SitesBLAST
Comparing WP_012536942.1 NCBI__GCF_000021485.1:WP_012536942.1 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)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
48% identity, 90% coverage: 34:396/404 of query aligns to 27:390/396 of 4omaA
- active site: R59 (= R66), Y112 (≠ F119), D184 (= D191), K209 (= K216)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G94), I88 (≠ M95), Y112 (≠ F119), D184 (= D191), S206 (= S213), T208 (= T215), K209 (= K216), V337 (≠ A343), S338 (≠ N344), R373 (= R379)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
48% identity, 90% coverage: 34:396/404 of query aligns to 27:390/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
48% identity, 90% coverage: 34:396/404 of query aligns to 27:390/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
48% identity, 90% coverage: 34:396/404 of query aligns to 27:390/396 of 3jw9A
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
48% identity, 90% coverage: 34:396/404 of query aligns to 26:389/395 of 5m3zA
- active site: R58 (= R66), Y111 (≠ F119), D183 (= D191), K208 (= K216)
- binding norleucine: Y111 (≠ F119), H113 (≠ T121), K208 (= K216), V336 (≠ A343), S337 (≠ N344)
- binding pyridoxal-5'-phosphate: G86 (= G94), I87 (≠ M95), Y111 (≠ F119), E154 (= E162), D183 (= D191), T185 (≠ C193), S205 (= S213), T207 (= T215), K208 (= K216)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G94), I87 (≠ M95), Y111 (≠ F119), D183 (= D191), S205 (= S213), T207 (= T215), K208 (= K216), V336 (≠ A343), S337 (≠ N344), R372 (= R379)
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
48% identity, 90% coverage: 34:395/404 of query aligns to 27:389/396 of 4hf8A
- active site: R59 (= R66), Y112 (≠ F119), D184 (= D191), K209 (= K216)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G94), I88 (≠ M95), Y112 (≠ F119), E155 (= E162), N159 (= N166), D184 (= D191), S206 (= S213), K209 (= K216), S338 (≠ N344), R373 (= R379)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
48% identity, 90% coverage: 34:396/404 of query aligns to 27:390/396 of 6egrA
P9WGB5 O-succinylhomoserine sulfhydrylase; OSH sulfhydrylase; OSHS sulfhydrylase; EC 2.5.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
46% identity, 96% coverage: 12:399/404 of query aligns to 15:406/406 of P9WGB5
- K219 (= K216) modified: N6-(pyridoxal phosphate)lysine
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
44% identity, 91% coverage: 37:402/404 of query aligns to 30:398/399 of 5dx5A
- active site: R59 (= R66), Y112 (≠ F119), D186 (= D191), K211 (= K216)
- binding pyridoxal-5'-phosphate: Y57 (= Y64), R59 (= R66), S86 (= S93), G87 (= G94), M88 (= M95), Y112 (≠ F119), D186 (= D191), F189 (= F194), S208 (= S213), T210 (= T215), K211 (= K216)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
47% identity, 90% coverage: 34:396/404 of query aligns to 27:379/386 of 3mkjA
- active site: Y101 (≠ F119), D173 (= D191), K198 (= K216)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G94), I77 (≠ M95), Y101 (≠ F119), E144 (= E162), D173 (= D191), F176 (= F194), S195 (= S213), T197 (= T215), K198 (= K216)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
40% identity, 97% coverage: 12:402/404 of query aligns to 1:393/393 of 1e5fA
- active site: R55 (= R66), Y108 (≠ F119), D181 (= D191), K206 (= K216)
- binding pyridoxal-5'-phosphate: Y53 (= Y64), R55 (= R66), G83 (= G94), M84 (= M95), Y108 (≠ F119), D181 (= D191), S203 (= S213), K206 (= K216)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
40% identity, 97% coverage: 12:402/404 of query aligns to 1:393/394 of 1e5eA
- active site: R55 (= R66), Y108 (≠ F119), D181 (= D191), K206 (= K216)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y64), R55 (= R66), G83 (= G94), M84 (= M95), Y108 (≠ F119), N155 (= N166), D181 (= D191), S203 (= S213), T205 (= T215), K206 (= K216), S335 (≠ N344), T350 (= T359), R370 (= R379)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
43% identity, 95% coverage: 19:400/404 of query aligns to 10:396/398 of 1pg8A
- active site: R61 (= R66), Y114 (≠ F119), D186 (= D191), K211 (= K216)
- binding pyridoxal-5'-phosphate: Y59 (= Y64), R61 (= R66), S88 (= S93), G89 (= G94), M90 (= M95), Y114 (≠ F119), D186 (= D191), S208 (= S213), T210 (= T215), K211 (= K216)
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)
43% identity, 95% coverage: 19:400/404 of query aligns to 10:396/398 of P13254
- YSR 59:61 (≠ YAR 64:66) binding
- R61 (= R66) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 94:95) binding in other chain
- Y114 (≠ F119) binding
- C116 (≠ T121) 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 213:215) binding in other chain
- K211 (= K216) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ R241) 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 (≠ N242) 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 (= R379) binding
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
43% identity, 95% coverage: 19:400/404 of query aligns to 5:391/393 of 5x30C
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
43% identity, 95% coverage: 19:400/404 of query aligns to 4:390/392 of 5x2xA
- active site: R55 (= R66), Y108 (≠ F119), D180 (= D191), K205 (= K216)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y64), R55 (= R66), G83 (= G94), M84 (= M95), Y108 (≠ F119), N155 (= N166), D180 (= D191), S202 (= S213), T204 (= T215), K205 (= K216), V333 (≠ A343), S334 (≠ N344), R369 (= R379)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
43% identity, 95% coverage: 19:400/404 of query aligns to 4:390/392 of 5x2wA
- active site: R55 (= R66), Y108 (≠ F119), D180 (= D191), K205 (= K216)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y64), R55 (= R66), S82 (= S93), G83 (= G94), M84 (= M95), Y108 (≠ F119), D180 (= D191), S202 (= S213), K205 (= K216), V333 (≠ A343), S334 (≠ N344), R369 (= R379)
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
43% identity, 95% coverage: 19:400/404 of query aligns to 9:395/397 of 3vk3A
3aeoA Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 containing methionine alpha, beta-enamine-pyridoxamine- 5'-phosphate
36% identity, 91% coverage: 31:398/404 of query aligns to 18:384/387 of 3aeoA
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y51 (= Y64), R53 (= R66), G81 (= G94), M82 (= M95), Y106 (≠ F119), E149 (= E162), N153 (= N166), D178 (= D191), S200 (= S213), S202 (≠ T215), K203 (= K216), V329 (≠ A343), S330 (≠ N344), T345 (= T359), R365 (= R379)
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
36% identity, 91% coverage: 31:398/404 of query aligns to 18:384/387 of 3aelA
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]-4-(methylsulfanyl)butanoic acid: Y51 (= Y64), R53 (= R66)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: G81 (= G94), M82 (= M95), Y106 (≠ F119), E149 (= E162), N153 (= N166), D178 (= D191), T180 (≠ C193), S200 (= S213), S202 (≠ T215), K203 (= K216), S330 (≠ N344), T345 (= T359), R365 (= R379)
Query Sequence
>WP_012536942.1 NCBI__GCF_000021485.1:WP_012536942.1
MNTKNTNPDWADRLRPETIAIRAGIHRTQEQEHSEAIFPTSSFVFDSAEEAADRFAGRVP
GNIYARFTNPTVRTFEERLAALEGAEACVATASGMAACLTAFMGILKAGDHVVASRSIFG
TTVQLLGNILSRFGVETSFVPLADVPAWRAALRPNTRMLFLETPSNPLTEIGDMQALADL
AHVHDAWLVVDNCFCTPALQQPLKFGADLVIHSATKYLDGQGRTLGGAVCGSTELLNSGP
RNFVRTAGPSLSPFNAWVQLKGLETLGLRMERHCANAQKIAEWLEARPEVARVYYPGLDS
HPQQALAARQQRLPGAILSFDLHGGQKAAWAFVDALRLLSLTANLGDAKTTITHPASTTH
SRVSPEARAAAGVGDGLLRISVGLEHADDLREDMERGFAALVAR
Or try a new SitesBLAST search
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