 of 5i5yA
- active site: K200 (= K184)
- binding {2-[(5-methyl-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-6-carbonyl)amino]phenyl}acetic acid: F28 (= F13), Y68 (= Y53), F73 (= F58), K77 (= K62), Y139 (= Y125), V153 (= V139), Y171 (= Y157), T238 (≠ S223), T311 (= T285), A312 (= A286)
- binding pyridoxal-5'-phosphate: R97 (= R82), R190 (= R174), K200 (= K184), Y205 (= Y189), E235 (= E220), T238 (≠ S223), L264 (= L244), G266 (= G246), V267 (≠ I247), V268 (≠ T248), T311 (= T285)
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)
32% identity, 94% coverage: 9:327/339 of query aligns to 24:353/363 of 5i5uA
- active site: K200 (= K184)
- binding 2-hydroxy-N-[(1R)-1,2,3,4-tetrahydronaphthalen-1-yl]acetamide: F28 (= F13), Y68 (= Y53), F73 (= F58), V153 (= V139), K200 (= K184), Y205 (= Y189), T238 (≠ S223), G310 (= G284), T311 (= T285), A312 (= A286)
- binding pyridoxal-5'-phosphate: R97 (= R82), R190 (= R174), K200 (= K184), Y205 (= Y189), E235 (= E220), T238 (≠ S223), M239 (≠ A224), L264 (= L244), G266 (= G246), V267 (≠ I247), V268 (≠ T248), G310 (= G284), T311 (= T285)
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)
32% identity, 94% coverage: 9:327/339 of query aligns to 53:382/392 of O15382
- Y168 (= Y125) binding
- R170 (= R127) to Q: in HVLI; reduced catalytic activity; dbSNP:rs749866079
- T186 (≠ P143) to R: in dbSNP:rs11548193
- K229 (= K184) modified: N6-(pyridoxal phosphate)lysine
- E264 (= E220) to K: in HVLI; reduced catalytic activity; dbSNP:rs767653663
- C342 (≠ A287) mutation to A: Reduces activity about 6-fold.
- C345 (≠ T290) mutation to A: Slight reduction of activity.
1ktaA Human branched chain amino acid aminotransferase : three dimensional structure of the enzyme in its pyridoxamine phosphate form. (see paper)
32% identity, 94% coverage: 9:327/339 of query aligns to 26:355/365 of 1ktaA
- binding 3-methyl-2-oxobutanoic acid: F75 (= F58), K202 (= K184), Y207 (= Y189)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: R99 (= R82), R192 (= R174), K202 (= K184), Y207 (= Y189), E237 (= E220), T240 (≠ S223), M241 (≠ A224), N242 (= N225), L266 (= L244), G268 (= G246), V269 (≠ I247), V270 (≠ T248), G312 (= G284), T313 (= T285)
1ekfA Crystallographic structure of human branched chain amino acid aminotransferase (mitochondrial) complexed with pyridoxal-5'- phosphate at 1.95 angstroms (orthorhombic form) (see paper)
32% identity, 94% coverage: 9:327/339 of query aligns to 26:355/365 of 1ekfA
- active site: K202 (= K184)
- binding pyridoxal-5'-phosphate: R99 (= R82), R192 (= R174), K202 (= K184), Y207 (= Y189), E237 (= E220), T240 (≠ S223), M241 (≠ A224), N242 (= N225), L266 (= L244), G268 (= G246), V269 (≠ I247), V270 (≠ T248), T313 (= T285)
5cr5A X-ray crystal structure at 1.61a resolution of human mitochondrial branched chain aminotransferase (bcatm) complexed with a biphenyl pyrrolidine ether compound and an internal aldimine linked plp cofactor. (see paper)
32% identity, 94% coverage: 11:327/339 of query aligns to 21:348/358 of 5cr5A
- active site: K195 (= K184)
- binding 3-({(3R)-1-[(5-bromothiophen-2-yl)carbonyl]pyrrolidin-3-yl}oxy)-N-methyl-2'-[(methylsulfonyl)amino]biphenyl-4-carboxamide: F23 (= F13), F68 (= F58), Y166 (= Y157), V175 (≠ H165), Q217 (≠ D206), V231 (= V221), G232 (= G222), T233 (≠ S223), M234 (≠ A224), G305 (= G284), A307 (= A286), C311 (≠ T290)
- binding pyridoxal-5'-phosphate: R92 (= R82), K195 (= K184), Y200 (= Y189), E230 (= E220), T233 (≠ S223), N235 (= N225), L259 (= L244), G261 (= G246), V262 (≠ I247), V263 (≠ T248), T306 (= T285)
2a1hA X-ray crystal structure of human mitochondrial branched chain aminotransferase (bcatm) complexed with gabapentin (see paper)
32% identity, 94% coverage: 9:327/339 of query aligns to 24:353/363 of 2a1hA
- active site: K200 (= K184)
- binding [1-(aminomethyl)cyclohexyl]acetic acid: Y68 (= Y53), R141 (= R127), V153 (= V139), T238 (≠ S223), G310 (= G284), T311 (= T285), A312 (= A286)
- binding pyridoxal-5'-phosphate: R97 (= R82), R190 (= R174), K200 (= K184), Y205 (= Y189), E235 (= E220), T238 (≠ S223), M239 (≠ A224), N240 (= N225), L264 (= L244), G266 (= G246), V267 (≠ I247), V268 (≠ T248), T311 (= T285)
7nwmA Crystal structure of human cytosolic branched-chain aminotransferase (bcat1) in complex with plp and inhibitor compound 12 (see paper)
32% identity, 88% coverage: 31:330/339 of query aligns to 47:357/365 of 7nwmA
- binding pyridoxal-5'-phosphate: R98 (= R82), R191 (= R174), K201 (= K184), Y206 (= Y189), E236 (= E220), T239 (≠ S223), M240 (≠ A224), L265 (= L244), G267 (= G246), V268 (≠ I247), T269 (= T248), G311 (= G284), T312 (= T285)
- binding 4-[2,4-bis(oxidanylidene)-6-(trifluoromethyl)-1H-pyrimidin-3-yl]-5-methoxy-2-(2-methylphenoxy)benzenecarbonitrile: Y69 (= Y53), F74 (= F58), Y140 (= Y125), G153 (= G138), V154 (= V139), Y172 (= Y157), Q213 (≠ G196), Q223 (≠ D206), T239 (≠ S223), A313 (= A286)
Sites not aligning to the query:
7nweA Crystal structure of human cytosolic branched-chain aminotransferase (bcat1) in complex with plp and inhibitor compound 10 (see paper)
32% identity, 88% coverage: 31:330/339 of query aligns to 47:357/365 of 7nweA
- binding pyridoxal-5'-phosphate: R98 (= R82), K201 (= K184), Y206 (= Y189), E236 (= E220), T239 (≠ S223), M240 (≠ A224), L265 (= L244), G267 (= G246), V268 (≠ I247), T269 (= T248), G311 (= G284), T312 (= T285)
- binding 4-[2,4-bis(oxidanylidene)-6-(trifluoromethyl)-1H-pyrimidin-3-yl]-5-methyl-2-(2-methylphenoxy)benzenecarbonitrile: Y69 (= Y53), F74 (= F58), Y140 (= Y125), G153 (= G138), V154 (= V139), Y172 (= Y157), Q213 (≠ G196), Q223 (≠ D206), T239 (≠ S223), A313 (= A286)
Sites not aligning to the query:
Query Sequence
>PfGW456L13_3544 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3544
MGNESINWDKLGFDYIKTDKRYLSYFRNGEWDKGTLTEDNVLHISEGSTALHYGQQCFEG
MKAYRCKDGSINLFRPDQNALRMQRSCARLLMPQVETEQFIEACKEVVRANERFIPPYGT
GGALYLRPFVIGVGDNIGVRTAPEFIFSIFCIPVGAYFKGGLTPHNFLISSYDRAAPQGT
GAAKVGGNYAASLMPGSQAKKAHFADCIYLDPLTHTKIEEVGSANFFGITHDNKFVTPNS
PSVLPGITRLSLIELARSRLGLDVVEGDVFIDKLADFKEAGACGTAAVITPIGGINYNDH
LHVFHSETEVGPITQKLYKELTGVQTGDIEAPAGWIVKV
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