SitesBLAST
Comparing WP_086510355.1 NCBI__GCF_002151265.1:WP_086510355.1 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)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
64% identity, 95% coverage: 21:415/415 of query aligns to 4:398/398 of 1pg8A
- active site: R61 (= R78), Y114 (= Y131), D186 (= D203), K211 (= K228)
- binding pyridoxal-5'-phosphate: Y59 (= Y76), R61 (= R78), S88 (= S105), G89 (= G106), M90 (= M107), Y114 (= Y131), D186 (= D203), S208 (= S225), T210 (= T227), K211 (= K228)
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)
64% identity, 95% coverage: 21:415/415 of query aligns to 4:398/398 of P13254
- YSR 59:61 (= YSR 76:78) binding
- R61 (= R78) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 106:107) binding in other chain
- Y114 (= Y131) binding
- C116 (= C133) 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 225:227) binding in other chain
- K211 (= K228) modified: N6-(pyridoxal phosphate)lysine
- K240 (= K257) 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 (= D258) 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 (= R392) binding
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
64% identity, 94% coverage: 26:415/415 of query aligns to 3:392/392 of 5x2xA
- active site: R55 (= R78), Y108 (= Y131), D180 (= D203), K205 (= K228)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y76), R55 (= R78), G83 (= G106), M84 (= M107), Y108 (= Y131), N155 (= N178), D180 (= D203), S202 (= S225), T204 (= T227), K205 (= K228), V333 (= V356), S334 (= S357), R369 (= R392)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
64% identity, 94% coverage: 26:415/415 of query aligns to 3:392/392 of 5x2wA
- active site: R55 (= R78), Y108 (= Y131), D180 (= D203), K205 (= K228)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y76), R55 (= R78), S82 (= S105), G83 (= G106), M84 (= M107), Y108 (= Y131), D180 (= D203), S202 (= S225), K205 (= K228), V333 (= V356), S334 (= S357), R369 (= R392)
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
63% identity, 95% coverage: 21:415/415 of query aligns to 3:397/397 of 3vk3A
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
64% identity, 94% coverage: 26:415/415 of query aligns to 4:393/393 of 5x30C
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
56% identity, 93% coverage: 26:412/415 of query aligns to 7:393/396 of 4hf8A
- active site: R59 (= R78), Y112 (= Y131), D184 (= D203), K209 (= K228)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G106), I88 (≠ M107), Y112 (= Y131), E155 (= E174), N159 (= N178), D184 (= D203), S206 (= S225), K209 (= K228), S338 (= S357), R373 (= R392)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
56% identity, 93% coverage: 26:412/415 of query aligns to 7:393/396 of 4omaA
- active site: R59 (= R78), Y112 (= Y131), D184 (= D203), K209 (= K228)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G106), I88 (≠ M107), Y112 (= Y131), D184 (= D203), S206 (= S225), T208 (= T227), K209 (= K228), V337 (= V356), S338 (= S357), R373 (= R392)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
56% identity, 93% coverage: 26:412/415 of query aligns to 7:393/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
56% identity, 93% coverage: 26:412/415 of query aligns to 7:393/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
56% identity, 93% coverage: 26:412/415 of query aligns to 7:393/396 of 3jw9A
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
56% identity, 93% coverage: 26:412/415 of query aligns to 7:393/396 of 6egrA
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
55% identity, 93% coverage: 26:412/415 of query aligns to 6:392/395 of 5m3zA
- active site: R58 (= R78), Y111 (= Y131), D183 (= D203), K208 (= K228)
- binding norleucine: Y111 (= Y131), H113 (≠ C133), K208 (= K228), V336 (= V356), S337 (= S357)
- binding pyridoxal-5'-phosphate: G86 (= G106), I87 (≠ M107), Y111 (= Y131), E154 (= E174), D183 (= D203), T185 (= T205), S205 (= S225), T207 (= T227), K208 (= K228)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G106), I87 (≠ M107), Y111 (= Y131), D183 (= D203), S205 (= S225), T207 (= T227), K208 (= K228), V336 (= V356), S337 (= S357), R372 (= R392)
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
53% identity, 93% coverage: 26:413/415 of query aligns to 7:396/399 of 5dx5A
- active site: R59 (= R78), Y112 (= Y131), D186 (= D203), K211 (= K228)
- binding pyridoxal-5'-phosphate: Y57 (= Y76), R59 (= R78), S86 (= S105), G87 (= G106), M88 (= M107), Y112 (= Y131), D186 (= D203), F189 (≠ Y206), S208 (= S225), T210 (= T227), K211 (= K228)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
55% identity, 93% coverage: 26:412/415 of query aligns to 7:382/386 of 3mkjA
- active site: Y101 (= Y131), D173 (= D203), K198 (= K228)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G106), I77 (≠ M107), Y101 (= Y131), E144 (= E174), D173 (= D203), F176 (≠ Y206), S195 (= S225), T197 (= T227), K198 (= K228)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
50% identity, 93% coverage: 28:411/415 of query aligns to 6:389/393 of 1e5fA
- active site: R55 (= R78), Y108 (= Y131), D181 (= D203), K206 (= K228)
- binding pyridoxal-5'-phosphate: Y53 (= Y76), R55 (= R78), G83 (= G106), M84 (= M107), Y108 (= Y131), D181 (= D203), S203 (= S225), K206 (= K228)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
50% identity, 93% coverage: 28:411/415 of query aligns to 6:389/394 of 1e5eA
- active site: R55 (= R78), Y108 (= Y131), D181 (= D203), K206 (= K228)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y76), R55 (= R78), G83 (= G106), M84 (= M107), Y108 (= Y131), N155 (= N178), D181 (= D203), S203 (= S225), T205 (= T227), K206 (= K228), S335 (= S357), T350 (= T372), R370 (= R392)
3aeoA Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 containing methionine alpha, beta-enamine-pyridoxamine- 5'-phosphate
44% identity, 88% coverage: 48:413/415 of query aligns to 23:386/387 of 3aeoA
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y51 (= Y76), R53 (= R78), G81 (= G106), M82 (= M107), Y106 (= Y131), E149 (= E174), N153 (= N178), D178 (= D203), S200 (= S225), S202 (≠ T227), K203 (= K228), V329 (= V356), S330 (= S357), T345 (= T372), R365 (= R392)
3aelA Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 containing methionine imine-pyridoxamine-5'-phosphate and alpha-amino-alpha, beta-butenoic acid-pyridoxal-5'-phosphate
44% identity, 88% coverage: 48:413/415 of query aligns to 23:386/387 of 3aelA
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]-4-(methylsulfanyl)butanoic acid: Y51 (= Y76), R53 (= R78)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: G81 (= G106), M82 (= M107), Y106 (= Y131), E149 (= E174), N153 (= N178), D178 (= D203), T180 (= T205), S200 (= S225), S202 (≠ T227), K203 (= K228), S330 (= S357), T345 (= T372), R365 (= R392)
3aejC Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 tetramer containing michaelis complex and methionine- pyridoxal-5'-phosphate
44% identity, 88% coverage: 48:413/415 of query aligns to 23:386/387 of 3aejC
- active site: R53 (= R78), Y106 (= Y131), D178 (= D203), K203 (= K228)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: F42 (= F67), Y51 (= Y76), R53 (= R78)
- binding methionine: Y106 (= Y131), K203 (= K228), S330 (= S357), L331 (= L358), T345 (= T372), R365 (= R392)
Query Sequence
>WP_086510355.1 NCBI__GCF_002151265.1:WP_086510355.1
MQQRHSQQGNSQQGHSQQGHSQQGQGFATRAIHAAYDSRDEQGALTPPMHLTSTFTFESV
EQGAERFAGEAPGHFYSRISNPTVATLEQRMANLEGAEAGLATASGMGAITALMWSLLRP
GDELITDSHLYGCTHAFFHHGLTEFGIRVKHVDLSQPAALEVAIGERTKLVYFETPANPT
MRLVDIEAVSRIAHRHGARVVVDNTYATPVITRPIEQGADFVVHSATKYLGGHGDLIAGV
LVGSVDDIHRVRLTGLKDFTGAVMSPFTAFLIMRGLKTLEIRMQRQSASALEVARWLERH
PAVERVHYPGLTSFPQHELARRQMSDYGGIIAFELAGGLEAGRRFMNRLELIQRAVSLGD
AESLIQHPASMTHSVLSPEERAEHGISETLIRLSVGLETPSDLRADLAQALKVRA
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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