SitesBLAST
Comparing WP_019896009.1 NCBI__GCF_000384235.1:WP_019896009.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
45% identity, 96% coverage: 9:390/399 of query aligns to 20:405/406 of P9WGB5
- K219 (= K208) modified: N6-(pyridoxal phosphate)lysine
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
43% identity, 91% coverage: 26:390/399 of query aligns to 27:392/396 of 4omaA
- active site: R59 (= R58), Y112 (≠ F111), D184 (= D183), K209 (= K208)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G86), I88 (≠ M87), Y112 (≠ F111), D184 (= D183), S206 (= S205), T208 (= T207), K209 (= K208), V337 (≠ A335), S338 (≠ N336), R373 (= R371)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
43% identity, 91% coverage: 26:390/399 of query aligns to 27:392/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
43% identity, 91% coverage: 26:390/399 of query aligns to 27:392/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
43% identity, 91% coverage: 26:390/399 of query aligns to 27:392/396 of 3jw9A
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
43% identity, 91% coverage: 26:390/399 of query aligns to 26:391/395 of 5m3zA
- active site: R58 (= R58), Y111 (≠ F111), D183 (= D183), K208 (= K208)
- binding norleucine: Y111 (≠ F111), H113 (≠ T113), K208 (= K208), V336 (≠ A335), S337 (≠ N336)
- binding pyridoxal-5'-phosphate: G86 (= G86), I87 (≠ M87), Y111 (≠ F111), E154 (= E154), D183 (= D183), T185 (≠ C185), S205 (= S205), T207 (= T207), K208 (= K208)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G86), I87 (≠ M87), Y111 (≠ F111), D183 (= D183), S205 (= S205), T207 (= T207), K208 (= K208), V336 (≠ A335), S337 (≠ N336), R372 (= R371)
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
43% identity, 91% coverage: 26:390/399 of query aligns to 27:392/396 of 4hf8A
- active site: R59 (= R58), Y112 (≠ F111), D184 (= D183), K209 (= K208)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G86), I88 (≠ M87), Y112 (≠ F111), E155 (= E154), N159 (= N158), D184 (= D183), S206 (= S205), K209 (= K208), S338 (≠ N336), R373 (= R371)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
43% identity, 91% coverage: 26:390/399 of query aligns to 27:392/396 of 6egrA
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
41% identity, 97% coverage: 5:393/399 of query aligns to 5:397/399 of 5dx5A
- active site: R59 (= R58), Y112 (≠ F111), D186 (= D183), K211 (= K208)
- binding pyridoxal-5'-phosphate: Y57 (= Y56), R59 (= R58), S86 (= S85), G87 (= G86), M88 (= M87), Y112 (≠ F111), D186 (= D183), F189 (= F186), S208 (= S205), T210 (= T207), K211 (= K208)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
43% identity, 91% coverage: 26:390/399 of query aligns to 27:381/386 of 3mkjA
- active site: Y101 (≠ F111), D173 (= D183), K198 (= K208)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G86), I77 (≠ M87), Y101 (≠ F111), E144 (= E154), D173 (= D183), F176 (= F186), S195 (= S205), T197 (= T207), K198 (= K208)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
41% identity, 96% coverage: 8:390/399 of query aligns to 10:394/398 of 1pg8A
- active site: R61 (= R58), Y114 (≠ F111), D186 (= D183), K211 (= K208)
- binding pyridoxal-5'-phosphate: Y59 (= Y56), R61 (= R58), S88 (= S85), G89 (= G86), M90 (= M87), Y114 (≠ F111), D186 (= D183), S208 (= S205), T210 (= T207), K211 (= K208)
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)
41% identity, 96% coverage: 8:390/399 of query aligns to 10:394/398 of P13254
- YSR 59:61 (= YSR 56:58) binding
- R61 (= R58) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 86:87) binding in other chain
- Y114 (≠ F111) binding
- C116 (≠ T113) 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 205:207) binding in other chain
- K211 (= K208) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ M236) 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 (≠ R237) 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 (= R371) binding
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
38% identity, 96% coverage: 9:390/399 of query aligns to 6:389/394 of 1e5eA
- active site: R55 (= R58), Y108 (≠ F111), D181 (= D183), K206 (= K208)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y56), R55 (= R58), G83 (= G86), M84 (= M87), Y108 (≠ F111), N155 (= N158), D181 (= D183), S203 (= S205), T205 (= T207), K206 (= K208), S335 (≠ N336), T350 (= T351), R370 (= R371)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
38% identity, 96% coverage: 9:390/399 of query aligns to 6:389/393 of 1e5fA
- active site: R55 (= R58), Y108 (≠ F111), D181 (= D183), K206 (= K208)
- binding pyridoxal-5'-phosphate: Y53 (= Y56), R55 (= R58), G83 (= G86), M84 (= M87), Y108 (≠ F111), D181 (= D183), S203 (= S205), K206 (= K208)
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
41% identity, 96% coverage: 8:390/399 of query aligns to 9:393/397 of 3vk3A
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
41% identity, 96% coverage: 8:390/399 of query aligns to 4:388/392 of 5x2xA
- active site: R55 (= R58), Y108 (≠ F111), D180 (= D183), K205 (= K208)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y56), R55 (= R58), G83 (= G86), M84 (= M87), Y108 (≠ F111), N155 (= N158), D180 (= D183), S202 (= S205), T204 (= T207), K205 (= K208), V333 (≠ A335), S334 (≠ N336), R369 (= R371)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
41% identity, 96% coverage: 8:390/399 of query aligns to 4:388/392 of 5x2wA
- active site: R55 (= R58), Y108 (≠ F111), D180 (= D183), K205 (= K208)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y56), R55 (= R58), S82 (= S85), G83 (= G86), M84 (= M87), Y108 (≠ F111), D180 (= D183), S202 (= S205), K205 (= K208), V333 (≠ A335), S334 (≠ N336), R369 (= R371)
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
41% identity, 96% coverage: 8:390/399 of query aligns to 5:389/393 of 5x30C
4iyoB Crystal structure of cystathionine gamma lyase from xanthomonas oryzae pv. Oryzae (xometc) in complex with e-site serine, a-site serine, a- site external aldimine structure with aminoacrylate and a-site iminopropionate intermediates (see paper)
43% identity, 96% coverage: 6:390/399 of query aligns to 2:380/381 of 4iyoB
- active site: R47 (= R58), Y99 (≠ F111), D172 (= D183), K197 (= K208)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: Y45 (= Y56), R47 (= R58)
- binding amino-acrylate: Y99 (≠ F111), K197 (= K208), S326 (≠ N336), T341 (= T351), R361 (= R371)
- binding pyruvic acid: Q221 (≠ K231), F224 (≠ G234)
- binding serine: Y45 (= Y56), T48 (≠ F59), Y99 (≠ F111), R104 (≠ V116), N227 (≠ R237), E325 (≠ A335)
4iy7B Crystal structure of cystathionine gamma lyase (xometc) from xanthomonas oryzae pv. Oryzae in complex with e-site serine, a-site external aldimine structure with serine and a-site external aldimine structure with aminoacrylate intermediates (see paper)
43% identity, 96% coverage: 6:390/399 of query aligns to 2:380/381 of 4iy7B
- active site: R47 (= R58), Y99 (≠ F111), D172 (= D183), K197 (= K208)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: Y45 (= Y56), R47 (= R58)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: G75 (= G86), M76 (= M87), Y99 (≠ F111), E143 (= E154), N147 (= N158), D172 (= D183), S194 (= S205), K197 (= K208), S326 (≠ N336), L327 (= L337), T341 (= T351), R361 (= R371)
- binding pyruvic acid: Q221 (≠ K231), F224 (≠ G234)
- binding serine: Y45 (= Y56), T48 (≠ F59), Y99 (≠ F111), R104 (≠ V116), N227 (≠ R237), E325 (≠ A335)
Query Sequence
>WP_019896009.1 NCBI__GCF_000384235.1:WP_019896009.1
MDETQLDMATLAIRAGYQQTAEQENSEAIFPTSSFRYHSAQQAADRFSGDEPGNVYSRFT
NPTVQAFERRLAAMEEGEACVATASGMSAILASMMGLLQAGDHLVCSQSVFGTTRVLFDQ
YLRKFGIEVTYVPLTDYAAWQNALQDNTRLLFLETPSNPLSEIADIARLGELARANQAWL
VVDNCFCTPALQKPLTLGADLVVHSATKFLDGQGRVVGGAVVGPAALVDEKIRGVMRTAG
PSMSPFNAWVFLKGLETLALRMKAHSEQAQALADWLVAQPAVKQVYFPGLASHPQRALIA
RQQSGPGGLLAFEVAGGREAAWTVIDQTRMISITANLGDVKTSITHPATTTHARVSQADR
EASGISESLVRVSVGLEAIEDIQADLARGLGMIGSSQQD
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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