SitesBLAST
Comparing Ga0059261_3194 FitnessBrowser__Korea:Ga0059261_3194 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)
P9WGB5 O-succinylhomoserine sulfhydrylase; OSH sulfhydrylase; OSHS sulfhydrylase; EC 2.5.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
48% identity, 95% coverage: 18:397/402 of query aligns to 20:405/406 of P9WGB5
- K219 (= K217) modified: N6-(pyridoxal phosphate)lysine
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
44% identity, 91% coverage: 32:397/402 of query aligns to 23:391/395 of 5m3zA
- active site: R58 (= R67), Y111 (≠ F120), D183 (= D192), K208 (= K217)
- binding norleucine: Y111 (≠ F120), H113 (≠ S122), K208 (= K217), V336 (≠ N342), S337 (≠ N343)
- binding pyridoxal-5'-phosphate: G86 (= G95), I87 (≠ M96), Y111 (≠ F120), E154 (= E163), D183 (= D192), T185 (≠ A194), S205 (= S214), T207 (= T216), K208 (= K217)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G95), I87 (≠ M96), Y111 (≠ F120), D183 (= D192), S205 (= S214), T207 (= T216), K208 (= K217), V336 (≠ N342), S337 (≠ N343), R372 (= R378)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
44% identity, 91% coverage: 32:397/402 of query aligns to 24:392/396 of 4omaA
- active site: R59 (= R67), Y112 (≠ F120), D184 (= D192), K209 (= K217)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G95), I88 (≠ M96), Y112 (≠ F120), D184 (= D192), S206 (= S214), T208 (= T216), K209 (= K217), V337 (≠ N342), S338 (≠ N343), R373 (= R378)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
44% identity, 91% coverage: 32:397/402 of query aligns to 24:392/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
44% identity, 91% coverage: 32:397/402 of query aligns to 24:392/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
44% identity, 91% coverage: 32:397/402 of query aligns to 24:392/396 of 3jw9A
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
44% identity, 91% coverage: 32:397/402 of query aligns to 24:392/396 of 4hf8A
- active site: R59 (= R67), Y112 (≠ F120), D184 (= D192), K209 (= K217)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G95), I88 (≠ M96), Y112 (≠ F120), E155 (= E163), N159 (= N167), D184 (= D192), S206 (= S214), K209 (= K217), S338 (≠ N343), R373 (= R378)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
44% identity, 91% coverage: 32:397/402 of query aligns to 24:392/396 of 6egrA
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
44% identity, 91% coverage: 32:397/402 of query aligns to 24:381/386 of 3mkjA
- active site: Y101 (≠ F120), D173 (= D192), K198 (= K217)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G95), I77 (≠ M96), Y101 (≠ F120), E144 (= E163), D173 (= D192), F176 (= F195), S195 (= S214), T197 (= T216), K198 (= K217)
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
41% identity, 95% coverage: 18:397/402 of query aligns to 9:394/399 of 5dx5A
- active site: R59 (= R67), Y112 (≠ F120), D186 (= D192), K211 (= K217)
- binding pyridoxal-5'-phosphate: Y57 (= Y65), R59 (= R67), S86 (= S94), G87 (= G95), M88 (= M96), Y112 (≠ F120), D186 (= D192), F189 (= F195), S208 (= S214), T210 (= T216), K211 (= K217)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
39% identity, 97% coverage: 13:400/402 of query aligns to 1:392/393 of 1e5fA
- active site: R55 (= R67), Y108 (≠ F120), D181 (= D192), K206 (= K217)
- binding pyridoxal-5'-phosphate: Y53 (= Y65), R55 (= R67), G83 (= G95), M84 (= M96), Y108 (≠ F120), D181 (= D192), S203 (= S214), K206 (= K217)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
39% identity, 97% coverage: 13:400/402 of query aligns to 1:392/394 of 1e5eA
- active site: R55 (= R67), Y108 (≠ F120), D181 (= D192), K206 (= K217)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y65), R55 (= R67), G83 (= G95), M84 (= M96), Y108 (≠ F120), N155 (= N167), D181 (= D192), S203 (= S214), T205 (= T216), K206 (= K217), S335 (≠ N343), T350 (= T358), R370 (= R378)
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
40% identity, 95% coverage: 18:397/402 of query aligns to 10:393/397 of 3vk3A
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
40% identity, 95% coverage: 18:397/402 of query aligns to 6:389/393 of 5x30C
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
40% identity, 95% coverage: 18:397/402 of query aligns to 11:394/398 of 1pg8A
- active site: R61 (= R67), Y114 (≠ F120), D186 (= D192), K211 (= K217)
- binding pyridoxal-5'-phosphate: Y59 (= Y65), R61 (= R67), S88 (= S94), G89 (= G95), M90 (= M96), Y114 (≠ F120), D186 (= D192), S208 (= S214), T210 (= T216), K211 (= K217)
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)
40% identity, 95% coverage: 18:397/402 of query aligns to 11:394/398 of P13254
- YSR 59:61 (= YSR 65:67) binding
- R61 (= R67) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 95:96) binding in other chain
- Y114 (≠ F120) binding
- C116 (≠ S122) 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 214:216) binding in other chain
- K211 (= K217) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ R246) 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 (≠ N247) 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 (= R378) binding
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
40% identity, 95% coverage: 18:397/402 of query aligns to 5:388/392 of 5x2xA
- active site: R55 (= R67), Y108 (≠ F120), D180 (= D192), K205 (= K217)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y65), R55 (= R67), G83 (= G95), M84 (= M96), Y108 (≠ F120), N155 (= N167), D180 (= D192), S202 (= S214), T204 (= T216), K205 (= K217), V333 (≠ N342), S334 (≠ N343), R369 (= R378)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
40% identity, 95% coverage: 18:397/402 of query aligns to 5:388/392 of 5x2wA
- active site: R55 (= R67), Y108 (≠ F120), D180 (= D192), K205 (= K217)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y65), R55 (= R67), S82 (= S94), G83 (= G95), M84 (= M96), Y108 (≠ F120), D180 (= D192), S202 (= S214), K205 (= K217), V333 (≠ N342), S334 (≠ N343), R369 (= R378)
3aeoA Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 containing methionine alpha, beta-enamine-pyridoxamine- 5'-phosphate
37% identity, 90% coverage: 38:397/402 of query aligns to 24:384/387 of 3aeoA
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y51 (= Y65), R53 (= R67), G81 (= G95), M82 (= M96), Y106 (≠ F120), E149 (= E163), N153 (= N167), D178 (= D192), S200 (= S214), S202 (≠ T216), K203 (= K217), V329 (≠ N342), S330 (≠ N343), T345 (= T358), R365 (= R378)
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, 90% coverage: 38:397/402 of query aligns to 24:384/387 of 3aelA
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]-4-(methylsulfanyl)butanoic acid: Y51 (= Y65), R53 (= R67)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: G81 (= G95), M82 (= M96), Y106 (≠ F120), E149 (= E163), N153 (= N167), D178 (= D192), T180 (≠ A194), S200 (= S214), S202 (≠ T216), K203 (= K217), S330 (≠ N343), T345 (= T358), R365 (= R378)
Query Sequence
>Ga0059261_3194 FitnessBrowser__Korea:Ga0059261_3194
MKRRTGQDRSITQNWKPATQAIRGGTARSEWGETSEALFLTSGYAYDCAGDAAARFSGDQ
QGMTYSRLQNPTVEMLEQRIALLEGAEACRATASGMAAMTAALLCQLSAGDHLIGGRAAF
GSCRWLTDTQLPKFGIETTVVDARDPQQFIDAIRPNTKVFFFETPANPTMDVVDLKAVCA
IARERGIVTVVDNAFATPALQRPMDFGADVVAYSATKMMDGQGRVLAGAVCGTEEFINNT
LLPFHRNTGPTLSPFNAWVVLKGLETLDLRIQRQSENALKVARFLEGRVPRVNFPGLPSH
PQHNLAMSQMAAAGPIFSIELDGGRTQAHGLLDALGLIDISNNIGDSRSLMTHPASTTHS
GVAEDQRLLMGVGEGMLRLNVGLEDPEDLIADLDQALGSVGL
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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