SitesBLAST
Comparing Echvi_0145 FitnessBrowser__Cola:Echvi_0145 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)
7bxsA 2-amino-3-ketobutyrate coa ligase from cupriavidus necator glycine binding form
65% identity, 99% coverage: 3:397/397 of query aligns to 5:399/399 of 7bxsA
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: N52 (= N50), V81 (= V79), S112 (≠ A110), A113 (= A111), F114 (= F112), N117 (= N115), H138 (= H136), S140 (= S138), D183 (= D181), S187 (= S185), D212 (= D210), C214 (= C212), H215 (= H213), T243 (= T241), F275 (= F273), S276 (= S274), N277 (= N275), R370 (= R368)
7bxrA 2-amino-3-ketobutyrate coa ligase from cupriavidus necator 3- hydroxynorvaline binding form
65% identity, 99% coverage: 3:397/397 of query aligns to 5:399/399 of 7bxrA
- binding (2S,3R)-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]-3-oxidanyl-pentanoic acid: N52 (= N50), F83 (= F81), S112 (≠ A110), A113 (= A111), F114 (= F112), N117 (= N115), H138 (= H136), S140 (= S138), D183 (= D181), S187 (= S185), M188 (= M186), D212 (= D210), C214 (= C212), H215 (= H213), T243 (= T241), L274 (= L272), F275 (= F273), S276 (= S274), N277 (= N275), R370 (= R368)
7bxqA 2-amino-3-ketobutyrate coa ligase from cupriavidus necator l-threonine binding form
65% identity, 99% coverage: 3:397/397 of query aligns to 5:399/399 of 7bxqA
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-allothreonine: N52 (= N50), V81 (= V79), S112 (≠ A110), A113 (= A111), F114 (= F112), N117 (= N115), H138 (= H136), S140 (= S138), D183 (= D181), S187 (= S185), M188 (= M186), D212 (= D210), C214 (= C212), H215 (= H213), T243 (= T241), L274 (= L272), F275 (= F273), S276 (= S274), N277 (= N275), R370 (= R368)
3tqxA Structure of the 2-amino-3-ketobutyrate coenzyme a ligase (kbl) from coxiella burnetii (see paper)
64% identity, 98% coverage: 8:397/397 of query aligns to 7:396/396 of 3tqxA
- active site: N48 (= N50), H134 (= H136), D179 (= D181), S183 (= S185), D208 (= D210), H211 (= H213), K242 (= K244)
- binding pyridoxal-5'-phosphate: S108 (≠ A110), C109 (≠ A111), F110 (= F112), N113 (= N115), H134 (= H136), S136 (= S138), D208 (= D210), S210 (≠ C212), H211 (= H213), T239 (= T241), K242 (= K244), F271 (= F273), S272 (= S274), N273 (= N275)
P0AB77 2-amino-3-ketobutyrate coenzyme A ligase; AKB ligase; Glycine acetyltransferase; EC 2.3.1.29 from Escherichia coli (strain K12) (see paper)
61% identity, 100% coverage: 1:397/397 of query aligns to 5:397/398 of P0AB77
- H136 (= H136) binding
- S185 (= S185) binding in other chain
- R368 (= R368) binding
1fc4A 2-amino-3-ketobutyrate coa ligase (see paper)
61% identity, 100% coverage: 1:397/397 of query aligns to 8:400/401 of 1fc4A
- active site: N53 (= N50), H139 (= H136), D184 (= D181), S188 (= S185), D213 (= D210), H216 (= H213), K247 (= K244)
- binding 2-amino-3-ketobutyric acid: N53 (= N50), H139 (= H136), S188 (= S185), M189 (= M186), H216 (= H213), K247 (= K244), R371 (= R368)
- binding pyridoxal-5'-phosphate: S113 (≠ A110), C114 (≠ A111), F115 (= F112), H139 (= H136), D184 (= D181), S188 (= S185), D213 (= D210), S215 (≠ C212), H216 (= H213), T244 (= T241), K247 (= K244), F276 (= F273), S277 (= S274), N278 (= N275)
7v58B Structural insights into the substrate selectivity of acyl-coa transferase (see paper)
65% identity, 95% coverage: 20:397/397 of query aligns to 22:399/400 of 7v58B
Q0P5L8 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial; AKB ligase; Aminoacetone synthase; Glycine acetyltransferase; EC 2.3.1.29 from Bos taurus (Bovine) (see paper)
56% identity, 99% coverage: 5:397/397 of query aligns to 27:418/419 of Q0P5L8
- K265 (= K244) modified: N6-(pyridoxal phosphate)lysine
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
7poaA An irreversible, promiscuous and highly thermostable claisen- condensation biocatalyst drives the synthesis of substituted pyrroles
40% identity, 99% coverage: 5:397/397 of query aligns to 8:397/398 of 7poaA
- binding pyridoxal-5'-phosphate: S112 (≠ A110), G113 (≠ A111), F114 (= F112), N117 (= N115), H138 (= H136), S140 (= S138), D181 (= D181), D210 (= D210), A212 (≠ C212), H213 (= H213), T242 (= T241), S244 (≠ G243), K245 (= K244), F273 (= F273), S274 (= S274), T275 (≠ N275)
8h29A Serine palmitoyltransferase (see paper)
36% identity, 96% coverage: 11:393/397 of query aligns to 13:391/394 of 8h29A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-threonine: N51 (= N50), T111 (≠ A110), G112 (≠ A111), F113 (= F112), N116 (= N115), H137 (= H136), S139 (= S138), D180 (= D181), D209 (= D210), A211 (≠ C212), H212 (= H213), T240 (= T241), S242 (≠ G243), K243 (= K244)
8h21A Serine palmitoyltransferase (see paper)
36% identity, 96% coverage: 11:393/397 of query aligns to 13:391/394 of 8h21A
- binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: T111 (≠ A110), G112 (≠ A111), F113 (= F112), N116 (= N115), H137 (= H136), S139 (= S138), D180 (= D181), D209 (= D210), A211 (≠ C212), H212 (= H213), T240 (= T241), S242 (≠ G243), K243 (= K244)
8h20A Serine palmitoyltransferase (see paper)
36% identity, 96% coverage: 11:393/397 of query aligns to 13:391/394 of 8h20A