SitesBLAST
Comparing Ga0059261_1458 FitnessBrowser__Korea:Ga0059261_1458 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)
5ijgB Crystal structure of o-acetylhomoserine sulfhydrolase from brucella melitensis at 2.0 a resolution
53% identity, 93% coverage: 29:439/440 of query aligns to 5:403/403 of 5ijgB
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
40% identity, 93% coverage: 32:440/440 of query aligns to 1:392/393 of 1e5fA
- active site: R55 (= R94), Y108 (= Y147), D181 (= D229), K206 (= K254)
- binding pyridoxal-5'-phosphate: Y53 (= Y92), R55 (= R94), G83 (= G122), M84 (= M123), Y108 (= Y147), D181 (= D229), S203 (= S251), K206 (= K254)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
40% identity, 93% coverage: 32:440/440 of query aligns to 1:392/394 of 1e5eA
- active site: R55 (= R94), Y108 (= Y147), D181 (= D229), K206 (= K254)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y92), R55 (= R94), G83 (= G122), M84 (= M123), Y108 (= Y147), N155 (= N199), D181 (= D229), S203 (= S251), T205 (= T253), K206 (= K254), S335 (= S383), T350 (= T398), R370 (= R418)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
38% identity, 91% coverage: 38:438/440 of query aligns to 10:393/396 of 4omaA
- active site: R59 (= R94), Y112 (= Y147), D184 (= D229), K209 (= K254)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G122), I88 (≠ M123), Y112 (= Y147), D184 (= D229), S206 (= S251), T208 (= T253), K209 (= K254), V337 (= V382), S338 (= S383), R373 (= R418)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
38% identity, 91% coverage: 38:438/440 of query aligns to 10:393/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
38% identity, 91% coverage: 38:438/440 of query aligns to 10:393/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
38% identity, 91% coverage: 38:438/440 of query aligns to 10:393/396 of 3jw9A
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
38% identity, 91% coverage: 38:438/440 of query aligns to 10:393/396 of 4hf8A
- active site: R59 (= R94), Y112 (= Y147), D184 (= D229), K209 (= K254)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G122), I88 (≠ M123), Y112 (= Y147), E155 (= E195), N159 (= N199), D184 (= D229), S206 (= S251), K209 (= K254), S338 (= S383), R373 (= R418)
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
38% identity, 91% coverage: 38:438/440 of query aligns to 9:392/395 of 5m3zA
- active site: R58 (= R94), Y111 (= Y147), D183 (= D229), K208 (= K254)
- binding norleucine: Y111 (= Y147), H113 (≠ A149), K208 (= K254), V336 (= V382), S337 (= S383)
- binding pyridoxal-5'-phosphate: G86 (= G122), I87 (≠ M123), Y111 (= Y147), E154 (= E195), D183 (= D229), T185 (= T231), S205 (= S251), T207 (= T253), K208 (= K254)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G122), I87 (≠ M123), Y111 (= Y147), D183 (= D229), S205 (= S251), T207 (= T253), K208 (= K254), V336 (= V382), S337 (= S383), R372 (= R418)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
37% identity, 91% coverage: 38:438/440 of query aligns to 10:393/396 of 6egrA
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
37% identity, 88% coverage: 52:440/440 of query aligns to 24:397/399 of 5dx5A
- active site: R59 (= R94), Y112 (= Y147), D186 (= D229), K211 (= K254)
- binding pyridoxal-5'-phosphate: Y57 (= Y92), R59 (= R94), S86 (= S121), G87 (= G122), M88 (= M123), Y112 (= Y147), D186 (= D229), F189 (= F232), S208 (= S251), T210 (= T253), K211 (= K254)
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
38% identity, 92% coverage: 37:439/440 of query aligns to 5:390/392 of 5x2xA
- active site: R55 (= R94), Y108 (= Y147), D180 (= D229), K205 (= K254)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y92), R55 (= R94), G83 (= G122), M84 (= M123), Y108 (= Y147), N155 (= N199), D180 (= D229), S202 (= S251), T204 (= T253), K205 (= K254), V333 (= V382), S334 (= S383), R369 (= R418)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
38% identity, 92% coverage: 37:439/440 of query aligns to 5:390/392 of 5x2wA
- active site: R55 (= R94), Y108 (= Y147), D180 (= D229), K205 (= K254)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y92), R55 (= R94), S82 (= S121), G83 (= G122), M84 (= M123), Y108 (= Y147), D180 (= D229), S202 (= S251), K205 (= K254), V333 (= V382), S334 (= S383), R369 (= R418)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
37% identity, 91% coverage: 38:438/440 of query aligns to 10:382/386 of 3mkjA
- active site: Y101 (= Y147), D173 (= D229), K198 (= K254)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G122), I77 (≠ M123), Y101 (= Y147), E144 (= E195), D173 (= D229), F176 (= F232), S195 (= S251), T197 (= T253), K198 (= K254)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
38% identity, 92% coverage: 37:439/440 of query aligns to 11:396/398 of 1pg8A
- active site: R61 (= R94), Y114 (= Y147), D186 (= D229), K211 (= K254)
- binding pyridoxal-5'-phosphate: Y59 (= Y92), R61 (= R94), S88 (= S121), G89 (= G122), M90 (= M123), Y114 (= Y147), D186 (= D229), S208 (= S251), T210 (= T253), K211 (= K254)
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)
38% identity, 92% coverage: 37:439/440 of query aligns to 11:396/398 of P13254
- YSR 59:61 (= YSR 92:94) binding
- R61 (= R94) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 122:123) binding in other chain
- Y114 (= Y147) binding
- C116 (≠ A149) 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 (≠ SLT 251:253) binding in other chain
- K211 (= K254) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ R281) 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 (≠ N282) 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 (= R418) binding
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
38% identity, 92% coverage: 37:439/440 of query aligns to 6:391/393 of 5x30C
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
38% identity, 92% coverage: 37:439/440 of query aligns to 10:395/397 of 3vk3A
3aeoA Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 containing methionine alpha, beta-enamine-pyridoxamine- 5'-phosphate
37% identity, 87% coverage: 57:438/440 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 (= Y92), R53 (= R94), G81 (= G122), M82 (= M123), Y106 (= Y147), E149 (= E195), N153 (= N199), D178 (= D229), S200 (= S251), S202 (≠ T253), K203 (= K254), V329 (= V382), S330 (= S383), T345 (= T398), R365 (= R418)
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
37% identity, 87% coverage: 57:438/440 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 (= Y92), R53 (= R94)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: G81 (= G122), M82 (= M123), Y106 (= Y147), E149 (= E195), N153 (= N199), D178 (= D229), T180 (= T231), S200 (= S251), S202 (≠ T253), K203 (= K254), S330 (= S383), T345 (= T398), R365 (= R418)
Query Sequence
>Ga0059261_1458 FitnessBrowser__Korea:Ga0059261_1458
MTDKPVKPDEAALTSTTPRRRPKPSVETVGGRQLSPATLMMGHGYDPMLSEGSLKPPIFA
TSTFVFPNAAAGKRHFEGVTGKRPGGAEGLVYSRFNGPNQEILEDRLGIWEEAEDALAFS
SGMSAIATLFLAMVKPGDTIVHSGPLYAATETLIARILGKFGVHWLDFPAGATREEIDAV
LSKAASGNVALIYLESPANPTNALVDVEAVAASRDAIFTGASKPPIAIDNTFLGPLWAKP
LQQGADLVVYSLTKYAGGHSDLVAGGVLGSKELINTIRLMRNTIGTICDPNTAWMLLRSL
ETLELRMSRAGENAIKVCEYLRTHPKVESVGYLGFLPEGSRQRDIYDRHCTGAGSTFSLY
LKGGEKEAFAFLDSLKIAKLAVSLGGTETLASAPAAMTHLSVPDARKKALGITDNLVRIS
IGVEDADDLIADFEEALKAV
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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