SitesBLAST
Comparing CA265_RS13080 FitnessBrowser__Pedo557:CA265_RS13080 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)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
43% identity, 94% coverage: 24:387/388 of query aligns to 27:392/396 of 4omaA
- active site: R59 (= R56), Y112 (≠ F109), D184 (= D181), K209 (= K206)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G84), I88 (≠ M85), Y112 (≠ F109), D184 (= D181), S206 (= S203), T208 (= T205), K209 (= K206), V337 (≠ A332), S338 (≠ N333), R373 (= R368)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
43% identity, 94% coverage: 24:387/388 of query aligns to 27:392/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
43% identity, 94% coverage: 24:387/388 of query aligns to 27:392/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
43% identity, 94% coverage: 24:387/388 of query aligns to 27:392/396 of 3jw9A
P9WGB5 O-succinylhomoserine sulfhydrylase; OSH sulfhydrylase; OSHS sulfhydrylase; EC 2.5.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
45% identity, 98% coverage: 8:388/388 of query aligns to 21:406/406 of P9WGB5
- K219 (= K206) modified: N6-(pyridoxal phosphate)lysine
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
43% identity, 94% coverage: 24:387/388 of query aligns to 27:392/396 of 4hf8A
- active site: R59 (= R56), Y112 (≠ F109), D184 (= D181), K209 (= K206)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G84), I88 (≠ M85), Y112 (≠ F109), E155 (= E152), N159 (= N156), D184 (= D181), S206 (= S203), K209 (= K206), S338 (≠ N333), R373 (= R368)
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
43% identity, 94% coverage: 24:387/388 of query aligns to 26:391/395 of 5m3zA
- active site: R58 (= R56), Y111 (≠ F109), D183 (= D181), K208 (= K206)
- binding norleucine: Y111 (≠ F109), H113 (≠ S111), K208 (= K206), V336 (≠ A332), S337 (≠ N333)
- binding pyridoxal-5'-phosphate: G86 (= G84), I87 (≠ M85), Y111 (≠ F109), E154 (= E152), D183 (= D181), T185 (≠ C183), S205 (= S203), T207 (= T205), K208 (= K206)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G84), I87 (≠ M85), Y111 (≠ F109), D183 (= D181), S205 (= S203), T207 (= T205), K208 (= K206), V336 (≠ A332), S337 (≠ N333), R372 (= R368)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
43% identity, 94% coverage: 24:387/388 of query aligns to 27:392/396 of 6egrA
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
42% identity, 94% coverage: 24:387/388 of query aligns to 27:381/386 of 3mkjA
- active site: Y101 (≠ F109), D173 (= D181), K198 (= K206)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G84), I77 (≠ M85), Y101 (≠ F109), E144 (= E152), D173 (= D181), F176 (= F184), S195 (= S203), T197 (= T205), K198 (= K206)
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
41% identity, 93% coverage: 26:387/388 of query aligns to 25:388/392 of 5x2xA
- active site: R55 (= R56), Y108 (≠ F109), D180 (= D181), K205 (= K206)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y54), R55 (= R56), G83 (= G84), M84 (= M85), Y108 (≠ F109), N155 (= N156), D180 (= D181), S202 (= S203), T204 (= T205), K205 (= K206), V333 (≠ A332), S334 (≠ N333), R369 (= R368)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
41% identity, 93% coverage: 26:387/388 of query aligns to 25:388/392 of 5x2wA
- active site: R55 (= R56), Y108 (≠ F109), D180 (= D181), K205 (= K206)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y54), R55 (= R56), S82 (≠ T83), G83 (= G84), M84 (= M85), Y108 (≠ F109), D180 (= D181), S202 (= S203), K205 (= K206), V333 (≠ A332), S334 (≠ N333), R369 (= R368)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
41% identity, 93% coverage: 26:387/388 of query aligns to 31:394/398 of 1pg8A
- active site: R61 (= R56), Y114 (≠ F109), D186 (= D181), K211 (= K206)
- binding pyridoxal-5'-phosphate: Y59 (= Y54), R61 (= R56), S88 (≠ T83), G89 (= G84), M90 (= M85), Y114 (≠ F109), D186 (= D181), S208 (= S203), T210 (= T205), K211 (= K206)
P13254 L-methionine gamma-lyase; MGL; Homocysteine desulfhydrase; L-methioninase; EC 4.4.1.11; EC 4.4.1.2 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 3 papers)
41% identity, 93% coverage: 26:387/388 of query aligns to 31:394/398 of P13254
- YSR 59:61 (= YSR 54:56) binding
- R61 (= R56) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 84:85) binding in other chain
- Y114 (≠ F109) binding
- C116 (≠ S111) mutation to H: Drastic decrease of the catalytic efficiency of the elimination reaction with L-methionine, by 6700-fold, and increases that with L-cysteine by 7-fold, mainly due to changes in kcat. Loss of ability to catalyze replacement reaction between L-methionine and 2-mercaptoethanol.; mutation to S: 9% of wild-type elimination activity against L-methionine.; mutation to T: 40% of wild-type elimination activity against L-methionine.
- SAT 208:210 (= SAT 203:205) binding in other chain
- K211 (= K206) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ A233) mutation K->D,E: Marked decrease in elimination activity against both L-methionine and DL-homocysteine.; mutation to M: 50% reduction in alpha,gamma-elimination activity against DL-homocysteine, while retaining elimination activity against L-methionine and L-cysteine.
- D241 (≠ R234) mutation D->H,R: 5 to 14-fold reduction in alpha,gamma-elimination activity against L-methionine, while no change in affinity for L-methionine.
- R375 (= R368) binding
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
41% identity, 93% coverage: 26:387/388 of query aligns to 30:393/397 of 3vk3A
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
41% identity, 93% coverage: 26:387/388 of query aligns to 26:389/393 of 5x30C
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
38% identity, 94% coverage: 24:387/388 of query aligns to 27:394/399 of 5dx5A
- active site: R59 (= R56), Y112 (≠ F109), D186 (= D181), K211 (= K206)
- binding pyridoxal-5'-phosphate: Y57 (= Y54), R59 (= R56), S86 (≠ T83), G87 (= G84), M88 (= M85), Y112 (≠ F109), D186 (= D181), F189 (= F184), S208 (= S203), T210 (= T205), K211 (= K206)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
38% identity, 93% coverage: 26:387/388 of query aligns to 25:389/394 of 1e5eA
- active site: R55 (= R56), Y108 (≠ F109), D181 (= D181), K206 (= K206)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y54), R55 (= R56), G83 (= G84), M84 (= M85), Y108 (≠ F109), N155 (= N156), D181 (= D181), S203 (= S203), T205 (= T205), K206 (= K206), S335 (≠ N333), T350 (= T348), R370 (= R368)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
38% identity, 93% coverage: 26:387/388 of query aligns to 25:389/393 of 1e5fA
- active site: R55 (= R56), Y108 (≠ F109), D181 (= D181), K206 (= K206)
- binding pyridoxal-5'-phosphate: Y53 (= Y54), R55 (= R56), G83 (= G84), M84 (= M85), Y108 (≠ F109), D181 (= D181), S203 (= S203), K206 (= K206)
5x5hA Crystal structure of metb from corynebacterium glutamicum (see paper)
39% identity, 99% coverage: 3:387/388 of query aligns to 5:381/385 of 5x5hA
- active site: R52 (= R56), Y105 (≠ F109), D177 (= D181), K202 (= K206)
- binding magnesium ion: F36 (≠ Y33), Q38 (≠ F35), E49 (≠ V53), E69 (= E73), Q187 (= Q191), P188 (= P192), L189 (≠ I193)
- binding pyridoxal-5'-phosphate: G80 (= G84), M81 (= M85), Y105 (≠ F109), D177 (= D181), S199 (= S203), T201 (= T205), K202 (= K206)
6cjaA Crystal structure of cystathionine beta-lyase from legionella pneumophila philadelphia 1 in complex with alanyl-plp and serine
41% identity, 94% coverage: 25:388/388 of query aligns to 24:381/381 of 6cjaA
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-alanine: Y45 (= Y54), R47 (= R56), S74 (≠ T83), G75 (= G84), M76 (= M85), Y99 (≠ F109), N147 (= N156), D172 (= D181), S194 (= S203), T196 (= T205), K197 (= K206), S326 (≠ N333), T341 (= T348), R361 (= R368)
- binding serine: E44 (≠ V53), R47 (= R56), T48 (≠ Y57), R104 (≠ Q114), E325 (≠ A332)
Query Sequence
>CA265_RS13080 FitnessBrowser__Pedo557:CA265_RS13080
MKSENFETIAIRTQTERSLHKEHSSPIYLTSSYKFEDAEEMRALFANEKEGNVYSRYSNP
NTSEFIEKMCLLEGAEDGFATATGMAAIFTTFGAFLKNGDHLVSSRSVFGSTHQLLTNVF
SNWGVTFDYADLDKPQDWEALIKPNTKMIFVETPSNPGIDIIDLEFLGDLAKKHNVLLVV
DNCFATPYLQQPIKFGAHISIHSATKYIDGQGRVLGGVILGTKELIADVIGFARHSGPAL
SPFNAWILSKSLETLAIRMDRHCENALKVAEYLEKHPKIKLVKYPFLPSHPQYDIAKKQM
KQGGGIVTIVVEGGIDAARKFMDGLQMFSISANLADTRSIATHPATSTHSKLTEEQRNEV
GIEQGSIRLSIGLEHINDILADIEQALA
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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