SitesBLAST
Comparing GFF1919 FitnessBrowser__Phaeo:GFF1919 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)
36% identity, 96% coverage: 11:374/381 of query aligns to 21:396/397 of 3vk3A
5x30C Crystal structure of pseudomonas putida methionine gamma-lyase c116h mutant with l-homocysteine intermediates. (see paper)
36% identity, 96% coverage: 11:374/381 of query aligns to 17:392/393 of 5x30C
1pg8A Crystal structure of l-methionine alpha-, gamma-lyase
36% identity, 96% coverage: 11:374/381 of query aligns to 22:397/398 of 1pg8A
- active site: R61 (= R50), Y114 (= Y103), D186 (= D174), K211 (= K199)
- binding pyridoxal-5'-phosphate: Y59 (= Y48), R61 (= R50), S88 (= S77), G89 (= G78), M90 (= M79), Y114 (= Y103), D186 (= D174), S208 (= S196), T210 (≠ S198), K211 (= K199)
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)
36% identity, 96% coverage: 11:374/381 of query aligns to 22:397/398 of P13254
- YSR 59:61 (= YSR 48:50) binding
- R61 (= R50) mutation R->A,E,F: Loss of elimination activity against L-methionine.
- GM 89:90 (= GM 78:79) binding in other chain
- Y114 (= Y103) binding
- C116 (≠ D105) 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 (≠ SIS 196:198) binding in other chain
- K211 (= K199) modified: N6-(pyridoxal phosphate)lysine
- K240 (≠ P228) 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 (vs. gap) 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 (= R352) binding
5x2xA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-homocysteine intermediates (see paper)
36% identity, 96% coverage: 11:374/381 of query aligns to 16:391/392 of 5x2xA
- active site: R55 (= R50), Y108 (= Y103), D180 (= D174), K205 (= K199)
- binding (2E)-2-{[(1E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}but-2-enoic acid: Y53 (= Y48), R55 (= R50), G83 (= G78), M84 (= M79), Y108 (= Y103), N155 (≠ S149), D180 (= D174), S202 (= S196), T204 (≠ S198), K205 (= K199), V333 (= V316), S334 (= S317), R369 (= R352)
5x2wA Crystal structure of pseudomonas putida methionine gamma-lyase wild type with l-methionine intermediates (see paper)
36% identity, 96% coverage: 11:374/381 of query aligns to 16:391/392 of 5x2wA
- active site: R55 (= R50), Y108 (= Y103), D180 (= D174), K205 (= K199)
- binding (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid: Y53 (= Y48), R55 (= R50), S82 (= S77), G83 (= G78), M84 (= M79), Y108 (= Y103), D180 (= D174), S202 (= S196), K205 (= K199), V333 (= V316), S334 (= S317), R369 (= R352)
5m3zA Crystal structure of citrobacter freundii methionine gamma-lyase with c115h replacement in the complex with l-norleucine (see paper)
33% identity, 98% coverage: 2:374/381 of query aligns to 10:394/395 of 5m3zA
- active site: R58 (= R50), Y111 (= Y103), D183 (= D174), K208 (= K199)
- binding norleucine: Y111 (= Y103), H113 (≠ D105), K208 (= K199), V336 (= V316), S337 (= S317)
- binding pyridoxal-5'-phosphate: G86 (= G78), I87 (≠ M79), Y111 (= Y103), E154 (= E145), D183 (= D174), T185 (≠ S176), S205 (= S196), T207 (≠ S198), K208 (= K199)
- binding 2-[o-phosphonopyridoxyl]-amino-hexanoic acid: G86 (= G78), I87 (≠ M79), Y111 (= Y103), D183 (= D174), S205 (= S196), T207 (≠ S198), K208 (= K199), V336 (= V316), S337 (= S317), R372 (= R352)
4omaA The crystal structure of methionine gamma-lyase from citrobacter freundii in complex with l-cycloserine pyridoxal-5'-phosphate (see paper)
33% identity, 98% coverage: 2:374/381 of query aligns to 11:395/396 of 4omaA
- active site: R59 (= R50), Y112 (= Y103), D184 (= D174), K209 (= K199)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G87 (= G78), I88 (≠ M79), Y112 (= Y103), D184 (= D174), S206 (= S196), T208 (≠ S198), K209 (= K199), V337 (= V316), S338 (= S317), R373 (= R352)
3jwbA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with norleucine (see paper)
33% identity, 98% coverage: 2:374/381 of query aligns to 11:395/396 of 3jwbA
3jwaA Crystal structure of l-methionine gamma-lyase from citrobacter freundii with methionine phosphinate (see paper)
33% identity, 98% coverage: 2:374/381 of query aligns to 11:395/396 of 3jwaA
3jw9A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with s-ethyl-cysteine (see paper)
33% identity, 98% coverage: 2:374/381 of query aligns to 11:395/396 of 3jw9A
6egrA Crystal structure of citrobacter freundii methionine gamma-lyase with v358y replacement (see paper)
33% identity, 98% coverage: 2:374/381 of query aligns to 11:395/396 of 6egrA
1e5eA Methionine gamma-lyase (mgl) from trichomonas vaginalis in complex with propargylglycine
34% identity, 97% coverage: 5:373/381 of query aligns to 10:391/394 of 1e5eA
- active site: R55 (= R50), Y108 (= Y103), D181 (= D174), K206 (= K199)
- binding n-(hydroxy{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)norvaline: Y53 (= Y48), R55 (= R50), G83 (= G78), M84 (= M79), Y108 (= Y103), N155 (≠ S149), D181 (= D174), S203 (= S196), T205 (≠ S198), K206 (= K199), S335 (= S317), T350 (≠ A331), R370 (= R352)
1e5fA Methionine gamma-lyase (mgl) from trichomonas vaginalis
34% identity, 97% coverage: 5:373/381 of query aligns to 10:391/393 of 1e5fA
- active site: R55 (= R50), Y108 (= Y103), D181 (= D174), K206 (= K199)
- binding pyridoxal-5'-phosphate: Y53 (= Y48), R55 (= R50), G83 (= G78), M84 (= M79), Y108 (= Y103), D181 (= D174), S203 (= S196), K206 (= K199)
4hf8A Crystal structure of l-methionine gamma-lyase from citrobacter freundii with glycine (see paper)
33% identity, 98% coverage: 2:374/381 of query aligns to 11:395/396 of 4hf8A
- active site: R59 (= R50), Y112 (= Y103), D184 (= D174), K209 (= K199)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: G87 (= G78), I88 (≠ M79), Y112 (= Y103), E155 (= E145), N159 (≠ S149), D184 (= D174), S206 (= S196), K209 (= K199), S338 (= S317), R373 (= R352)
5dx5A Crystal structure of methionine gamma-lyase from clostridium sporogenes (see paper)
34% identity, 95% coverage: 11:371/381 of query aligns to 20:394/399 of 5dx5A
- active site: R59 (= R50), Y112 (= Y103), D186 (= D174), K211 (= K199)
- binding pyridoxal-5'-phosphate: Y57 (= Y48), R59 (= R50), S86 (= S77), G87 (= G78), M88 (= M79), Y112 (= Y103), D186 (= D174), F189 (= F177), S208 (= S196), T210 (≠ S198), K211 (= K199)
3mkjA Methionine gamma-lyase from citrobacter freundii with pyridoximine-5'- phosphate (see paper)
32% identity, 98% coverage: 2:374/381 of query aligns to 11:384/386 of 3mkjA
- active site: Y101 (= Y103), D173 (= D174), K198 (= K199)
- binding [5-hydroxy-4-(iminomethyl)-6-methyl-pyridin-3-yl]methyl dihydrogen phosphate: G76 (= G78), I77 (≠ M79), Y101 (= Y103), E144 (= E145), D173 (= D174), F176 (= F177), S195 (= S196), T197 (≠ S198), K198 (= K199)
4l0oH Structure determination of cystathionine gamma-synthase from helicobacter pylori
34% identity, 95% coverage: 11:371/381 of query aligns to 15:370/373 of 4l0oH
- active site: R40 (= R50), Y92 (= Y103), D164 (= D174), K189 (= K199)
- binding pyridoxal-5'-phosphate: Y38 (= Y48), R40 (= R50), S67 (= S77), G68 (= G78), L69 (≠ M79), Y92 (= Y103), D164 (= D174), S186 (= S196), T188 (≠ S198), K189 (= K199)
6ld9A Crystal structure of cystathionine gamma synthase from xanthomonas oryzae pv. Oryzae in complex with cystathionine
36% identity, 96% coverage: 11:376/381 of query aligns to 17:385/387 of 6ld9A
- binding (2~{S})-4-[(2~{R})-2-azanyl-3-oxidanyl-3-oxidanylidene-propyl]sulfanyl-2-[(~{E})-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]butanoic acid: Y46 (= Y48), R48 (= R50), S49 (≠ T51), G76 (= G78), M77 (= M79), Y101 (= Y103), R106 (= R108), N148 (≠ S149), D173 (= D174), S195 (= S196), T197 (≠ S198), K198 (= K199), N227 (≠ P228), E325 (≠ V316), S326 (= S317), T341 (≠ A332), R361 (= R352)
7d7oB Crystal structure of cystathionine gamma-lyase from bacillus cereus atcc 14579 (see paper)
32% identity, 94% coverage: 15:371/381 of query aligns to 19:376/377 of 7d7oB
Query Sequence
>GFF1919 FitnessBrowser__Phaeo:GFF1919
MQLLLSSNEVDDAFGSVAPAIHQSSLFTFPTYDALEERFSGKSEADIYSRTSNPTVRLLE
DKLAKLERGDAAIAFGSGMAAISGAVLSLVKAGDRIVSTFNTYSDAYRLFEILMARLGVS
VTYVDCNDIDELSNALVGARLLFLESPSSYVFETCDIKKATDVAKQHGVITIFDNSFASP
LGQKPLLHGADIVVHSISKYLSGHSDVVAGCVVGSHDLINQIRDTALPLLGAKLSAMEAW
LVIRGLRTLPMRLREHQEAADFVVGKLKDDSRIAKIHRAMPSSTLSGAGGLFTVELADGL
DVRAFCDALKVFRLGVSWGGFESLALPASVAARIDSGPNALQKFGVSRNAIRLFTGLEGR
EVLLADICQALTAAESMEKSR
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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