SitesBLAST
Comparing WP_012171767.1 NCBI__GCF_000010525.1:WP_012171767.1 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)
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
42% identity, 93% coverage: 25:384/389 of query aligns to 26:393/397 of 3vk3A
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
42% identity, 93% coverage: 25:384/389 of query aligns to 22:389/393 of 5x30C
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
42% identity, 93% coverage: 25:384/389 of query aligns to 21:388/392 of 5x2xA
- active site: R55 (= R59), Y108 (= Y112), 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 (= Y57), R55 (= R59), G83 (= G87), M84 (= M88), Y108 (= Y112), N155 (≠ S158), D180 (= D183), S202 (≠ A205), T204 (≠ S207), K205 (= K208), V333 (= V330), S334 (= S331), R369 (= R365)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
42% identity, 93% coverage: 25:384/389 of query aligns to 21:388/392 of 5x2wA
- active site: R55 (= R59), Y108 (= Y112), 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 (= Y57), R55 (= R59), S82 (= S86), G83 (= G87), M84 (= M88), Y108 (= Y112), D180 (= D183), S202 (≠ A205), K205 (= K208), V333 (= V330), S334 (= S331), R369 (= R365)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
42% identity, 93% coverage: 25:384/389 of query aligns to 27:394/398 of 1pg8A
- active site: R61 (= R59), Y114 (= Y112), D186 (= D183), K211 (= K208)
- binding pyridoxal-5'-phosphate: Y59 (= Y57), R61 (= R59), S88 (= S86), G89 (= G87), M90 (= M88), Y114 (= Y112), D186 (= D183), S208 (≠ A205), T210 (≠ S207), 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)
42% identity, 93% coverage: 25:384/389 of query aligns to 27:394/398 of P13254
- YSR 59:61 (= YSR 57:59) binding pyridoxal 5'-phosphate
- 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 substrate
- C116 (≠ D114) 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 (≠ AAS 205:207) binding in other chain
- K211 (= K208) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ A237) 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 (≠ Y238) 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 (= R365) binding substrate
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
36% identity, 93% coverage: 23:384/389 of query aligns to 19:389/393 of 1e5fA
- active site: R55 (= R59), Y108 (= Y112), D181 (= D183), K206 (= K208)
- binding pyridoxal-5'-phosphate: Y53 (= Y57), R55 (= R59), G83 (= G87), M84 (= M88), Y108 (= Y112), D181 (= D183), S203 (≠ A205), K206 (= K208)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
36% identity, 94% coverage: 23:389/389 of query aligns to 19:394/394 of 1e5eA
- active site: R55 (= R59), Y108 (= Y112), D181 (= D183), K206 (= K208)
- 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 (≠ S158), D181 (= D183), S203 (≠ A205), T205 (≠ S207), K206 (= K208), S335 (= S331), T350 (≠ V340), R370 (= R365)
4l0oH Structure determination of cystathionine gamma-synthase from helicobacter pylori
37% identity, 96% coverage: 13:384/389 of query aligns to 9:370/373 of 4l0oH
- active site: R40 (= R59), Y92 (= Y112), D164 (= D183), K189 (= K208)
- binding pyridoxal-5'-phosphate: Y38 (= Y57), R40 (= R59), S67 (= S86), G68 (= G87), L69 (≠ M88), Y92 (= Y112), D164 (= D183), S186 (≠ A205), T188 (≠ S207), K189 (= K208)
7mcyH Crystal structure of staphylococcus aureus cystathionine gamma lyase, holoenzyme with bound nl3 (see paper)
37% identity, 96% coverage: 13:384/389 of query aligns to 9:377/380 of 7mcyH
- binding 3-{[6-(7-chloro-1-benzothiophen-2-yl)-1H-indol-1-yl]methyl}-1H-pyrazole-5-carboxylic acid: D97 (≠ N110), V98 (= V111), Y99 (= Y112), G100 (≠ S113), Y103 (= Y116), N146 (≠ S158), P147 (≠ L159), T338 (≠ P345), H339 (≠ L346), I342 (≠ A349)
- binding pyridoxal-5'-phosphate: H9 (≠ Q13), G10 (= G14)
Sites not aligning to the query:
7mcuH Crystal structure of staphylococcus aureus cystathionine gamma lyase, holoenzyme with bound nl2 (see paper)
37% identity, 96% coverage: 13:384/389 of query aligns to 9:377/380 of 7mcuH
Sites not aligning to the query:
7mctH Crystal structure of staphylococcus aureus cystathionine gamma lyase, holoenzyme with bound nl1 (see paper)
37% identity, 96% coverage: 13:384/389 of query aligns to 9:377/380 of 7mctH
Sites not aligning to the query:
7mcqA Crystal structure of staphylococcus aureus cystathionine gamma lyase, aoaa-bound enzyme in dimeric form (see paper)
37% identity, 96% coverage: 13:384/389 of query aligns to 9:377/380 of 7mcqA
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Y45 (= Y57), R47 (= R59), S74 (= S86), G75 (= G87), V76 (≠ M88), Y99 (= Y112), D171 (= D183), S193 (≠ A205), T195 (≠ S207), K196 (= K208), E322 (≠ V330), S323 (= S331)
7mcbH Crystal structure of staphylococcus aureus cystathionine gamma lyase holoenzyme (see paper)
37% identity, 96% coverage: 13:384/389 of query aligns to 9:377/380 of 7mcbH
Sites not aligning to the query:
3aeoA Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 containing methionine alpha, beta-enamine-pyridoxamine- 5'-phosphate
36% identity, 92% coverage: 29:384/389 of query aligns to 23:384/387 of 3aeoA
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y51 (= Y57), R53 (= R59), G81 (= G87), M82 (= M88), Y106 (= Y112), E149 (= E154), N153 (≠ S158), D178 (= D183), S200 (≠ A205), S202 (= S207), K203 (= K208), V329 (= V330), S330 (= S331), T345 (≠ P345), R365 (= R365)
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, 92% coverage: 29:384/389 of query aligns to 23:384/387 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 (= E154), N153 (≠ S158), D178 (= D183), T180 (≠ S185), S200 (≠ A205), S202 (= S207), K203 (= K208), S330 (= S331), T345 (≠ P345), R365 (= R365)
3aejC Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 tetramer containing michaelis complex and methionine- pyridoxal-5'-phosphate
36% identity, 92% coverage: 29:384/389 of query aligns to 23:384/387 of 3aejC
- active site: R53 (= R59), Y106 (= Y112), D178 (= D183), K203 (= K208)
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: F42 (≠ Y48), Y51 (= Y57), R53 (= R59)
- binding methionine: Y106 (= Y112), K203 (= K208), S330 (= S331), L331 (≠ W332), T345 (≠ P345), R365 (= R365)
3aejA Reaction intermediate structure of entamoeba histolytica methionine gamma-lyase 1 tetramer containing michaelis complex and methionine- pyridoxal-5'-phosphate
36% identity, 92% coverage: 29:384/389 of query aligns to 23:384/387 of 3aejA
- binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: Y51 (= Y57), R53 (= R59), G81 (= G87), M82 (= M88), Y106 (= Y112), E149 (= E154), N153 (≠ S158), D178 (= D183), S200 (≠ A205), S202 (= S207), K203 (= K208), S330 (= S331), L331 (≠ W332), T345 (≠ P345), R365 (= R365)
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
36% identity, 92% coverage: 29:387/389 of query aligns to 28:394/395 of 5m3zA
- active site: R58 (= R59), Y111 (= Y112), D183 (= D183), K208 (= K208)
- binding norleucine: Y111 (= Y112), H113 (≠ D114), K208 (= K208), V336 (= V330), S337 (= S331)
- binding pyridoxal-5'-phosphate: G86 (= G87), I87 (≠ M88), Y111 (= Y112), E154 (= E154), D183 (= D183), T185 (≠ S185), S205 (≠ A205), T207 (≠ S207), K208 (= K208)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G87), I87 (≠ M88), Y111 (= Y112), D183 (= D183), S205 (≠ A205), T207 (≠ S207), K208 (= K208), V336 (= V330), S337 (= S331), R372 (= R365)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
36% identity, 92% coverage: 29:387/389 of query aligns to 29:395/396 of 4omaA
- active site: R59 (= R59), Y112 (= Y112), 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 (= G87), I88 (≠ M88), Y112 (= Y112), D184 (= D183), S206 (≠ A205), T208 (≠ S207), K209 (= K208), V337 (= V330), S338 (= S331), R373 (= R365)
Query Sequence
>WP_012171767.1 NCBI__GCF_000010525.1:WP_012171767.1
MNKPLDHEALPAQGGWSREVNLLAAAVPPIFQTSLFTFDTYADMAAVYAGRSHQLIYSRG
DNPTVMAFERAVAELEGAEAGRAFSSGMGAISATVLALVSAGDRIVTVRNVYSDAYRLFE
LMLSRFGVVVDYVDGTDAEAVEAVLPGAKLLYLESPTSLAFELQDIARLARAARTHGVVS
VIDNSWATPLFQRPIAHGVDLVVHAASKYLGGHSDTVAGVVVGSAELVGRINASSYAYLG
AKLSPFEAWLLLRGLHTLPMRMARHMSSGLALAERLRAHPDVELVRHPAFSDHPGRASLS
GFAGVFSFEVGEAIDVPTFVDALRLVRIGVSWGGPESLVVPALAPLQLAKANCFARFGIS
PRLIRLSAGMEDETLIWADIEQALHGARR
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