SitesBLAST
Comparing CCNA_03271 FitnessBrowser__Caulo:CCNA_03271 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)
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
63% identity, 97% coverage: 7:393/401 of query aligns to 3:389/392 of 5x2xA
- active site: R55 (= R59), Y108 (= Y112), D180 (= D184), K205 (= K209)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y57), R55 (= R59), G83 (= G87), M84 (= M88), Y108 (= Y112), N155 (= N159), D180 (= D184), S202 (= S206), T204 (= T208), K205 (= K209), V333 (= V337), S334 (= S338), R369 (= R373)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
63% identity, 97% coverage: 7:393/401 of query aligns to 3:389/392 of 5x2wA
- active site: R55 (= R59), Y108 (= Y112), D180 (= D184), K205 (= K209)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y57), R55 (= R59), S82 (= S86), G83 (= G87), M84 (= M88), Y108 (= Y112), D180 (= D184), S202 (= S206), K205 (= K209), V333 (= V337), S334 (= S338), R369 (= R373)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
63% identity, 97% coverage: 7:393/401 of query aligns to 9:395/398 of 1pg8A
- active site: R61 (= R59), Y114 (= Y112), D186 (= D184), K211 (= K209)
- binding pyridoxal-5'-phosphate: Y59 (= Y57), R61 (= R59), S88 (= S86), G89 (= G87), M90 (= M88), Y114 (= Y112), D186 (= D184), S208 (= S206), T210 (= T208), K211 (= K209)
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)
63% identity, 97% coverage: 7:393/401 of query aligns to 9:395/398 of P13254
- YSR 59:61 (= YSR 57:59) binding
- R61 (= R59) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 87:88) binding in other chain
- Y114 (= Y112) binding
- C116 (= C114) 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 206:208) binding in other chain
- K211 (= K209) modified: N6-(pyridoxal phosphate)lysine
- K240 (= K238) 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 (= D239) 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 (= R373) binding
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
62% identity, 97% coverage: 7:393/401 of query aligns to 4:390/393 of 5x30C
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
62% identity, 97% coverage: 7:393/401 of query aligns to 8:394/397 of 3vk3A
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
56% identity, 97% coverage: 5:393/401 of query aligns to 5:395/399 of 5dx5A
- active site: R59 (= R59), Y112 (= Y112), D186 (= D184), K211 (= K209)
- binding pyridoxal-5'-phosphate: Y57 (= Y57), R59 (= R59), S86 (= S86), G87 (= G87), M88 (= M88), Y112 (= Y112), D186 (= D184), F189 (≠ Y187), S208 (= S206), T210 (= T208), K211 (= K209)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
54% identity, 96% coverage: 7:392/401 of query aligns to 7:392/396 of 6egrA
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
53% identity, 96% coverage: 7:392/401 of query aligns to 7:392/396 of 4hf8A
- active site: R59 (= R59), Y112 (= Y112), D184 (= D184), K209 (= K209)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G87), I88 (≠ M88), Y112 (= Y112), E155 (= E155), N159 (= N159), D184 (= D184), S206 (= S206), K209 (= K209), S338 (= S338), R373 (= R373)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
53% identity, 96% coverage: 7:392/401 of query aligns to 7:392/396 of 4omaA
- active site: R59 (= R59), Y112 (= Y112), D184 (= D184), K209 (= K209)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G87), I88 (≠ M88), Y112 (= Y112), D184 (= D184), S206 (= S206), T208 (= T208), K209 (= K209), V337 (= V337), S338 (= S338), R373 (= R373)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
53% identity, 96% coverage: 7:392/401 of query aligns to 7:392/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
53% identity, 96% coverage: 7:392/401 of query aligns to 7:392/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
53% identity, 96% coverage: 7:392/401 of query aligns to 7:392/396 of 3jw9A
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
53% identity, 96% coverage: 7:392/401 of query aligns to 6:391/395 of 5m3zA
- active site: R58 (= R59), Y111 (= Y112), D183 (= D184), K208 (= K209)
- binding norleucine: Y111 (= Y112), H113 (≠ C114), K208 (= K209), V336 (= V337), S337 (= S338)
- binding pyridoxal-5'-phosphate: G86 (= G87), I87 (≠ M88), Y111 (= Y112), E154 (= E155), D183 (= D184), T185 (= T186), S205 (= S206), T207 (= T208), K208 (= K209)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G87), I87 (≠ M88), Y111 (= Y112), D183 (= D184), S205 (= S206), T207 (= T208), K208 (= K209), V336 (= V337), S337 (= S338), R372 (= R373)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
53% identity, 96% coverage: 7:392/401 of query aligns to 7:381/386 of 3mkjA
- active site: Y101 (= Y112), D173 (= D184), K198 (= K209)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G87), I77 (≠ M88), Y101 (= Y112), E144 (= E155), D173 (= D184), F176 (≠ Y187), S195 (= S206), T197 (= T208), K198 (= K209)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
46% identity, 97% coverage: 9:395/401 of query aligns to 6:392/393 of 1e5fA
- active site: R55 (= R59), Y108 (= Y112), D181 (= D184), K206 (= K209)
- binding pyridoxal-5'-phosphate: Y53 (= Y57), R55 (= R59), G83 (= G87), M84 (= M88), Y108 (= Y112), D181 (= D184), S203 (= S206), K206 (= K209)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
46% identity, 97% coverage: 9:395/401 of query aligns to 6:392/394 of 1e5eA
- active site: R55 (= R59), Y108 (= Y112), D181 (= D184), K206 (= K209)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y57), R55 (= R59), G83 (= G87), M84 (= M88), Y108 (= Y112), N155 (= N159), D181 (= D184), S203 (= S206), T205 (= T208), K206 (= K209), S335 (= S338), T350 (= T353), R370 (= R373)
3aeoA Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 containing methionine alpha, beta-enamine-pyridoxamine- 5'-phosphate
44% identity, 91% coverage: 29:393/401 of query aligns to 23:385/387 of 3aeoA
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y51 (= Y57), R53 (= R59), G81 (= G87), M82 (= M88), Y106 (= Y112), E149 (= E155), N153 (= N159), D178 (= D184), S200 (= S206), S202 (≠ T208), K203 (= K209), V329 (= V337), S330 (= S338), T345 (= T353), R365 (= R373)
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, 91% coverage: 29:393/401 of query aligns to 23:385/387 of 3aelA
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]-4-(methylsulfanyl)butanoic acid: Y51 (= Y57), R53 (= R59)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: G81 (= G87), M82 (= M88), Y106 (= Y112), E149 (= E155), N153 (= N159), D178 (= D184), T180 (= T186), S200 (= S206), S202 (≠ T208), K203 (= K209), S330 (= S338), T345 (= T353), R365 (= R373)
3aejC Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 tetramer containing michaelis complex and methionine- pyridoxal-5'-phosphate
44% identity, 91% coverage: 29:393/401 of query aligns to 23:385/387 of 3aejC
- active site: R53 (= R59), Y106 (= Y112), D178 (= D184), K203 (= K209)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: F42 (= F48), Y51 (= Y57), R53 (= R59)
- binding methionine: Y106 (= Y112), K203 (= K209), S330 (= S338), L331 (= L339), T345 (= T353), R365 (= R373)
Query Sequence
>CCNA_03271 FitnessBrowser__Caulo:CCNA_03271
MRDDQTGFSTRAIHAGYDPADEHGALTPPLHLTSTFAFESAEAGGEMFAGTREGHFYSRI
SNPTTDLLERRLASLEGAEAAVATASGMGAITATLWSFLRAGDEVITDQTLYGCTFAFLR
DGLTRFGVTVKQVDMTRPETLAAAISDQTRIVYFETPANPNMRLVDIAAITRIAHAAGAK
VVVDNTYATPCLTRPLALGADIVVHSATKYLGGHGDLVGGIAAGGIEDMARVRLCGVKDM
TGAVMSPFTAFLVLRGLKTLSLRMARHSQSAQAVARWLEDHPAVEQVFYPGLQSFPQRDL
AARQMAAGGGMMAFELKGGHAAGVAMMNRLALIRRAVSLGDAETLIQHPASMTHSPYTPE
ERAAAGIGEGMVRLSVGLEDVADILADLAMALEPLKVAQPA
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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