SitesBLAST
Comparing PP_1308 FitnessBrowser__Putida:PP_1308 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)
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
83% identity, 100% coverage: 1:398/398 of query aligns to 1:398/398 of 1pg8A
- active site: R61 (= R61), Y114 (= Y114), D186 (= D186), K211 (= K211)
- binding pyridoxal-5'-phosphate: Y59 (= Y59), R61 (= R61), S88 (= S88), G89 (= G89), M90 (= M90), Y114 (= Y114), D186 (= D186), S208 (= S208), T210 (= T210), K211 (= K211)
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)
83% identity, 100% coverage: 1:398/398 of query aligns to 1:398/398 of P13254
- YSR 59:61 (= YSR 59:61) binding
- R61 (= R61) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 89:90) binding in other chain
- Y114 (= Y114) binding
- C116 (= C116) 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 208:210) binding in other chain
- K211 (= K211) modified: N6-(pyridoxal phosphate)lysine
- K240 (= K240) 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 (= D241) 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 (= R375) binding
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
84% identity, 98% coverage: 9:398/398 of query aligns to 3:392/392 of 5x2xA
- active site: R55 (= R61), Y108 (= Y114), D180 (= D186), K205 (= K211)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y59), R55 (= R61), G83 (= G89), M84 (= M90), Y108 (= Y114), N155 (= N161), D180 (= D186), S202 (= S208), T204 (= T210), K205 (= K211), V333 (= V339), S334 (= S340), R369 (= R375)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
84% identity, 98% coverage: 9:398/398 of query aligns to 3:392/392 of 5x2wA
- active site: R55 (= R61), Y108 (= Y114), D180 (= D186), K205 (= K211)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y59), R55 (= R61), S82 (= S88), G83 (= G89), M84 (= M90), Y108 (= Y114), D180 (= D186), S202 (= S208), K205 (= K211), V333 (= V339), S334 (= S340), R369 (= R375)
3vk3A Crystal structure of l-methionine gamma-lyase from pseudomonas putida c116h mutant complexed with l-methionine (see paper)
84% identity, 98% coverage: 9:398/398 of query aligns to 8:397/397 of 3vk3A
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
84% identity, 98% coverage: 9:398/398 of query aligns to 4:393/393 of 5x30C
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
54% identity, 97% coverage: 9:394/398 of query aligns to 7:394/399 of 5dx5A
- active site: R59 (= R61), Y112 (= Y114), D186 (= D186), K211 (= K211)
- binding pyridoxal-5'-phosphate: Y57 (= Y59), R59 (= R61), S86 (= S88), G87 (= G89), M88 (= M90), Y112 (= Y114), D186 (= D186), F189 (≠ Y189), S208 (= S208), T210 (= T210), K211 (= K211)
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
52% identity, 97% coverage: 9:395/398 of query aligns to 7:393/396 of 6egrA
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
52% identity, 97% coverage: 9:395/398 of query aligns to 7:393/396 of 4hf8A
- active site: R59 (= R61), Y112 (= Y114), D184 (= D186), K209 (= K211)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G89), I88 (≠ M90), Y112 (= Y114), E155 (= E157), N159 (= N161), D184 (= D186), S206 (= S208), K209 (= K211), S338 (= S340), R373 (= R375)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
52% identity, 97% coverage: 9:395/398 of query aligns to 7:393/396 of 4omaA
- active site: R59 (= R61), Y112 (= Y114), D184 (= D186), K209 (= K211)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G89), I88 (≠ M90), Y112 (= Y114), D184 (= D186), S206 (= S208), T208 (= T210), K209 (= K211), V337 (= V339), S338 (= S340), R373 (= R375)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
52% identity, 97% coverage: 9:395/398 of query aligns to 7:393/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
52% identity, 97% coverage: 9:395/398 of query aligns to 7:393/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
52% identity, 97% coverage: 9:395/398 of query aligns to 7:393/396 of 3jw9A
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
51% identity, 97% coverage: 9:395/398 of query aligns to 6:392/395 of 5m3zA
- active site: R58 (= R61), Y111 (= Y114), D183 (= D186), K208 (= K211)
- binding norleucine: Y111 (= Y114), H113 (≠ C116), K208 (= K211), V336 (= V339), S337 (= S340)
- binding pyridoxal-5'-phosphate: G86 (= G89), I87 (≠ M90), Y111 (= Y114), E154 (= E157), D183 (= D186), T185 (= T188), S205 (= S208), T207 (= T210), K208 (= K211)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G89), I87 (≠ M90), Y111 (= Y114), D183 (= D186), S205 (= S208), T207 (= T210), K208 (= K211), V336 (= V339), S337 (= S340), R372 (= R375)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
50% identity, 97% coverage: 9:395/398 of query aligns to 7:382/386 of 3mkjA
- active site: Y101 (= Y114), D173 (= D186), K198 (= K211)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G89), I77 (≠ M90), Y101 (= Y114), E144 (= E157), D173 (= D186), F176 (≠ Y189), S195 (= S208), T197 (= T210), K198 (= K211)
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
45% identity, 93% coverage: 26:396/398 of query aligns to 20:391/394 of 1e5eA
- active site: R55 (= R61), Y108 (= Y114), D181 (= D186), K206 (= K211)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y59), R55 (= R61), G83 (= G89), M84 (= M90), Y108 (= Y114), N155 (= N161), D181 (= D186), S203 (= S208), T205 (= T210), K206 (= K211), S335 (= S340), T350 (= T355), R370 (= R375)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
45% identity, 93% coverage: 26:396/398 of query aligns to 20:391/393 of 1e5fA
- active site: R55 (= R61), Y108 (= Y114), D181 (= D186), K206 (= K211)
- binding pyridoxal-5'-phosphate: Y53 (= Y59), R55 (= R61), G83 (= G89), M84 (= M90), Y108 (= Y114), D181 (= D186), S203 (= S208), K206 (= K211)
7ba4A Structure of cystathionine gamma-lyase from pseudomonas aeruginosa
45% identity, 97% coverage: 10:394/398 of query aligns to 7:371/377 of 7ba4A
4iyoD 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)
47% identity, 97% coverage: 10:394/398 of query aligns to 4:380/384 of 4iyoD
- active site: R47 (= R61), Y99 (= Y114), D172 (= D186), K197 (= K211)
- binding serine: Y45 (= Y59), T48 (≠ I62), Y99 (= Y114), Y99 (= Y114), R104 (≠ A119), K197 (= K211), N227 (≠ D241), E325 (≠ V339), S326 (= S340), T341 (= T355), R361 (= R375)
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)
47% identity, 97% coverage: 10:394/398 of query aligns to 4:380/381 of 4iyoB
- active site: R47 (= R61), Y99 (= Y114), D172 (= D186), K197 (= K211)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: Y45 (= Y59), R47 (= R61)
- binding amino-acrylate: Y99 (= Y114), K197 (= K211), S326 (= S340), T341 (= T355), R361 (= R375)
- binding pyruvic acid: Q221 (≠ R235), F224 (≠ G238)
- binding serine: Y45 (= Y59), T48 (≠ I62), Y99 (= Y114), R104 (≠ A119), N227 (≠ D241), E325 (≠ V339)
Query Sequence
>PP_1308 FitnessBrowser__Putida:PP_1308
MRDSHHNTGFSTRAIHHGYDPLSHGGALVPPVYQTATYAFPTVEYGAACFAGEEPGHFYS
RISNPTLALLEQRMASLEGGEAGLALASGMGAITSTLWTLLRPGDELIVGRTLYGCTFAF
LHHGIGEFGVKVRHVDLNDAKALKAAISSKTRMIYFETPANPNMQLVDIAAVVEAVRGHD
VHVVVDNTYCTPYLQRPLELGADLVVHSATKYLSGHGDITAGLVVGRKVLVDRIRLEGLK
DMTGAVLSPHDAALLMRGIKTLALRMDRHCANAQQVAEFLVRQPQVELIHYPGLPSFAQY
ALAQRQMRLPGGMIAFELKGGIEAGRRFMNALQLFARAVSLGDAESLAQHPASMTHSSYT
PQERAHHGISEGLVRLSVGLEDVEDLLADVEQALQACC
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